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Conserved domains on  [gi|21389617|ref|NP_653305|]
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apoptosis-inducing factor 3 isoform 1 [Homo sapiens]

Protein Classification

pyridine nucleotide-disulfide oxidoreductase (domain architecture ID 11556476)

pyridine nucleotide-disulfide oxidoreductase containing a Rieske (2Fe-2S)-binding domain, similar to human apoptosis-inducing factor 3

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
195-493 5.30e-74

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


:

Pssm-ID: 311792 [Multi-domain]  Cd Length: 301  Bit Score: 238.76  E-value: 5.30e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   195 TNVLIVGAGAAGLVCAETLRQEGFsdRIVLCTLDRHLPYDRPKLSKSLD---------TQPEQLALRPKE--FFRAYGIE 263
Cdd:pfam07992   1 YDVVIIGGGPAGLAAALTLARAGG--KVTLIEDEGTCPYGGCVLSKALLgaaeapeiaSLWAELYERKEEvvKKLNNGIE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   264 VLTEAQVVTVDVRTKKVVFK-----DGFKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDANRVVRLARGRNVVVV 338
Cdd:pfam07992  79 VLLGTEVVSIDPGAKKVVLEnlvdgDGETITYDRLVIATGARPRLPPIPGVELNVGKLVRTLDSAEALRLKLLPKRLVVV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   339 GAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSELRGqEGKLKEVVLKSSKVV 418
Cdd:pfam07992 159 GGGYIGVELAAALAKLGKEVTLIEALDRLLRAF-DEEISAILEKALKKNGVEVRLGTSVKEIIG-DGDVVKVILKDGTEI 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21389617   419 RADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAvtfplawrnnRKVNIPHWQMAHAQG 493
Cdd:pfam07992 237 DADLVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDC----------RVGGPELAQNAVAQG 301
Rieske_AIFL_N cd03478
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ...
70-164 2.18e-55

AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family show similarity to human AIFL, containing an N-terminal Rieske domain and a C-terminal pyridine nucleotide-disulfide oxidoreductase domain (Pyr_redox). The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. AIFL shares 35% homology with human AIF (apoptosis-inducing factor), mainly in the Pyr_redox domain. AIFL is predominantly localized to the mitochondria. AIFL induces apoptosis in a caspase-dependent manner.


:

Pssm-ID: 239560 [Multi-domain]  Cd Length: 95  Bit Score: 182.05  E-value: 2.18e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  70 AAVCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDFPGLD 149
Cdd:cd03478   1 AVVCRLSDLGDGEMKEVDVGDGKVLLVRQGGEVHAIGAKCPHYGAPLAKGVLTDGRIRCPWHGACFNLRTGDIEDAPALD 80
                        90
                ....*....|....*
gi 21389617 150 SLHKFQVKIEKEKVY 164
Cdd:cd03478  81 SLPCYEVEVEDGRVY 95
Reductase_C super family cl20683
Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, ...
512-562 1.37e-08

Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, including putidaredoxin reductase, ferredoxin reductase, 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component, benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase subunit, rhodocoxin reductase, biphenyl dioxygenase system ferredoxin--NAD(+) reductase component, rubredoxin-NAD(+) reductase and toluene 1,2-dioxygenase system ferredoxin--NAD(+) reductase component. In putidaredoxin reductase this domain is involved in dimerization. In the FAD-containing NADH-ferredoxin reductase (BphA4) it is responsible for interaction with the Rieske-type [2Fe-2S] ferredoxin (BphA3).


The actual alignment was detected with superfamily member pfam14759:

Pssm-ID: 339364  Cd Length: 85  Bit Score: 51.77  E-value: 1.37e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 21389617   512 YLWTAMFGKSLRYAGYGEGFDDVIIQGDLEELKFVAFYTKGDEVIAVASMN 562
Cdd:pfam14759   1 WFWSDQYDLKLQIAGLPTGADEVVVRGDPEDGSFSVFYLRDGRLVAVDAVN 51
 
Name Accession Description Interval E-value
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
195-493 5.30e-74

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 311792 [Multi-domain]  Cd Length: 301  Bit Score: 238.76  E-value: 5.30e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   195 TNVLIVGAGAAGLVCAETLRQEGFsdRIVLCTLDRHLPYDRPKLSKSLD---------TQPEQLALRPKE--FFRAYGIE 263
Cdd:pfam07992   1 YDVVIIGGGPAGLAAALTLARAGG--KVTLIEDEGTCPYGGCVLSKALLgaaeapeiaSLWAELYERKEEvvKKLNNGIE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   264 VLTEAQVVTVDVRTKKVVFK-----DGFKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDANRVVRLARGRNVVVV 338
Cdd:pfam07992  79 VLLGTEVVSIDPGAKKVVLEnlvdgDGETITYDRLVIATGARPRLPPIPGVELNVGKLVRTLDSAEALRLKLLPKRLVVV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   339 GAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSELRGqEGKLKEVVLKSSKVV 418
Cdd:pfam07992 159 GGGYIGVELAAALAKLGKEVTLIEALDRLLRAF-DEEISAILEKALKKNGVEVRLGTSVKEIIG-DGDVVKVILKDGTEI 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21389617   419 RADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAvtfplawrnnRKVNIPHWQMAHAQG 493
Cdd:pfam07992 237 DADLVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDC----------RVGGPELAQNAVAQG 301
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
197-535 5.37e-60

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 223523 [Multi-domain]  Cd Length: 415  Bit Score: 205.53  E-value: 5.37e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 197 VLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRPKLSKSLDTQ--PEQLALRPKEFFRAYGIEVLTEAQVVTVD 274
Cdd:COG0446   1 IVIVGGGAAGLSAATTLRRLLLAAEITLIGREPKYSYYRCPLSLYVGGGiaSLEDLRYPPRFNRATGIDVRTGTEVTSID 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 275 VRTKKVVFKDGfKLEYSKLLLAPGSSPKTLSCKGKEveNVFTIRTPEDANRVV-RLARGRNVVVVGAGFLGMEVAAYLTE 353
Cdd:COG0446  81 PENKVVLLDDG-EIEYDYLVLATGARPRPPPISDWE--GVVTLRLREDAEALKgGAEPPKDVVVVGAGPIGLEAAEAAAK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 354 KAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRGQEGKL--KEVVLKSSKVVRADVCVVGIGAVP 431
Cdd:COG0446 158 RGKKVTLIEAADRLGGQLLDPEVAEELAELLEKYGVELLLGTKVVGVEGKGNTLvvERVVGIDGEEIKADLVIIGPGERP 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 432 ATGFLRQSGIGLDSR-GFIPVNKMMQT-NVPGVFAAGDAVTFPlAWRNNRKVNIPHWQMAHAQGRVAAQNMLAQEAEMST 509
Cdd:COG0446 238 NVVLANDALPGLALAgGAVLVDERGGTsKDPDVYAAGDVAEIP-AAETGKGGRIALWAIAVAAGRIAAENIAGALRIPGL 316
                       330       340
                ....*....|....*....|....*.
gi 21389617 510 VPYLWTAMFGKSLRYAGYGEGFDDVI 535
Cdd:COG0446 317 LGTVISDVGDLCAASTGLTEGKERGI 342
Rieske_AIFL_N cd03478
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ...
70-164 2.18e-55

AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family show similarity to human AIFL, containing an N-terminal Rieske domain and a C-terminal pyridine nucleotide-disulfide oxidoreductase domain (Pyr_redox). The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. AIFL shares 35% homology with human AIF (apoptosis-inducing factor), mainly in the Pyr_redox domain. AIFL is predominantly localized to the mitochondria. AIFL induces apoptosis in a caspase-dependent manner.


Pssm-ID: 239560 [Multi-domain]  Cd Length: 95  Bit Score: 182.05  E-value: 2.18e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  70 AAVCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDFPGLD 149
Cdd:cd03478   1 AVVCRLSDLGDGEMKEVDVGDGKVLLVRQGGEVHAIGAKCPHYGAPLAKGVLTDGRIRCPWHGACFNLRTGDIEDAPALD 80
                        90
                ....*....|....*
gi 21389617 150 SLHKFQVKIEKEKVY 164
Cdd:cd03478  81 SLPCYEVEVEDGRVY 95
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
194-585 6.00e-55

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 191.29  E-value: 6.00e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  194 STNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRPKLSKSLDTQPEQL--ALRPKEFFRAYGIEVLTEAQVV 271
Cdd:PRK09754   3 EKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQlqQVLPANWWQENNVHLHSGVTIK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  272 TVDVRTKKVVFKDGFKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDANRVVR-LARGRNVVVVGAGFLGMEVAAY 350
Cdd:PRK09754  83 TLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREvLQPERSVVIVGAGTIGLELAAS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  351 LTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELrgQEGKLKEVVLKSSKVVRADVCVVGIGAV 430
Cdd:PRK09754 163 ATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHV--VDGEKVELTLQSGETLQADVVIYGIGIS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  431 PATGFLRQSgiGLDSRGFIPVNKMMQTNVPGVFAAGDAVT--FPLAWRNNRKVniphWQMAHAQGRVAAQNMLAQEAEMS 508
Cdd:PRK09754 241 ANDQLAREA--NLDTANGIVIDEACRTCDPAIFAGGDVAItrLDNGALHRCES----WENANNQAQIAAAAMLGLPLPLL 314
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21389617  509 TVPYLWTAMFGKSLRYAGYGEGfDDVIIQGDLEELKFVAFYTKGDEVIAVASMNYDPIVSKVAEVLASGRAIRKREV 585
Cdd:PRK09754 315 PPPWFWSDQYSDNLQFIGDMRG-DDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLL 390
CoA_CoA_reduc TIGR03385
CoA-disulfide reductase; Members of this protein family are CoA-disulfide reductase (EC 1.8.1. ...
249-506 1.33e-43

CoA-disulfide reductase; Members of this protein family are CoA-disulfide reductase (EC 1.8.1.14), as characterized in Staphylococcus aureus, Pyrococcus horikoshii, and Borrelia burgdorferi, and inferred in several other species on the basis of high levels of CoA and an absence of glutathione as a protective thiol. [Cellular processes, Detoxification]


Pssm-ID: 163244 [Multi-domain]  Cd Length: 427  Bit Score: 161.06  E-value: 1.33e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   249 LALRPKEFFRAYGIEVLTEAQVVTVDVRTKKVVFKDG-----FKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDA 323
Cdd:TIGR03385  46 LAYTPEVFIKKRGIDVKTNHEVIEVNDERQTVVVRNNktnetYEESYDYLILSPGASPIVPNIEGINLDIVFTLRNLEDT 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   324 NRVVRLARG---RNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSEL 400
Cdd:TIGR03385 126 DAIKQYIDKnkvENVVIIGGGYIGIEMAEALRERGKNVTLIHRSERILNKLFDEEMNQIVEEELKKHEINLRLNEEVDSI 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   401 RGQEgklKEVVLKSSKVVRADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTfplawRNNRK 480
Cdd:TIGR03385 206 EGEE---RVKVFTSGGVYQADMVILATGIKPNSELAKDSGLKLGETGAIWVNEKFQTSVPNIYAAGDVAE-----SHNII 277
                         250       260       270
                  ....*....|....*....|....*....|
gi 21389617   481 VNIPHW----QMAHAQGRVAAQNMLAQEAE 506
Cdd:TIGR03385 278 TKKPAWvplaWGANKMGRIAGENIAGNDIE 307
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
72-154 6.12e-24

Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines coordinate one Fe ion, while the other Fe ion is coordinated by two conserved histidines. In hyperthermophilic archaea there is a SKTPCX(2-3)C motif at the C-terminus. The cysteines in this motif form a disulphide bridge, which stabilizes the protein.


Pssm-ID: 334028 [Multi-domain]  Cd Length: 87  Bit Score: 95.85  E-value: 6.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617    72 VCHVKDLENGQMREVELGWGKVLLVKD-NGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNIsTGDLEDFPGLDS 150
Cdd:pfam00355   4 VCASSELPEGDPLGVEVGGEPLVVFRDeDGELYALEDRCPHRGAPLSEGKVDGDRIECPYHGWRFDG-TGKVKKVPALRP 82

                  ....
gi 21389617   151 LHKF 154
Cdd:pfam00355  83 LKTY 86
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
71-166 8.25e-21

Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 225057 [Multi-domain]  Cd Length: 106  Bit Score: 87.40  E-value: 8.25e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  71 AVCHVKDLENGQMREVELGWGK-VLLVKDNGEFHALGHKCPHYGAPLVKGVLS-RGRVRCPWHGACFNISTGDLEDFPGL 148
Cdd:COG2146   7 RICKVDDLPEGGGVRVLVGGGRfALVVRADGEVFAIDNRCPHAGAPLSRGLVEgDETVVCPLHGARFDLRTGECLEPPAG 86
                        90
                ....*....|....*...
gi 21389617 149 DSLHKFQVKIEKEKVYVR 166
Cdd:COG2146  87 KTLKTYPVRVEGGRVFVD 104
PRK09965 PRK09965
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
71-165 8.58e-09

3-phenylpropionate dioxygenase ferredoxin subunit; Provisional


Pssm-ID: 170182 [Multi-domain]  Cd Length: 106  Bit Score: 53.24  E-value: 8.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   71 AVCHVKDLENGQMREVELGwGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLS-RGRVRCPWHGACFNISTGDLEDFPGLD 149
Cdd:PRK09965   5 YACPVADLPEGEALRVDTS-PVIALFNVGGEFYAIDDRCSHGNASLSEGYLEdDATVECPLHAASFCLRTGKALCLPATD 83
                         90
                 ....*....|....*.
gi 21389617  150 SLHKFQVKIEKEKVYV 165
Cdd:PRK09965  84 PLRTYPVHVEGGDIFI 99
Reductase_C pfam14759
Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, ...
512-562 1.37e-08

Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, including putidaredoxin reductase, ferredoxin reductase, 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component, benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase subunit, rhodocoxin reductase, biphenyl dioxygenase system ferredoxin--NAD(+) reductase component, rubredoxin-NAD(+) reductase and toluene 1,2-dioxygenase system ferredoxin--NAD(+) reductase component. In putidaredoxin reductase this domain is involved in dimerization. In the FAD-containing NADH-ferredoxin reductase (BphA4) it is responsible for interaction with the Rieske-type [2Fe-2S] ferredoxin (BphA3).


Pssm-ID: 339364  Cd Length: 85  Bit Score: 51.77  E-value: 1.37e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 21389617   512 YLWTAMFGKSLRYAGYGEGFDDVIIQGDLEELKFVAFYTKGDEVIAVASMN 562
Cdd:pfam14759   1 WFWSDQYDLKLQIAGLPTGADEVVVRGDPEDGSFSVFYLRDGRLVAVDAVN 51
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
71-166 1.22e-05

nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of nitrite reductase [NAD(P)H] (the assimilatory nitrite reductase), which associates with NirB, the large subunit (TIGR02374). In a few bacteria such as Klebsiella pneumoniae and in Fungi, the two regions are fused. [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 131431 [Multi-domain]  Cd Length: 105  Bit Score: 44.23  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617    71 AVCHVKDLENGQMREVELGWGKVLLVKDNG-EFHALGHKCPHYGAplvkGVLSRG---------RVRCPWHGACFNISTG 140
Cdd:TIGR02378   4 DICAIDDIPEETGVCVLLGDTQIAIFRVPGdQVFAIQNMCPHKRA----FVLSRGivgdaqgelWVACPLHKRNFRLEDG 79
                          90       100
                  ....*....|....*....|....*..
gi 21389617   141 D-LEDFPGldSLHKFQVKIEKEKVYVR 166
Cdd:TIGR02378  80 RcLEDDSG--SVRTYEVRVEDGRVYVA 104
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
327-379 4.07e-03

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 39.18  E-value: 4.07e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21389617 327 VRLAR---GRNVVVVGAGFLGMeVAAYLTEKAHSVSVVELEETPFRRFLGERVGRA 379
Cdd:cd08255  90 VRDAEprlGERVAVVGLGLVGL-LAAQLAKAAGAREVVGVDPDAARRELAEALGPA 144
 
Name Accession Description Interval E-value
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
195-493 5.30e-74

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 311792 [Multi-domain]  Cd Length: 301  Bit Score: 238.76  E-value: 5.30e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   195 TNVLIVGAGAAGLVCAETLRQEGFsdRIVLCTLDRHLPYDRPKLSKSLD---------TQPEQLALRPKE--FFRAYGIE 263
Cdd:pfam07992   1 YDVVIIGGGPAGLAAALTLARAGG--KVTLIEDEGTCPYGGCVLSKALLgaaeapeiaSLWAELYERKEEvvKKLNNGIE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   264 VLTEAQVVTVDVRTKKVVFK-----DGFKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDANRVVRLARGRNVVVV 338
Cdd:pfam07992  79 VLLGTEVVSIDPGAKKVVLEnlvdgDGETITYDRLVIATGARPRLPPIPGVELNVGKLVRTLDSAEALRLKLLPKRLVVV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   339 GAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSELRGqEGKLKEVVLKSSKVV 418
Cdd:pfam07992 159 GGGYIGVELAAALAKLGKEVTLIEALDRLLRAF-DEEISAILEKALKKNGVEVRLGTSVKEIIG-DGDVVKVILKDGTEI 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21389617   419 RADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAvtfplawrnnRKVNIPHWQMAHAQG 493
Cdd:pfam07992 237 DADLVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDC----------RVGGPELAQNAVAQG 301
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
197-535 5.37e-60

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 223523 [Multi-domain]  Cd Length: 415  Bit Score: 205.53  E-value: 5.37e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 197 VLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRPKLSKSLDTQ--PEQLALRPKEFFRAYGIEVLTEAQVVTVD 274
Cdd:COG0446   1 IVIVGGGAAGLSAATTLRRLLLAAEITLIGREPKYSYYRCPLSLYVGGGiaSLEDLRYPPRFNRATGIDVRTGTEVTSID 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 275 VRTKKVVFKDGfKLEYSKLLLAPGSSPKTLSCKGKEveNVFTIRTPEDANRVV-RLARGRNVVVVGAGFLGMEVAAYLTE 353
Cdd:COG0446  81 PENKVVLLDDG-EIEYDYLVLATGARPRPPPISDWE--GVVTLRLREDAEALKgGAEPPKDVVVVGAGPIGLEAAEAAAK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 354 KAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRGQEGKL--KEVVLKSSKVVRADVCVVGIGAVP 431
Cdd:COG0446 158 RGKKVTLIEAADRLGGQLLDPEVAEELAELLEKYGVELLLGTKVVGVEGKGNTLvvERVVGIDGEEIKADLVIIGPGERP 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 432 ATGFLRQSGIGLDSR-GFIPVNKMMQT-NVPGVFAAGDAVTFPlAWRNNRKVNIPHWQMAHAQGRVAAQNMLAQEAEMST 509
Cdd:COG0446 238 NVVLANDALPGLALAgGAVLVDERGGTsKDPDVYAAGDVAEIP-AAETGKGGRIALWAIAVAAGRIAAENIAGALRIPGL 316
                       330       340
                ....*....|....*....|....*.
gi 21389617 510 VPYLWTAMFGKSLRYAGYGEGFDDVI 535
Cdd:COG0446 317 LGTVISDVGDLCAASTGLTEGKERGI 342
Rieske_AIFL_N cd03478
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ...
70-164 2.18e-55

AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family show similarity to human AIFL, containing an N-terminal Rieske domain and a C-terminal pyridine nucleotide-disulfide oxidoreductase domain (Pyr_redox). The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. AIFL shares 35% homology with human AIF (apoptosis-inducing factor), mainly in the Pyr_redox domain. AIFL is predominantly localized to the mitochondria. AIFL induces apoptosis in a caspase-dependent manner.


Pssm-ID: 239560 [Multi-domain]  Cd Length: 95  Bit Score: 182.05  E-value: 2.18e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  70 AAVCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDFPGLD 149
Cdd:cd03478   1 AVVCRLSDLGDGEMKEVDVGDGKVLLVRQGGEVHAIGAKCPHYGAPLAKGVLTDGRIRCPWHGACFNLRTGDIEDAPALD 80
                        90
                ....*....|....*
gi 21389617 150 SLHKFQVKIEKEKVY 164
Cdd:cd03478  81 SLPCYEVEVEDGRVY 95
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
194-585 6.00e-55

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 191.29  E-value: 6.00e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  194 STNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRPKLSKSLDTQPEQL--ALRPKEFFRAYGIEVLTEAQVV 271
Cdd:PRK09754   3 EKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQlqQVLPANWWQENNVHLHSGVTIK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  272 TVDVRTKKVVFKDGFKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDANRVVR-LARGRNVVVVGAGFLGMEVAAY 350
Cdd:PRK09754  83 TLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREvLQPERSVVIVGAGTIGLELAAS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  351 LTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELrgQEGKLKEVVLKSSKVVRADVCVVGIGAV 430
Cdd:PRK09754 163 ATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHV--VDGEKVELTLQSGETLQADVVIYGIGIS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  431 PATGFLRQSgiGLDSRGFIPVNKMMQTNVPGVFAAGDAVT--FPLAWRNNRKVniphWQMAHAQGRVAAQNMLAQEAEMS 508
Cdd:PRK09754 241 ANDQLAREA--NLDTANGIVIDEACRTCDPAIFAGGDVAItrLDNGALHRCES----WENANNQAQIAAAAMLGLPLPLL 314
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21389617  509 TVPYLWTAMFGKSLRYAGYGEGfDDVIIQGDLEELKFVAFYTKGDEVIAVASMNYDPIVSKVAEVLASGRAIRKREV 585
Cdd:PRK09754 315 PPPWFWSDQYSDNLQFIGDMRG-DDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLL 390
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
193-506 8.86e-44

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 224171 [Multi-domain]  Cd Length: 793  Bit Score: 167.11  E-value: 8.86e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 193 SSTNVLIVGAGAAGLVCAET-LRQEGFSDRIVLCTLDRHLPYDRPKLSKSL--DTQPEQLALRPKEFFRAYGIEVLTEAQ 269
Cdd:COG1251   2 KKQKLVIIGNGMAGHRTIEElLESAPDLYDITVFGEEPRPNYNRILLSSVLagEKTAEDISLNRNDWYEENGITLYTGEK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 270 VVTVDVRTKKVVFKDGFKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDANRVVRLARG-RNVVVVGAGFLGMEVA 348
Cdd:COG1251  82 VIQIDRANKVVTTDAGRTVSYDKLIIATGSYPFILPIPGSDLPGVFVYRTIDDVEAMLDCARNkKKAVVIGGGLLGLEAA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 349 AYLTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELrGQEGKLKEVVLKSSKVVRADVCVVGIG 428
Cdd:COG1251 162 RGLKDLGMEVTVVHIAPTLMERQLDRTAGRLLRRKLEDLGIKVLLEKNTEEI-VGEDKVEGVRFADGTEIPADLVVMAVG 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21389617 429 AVPATGFLRQSGIGLDsRGfIPVNKMMQTNVPGVFAAGDAVtfplAWRN-NRKVNIPHWQMAhaqgRVAAQNMLAQEAE 506
Cdd:COG1251 241 IRPNDELAKEAGLAVN-RG-IVVNDYMQTSDPDIYAVGECA----EHRGkVYGLVAPLYEQA----KVLADHLCGGEAE 309
CoA_CoA_reduc TIGR03385
CoA-disulfide reductase; Members of this protein family are CoA-disulfide reductase (EC 1.8.1. ...
249-506 1.33e-43

CoA-disulfide reductase; Members of this protein family are CoA-disulfide reductase (EC 1.8.1.14), as characterized in Staphylococcus aureus, Pyrococcus horikoshii, and Borrelia burgdorferi, and inferred in several other species on the basis of high levels of CoA and an absence of glutathione as a protective thiol. [Cellular processes, Detoxification]


Pssm-ID: 163244 [Multi-domain]  Cd Length: 427  Bit Score: 161.06  E-value: 1.33e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   249 LALRPKEFFRAYGIEVLTEAQVVTVDVRTKKVVFKDG-----FKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDA 323
Cdd:TIGR03385  46 LAYTPEVFIKKRGIDVKTNHEVIEVNDERQTVVVRNNktnetYEESYDYLILSPGASPIVPNIEGINLDIVFTLRNLEDT 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   324 NRVVRLARG---RNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSEL 400
Cdd:TIGR03385 126 DAIKQYIDKnkvENVVIIGGGYIGIEMAEALRERGKNVTLIHRSERILNKLFDEEMNQIVEEELKKHEINLRLNEEVDSI 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   401 RGQEgklKEVVLKSSKVVRADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTfplawRNNRK 480
Cdd:TIGR03385 206 EGEE---RVKVFTSGGVYQADMVILATGIKPNSELAKDSGLKLGETGAIWVNEKFQTSVPNIYAAGDVAE-----SHNII 277
                         250       260       270
                  ....*....|....*....|....*....|
gi 21389617   481 VNIPHW----QMAHAQGRVAAQNMLAQEAE 506
Cdd:TIGR03385 278 TKKPAWvplaWGANKMGRIAGENIAGNDIE 307
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
195-490 7.64e-35

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 136.84  E-value: 7.64e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  195 TNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRH-------LPYdrpKLSKSLDTQPEQLALRPKEFFRAYGIEVLTE 267
Cdd:PRK13512   2 PKIIVVGAVAGGATCASQIRRLDKESDIIIFEKDRDmsfancaLPY---YIGEVVEDRKYALAYTPEKFYDRKQITVKTY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  268 AQVVTVDVRTKKVVFKD-----GFKLEYSKLLLAPGSSPKTLsckGKEVENVFTIRTPEDANRV---VRLARGRNVVVVG 339
Cdd:PRK13512  79 HEVIAINDERQTVTVLNrktneQFEESYDKLILSPGASANSL---GFESDITFTLRNLEDTDAIdqfIKANQVDKALVVG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  340 AGFLGMEVAAYLTEKAHSVSVVElEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRGQEgklkeVVLKSSKVVR 419
Cdd:PRK13512 156 AGYISLEVLENLYERGLHPTLIH-RSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGNE-----VTFKSGKVEH 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  420 ADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVT-----------FPLAWRNNRKVNIPHWQM 488
Cdd:PRK13512 230 YDMIIEGVGTHPNSKFIESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITshyrhvdlpasVPLAWGAHRAASIVAEQI 309

                 ..
gi 21389617  489 AH 490
Cdd:PRK13512 310 AG 311
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
197-506 2.69e-33

nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 135.73  E-value: 2.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   197 VLIVGAGAAGLVCAETLRQEGFSD-RIVLCTLDRHLPYDRPKLSKSL--DTQPEQLALRPKEFFRAYGIEVLTEAQVVTV 273
Cdd:TIGR02374   1 LVLVGNGMAGHRCIEEVLKLNRHMfEITIFGEEPHPNYNRILLSSVLqgEADLDDITLNSKDWYEKHGITLYTGETVIQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   274 DVRTKKVVFKDGFKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDANRVVRLA-RGRNVVVVGAGFLGMEVAAYLT 352
Cdd:TIGR02374  81 DTDQKQVITDAGRTLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMAMAqRFKKAAVIGGGLLGLEAAVGLQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   353 EKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRGqEGKLKEVVLKSSKVVRADVCVVGIGAVPA 432
Cdd:TIGR02374 161 NLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVG-ATKADRIRFKDGSSLEADLIVMAAGIRPN 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21389617   433 TGFLRQSGIGLdSRGFIpVNKMMQTNVPGVFAAGDAvtfplAWRNNRKVNI--PHWQMAhaqgRVAAQNMLAQEAE 506
Cdd:TIGR02374 240 DELAVSAGIKV-NRGII-VNDSMQTSDPDIYAVGEC-----AEHNGRVYGLvaPLYEQA----KVLADHICGVECE 304
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
197-508 3.98e-33

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 132.09  E-value: 3.98e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  197 VLIVGAGAAGLVCAETLRQEGFSDRIVL-----------CTLdrhlPYdrpKLSKSLDtQPEQLALRPKEFFRAYGIEVL 265
Cdd:PRK09564   3 IIIIGGTAAGMSAAAKAKRLNKELEITVyektdivsfgaCGL----PY---FVGGFFD-DPNTMIARTPEEFIKSGIDVK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  266 TEAQVVTVDVRTKKVVFKDG-----FKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDANRVVRLARG---RNVVV 337
Cdd:PRK09564  75 TEHEVVKVDAKNKTITVKNLktgsiFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKELLKDeeiKNIVI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  338 VGAGFLGMEVAAYLTEKAHSVSVVELEEtpfrRFLGERVGRALMKMFEN----NRVKFYMQTEVSELRGqEGKLKEVVLK 413
Cdd:PRK09564 155 IGAGFIGLEAVEAAKHLGKNVRIIQLED----RILPDSFDKEITDVMEEelreNGVELHLNEFVKSLIG-EDKVEGVVTD 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  414 SSKVVrADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGD-AVTFPLAwrNNRKVNIPHWQMAHAQ 492
Cdd:PRK09564 230 KGEYE-ADVVIVATGVKPNTEFLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDcATIYNIV--SNKNVYVPLATTANKL 306
                        330
                 ....*....|....*.
gi 21389617  493 GRVAAQNMLAQEAEMS 508
Cdd:PRK09564 307 GRMVGENLAGRHVSFK 322
Lpd COG1249
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase (E3) component ...
197-512 1.41e-32

Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase (E3) component or related enzyme [Energy production and conversion];


Pssm-ID: 224169 [Multi-domain]  Cd Length: 454  Bit Score: 130.41  E-value: 1.41e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 197 VLIVGAGAAGLVCAETLRQEGFSDRIV--------LCTLD------------------RHLPY-----------DRPKLS 239
Cdd:COG1249   7 VVVIGAGPAGYVAAIRAAQLGLKVALVekgerlggTCLNVgcipskallhaaevieeaRHAAKeygisaevpkiDFEKLL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 240 KSLDTQPEQLALRPKEFFRAYGIEVLT-EAQVVtvDVRTKKVVFKDGFKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIR 318
Cdd:COG1249  87 ARKDKVVRLLTGGVEGLLKKNGVDVIRgEARFV--DPHTVEVTGEDKETITADNIIIATGSRPRIPPGPGIDGARILDSS 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 319 TPEDANRVvrlarGRNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFLGErVGRALMKMFENNRVKFYMQTEVS 398
Cdd:COG1249 165 DALFLLEL-----PKSLVIVGGGYIGLEFASVFAALGSKVTVVERGDRILPGEDPE-ISKELTKQLEKGGVKILLNTKVT 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 399 ELRGQEGKLkEVVLKSSK--VVRADVCVVGIGAVPATGF--LRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFPla 474
Cdd:COG1249 239 AVEKKDDGV-LVTLEDGEggTIEADAVLVAIGRKPNTDGlgLENAGVELDDRGFIKVDDQMTTNVPGIYAIGDVIGGP-- 315
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 21389617 475 wrnnrkvniphwQMAH---AQGRVAAQNMLAQEAE---MSTVPY 512
Cdd:COG1249 316 ------------MLAHvamAEGRIAAENIAGGKRTpidYRLIPS 347
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
192-512 6.86e-30

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 224172 [Multi-domain]  Cd Length: 405  Bit Score: 121.59  E-value: 6.86e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 192 SSSTNVLIVGAGAAGLVCAETLRQEGFSDRIVLctLDRHlPYD--RPKL----SKSLDtqPEQLALRPKEFFRAYGIEVL 265
Cdd:COG1252   1 MMKKRIVILGGGFGGLSAAKRLARKLPDVEITL--VDRR-DYHlfTPLLyevaTGTLS--ESEIAIPLRALLRKSGNVQF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 266 TEAQVVTVDVRTKKVVFKDGFKLEYSKLLLAPGSSPKTLSCKGKEvENVFTIRTPEDANRV--------------VRLAR 331
Cdd:COG1252  76 VQGEVTDIDRDAKKVTLADLGEISYDYLVVALGSETNYFGIPGAA-EYAFGLKTLEDALRLrrhlleafekasqeEDDRA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 332 GRNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRF------------LGERVGRALMKMFENNRVKFYMQTEVSE 399
Cdd:COG1252 155 LLTIVIVGGGPTGVELAGELAERLHRLLKKFRVDPSELRVilveagprilpmFPPKLSKYAERALEKLGVEVLLGTPVTE 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 400 LRgQEG---KLKEVVLKSSKVVRAdvcvVGIGAVPATGFLrqSGIGLDSRGFIPVNKMMQ-TNVPGVFAAGDAVTFPlaw 475
Cdd:COG1252 235 VT-PDGvtlKDGEEEIPADTVVWA----AGVRASPLLKDL--SGLETDRRGRLVVNPTLQvPGHPDIFAAGDCAAVI--- 304
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 21389617 476 rnNRKVNIPHWQMAHAQGRVAAQNMLAQEAEMSTVPY 512
Cdd:COG1252 305 --DPRPVPPTAQAAHQQGEYAAKNIKARLKGKPLKPF 339
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
197-500 9.55e-27

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223566 [Multi-domain]  Cd Length: 305  Bit Score: 110.46  E-value: 9.55e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 197 VLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRPKLSKSL-----DTQPEQLALRPKEFFRAYGIEVLTEaQVV 271
Cdd:COG0492   6 VIIIGGGPAGLTAAIYAARAGLKVVLILEGGEPGGQLTKTTDVENYpgfpgGILGPELMEQMKEQAEKFGVEIVED-EVE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 272 TVDV--RTKKVVFKDG-FKLEYskLLLAPGSSPKTLSCKGkevenvftirTPEDANRVV-------RLARGRNVVVVGAG 341
Cdd:COG0492  85 KVELegGPFKVKTDKGtYEAKA--VIIATGAGARKLGVPG----------EEEFEGKGVsycatcdGFFKGKDVVVIGGG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 342 FLGMEVAAYLTEKAHSVSVVeleetpFRR--FLGERVGRAlmKMFENNRVKFYMQTEVSELRGQEgkLKEVVLK----SS 415
Cdd:COG0492 153 DSAVEEALYLSKIAKKVTLV------HRRdeFRAEEILVE--RLKKNVKIEVLTNTVVKEILGDD--VEGVVLKnvkgEE 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 416 KVVRADVCVVGIGAVPATGFLRQSGIgLDSRGFIPVNKMMQTNVPGVFAAGDAVTfplawrnnrkvnIPHWQMAHA--QG 493
Cdd:COG0492 223 KELPVDGVFIAIGHLPNTELLKGLGV-LDENGYIVVDEEMETSVPGIFAAGDVAD------------KNGRQIATAagDG 289

                ....*..
gi 21389617 494 RVAAQNM 500
Cdd:COG0492 290 AIAALSA 296
TRX_reduct TIGR01292
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ...
197-467 9.86e-25

thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]


Pssm-ID: 273540 [Multi-domain]  Cd Length: 299  Bit Score: 104.63  E-value: 9.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   197 VLIVGAGAAGLVCA--------ETLRQEGFS--DRIVLCTLDRHLPYDRPKLSKSldtqpeQLALRPKEFFRAYGIEVLT 266
Cdd:TIGR01292   2 VIIIGAGPAGLTAAiyaaranlKPLLIEGMEpgGQLTTTTEVENYPGFPEGISGP------ELMEKMKEQAVKFGAEIIY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   267 EaQVVTVD--VRTKKVVFKDGFKLEYSKLLLAPGSSPKTLSCKGkevENVFTIR-----TPEDANrvvrLARGRNVVVVG 339
Cdd:TIGR01292  76 E-EVIKVDksDRPFKVYTGDGKEYTAKAVIIATGASARKLGIPG---EDEFWGRgvsycATCDGP----FFKNKEVAVVG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   340 AGFLGMEVAAYLTEKAHSVSVVELEETpFR--RFLGERVgralmkmFENNRVKFYMQTEVSELRGQEG----KLKEVVLK 413
Cdd:TIGR01292 148 GGDSAIEEALYLTRIAKKVTLVHRRDK-FRaeKILLDRL-------KKNPKIEFLWNSTVEEIVGDNKvegvKIKNTVTG 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 21389617   414 SSKVVRADVCVVGIGAVPATGFLRQSGIgLDSRGFIPVNKMMQTNVPGVFAAGD 467
Cdd:TIGR01292 220 EEEELEVDGVFIAIGHEPNTELLKGLLE-LDENGYIVTDEGMRTSVPGVFAAGD 272
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
72-154 6.12e-24

Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines coordinate one Fe ion, while the other Fe ion is coordinated by two conserved histidines. In hyperthermophilic archaea there is a SKTPCX(2-3)C motif at the C-terminus. The cysteines in this motif form a disulphide bridge, which stabilizes the protein.


Pssm-ID: 334028 [Multi-domain]  Cd Length: 87  Bit Score: 95.85  E-value: 6.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617    72 VCHVKDLENGQMREVELGWGKVLLVKD-NGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNIsTGDLEDFPGLDS 150
Cdd:pfam00355   4 VCASSELPEGDPLGVEVGGEPLVVFRDeDGELYALEDRCPHRGAPLSEGKVDGDRIECPYHGWRFDG-TGKVKKVPALRP 82

                  ....
gi 21389617   151 LHKF 154
Cdd:pfam00355  83 LKTY 86
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
194-512 1.00e-22

dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.


Pssm-ID: 273568 [Multi-domain]  Cd Length: 460  Bit Score: 101.18  E-value: 1.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   194 STNVLIVGAGAAGLVCAETLRQEGFSDRIV-------LCT----------------------LDRH------LPYDRPKL 238
Cdd:TIGR01350   1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVekeylggTCLnvgciptkallhsaevydeikhAKDLgievenVSVDWEKM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   239 SKSLDTQPEQLALRPKEFFRAYGIEVLT-EAQVV---TVDVRTKKvvfkDGFKLEYSKLLLAPGSSPKTLSCKGKEVENV 314
Cdd:TIGR01350  81 QKRKNKVVKKLVGGVSGLLKKNKVTVIKgEAKFLdpgTVSVTGEN----GEETLEAKNIIIATGSRPRSLPGPFDFDGKV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   315 ftIRTPEDANRVVRLARgrNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEEtpfrRFLG---ERVGRALMKMFENNRVKF 391
Cdd:TIGR01350 157 --VITSTGALNLEEVPE--SLVIIGGGVIGIEFASIFASLGSKVTVIEMLD----RILPgedAEVSKVLQKALKKKGVKI 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   392 YMQTEVSELRGQEGKLK-EVVLKSSKVVRADVCVVGIGAVPATGF--LRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDA 468
Cdd:TIGR01350 229 LTNTKVTAVEKNDDQVTyENKGGETETLTGEKVLVAVGRKPNTEGlgLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDV 308
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 21389617   469 vtfplawrnnrkvnIPHWQMAH---AQGRVAAQNMLAQE-AEM--STVPY 512
Cdd:TIGR01350 309 --------------IGGPMLAHvasHEGIVAAENIAGKEpAHIdyDAVPS 344
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
71-165 2.80e-22

Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron oxygenase (RO) systems such as naphthalene and biphenyl dioxygenases, as well as in plant/cyanobacterial chloroplast b6f and mitochondrial cytochrome bc(1) complexes. The Rieske domain can be divided into two subdomains, with an incomplete six-stranded, antiparallel beta-barrel at one end, and an iron-sulfur cluster binding subdomain at the other. The Rieske iron-sulfur center contains a [2Fe-2S] cluster, which is involved in electron transfer, and is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In RO systems, the N-terminal Rieske domain of the alpha subunit acts as an electron shuttle that accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron in the alpha subunit C-terminal domain to be used for catalysis.


Pssm-ID: 239550 [Multi-domain]  Cd Length: 98  Bit Score: 91.40  E-value: 2.80e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  71 AVCHVKDLENGQMREVELGWGKVLLV-KDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDFPGLD 149
Cdd:cd03467   3 VVGALSELPPGGGRVVVVGGGPVVVVrREGGEVYALSNRCTHQGCPLSEGEGEDGCIVCPCHGSRFDLRTGEVVSGPAPR 82
                        90
                ....*....|....*.
gi 21389617 150 SLHKFQVKIEKEKVYV 165
Cdd:cd03467  83 PLPKYPVKVEGDGVVW 98
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
193-508 1.02e-21

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 99.81  E-value: 1.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  193 SSTNVLIVGAGAAGLVCAETLRQEGFSDRI---VLCTLDRhLPYDRPKLSKSLDTQ-PEQLALRPKEFFRAYGIEVLTEA 268
Cdd:PRK14989   2 SKVRLAIIGNGMVGHRFIEDLLDKADAANFditVFCEEPR-IAYDRVHLSSYFSHHtAEELSLVREGFYEKHGIKVLVGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  269 QVVTVDvRTKKVVFKD-GFKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDANRVVRLA-RGRNVVVVGAGFLGME 346
Cdd:PRK14989  81 RAITIN-RQEKVIHSSaGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACArRSKRGAVVGGGLLGLE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  347 VAAYLTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSEL--RGQEGKlKEVVLKSSKVVRADVCV 424
Cdd:PRK14989 160 AAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIvqEGVEAR-KTMRFADGSELEVDFIV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  425 VGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVtfplAWrNNRKVNI--PHWQMAhaqgRVAAQNMLA 502
Cdd:PRK14989 239 FSTGIRPQDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGECA----SW-NNRVFGLvaPGYKMA----QVAVDHLLG 309
                        330
                 ....*....|.
gi 21389617  503 QE-----AEMS 508
Cdd:PRK14989 310 SEnafegADLS 320
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
71-166 8.25e-21

Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 225057 [Multi-domain]  Cd Length: 106  Bit Score: 87.40  E-value: 8.25e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  71 AVCHVKDLENGQMREVELGWGK-VLLVKDNGEFHALGHKCPHYGAPLVKGVLS-RGRVRCPWHGACFNISTGDLEDFPGL 148
Cdd:COG2146   7 RICKVDDLPEGGGVRVLVGGGRfALVVRADGEVFAIDNRCPHAGAPLSRGLVEgDETVVCPLHGARFDLRTGECLEPPAG 86
                        90
                ....*....|....*...
gi 21389617 149 DSLHKFQVKIEKEKVYVR 166
Cdd:COG2146  87 KTLKTYPVRVEGGRVFVD 104
PRK05249 PRK05249
soluble pyridine nucleotide transhydrogenase; Provisional
273-512 1.47e-19

soluble pyridine nucleotide transhydrogenase; Provisional


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 91.37  E-value: 1.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  273 VDVRTKKVVFKDGFKLEYS--KLLLAPGSSPKtlscKGKEVEnvFTIRTPEDANRVVRLAR-GRNVVVVGAGFLGMEVAA 349
Cdd:PRK05249 119 VDPHTVEVECPDGEVETLTadKIVIATGSRPY----RPPDVD--FDHPRIYDSDSILSLDHlPRSLIIYGAGVIGCEYAS 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  350 YLTEKAHSVSVVELEETPFRrFLGERVGRALMKMFENNRVKFYMQTEVSELRGQEGKlKEVVLKSSKVVRADVCVVGIGA 429
Cdd:PRK05249 193 IFAALGVKVTLINTRDRLLS-FLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDG-VIVHLKSGKKIKADCLLYANGR 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  430 VPATGFLRQSGIGL--DSRGFIPVNKMMQTNVPGVFAAGDAVTFP-LAwrnnrkvniphwQMAHAQGRVAAQNMLAQEAE 506
Cdd:PRK05249 271 TGNTDGLNLENAGLeaDSRGQLKVNENYQTAVPHIYAVGDVIGFPsLA------------SASMDQGRIAAQHAVGEATA 338

                 ....*...
gi 21389617  507 M--STVPY 512
Cdd:PRK05249 339 HliEDIPT 346
Rieske_RO_ferredoxin cd03528
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ...
72-166 4.96e-19

Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the Rieske ferredoxin component of some three-component RO systems including biphenyl dioxygenase (BPDO) and carbazole 1,9a-dioxygenase (CARDO). The RO family comprise a large class of aromatic ring-hydroxylating dioxygenases found predominantly in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth. ROs consist of two or three components: reductase, oxygenase, and ferredoxin (in some cases) components. The ferredoxin component contains either a plant-type or Rieske-type [2Fe-2S] cluster. The Rieske ferredoxin component in this family carries an electron from the RO reductase component to the terminal RO oxygenase component. BPDO degrades biphenyls and polychlorinated biphenyls. BPDO ferredoxin (BphF) has structural features consistent with a minimal and perhaps archetypical Rieske protein in that the insertions that give other Rieske proteins unique structural features are missing. CARDO catalyzes dihydroxylation at the C1 and C9a positions of carbazole. Rieske ferredoxins are found as subunits of membrane oxidase complexes, cis-dihydrodiol-forming aromatic dioxygenases, bacterial assimilatory nitrite reductases, and arsenite oxidase. Rieske ferredoxins are also found as soluble electron carriers in bacterial dioxygenase and monooxygenase complexes.


Pssm-ID: 239604 [Multi-domain]  Cd Length: 98  Bit Score: 82.15  E-value: 4.96e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  72 VCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDFPGLDSL 151
Cdd:cd03528   4 VCAVDELPEGEPKRVDVGGRPIAVYRVDGEFYATDDLCTHGDASLSEGYVEGGVIECPLHGGRFDLRTGKALSLPATEPL 83
                        90
                ....*....|....*
gi 21389617 152 HKFQVKIEKEKVYVR 166
Cdd:cd03528  84 KTYPVKVEDGDVYVD 98
PRK04965 PRK04965
NADH:flavorubredoxin oxidoreductase; Provisional
194-513 9.93e-19

NADH:flavorubredoxin oxidoreductase; Provisional


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 88.05  E-value: 9.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  194 STNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRPKLSK--SLDTQPEQLA-LRPKEFFRAYGIEVLTEAQV 270
Cdd:PRK04965   2 SNGIVIIGSGFAARQLVKNIRKQDAHIPITLITADSGDEYNKPDLSHvfSQGQRADDLTrQSAGEFAEQFNLRLFPHTWV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  271 VTVDVRTKKVVFKDGfKLEYSKLLLAPGSSPKTLSCKGKEVenVFTI------RTPEDanrvvRLARGRNVVVVGAGFLG 344
Cdd:PRK04965  82 TDIDAEAQVVKSQGN-QWQYDKLVLATGASAFVPPIPGREL--MLTLnsqqeyRAAET-----QLRDAQRVLVVGGGLIG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  345 MEVAAYLTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRGQEGKLKeVVLKSSKVVRADVCV 424
Cdd:PRK04965 154 TELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIR-ATLDSGRSIEVDAVI 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  425 VGIGAVPATGFLRQSGIGLDsRGfIPVNKMMQTNVPGVFAAGDAVTFplawrnNRKVnIPHWQMAHAQGRVAAQNMLAQE 504
Cdd:PRK04965 233 AAAGLRPNTALARRAGLAVN-RG-IVVDSYLQTSAPDIYALGDCAEI------NGQV-LPFLQPIQLSAMALAKNLLGQN 303

                 ....*....
gi 21389617  505 AEMSTVPYL 513
Cdd:PRK04965 304 TPLKLPAML 312
gltD PRK12810
glutamate synthase subunit beta; Reviewed
197-469 5.91e-18

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 86.76  E-value: 5.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  197 VLIVGAGAAGLVCAETLRQEGFS----DRivlctldrhlpYDRP-----------KLSKSL-DTQPEQLalrpkeffRAY 260
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHKvtvfER-----------ADRIggllrygipdfKLEKEViDRRIELM--------EAE 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  261 GIEVLTEAQV-VTVDVrtkkvvfkDGFKLEYSKLLLAPGSS-PKTLSCKGKEVENV-----FTIrtpeDANRVVR----- 328
Cdd:PRK12810 207 GIEFRTNVEVgKDITA--------EELLAEYDAVFLGTGAYkPRDLGIPGRDLDGVhfamdFLI----QNTRRVLgdete 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  329 ---LARGRNVVVVGAGFLGME-VAAYLTEKAhsVSVVELEET---PFRRFLGERVGRALMKMfennRVK----------F 391
Cdd:PRK12810 275 pfiSAKGKHVVVIGGGDTGMDcVGTAIRQGA--KSVTQRDIMpmpPSRRNKNNPWPYWPMKL----EVSnaheegvereF 348
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  392 YMQTEvsELRGQEGKLKEV--------------VLKSSKVVRADVCVVGIGAVPA-TGFLRQSGIGLDSRGFIPVNKM-M 455
Cdd:PRK12810 349 NVQTK--EFEGENGKVTGVkvvrtelgegdfepVEGSEFVLPADLVLLAMGFTGPeAGLLAQFGVELDERGRVAAPDNaY 426
                        330
                 ....*....|....
gi 21389617  456 QTNVPGVFAAGDAV 469
Cdd:PRK12810 427 QTSNPKVFAAGDMR 440
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
257-507 9.75e-18

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 85.97  E-value: 9.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  257 FRAYGIEVLT-EAQVV---TVDVRTKKV----VFKDgfkleyskLLLAPGSSPKTLscKGKEVENVfTIRTPEDANRVVR 328
Cdd:PRK06416 102 LKKNKVDIIRgEAKLVdpnTVRVMTEDGeqtyTAKN--------IILATGSRPREL--PGIEIDGR-VIWTSDEALNLDE 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  329 LARgrNVVVVGAGFLGMEVA-AYLTEKAHsVSVVELEEtpfrRFLG---ERVGRALMKMFENNRVKFYMQTEVSEL-RGQ 403
Cdd:PRK06416 171 VPK--SLVVIGGGYIGVEFAsAYASLGAE-VTIVEALP----RILPgedKEISKLAERALKKRGIKIKTGAKAKKVeQTD 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  404 EG-KLKEVVLKSSKVVRADVCVVGIGAVPATgflrqSGIGLDS------RGFIPVNKMMQTNVPGVFAAGDAVTFPlawr 476
Cdd:PRK06416 244 DGvTVTLEDGGKEETLEADYVLVAVGRRPNT-----ENLGLEElgvktdRGFIEVDEQLRTNVPNIYAIGDIVGGP---- 314
                        250       260       270
                 ....*....|....*....|....*....|....
gi 21389617  477 nnrkvniphwQMAH---AQGRVAAQNMLAQEAEM 507
Cdd:PRK06416 315 ----------MLAHkasAEGIIAAEAIAGNPHPI 338
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
333-506 2.76e-16

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 81.38  E-value: 2.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  333 RNVVVVGAGFLGMEVAAYLtekaHS----VSVVELEEtpfrRFLG---ERVGRALMKMFENnRVKFYMQTEVSELRgQEG 405
Cdd:PRK06292 170 KSLAVIGGGVIGLELGQAL----SRlgvkVTVFERGD----RILPledPEVSKQAQKILSK-EFKIKLGAKVTSVE-KSG 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  406 KLKEVVLKS---SKVVRADVCVVGIGAVPAT---GfLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFPLawrnnr 479
Cdd:PRK06292 240 DEKVEELEKggkTETIEADYVLVATGRRPNTdglG-LENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKPP------ 312
                        170       180       190
                 ....*....|....*....|....*....|
gi 21389617  480 kvniphwqMAHA---QGRVAAQNMLAQEAE 506
Cdd:PRK06292 313 --------LLHEaadEGRIAAENAAGDVAG 334
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
197-470 5.20e-16

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 80.61  E-value: 5.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  197 VLIVGAGAAGLVCAETLRQEGFSdriVlcTL-DRHlpyDRP-----------KLSKSLdtqpeqlALRPKEFFRAYGIEV 264
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYD---V--TIfEAR---DKAggllrygipefRLPKDI-------VDREVERLLKLGVEI 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  265 LTEAQV---VTVDvrtkkvvfkdGFKLEYSKLLLAPG-SSPKTLSCKGKEVENVFT----IRTPEDANRVVRLARGRNVV 336
Cdd:PRK11749 208 RTNTEVgrdITLD----------ELRAGYDAVFIGTGaGLPRFLGIPGENLGGVYSavdfLTRVNQAVADYDLPVGKRVV 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  337 VVGAGFLGMEVAAylTEK---AHSVSVV---ELEETP---------------FR------RFLGERVGRALMKmfennrv 389
Cdd:PRK11749 278 VIGGGNTAMDAAR--TAKrlgAESVTIVyrrGREEMPaseeevehakeegveFEwlaapvEILGDEGRVTGVE------- 348
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  390 kfYMQTEVSELRGQeGKLKEVVLKSSKVVRADVCVVGIGAVPATGFLR-QSGIGLDSRG-FIPVNKMMQTNVPGVFAAGD 467
Cdd:PRK11749 349 --FVRMELGEPDAS-GRRRVPIEGSEFTLPADLVIKAIGQTPNPLILStTPGLELNRWGtIIADDETGRTSLPGVFAGGD 425

                 ...
gi 21389617  468 AVT 470
Cdd:PRK11749 426 IVT 428
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
334-411 1.79e-15

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 333813 [Multi-domain]  Cd Length: 79  Bit Score: 71.44  E-value: 1.79e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21389617   334 NVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPfRRFLGERVGRALMKMFENNRVKFYMQTEVSELRGQEGKLKEVV 411
Cdd:pfam00070   1 KVVVVGGGYIGLELAGALARLGSKVTVVERRDRL-LRGLDEEIAKILQERLEKNGIEVLLNTTVEAIEGNGDGVVVVL 77
AhpF_homolog TIGR03143
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ...
260-467 2.68e-15

putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase homologs is found adjacent to alkylhydroperoxide reductase C subunit predominantly in cases where there is only one C subunit in the genome and that genome is lacking the F subunit partner (also a thioredcxin reductase homolog) that is usually found (TIGR03140).


Pssm-ID: 132187 [Multi-domain]  Cd Length: 555  Bit Score: 78.67  E-value: 2.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   260 YGIEvLTEAQVVTVDVRTK-KVVFKDGFKLEYSKLLLAPGSSPKTLSCKGKEvenvftirtpEDANRVV--------RLA 330
Cdd:TIGR03143  73 FGVK-FLQAEVLDVDFDGDiKTIKTARGDYKTLAVLIATGASPRKLGFPGEE----------EFTGRGVaycatcdgEFF 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   331 RGRNVVVVGAGFLGMEVAAYLTEKAHSVSVVeLEETPFR--RFLGERVgralmkmFENNRVKFYMQTEVSELRGQeGKLK 408
Cdd:TIGR03143 142 TGMDVFVIGGGFAAAEEAVFLTRYASKVTVI-VREPDFTcaKLIAEKV-------KNHPKIEVKFNTELKEATGD-DGLR 212
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   409 EVVLKSSKV-------VRADVCVVGI----GAVPATGFLRQSgIGLDSRGFIPVNKMMQTNVPGVFAAGD 467
Cdd:TIGR03143 213 YAKFVNNVTgeiteykAPKDAGTFGVfvfvGYAPSSELFKGV-VELDKRGYIPTNEDMETNVPGVYAAGD 281
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
197-522 4.06e-15

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 78.04  E-value: 4.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  197 VLIVGAGAAGLVCAETLRQEGFSdriVLCTLDRHLPYDRPKL-----------SKSLDTQPEQLAlRPKEFFRAYGIEVl 265
Cdd:PRK06327   7 VVVIGAGPGGYVAAIRAAQLGLK---VACIEAWKNPKGKPALggtclnvgcipSKALLASSEEFE-NAGHHFADHGIHV- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  266 teaQVVTVDV-----RTKKVV--FKDG----FK--------------------------------LEYSKLLLAPGSSPK 302
Cdd:PRK06327  82 ---DGVKIDVakmiaRKDKVVkkMTGGieglFKknkitvlkgrgsfvgktdagyeikvtgedetvITAKHVIIATGSEPR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  303 TLSckgkevenvftiRTPEDANRVV-------------RLArgrnvvVVGAGFLGMEVAAYLTEKAHSVSVveLEETPfr 369
Cdd:PRK06327 159 HLP------------GVPFDNKIILdntgalnftevpkKLA------VIGAGVIGLELGSVWRRLGAEVTI--LEALP-- 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  370 RFLG---ERVGRALMKMFENNRVKFYMQTEVSELRGQEgklKEVVLK------SSKVVRADVCVVGIGAVPATGFLRQSG 440
Cdd:PRK06327 217 AFLAaadEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGG---KGVSVAytdadgEAQTLEVDKLIVSIGRVPNTDGLGLEA 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  441 IGL--DSRGFIPVNKMMQTNVPGVFAAGDAVtfplawrnnRKvniphWQMAHA---QGRVAAQNMLAQEAEM--STVPY- 512
Cdd:PRK06327 294 VGLklDERGFIPVDDHCRTNVPNVYAIGDVV---------RG-----PMLAHKaeeEGVAVAERIAGQKGHIdyNTIPWv 359
                        410
                 ....*....|....
gi 21389617  513 LWT----AMFGKSL 522
Cdd:PRK06327 360 IYTspeiAWVGKTE 373
AhpF TIGR03140
alkyl hydroperoxide reductase subunit F; This enzyme is the partner of the peroxiredoxin ...
196-472 1.39e-14

alkyl hydroperoxide reductase subunit F; This enzyme is the partner of the peroxiredoxin (alkyl hydroperoxide reductase) AhpC which contains the peroxide-reactive cysteine. AhpF contains the reductant (NAD(P)H) binding domain (pfam00070) and presumably acts to resolve the disulfide which forms after oxidation of the active site cysteine in AphC. This proteins contains two paired conserved cysteine motifs, CxxCP and CxHCDGP. [Cellular processes, Detoxification, Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 274444 [Multi-domain]  Cd Length: 515  Bit Score: 76.25  E-value: 1.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   196 NVLIVGAGAAGLVCA-----ETLRQEGFSDRI---VLCTLDRH----LPYdrpklsksldTQPEQLALRPKEFFRAYGIE 263
Cdd:TIGR03140 214 DVLVVGGGPAGAAAAiyaarKGLRTAMVAERIggqVKDTVGIEnlisVPY----------TTGSQLAANLEEHIKQYPID 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   264 VLTEAQVVTVDV--RTKKVVFKDGFKLEYSKLLLAPGSSPKTLSCKGKEvenvftirtpEDANRVVR--------LARGR 333
Cdd:TIGR03140 284 LMENQRAKKIETedGLIVVTLESGEVLKAKSVIVATGARWRKLGVPGEK----------EYIGKGVAycphcdgpFFKGK 353
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   334 NVVVVGAGFLGMEVAAYLTEKAHSVSVVEleetpfrrFLGE-RVGRALM-KMFENNRVKFYMQTEVSELRGQEGKLKEVV 411
Cdd:TIGR03140 354 DVAVIGGGNSGIEAAIDLAGIVRHVTVLE--------FADElKADKVLQdKLKSLPNVDILTSAQTTEIVGDGDKVTGIR 425
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21389617   412 LK-----SSKVVRADVCVVGIGAVPATGFLRQSgIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFP 472
Cdd:TIGR03140 426 YQdrnsgEEKQLDLDGVFVQIGLVPNTEWLKDA-VELNRRGEIVIDERGRTSVPGIFAAGDVTTVP 490
PRK07818 PRK07818
dihydrolipoamide dehydrogenase; Reviewed
273-504 3.04e-14

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 236106 [Multi-domain]  Cd Length: 466  Bit Score: 75.06  E-value: 3.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  273 VDVRTKKVVFKDGF--KLEYSKLLLAPGSSPKTLscKGKEV-ENVFT----IRTPEDAnrvvrlargRNVVVVGAGFLGM 345
Cdd:PRK07818 117 TDANTLEVDLNDGGteTVTFDNAIIATGSSTRLL--PGTSLsENVVTyeeqILSRELP---------KSIVIAGAGAIGM 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  346 EVAAYLTEKAHSVSVVELEEtpfrRFL---GERVGRALMKMFENNRVKFYMQTEVSELRgQEGKLKEVVLKS----SKVV 418
Cdd:PRK07818 186 EFAYVLKNYGVDVTIVEFLD----RALpneDAEVSKEIAKQYKKLGVKILTGTKVESID-DNGSKVTVTVSKkdgkAQEL 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  419 RADVCVVGIGAVPAT-GF-LRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDaVTFPLawrnnrkvniphwQMAH---AQG 493
Cdd:PRK07818 261 EADKVLQAIGFAPRVeGYgLEKTGVALTDRGAIAIDDYMRTNVPHIYAIGD-VTAKL-------------QLAHvaeAQG 326
                        250
                 ....*....|.
gi 21389617  494 RVAAQNMLAQE 504
Cdd:PRK07818 327 VVAAETIAGAE 337
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
260-501 4.05e-14

mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]


Pssm-ID: 273944 [Multi-domain]  Cd Length: 463  Bit Score: 74.77  E-value: 4.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   260 YGIEVLtEAQVVTVDVRTKKVvfKDGFKLEYSK-LLLAPGSSPKTLSCKG-KEVEnvftIRTPEDANRVVRLARgrNVVV 337
Cdd:TIGR02053 101 YGVDYL-RGRARFKDPKTVKV--DLGREVRGAKrFLIATGARPAIPPIPGlKEAG----YLTSEEALALDRIPE--SLAV 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   338 VGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFLGErVGRALMKMFENNRVKFYMQTEVSELRGQEGKLKEVVLKSSK- 416
Cdd:TIGR02053 172 IGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPE-ISAAVEEALAEEGIEVVTSAQVKAVSVRGGGKIITVEKPGGq 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   417 -VVRADVCVVGIGAVPATGFL--RQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDaVTFPLAWRNnrkvniphwqMAHAQG 493
Cdd:TIGR02053 251 gEVEADELLVATGRRPNTDGLglEKAGVKLDERGGILVDETLRTSNPGIYAAGD-VTGGLQLEY----------VAAKEG 319

                  ....*...
gi 21389617   494 RVAAQNML 501
Cdd:TIGR02053 320 VVAAENAL 327
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
245-500 5.90e-14

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 74.03  E-value: 5.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  245 QPeQLALRPKEFFRAYGIEVLTEAQVVTVDVRTKKV-VFKDGFKLEYSKLLLAPGSSPKTLSCKG--------KEVENVF 315
Cdd:PTZ00318  69 RP-ALAKLPNRYLRAVVYDVDFEEKRVKCGVVSKSNnANVNTFSVPYDKLVVAHGARPNTFNIPGveerafflKEVNHAR 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  316 TIR---------------TPEDANRVVrlargrNVVVVGAGFLGMEVAAYLTE--------------KAHSVSVVELEET 366
Cdd:PTZ00318 148 GIRkrivqcieraslpttSVEERKRLL------HFVVVGGGPTGVEFAAELADffrddvrnlnpelvEECKVTVLEAGSE 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  367 PFRRFlGERVGRALMKMFENNRVKFYMQTEVSELrgqegKLKEVVLKSSKVVRADVCV--VGIGAVPATgflRQSGIGLD 444
Cdd:PTZ00318 222 VLGSF-DQALRKYGQRRLRRLGVDIRTKTAVKEV-----LDKEVVLKDGEVIPTGLVVwsTGVGPGPLT---KQLKVDKT 292
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 21389617  445 SRGFIPVNKMMQT-NVPGVFAAGDAVTfplawrNNRKVNIPHWQMAHAQGRVAAQNM 500
Cdd:PTZ00318 293 SRGRISVDDHLRVkPIPNVFALGDCAA------NEERPLPTLAQVASQQGVYLAKEF 343
PRK09853 PRK09853
putative selenate reductase subunit YgfK; Provisional
161-504 8.73e-14

putative selenate reductase subunit YgfK; Provisional


Pssm-ID: 236630 [Multi-domain]  Cd Length: 1019  Bit Score: 74.63  E-value: 8.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   161 EKVYVRASKQALQLQRRTKVMAKCISPsAGYSSSTNVLIVGAGAAGLVCAETLRQEGFSDRIvlctLDRHlpyDRP-KLS 239
Cdd:PRK09853  507 EAVNIRELKKVALEKGWDEYKQRWHKP-AGIGSRKKVAVIGAGPAGLAAAYFLARAGHPVTV----FERE---ENAgGVV 578
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   240 KSLDTQ---PEQLALRPKEFFRAYGIEVLTEAQVvTVDVRTKKvvfKDGFKLeyskLLLAPG---SSPKTLSCKGKEVEN 313
Cdd:PRK09853  579 KNIIPQfriPAELIQHDIEFVKAHGVKFEFGCSP-DLTVEQLK---NEGYDY----VVVAIGadkNGGLKLEGGNQNVIK 650
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   314 VFTIrTPEDANRVVRLARGRNVVVVGAGFLGMEVA--AYLTEKAHSVSVV-------------ELEEtpfrrFLGERVgr 378
Cdd:PRK09853  651 ALPF-LEEYKNKGTALKLGKHVVVVGGGNTAMDAAraALRVPGVEKVTVVyrrtkqempawreEYEE-----ALEDGV-- 722
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   379 alMKMFENNRVKFYMQ----TEVSEL--RGQEGKLKEVVLKSSKVVRADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVN 452
Cdd:PRK09853  723 --EFKELLNPESFDADgtltCRVMKLgePDESGRRRPVETGETVTLEADTVITAIGEQVDTELLKANGIPLDKKGWPVVD 800
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 21389617   453 KMMQTNVPGVFAAGDAVTFPlawrnNRKVNiphwqmAHAQGRVAAQNMLAQE 504
Cdd:PRK09853  801 ANGETSLTNVYMIGDVQRGP-----STIVA------AIADARRAADAILSRE 841
PLN02507 PLN02507
glutathione reductase
249-468 4.82e-13

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 71.39  E-value: 4.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  249 LALRPKEFFRAYGI--EVLTEAQVV-------TVDVRTKKVVFKDGFKLEYS--KLLLAPGSSPKTLSCKGKEVEnvfti 317
Cdd:PLN02507 116 LQKKTDEILRLNGIykRLLANAGVKlyegegkIVGPNEVEVTQLDGTKLRYTakHILIATGSRAQRPNIPGKELA----- 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  318 RTPEDANRVVRLARgrNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFLGERvgRALM-KMFENNRVKFYMQTE 396
Cdd:PLN02507 191 ITSDEALSLEELPK--RAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEM--RAVVaRNLEGRGINLHPRTN 266
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21389617  397 VSELRGQEGKLKeVVLKSSKVVRADVCVVGIGAVPATGF--LRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDA 468
Cdd:PLN02507 267 LTQLTKTEGGIK-VITDHGEEFVADVVLFATGRAPNTKRlnLEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDV 339
GOGAT_sm_gam TIGR01317
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ...
197-468 5.83e-13

glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for the NADPH-dependent or NADH-dependent glutamate synthase (EC 1.4.1.13 and 1.4.1.14, respectively) small subunit or homologous region. TIGR01316 describes a family in several archaeal and deeply branched bacterial lineages of a homotetrameric form for which there is no large subunit. Another model describes glutamate synthase small subunit from gamma and some alpha subdivision Proteobacteria plus paralogs of unknown function. This model describes the small subunit, or homologous region of longer forms proteins, of eukaryotes, Gram-positive bacteria, cyanobacteria, and some other lineages. All members with known function participate in NADH or NADPH-dependent reactions to interconvert between glutamine plus 2-oxoglutarate and two molecules of glutamate.


Pssm-ID: 162300 [Multi-domain]  Cd Length: 485  Bit Score: 71.01  E-value: 5.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   197 VLIVGAGAAGLVCAETLRQEGfSDRIVLCTLDRH---LPYDRP--KLSKSldtqpeqLALRPKEFFRAYGIEVLTEAQVv 271
Cdd:TIGR01317 146 VAVVGSGPAGLAAADQLNRAG-HTVTVFEREDRCgglLMYGIPnmKLDKA-------IVDRRIDLLSAEGIDFVTNTEI- 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   272 tvdvrtKKVVFKDGFKLEYSKLLLAPGSS-PKTLSCKGKEVENV-FTIRTPEDANRVVR----------LARGRNVVVVG 339
Cdd:TIGR01317 217 ------GVDISADELKEQFDAVVLAGGATkPRDLPIPGRELKGIhYAMEFLPSATKALLgkdfkdiifiKAKGKKVVVIG 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   340 AGFLGME-VAAYLTEKAHSVSVVEL---------------------------EETPFRRFLGERVGRALMKMFE---NNR 388
Cdd:TIGR01317 291 GGDTGADcVGTSLRHGAASVHQFEImpkppearakdnpwpewprvyrvdyahEEAAAHYGRDPREYSILTKEFIgddEGK 370
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   389 VKFYMQTEVSELRGQEGKLKEV-VLKSSKVVRADVCVVGIGAV-PATGFLRQSGIGLDSRGFIPVN-KMMQTNVPGVFAA 465
Cdd:TIGR01317 371 VTALRTVRVEWKKSQDGKWQFVeIPGSEEVFEADLVLLAMGFVgPEQILLDDFGVKKTRRGNISAGyDDYSTSIPGVFAA 450

                  ...
gi 21389617   466 GDA 468
Cdd:TIGR01317 451 GDC 453
Se_ygfK TIGR03315
putative selenate reductase, YgfK subunit; Members of this protein family are YgfK, predicted ...
161-514 5.96e-13

putative selenate reductase, YgfK subunit; Members of this protein family are YgfK, predicted to be one subunit of a three-subunit, molybdopterin-containing selenate reductase. This enzyme is found, typically, in genomic regions associated with xanthine dehydrogenase homologs predicted to belong to the selenium-dependent molybdenum hydroxylases (SDMH). Therefore, the selenate reductase is suggested to play a role in furnishing selenide for SelD, the selenophosphate synthase.


Pssm-ID: 132358 [Multi-domain]  Cd Length: 1012  Bit Score: 71.74  E-value: 5.96e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617    161 EKVYVRASKQALQLQRRTKVMAKCiSPSAGYSSSTNVLIVGAGAAGLVCAETLRQEGfsdrIVLCTLDR-HLPYDRPKLS 239
Cdd:TIGR03315  505 ESVNIREMKKVAAEKGYDEYKTRW-HKPQGKSSAHKVAVIGAGPAGLSAGYFLARAG----HPVTVFEKkEKPGGVVKNI 579
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617    240 KSLDTQPEQLALRPKEFFRAYGIEVLTEAQVvTVDVRTKKvvfKDGFKleysKLLLAPG---SSPKTLSCKGKEVENVFT 316
Cdd:TIGR03315  580 IPEFRISAESIQKDIELVKFHGVEFKYGCSP-DLTVAELK---NQGYK----YVILAIGawkHGPLRLEGGGERVLKSLE 651
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617    317 -IRTPEDANRVVRLarGRNVVVVGAGFLGMEVA--AYLTEKAHSVSVV---ELEETP-FRRFLGERVGRALMKMFENNRV 389
Cdd:TIGR03315  652 fLRAFKEGPTINPL--GKHVVVVGGGNTAMDAAraALRVPGVEKVTVVyrrTKRYMPaSREELEEALEDGVDFKELLSPE 729
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617    390 KFYMQT---EVSEL--RGQEGKLKEVVLKSSKVVRADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNK-MMQTNVPGVF 463
Cdd:TIGR03315  730 SFEDGTltcEVMKLgePDASGRRRPVGTGETVDLPADTVIAAVGEQVDTDLLQKNGIPLDEYGWPVVNQaTGETNITNVF 809
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 21389617    464 AAGDAVTFPLAWRNnrkvniphwqmAHAQGRVAAQNMLAQEAEMSTVPYLW 514
Cdd:TIGR03315  810 VIGDANRGPATIVE-----------AIADGRKAANAILSREGLNSDVDKVF 849
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
197-472 2.24e-12

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 68.48  E-value: 2.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  197 VLIVGAGAAGLVCAETLRQEGFSDRIvlctldrhlpYDRpklsksldtQPEQLAL--------R-PKEFFRAyGIEVLTE 267
Cdd:PRK12770  21 VAIIGAGPAGLAAAGYLACLGYEVHV----------YDK---------LPEPGGLmlfgipefRiPIERVRE-GVKELEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  268 AQVVTVdVRTK------------------KVVFKDGFKlEYSKLLLAPGS-SPKTLSCKGKEVENV-------FTIRTPE 321
Cdd:PRK12770  81 AGVVFH-TRTKvccgeplheeegdefverIVSLEELVK-KYDAVLIATGTwKSRKLGIPGEDLPGVysaleylFRIRAAK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  322 DA---NRVVRLARGRNVVVVGAGFLGMEVA--AYLtEKAHSVSVV---ELEETPFRRFLGERVGRALMKMFEN-NRVKFY 392
Cdd:PRK12770 159 LGylpWEKVPPVEGKKVVVVGAGLTAVDAAleAVL-LGAEKVYLAyrrTINEAPAGKYEIERLIARGVEFLELvTPVRII 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  393 MQTEVSELRGQEGKLK----------EVVLKSSKVVRADVCVVGIGAVPATGFLRQS-GIGLDSRGFIPVNKMMQTNVPG 461
Cdd:PRK12770 238 GEGRVEGVELAKMRLGepdesgrprpVPIPGSEFVLEADTVVFAIGEIPTPPFAKEClGIELNRKGEIVVDEKHMTSREG 317
                        330
                 ....*....|.
gi 21389617  462 VFAAGDAVTFP 472
Cdd:PRK12770 318 VFAAGDVVTGP 328
PRK06116 PRK06116
glutathione reductase; Validated
335-467 2.88e-12

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 68.64  E-value: 2.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  335 VVVVGAGFLGMEVAAYLtekaHSVSV-VEL---EETPFRRFLGErVGRALMKMFENNRVKFYMQTEVSEL-RGQEGKLKe 409
Cdd:PRK06116 170 VAVVGAGYIAVEFAGVL----NGLGSeTHLfvrGDAPLRGFDPD-IRETLVEEMEKKGIRLHTNAVPKAVeKNADGSLT- 243
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  410 VVLKSSKVVRADVCVVGIGAVPAT-GF-LRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGD 467
Cdd:PRK06116 244 LTLEDGETLTVDCLIWAIGREPNTdGLgLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGD 303
acoL PRK06912
dihydrolipoamide dehydrogenase; Validated
335-497 3.74e-12

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 180743 [Multi-domain]  Cd Length: 458  Bit Score: 68.58  E-value: 3.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  335 VVVVGAGFLGMEVAAYLTEKAHSVSVVELEEtpfRRFLGE--RVGRALMKMFENNRVKFYMQTEVSELRGQEgklKEVVL 412
Cdd:PRK06912 173 LLIVGGGVIGCEFASIYSRLGTKVTIVEMAP---QLLPGEdeDIAHILREKLENDGVKIFTGAALKGLNSYK---KQALF 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  413 K---SSKVVRADVCVVGIGAVPATG--FLRQSGIGLDSRGfIPVNKMMQTNVPGVFAAGDAvtfplawrnnrkvnIPHWQ 487
Cdd:PRK06912 247 EyegSIQEVNAEFVLVSVGRKPRVQqlNLEKAGVQFSNKG-ISVNEHMQTNVPHIYACGDV--------------IGGIQ 311
                        170
                 ....*....|...
gi 21389617  488 MAHA---QGRVAA 497
Cdd:PRK06912 312 LAHVafhEGTTAA 324
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
72-174 6.08e-12

Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha subunit; The RO family comprise a large class of aromatic ring-hydroxylating dioxygenases found predominantly in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth. ROs consist of two or three components: reductase, oxygenase, and ferredoxin (in some cases) components. The oxygenase component may contain alpha and beta subunits, with the beta subunit having a purely structural function. Some oxygenase components contain only an alpha subunit. The oxygenase alpha subunit has two domains, an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from the reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Reduced pyridine nucleotide is used as the initial source of two electrons for dioxygen activation.


Pssm-ID: 239551 [Multi-domain]  Cd Length: 118  Bit Score: 62.61  E-value: 6.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  72 VCHVKDL-ENGQMREVELGWGKVLLVKD-NGEFHALGHKCPHYGAPLVKG-VLSRGRVRCPWHGACFNiSTGDL------ 142
Cdd:cd03469   4 VGHSSELpEPGDYVTLELGGEPLVLVRDrDGEVRAFHNVCPHRGARLCEGrGGNAGRLVCPYHGWTYD-LDGKLvgvpre 82
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 21389617 143 EDFPGLD----SLHKFQVKIEKEKVYVRASKQALQL 174
Cdd:cd03469  83 EGFPGFDkeklGLRTVPVEEWGGLIFVNLDPDAPPL 118
PRK06370 PRK06370
mercuric reductase; Validated
336-501 6.26e-12

mercuric reductase; Validated


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 67.92  E-value: 6.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  336 VVVGAGFLGMEVAAYLTEKAHSVSVVELEEtpfrRFLG---ERVGRALMKMFENNRVKFYMQTEVSELRGQEGKlKEVVL 412
Cdd:PRK06370 175 VIIGGGYIGLEFAQMFRRFGSEVTVIERGP----RLLPredEDVAAAVREILEREGIDVRLNAECIRVERDGDG-IAVGL 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  413 KS---SKVVRADVCVVGIGAVPATGF--LRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDavtfplawrnnrkVNIPhWQ 487
Cdd:PRK06370 250 DCnggAPEITGSHILVAVGRVPNTDDlgLEAAGVETDARGYIKVDDQLRTTNPGIYAAGD-------------CNGR-GA 315
                        170
                 ....*....|....*..
gi 21389617  488 MAH---AQGRVAAQNML 501
Cdd:PRK06370 316 FTHtayNDARIVAANLL 332
PRK14694 PRK14694
putative mercuric reductase; Provisional
227-511 1.01e-11

putative mercuric reductase; Provisional


Pssm-ID: 237790 [Multi-domain]  Cd Length: 468  Bit Score: 67.27  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  227 LDRHLPYD------RPKLSKSldTQPEQLALRPKEFFRAYGIEVLTEAQVVTV--------DVRTKKVVFKDGFK--LEY 290
Cdd:PRK14694  64 LRRESPFDdglsaqAPVVDRS--ALLAQQQARVEELRESKYQSILRENAAITVlngearfvDERTLTVTLNDGGEqtVHF 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  291 SKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDANRVvrlarGRNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEetpfrR 370
Cdd:PRK14694 142 DRAFIGTGARPAEPPVPGLAETPYLTSTSALELDHI-----PERLLVIGASVVALELAQAFARLGSRVTVLARS-----R 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  371 FLGER---VGRALMKMFENNRVKFYMQTEVSELRGQEgklKEVVLKS-SKVVRADVCVVGIGAVPATGFLRQSGIGLD-S 445
Cdd:PRK14694 212 VLSQEdpaVGEAIEAAFRREGIEVLKQTQASEVDYNG---REFILETnAGTLRAEQLLVATGRTPNTENLNLESIGVEtE 288
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21389617  446 RGFIPVNKMMQTNVPGVFAAGDAvtfplawrnnrkVNIPHW-QMAHAQGRVAAQNMLAQEA--EMSTVP 511
Cdd:PRK14694 289 RGAIRIDEHLQTTVSGIYAAGDC------------TDQPQFvYVAAAGGSRAAINMTGGDAslDLSAMP 345
PRK06467 PRK06467
dihydrolipoamide dehydrogenase; Reviewed
276-473 1.78e-11

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 180579 [Multi-domain]  Cd Length: 471  Bit Score: 66.52  E-value: 1.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  276 RTKKVVFKDGFK--LEYSKLLLAPGSSPktlsckgkeVENVFTirtPEDANRVV-------------RLargrnvVVVGA 340
Cdd:PRK06467 121 NTLEVTGEDGKTtvIEFDNAIIAAGSRP---------IQLPFI---PHDDPRIWdstdalelkevpkRL------LVMGG 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  341 GFLGMEVAAYLTEKAHSVSVVELeetpFRRFLG---ERVGRALMKMFENnRVKFYMQTEVSelrGQEGKLKEVVLKS--- 414
Cdd:PRK06467 183 GIIGLEMGTVYHRLGSEVDVVEM----FDQVIPaadKDIVKVFTKRIKK-QFNIMLETKVT---AVEAKEDGIYVTMegk 254
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21389617  415 ---SKVVRADVCVVGIGAVPATGFL--RQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFPL 473
Cdd:PRK06467 255 kapAEPQRYDAVLVAVGRVPNGKLLdaEKAGVEVDERGFIRVDKQCRTNVPHIFAIGDIVGQPM 318
Rieske_NirD_small_Bacillus cd03530
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ...
71-165 1.90e-11

Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar to the Bacillus subtilis small subunit of assimilatory nitrite reductase containing a Rieske domain. The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. Assimilatory nitrate and nitrite reductases convert nitrate through nitrite to ammonium.


Pssm-ID: 239606 [Multi-domain]  Cd Length: 98  Bit Score: 60.31  E-value: 1.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  71 AVCHVKDLENGQMREVELGWGKVLLVK-DNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDfPGLD 149
Cdd:cd03530   3 DIGALEDIPPRGARKVQTGGGEIAVFRtADDEVFALENRCPHKGGPLSEGIVHGEYVTCPLHNWVIDLETGEAQG-PDEG 81
                        90
                ....*....|....*.
gi 21389617 150 SLHKFQVKIEKEKVYV 165
Cdd:cd03530  82 CVRTFPVKVEDGRVYL 97
gluta_reduc_1 TIGR01421
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ...
293-469 2.98e-11

glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of animals, yeast, and a number of animal-resident bacteria. [Energy metabolism, Electron transport]


Pssm-ID: 273614 [Multi-domain]  Cd Length: 450  Bit Score: 65.63  E-value: 2.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   293 LLLAPGSSPKTLsckgkevENVFTIRTPEDANRVVRLAR-GRNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRF 371
Cdd:TIGR01421 133 ILIATGGKPSFP-------ENIPGAELGTDSDGFFALEElPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRHERVLRSF 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   372 lGERVGRALMKMFENNRVKFYMQTEVSEL-RGQEGKLKEVVLKSSKVVRADVCVVGIGAVPATG--FLRQSGIGLDSRGF 448
Cdd:TIGR01421 206 -DSMISETITEEYEKEGINVHKLSKPVKVeKTVEGKLVIHFEDGKSIDDVDELIWAIGRKPNTKglGLENVGIKLNEKGQ 284
                         170       180
                  ....*....|....*....|.
gi 21389617   449 IPVNKMMQTNVPGVFAAGDAV 469
Cdd:TIGR01421 285 IIVDEYQNTNVPGIYALGDVV 305
gltA TIGR01316
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ...
192-469 3.44e-11

glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of NADPH and NADH forms of glutamate synthase as found in eukaryotes and some bacteria. This protein is found in numerous species having no homolog of the glutamate synthase large subunit. The prototype of the family, from Pyrococcus sp. KOD1, was shown to be active as a homotetramer and to require NADPH. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 130383 [Multi-domain]  Cd Length: 449  Bit Score: 65.28  E-value: 3.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   192 SSSTNVLIVGAGAAGLVCAETLRQEGFSDRI--VLCTLDRHLPYDRP--KLSKS-LDTQPEQLALRPKEFFRAYGIevlt 266
Cdd:TIGR01316 131 STHKKVAVIGAGPAGLACASELAKAGHSVTVfeALHKPGGVVTYGIPefRLPKEiVVTEIKTLKKLGVTFRMNFLV---- 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   267 eaqvvtvdvrtKKVVFKDGFKLEYSKLLLAPGS-SPKTLSCKGKEVENVFT----------IRTPEDANRVVRLARGRNV 335
Cdd:TIGR01316 207 -----------GKTATLEELFSQYDAVFIGTGAgLPKLMNIPGEELCGVYSandfltranlMKAYEFPHADTPVYAGKSV 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   336 VVVGAGF-----------LGMEV-AAYLTEKAHSVSVVE----LEETPFR--------RFLGERVGRALMKMFEnnrvkf 391
Cdd:TIGR01316 276 VVIGGGNtavdsartalrLGAEVhCLYRRTREDMTARVEeiahAEEEGVKfhflcqpvEIIGDEEGNVRAVKFR------ 349
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21389617   392 ymQTEVSELRGQEGKLKEVVLKSSKVVRADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAV 469
Cdd:TIGR01316 350 --KMDCQEQIDSGERRFLPCGDAECKLEADAVIVAIGNGSNPIMAETTRLKTSERGTIVVDEDQRTSIPGVFAGGDII 425
AhpF COG3634
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
196-472 3.81e-11

Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];


Pssm-ID: 226160 [Multi-domain]  Cd Length: 520  Bit Score: 65.54  E-value: 3.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 196 NVLIVGAGAAGLVCA-----ETLRQEGFSDRI---VLCTLDRH----LPY-DRPKLSKSLdtqpeqlalrpKEFFRAYGI 262
Cdd:COG3634 213 DVLVVGGGPAGAAAAiyaarKGIRTGLVAERFggqVLDTMGIEnfisVPEtEGPKLAAAL-----------EAHVKQYDV 281
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 263 EVLTeAQVVTVDVRTK------KVVFKDGFKLEYSKLLLAPGSSPKTLSCKGKEvenvftirtpEDANRVVR-------- 328
Cdd:COG3634 282 DVMN-LQRASKLEPAAveggliEVELANGAVLKARTVILATGARWRNMNVPGED----------EYRNKGVAycphcdgp 350
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 329 LARGRNVVVVGAGFLGMEVAAYLTEKAHSVSVVEleetpfrrFLGERVGRALM--KMFENNRVKFYMQTEVSELRGQEGK 406
Cdd:COG3634 351 LFKGKRVAVIGGGNSGVEAAIDLAGIVEHVTLLE--------FAPELKADAVLqdKLRSLPNVTIITNAQTTEVKGDGDK 422
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21389617 407 L-----KEVVLKSSKVVRADVCVVGIGAVPATGFLRQSgIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFP 472
Cdd:COG3634 423 VtgleyRDRVSGEEHHLELEGVFVQIGLLPNTEWLKGA-VELNRRGEIIVDARGETNVPGVFAAGDCTTVP 492
PRK13748 PRK13748
putative mercuric reductase; Provisional
274-511 3.87e-11

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 65.56  E-value: 3.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  274 DVRTKKVVFKDGFKLE--YSKLLLAPGSSPKTLSCKG-KE------VENVFTIRTPEdanrvvRLArgrnvvVVGAGFLG 344
Cdd:PRK13748 215 DDQTLIVRLNDGGERVvaFDRCLIATGASPAVPPIPGlKEtpywtsTEALVSDTIPE------RLA------VIGSSVVA 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  345 MEVAAYLTEKAHSVSVVELEETPFRRflGERVGRALMKMFENNRVKFYMQTEVSELRGQEGklkEVVLKSSK-VVRADVC 423
Cdd:PRK13748 283 LELAQAFARLGSKVTILARSTLFFRE--DPAIGEAVTAAFRAEGIEVLEHTQASQVAHVDG---EFVLTTGHgELRADKL 357
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  424 VVGIGAVPATGFL--RQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFPlawrnnrkvniphwQ---MAHAQGRVAAQ 498
Cdd:PRK13748 358 LVATGRAPNTRSLalDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQP--------------QfvyVAAAAGTRAAI 423
                        250
                 ....*....|....*
gi 21389617  499 NMLAQEA--EMSTVP 511
Cdd:PRK13748 424 NMTGGDAalDLTAMP 438
PTZ00058 PTZ00058
glutathione reductase; Provisional
284-469 3.88e-11

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 65.41  E-value: 3.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  284 DGFKLEYSKLLLAPGSSPKTLSCKGKEvenvFTIrtpeDANRVVRLARGRNVVVVGAGFLGMEVAAYLTEKAHSVSVVEL 363
Cdd:PTZ00058 197 DGQVIEGKNILIAVGNKPIFPDVKGKE----FTI----SSDDFFKIKEAKRIGIAGSGYIAVELINVVNRLGAESYIFAR 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  364 EETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSELRGQEGK-LKEVVLKSSKVVRADVCVVGIGAVPATGFLRQSGIG 442
Cdd:PTZ00058 269 GNRLLRKF-DETIINELENDMKKNNINIITHANVEEIEKVKEKnLTIYLSDGRKYEHFDYVIYCVGRSPNTEDLNLKALN 347
                        170       180
                 ....*....|....*....|....*...
gi 21389617  443 -LDSRGFIPVNKMMQTNVPGVFAAGDAV 469
Cdd:PTZ00058 348 iKTPKGYIKVDDNQRTSVKHIYAVGDCC 375
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
255-467 5.77e-11

trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.


Pssm-ID: 200098 [Multi-domain]  Cd Length: 486  Bit Score: 64.99  E-value: 5.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   255 EFFRAYGieVLTEAQVVTV-DVRTKKVVFKDGFKLEYskLLLAPGSSPKTLSCKGKEV----ENVFTIRTPEdanrvvrl 329
Cdd:TIGR01423 120 TFFLGWG--ALEDKNVVLVrESADPKSAVKERLQAEH--ILLATGSWPQMLGIPGIEHcissNEAFYLDEPP-------- 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   330 argRNVVVVGAGFLGMEVAAYLTEKAHSVSVVEL--EETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRGQEGKL 407
Cdd:TIGR01423 188 ---RRVLTVGGGFISVEFAGIFNAYKPRGGKVTLcyRNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTLNADGS 264
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21389617   408 KEVVLKSSKVVRADVCVVGIGAVPATGFLR--QSGIGLDSRGFIPVNKMMQTNVPGVFAAGD 467
Cdd:TIGR01423 265 KHVTFESGKTLDVDVVMMAIGRVPRTQTLQldKVGVELTKKGAIQVDEFSRTNVPNIYAIGD 326
Nterm_to_SelD TIGR03169
pyridine nucleotide-disulfide oxidoreductase family protein; Members of this protein family ...
335-471 6.45e-11

pyridine nucleotide-disulfide oxidoreductase family protein; Members of this protein family include N-terminal sequence regions of (probable) bifunctional proteins whose C-terminal sequences are SelD, or selenide,water dikinase, the selenium donor protein necessary for selenium incorporation into protein (as selenocysteine), tRNA (as 2-selenouridine), or both. However, some members of this family occur in species that do not show selenium incorporation, and the function of this protein family is unknown.


Pssm-ID: 274465 [Multi-domain]  Cd Length: 364  Bit Score: 64.15  E-value: 6.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   335 VVVVGAGFLGMEVA---AY---LTEKAHSVSVVELEETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSELRGqegklK 408
Cdd:TIGR03169 147 IAVIGGGAAGVELAlamAHrlrQLGRNAEVTLIDRGNVLLPGH-NARVRRRLERALQERGVTLHLGATVAEVTA-----D 220
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21389617   409 EVVLKSSKVVRADVCVVGIGAVPAtGFLRQSGIGLDSRGFIPVNKMMQT-NVPGVFAAGDAVTF 471
Cdd:TIGR03169 221 AVRLEDGQTLPADFTFWATGARPP-GWLAESGLALDEDGFIRVGPTLQSlSHPDIFAAGDCAHL 283
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
197-511 2.62e-10

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only];


Pssm-ID: 223567 [Multi-domain]  Cd Length: 457  Bit Score: 62.69  E-value: 2.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 197 VLIVGAGAAGLVCAETLRQEGFsDRIVlctldrhlpYDRPKLSKSLDTQ--PEQLAlrPKEFFRAyGIEVLTEAQV-VTV 273
Cdd:COG0493 126 VAVIGAGPAGLAAADDLSRAGH-DVTV---------FERVALDGGLLLYgiPDFKL--PKDILDR-RLELLERSGVeFKL 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 274 DVRTKKVVFKDGFKLEYSKLLLAPGSS-PKTLSCKGKEVENVFTiRTP-----------EDANRVVRLARGRNVVVVGAG 341
Cdd:COG0493 193 NVRVGRDITLEELLKEYDAVFLATGAGkPRPLDIPGEDAKGVAF-ALDfltrlnkevlgDFAEDRTPPAKGKRVVVIGGG 271
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 342 FLGMEVAAylTEKAHSVSVV--------ELEETPF----RRFLGERVG-RALMKMFENNR-------------VKFYMQT 395
Cdd:COG0493 272 DTAMDCAG--TALRLGAKSVtcfyredrDDETNEWptwaAQLEVRSAGeEGVERLPFVQPkafigneggrvtgVKFGRVE 349
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 396 EVSELRGQEGKLKEVVLKSSKVVRADVCVVGIGAVP--ATGFLRQSGIGLDSRGFIPVNKMM-QTNVPGVFAAGDAVTFP 472
Cdd:COG0493 350 PGEYVDGWGRRGPVGVIGTEKTDAADTVILAIGFEGdaTDGLLLEFGLKLDKRGRIKVDENLqQTSIPGVFAGGDAVRGA 429
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 21389617 473 --LAWrnnrkvniphwqmAHAQGRVAAQNMLAQEAEMSTVP 511
Cdd:COG0493 430 alVVW-------------AIAEGREAAKAIDKELLLGKAVL 457
PRK07846 PRK07846
mycothione reductase; Reviewed
318-509 9.53e-10

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 60.74  E-value: 9.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  318 RTPEDANRVVRLARgrNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRF---LGERVGRALMKmfennRVKFYMQ 394
Cdd:PRK07846 154 HTSDTIMRLPELPE--SLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLdddISERFTELASK-----RWDVRLG 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  395 TEVSELRGQEGKLkEVVLKSSKVVRADVCVVGIGAVPATGFL--RQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDaVTFP 472
Cdd:PRK07846 227 RNVVGVSQDGSGV-TLRLDDGSTVEADVLLVATGRVPNGDLLdaAAAGVDVDEDGRVVVDEYQRTSAEGVFALGD-VSSP 304
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 21389617  473 lawrnnrkvniphWQMAH---AQGRVAAQNMLAQEAEMST 509
Cdd:PRK07846 305 -------------YQLKHvanHEARVVQHNLLHPDDLIAS 331
Rieske_T4moC cd03474
Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske ...
72-166 1.70e-09

Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. T4mo is a four-protein complex that catalyzes the NADH- and O2-dependent hydroxylation of toluene to form p-cresol. T4mo consists of an NADH oxidoreductase (T4moF), a diiron hydroxylase (T4moH), a catalytic effector protein (T4moD), and a Rieske ferredoxin (T4moC). T4moC contains a Rieske domain and functions as an obligate electron carrier between T4moF and T4moH. Rieske ferredoxins are found as subunits of membrane oxidase complexes, cis-dihydrodiol-forming aromatic dioxygenases, bacterial assimilatory nitrite reductases, and arsenite oxidase. Rieske ferredoxins are also found as soluble electron carriers in bacterial dioxygenase and monooxygenase complexes.


Pssm-ID: 239556 [Multi-domain]  Cd Length: 108  Bit Score: 55.42  E-value: 1.70e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  72 VCHVKDLENGQMREVELGWGKVLLV-KDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDfPGLDS 150
Cdd:cd03474   4 VCSLDDVWEGEMELVDVDGEEVLLVaPEGGEFRAFQGICPHQEIPLAEGGFDGGVLTCRAHLWQFDADTGEGLN-PRDCR 82
                        90
                ....*....|....*.
gi 21389617 151 LHKFQVKIEKEKVYVR 166
Cdd:cd03474  83 LARYPVKVEGGDILVD 98
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
409-496 2.00e-09

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 59.87  E-value: 2.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  409 EVVLKSSKVVRADVCVVGIGAVPAT---GfLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDaVT--FPLAwrnnrkvni 483
Cdd:PRK07845 252 VVTLTDGRTVEGSHALMAVGSVPNTaglG-LEEAGVELTPSGHITVDRVSRTSVPGIYAAGD-CTgvLPLA--------- 320
                         90
                 ....*....|...
gi 21389617  484 phwQMAHAQGRVA 496
Cdd:PRK07845 321 ---SVAAMQGRIA 330
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
187-512 4.58e-09

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 58.97  E-value: 4.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  187 PSAGYSSSTNVLIVGAGAAGLVCAETLRQEGFSDRIvlctldrhlpydrpklsksLDTQPEqlalrPKEFFRaYGI---- 262
Cdd:PRK12814 186 PERAPKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTI-------------------FDANEQ-----AGGMMR-YGIprfr 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  263 --EVLTEAQV-----VTVDVRTKKVVFKD----GFKLEYSKLLLAPGSS-PKTLSCKGKEVENVFT-IRTPEDANRVVRL 329
Cdd:PRK12814 241 lpESVIDADIaplraMGAEFRFNTVFGRDitleELQKEFDAVLLAVGAQkASKMGIPGEELPGVISgIDFLRNVALGTAL 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  330 ARGRNVVVVGAGFLGMEVA-AYLTEKAHSVSVV---ELEETPFRRF-----LGERVG-------RALMKMfeNNRVKFym 393
Cdd:PRK12814 321 HPGKKVVVIGGGNTAIDAArTALRLGAESVTILyrrTREEMPANRAeieeaLAEGVSlrelaapVSIERS--EGGLEL-- 396
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  394 qTEVSELRG---QEGKLKEVVLKSSK-VVRADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNK-MMQTNVPGVFAAGDA 468
Cdd:PRK12814 397 -TAIKMQQGepdESGRRRPVPVEGSEfTLQADTVISAIGQQVDPPIAEAAGIGTSRNGTVKVDPeTLQTSVAGVFAGGDC 475
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 21389617  469 VTFP-LAWRnnrkvniphwqmAHAQGRVAAQN----MLAQEAEMSTVPY 512
Cdd:PRK12814 476 VTGAdIAIN------------AVEQGKRAAHAidlfLNGKPVTAPVQPF 512
gluta_reduc_2 TIGR01424
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ...
233-468 4.63e-09

glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of plants and some bacteria, including cyanobacteria. [Energy metabolism, Electron transport]


Pssm-ID: 213618 [Multi-domain]  Cd Length: 446  Bit Score: 58.67  E-value: 4.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   233 YDRPKLSKSLDTQPEQLALRPKEFFRAYGIEVL-TEAQVV---TVDVRTKkvvfkdGFKLEYSKLLLAPGSSPKTLSCKG 308
Cdd:TIGR01424  76 FDWKKLLAAKDQEIARLSGLYRKGLANAGAELLdGRAELVgpnTVEVLAS------GKTYTAEKILIAVGGRPPKPALPG 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   309 KEV----ENVFTIRT-PEdanrvvrlargrNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFlGERVGRALMKM 383
Cdd:TIGR01424 150 HELgitsNEAFHLPTlPK------------SILIAGGGYIAVEFAGIFRGLGVQTTLIYRGKEILRGF-DDDMRRGLAAA 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   384 FENNRVKFYMQTEVSEL-RGQEGKLKEVVLKSSKVVrADVCVVGIGAVPAT-GF-LRQSGIGLDSRGFIPVNKMMQTNVP 460
Cdd:TIGR01424 217 LEERGIRILPEDSITSIsKDDDGRLKATLSKHEEIV-ADVVLFATGRSPNTnGLgLEAAGVRLNDLGAIAVDEYSRTSTP 295

                  ....*...
gi 21389617   461 GVFAAGDA 468
Cdd:TIGR01424 296 SIYAVGDV 303
PRK09965 PRK09965
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
71-165 8.58e-09

3-phenylpropionate dioxygenase ferredoxin subunit; Provisional


Pssm-ID: 170182 [Multi-domain]  Cd Length: 106  Bit Score: 53.24  E-value: 8.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   71 AVCHVKDLENGQMREVELGwGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLS-RGRVRCPWHGACFNISTGDLEDFPGLD 149
Cdd:PRK09965   5 YACPVADLPEGEALRVDTS-PVIALFNVGGEFYAIDDRCSHGNASLSEGYLEdDATVECPLHAASFCLRTGKALCLPATD 83
                         90
                 ....*....|....*.
gi 21389617  150 SLHKFQVKIEKEKVYV 165
Cdd:PRK09965  84 PLRTYPVHVEGGDIFI 99
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
197-472 1.17e-08

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 57.48  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  197 VLIVGAGAAGLVCA-----ETLRQEGFSDRI---VLCTLDRH----LPY-DRPKLSKSLdtqpeqlalrpKEFFRAYGIE 263
Cdd:PRK15317 214 VLVVGGGPAGAAAAiyaarKGIRTGIVAERFggqVLDTMGIEnfisVPEtEGPKLAAAL-----------EEHVKEYDVD 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  264 VLTEAQVVTVDVRT--KKVVFKDGFKLEYSKLLLAPGSSPKTLSCKGkEVENVftirtpedaNRVVR--------LARGR 333
Cdd:PRK15317 283 IMNLQRASKLEPAAglIEVELANGAVLKAKTVILATGARWRNMNVPG-EDEYR---------NKGVAycphcdgpLFKGK 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  334 NVVVVGAGFLGMEVAAYLTEKAHSVSVVEleetpfrrFLGE-RVGRALM-KMFENNRVKFYMQTEVSELRGQEGKL---- 407
Cdd:PRK15317 353 RVAVIGGGNSGVEAAIDLAGIVKHVTVLE--------FAPElKADQVLQdKLRSLPNVTIITNAQTTEVTGDGDKVtglt 424
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21389617  408 -KEVVLKSSKVVRADVCVVGIGAVPATGFLRQSgIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFP 472
Cdd:PRK15317 425 yKDRTTGEEHHLELEGVFVQIGLVPNTEWLKGT-VELNRRGEIIVDARGATSVPGVFAAGDCTTVP 489
Reductase_C pfam14759
Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, ...
512-562 1.37e-08

Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, including putidaredoxin reductase, ferredoxin reductase, 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component, benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase subunit, rhodocoxin reductase, biphenyl dioxygenase system ferredoxin--NAD(+) reductase component, rubredoxin-NAD(+) reductase and toluene 1,2-dioxygenase system ferredoxin--NAD(+) reductase component. In putidaredoxin reductase this domain is involved in dimerization. In the FAD-containing NADH-ferredoxin reductase (BphA4) it is responsible for interaction with the Rieske-type [2Fe-2S] ferredoxin (BphA3).


Pssm-ID: 339364  Cd Length: 85  Bit Score: 51.77  E-value: 1.37e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 21389617   512 YLWTAMFGKSLRYAGYGEGFDDVIIQGDLEELKFVAFYTKGDEVIAVASMN 562
Cdd:pfam14759   1 WFWSDQYDLKLQIAGLPTGADEVVVRGDPEDGSFSVFYLRDGRLVAVDAVN 51
PRK06115 PRK06115
dihydrolipoamide dehydrogenase; Reviewed
288-473 1.49e-08

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 180409 [Multi-domain]  Cd Length: 466  Bit Score: 57.17  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  288 LEYSKLLLAPGSSPKTLSckGKEVENVFTIrtpeDANRVVRLAR-GRNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEET 366
Cdd:PRK06115 135 LEAKDIVIATGSEPTPLP--GVTIDNQRII----DSTGALSLPEvPKHLVVIGAGVIGLELGSVWRRLGAQVTVVEYLDR 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  367 PFRRFLGErVGRALMKMFENNRVKFYMQTEVSELR----GQEGKLKEVVLKSSKVVRADVCVVGIGAVPATGFLRQSGIG 442
Cdd:PRK06115 209 ICPGTDTE-TAKTLQKALTKQGMKFKLGSKVTGATagadGVSLTLEPAAGGAAETLQADYVLVAIGRRPYTQGLGLETVG 287
                        170       180       190
                 ....*....|....*....|....*....|...
gi 21389617  443 L--DSRGFIpVNKMMQTNVPGVFAAGDAVTFPL 473
Cdd:PRK06115 288 LetDKRGML-ANDHHRTSVPGVWVIGDVTSGPM 319
Bthiol_YpdA TIGR04018
putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, ...
332-483 1.50e-08

putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, including YpdA from Bacillus subtilis, are apparent oxidoreductases present only in species with an active bacillithiol system. They have been suggested actually to be thiol disulfide oxidoreductases (TDOR), although the evidence is incomplete. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 188533 [Multi-domain]  Cd Length: 316  Bit Score: 56.42  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   332 GRNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETpfrrfLGERVGRALMKMFEN----NRVKFYMQTEVSELRGQEgkl 407
Cdd:TIGR04018 152 GQKVVVVGGSNSAVDAALELYRKGAEVTMVHRGDE-----VSSSVKYWVRPDIENrikeGSIKAYFNSRVKEITEDS--- 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   408 keVVLKSSK----VVRADVCVVGIGAVPATGFLRQSGIGLDSRGFIPV-NK-MMQTNVPGVFAAGDAVtfplAWRNNRKV 481
Cdd:TIGR04018 224 --VTLETPDgevhTIPNDFVFALTGYRPDFEFLESLGVELDEDTGIPVyNPeTMETNVPGLYLAGVIA----AGMDTNKI 297

                  ..
gi 21389617   482 NI 483
Cdd:TIGR04018 298 FI 299
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
187-361 1.72e-08

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 224983 [Multi-domain]  Cd Length: 443  Bit Score: 56.70  E-value: 1.72e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 187 PSAGYSSSTNVLIVGAGAAGLVCAETLRQEGFSDRIVL-----------------CTLD-----RHLPYdRPKL-SKSLD 243
Cdd:COG2072   1 MTVGVATHTDVAIIGAGQSGLAAAYALKQAGVPDFVIFekrddvggtwrynrypgLRLDspkwlLGFPF-LPFRwDEAFA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617 244 TQPEQLALRpKEFFRAYG----IEVLTEAQVVTVDVRTKK--VVFKDG--FKLEYSKLLLAPG--SSPKTLSCKGKEVEN 313
Cdd:COG2072  80 PFAEIKDYI-KDYLEKYGlrfqIRFNTRVEVADWDEDTKRwtVTTSDGgtGELTADFVVVATGhlSEPYIPDFAGLDEFK 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21389617 314 VFTIRTPEDANRVvrLARGRNVVVVGAGFLGMEVAAYLTEKAHSVSVV 361
Cdd:COG2072 159 GRILHSADWPNPE--DLRGKRVLVIGAGASAVDIAPELAEVGASVTLS 204
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
41-136 2.42e-08

Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 226985 [Multi-domain]  Cd Length: 367  Bit Score: 55.96  E-value: 2.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  41 QGNGTARHFHTE-------ERLSTPHPYPspqdcveaaVCHVKDLENGQMREVELGWGKVLLVKD-NGEFHALGHKCPHY 112
Cdd:COG4638   2 EGRLPPPFYTDPelfqlelERIFYKHWYV---------VAHSSELPKPDPLTVRIGGEPLVVVRDkDGQVHALADVCPHR 72
                        90       100
                ....*....|....*....|....*
gi 21389617 113 GAPLVKG-VLSRGRVRCPWHGACFN 136
Cdd:COG4638  73 GARLSEGrVGGKGRLTCPYHGWTYD 97
gltD_gamma_fam TIGR01318
glutamate synthase small subunit family protein, proteobacterial; This model represents one of ...
197-501 2.54e-08

glutamate synthase small subunit family protein, proteobacterial; This model represents one of three built for the NADPH-dependent or NADH-dependent glutamate synthase (EC 1.4.1.13 and 1.4.1.14, respectively) small subunit and homologs. TIGR01317 describes the small subunit (or equivalent region from longer forms) in eukaryotes, Gram-positive bacteria, and some other lineages, both NADH and NADPH-dependent. TIGR01316 describes a protein of similar length, from Archaea and a number of bacterial lineages, that forms glutamate synthase homotetramers without a large subunit. This model describes both glutatate synthase small subunit and closely related paralogs of unknown function from a number of gamma and alpha subdivision Proteobacteria, including E. coli.


Pssm-ID: 273553 [Multi-domain]  Cd Length: 467  Bit Score: 56.35  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   197 VLIVGAGAAGLVCAETLRQEGfsdrIVLCTLDRH------LPYDRP--KLSKSLDTqpeqlalRPKEFFRAYGIEVltea 268
Cdd:TIGR01318 144 VAVIGAGPAGLACADILARAG----VQVVVFDRHpeigglLTFGIPsfKLDKAVLS-------RRREIFTAMGIEF---- 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   269 qvvTVDVRTKKVVFKDGFKLEYSKLLLAPGS-SPKTLSCKGKEVENV-----FTIRT-------PEDANRVVRLARGRNV 335
Cdd:TIGR01318 209 ---RLNCEVGRDISLDDLLEDYDAVFLGVGTyRSMRGGLPGEDAPGVlpalpFLIANtrqlmglPEEPEEPLIDVEGKRV 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   336 VVVGAGFLGME-VAAYLTEKAHSVSVVeleetpFRR----FLGER--VGRALMK--MFENNRVKFYMQ------------ 394
Cdd:TIGR01318 286 VVLGGGDTAMDcVRTAIRLGATKVTCA------YRRdeanMPGSRreVANAREEgvEFLFNVQPVSIEsdedgqvigvtv 359
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   395 --TEVSELRGQEGKLKEVVLKSSKVVRADVCVVGIGAVP-ATGFLRQSGIGLDSRGFIPVNKM----MQTNVPGVFAAGD 467
Cdd:TIGR01318 360 vrTKLGEPDANGRRRPVPVAGSEFVLPADVVIMAFGFSPhLMPWLAAHGITLDSWGRIITALSsgltYQTTNPKIFAGGD 439
                         330       340       350
                  ....*....|....*....|....*....|....
gi 21389617   468 AVtfplawRNNRKVniphwQMAHAQGRVAAQNML 501
Cdd:TIGR01318 440 AV------RGADLV-----VTAVAEGRDAAQGIL 462
PRK07251 PRK07251
pyridine nucleotide-disulfide oxidoreductase; Provisional
337-467 2.80e-08

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 56.30  E-value: 2.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  337 VVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFlgERVGRALMKMF-ENNRVKFYMQTEVSELRGQEGKLkeVVLKSS 415
Cdd:PRK07251 162 IIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPRE--EPSVAALAKQYmEEDGITFLLNAHTTEVKNDGDQV--LVVTED 237
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 21389617  416 KVVRADVCVVGIGAVPATG--FLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGD 467
Cdd:PRK07251 238 ETYRFDALLYATGRKPNTEplGLENTDIELTERGAIKVDDYCQTSVPGVFAVGD 291
PRK14727 PRK14727
putative mercuric reductase; Provisional
184-511 4.21e-08

putative mercuric reductase; Provisional


Pssm-ID: 237806 [Multi-domain]  Cd Length: 479  Bit Score: 55.72  E-value: 4.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  184 CISPSAGYSSSTNVLIVGAGAAGLVCAETLRQEGFSDRIV--------------------------LCTLDRHLPYD--- 234
Cdd:PRK14727   6 SSNCMTRSKLQLHVAIIGSGSAAFAAAIKAAEHGARVTIIegadviggccvnvgcvpskiliraaqLAHQQRSNPFDgve 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  235 --RPKLSKSLDTQPEQLalRPKEFFRAYGIEVLTEAQVVTV--------DVRTKKVVFKDGFK--LEYSKLLLAPGSSPK 302
Cdd:PRK14727  86 avAPSIDRGLLLHQQQA--RVEELRHAKYQSILDGNPALTLlkgyarfkDGNTLVVRLHDGGErvLAADRCLIATGSTPT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  303 TLSCKG-------KEVENVFTIRTPedanrvvrlargRNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRR--FLG 373
Cdd:PRK14727 164 IPPIPGlmdtpywTSTEALFSDELP------------ASLTVIGSSVVAAEIAQAYARLGSRVTILARSTLLFREdpLLG 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  374 ERvgraLMKMFENNRVKFYMQTEVSELRGQEGKLkeVVLKSSKVVRADVCVVGIGAVPATG--FLRQSGIGLDSRGFIPV 451
Cdd:PRK14727 232 ET----LTACFEKEGIEVLNNTQASLVEHDDNGF--VLTTGHGELRAEKLLISTGRHANTHdlNLEAVGVTTDTSGAIVV 305
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21389617  452 NKMMQTNVPGVFAAGDAVTFPlawrnnrkvniPHWQMAHAQGRVAAQNMLAQEA--EMSTVP 511
Cdd:PRK14727 306 NPAMETSAPDIYAAGDCSDLP-----------QFVYVAAAAGSRAGINMTGGNAtlDLSAMP 356
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
197-500 6.48e-08

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 55.27  E-value: 6.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  197 VLIVGAGAAGLVCAETLRQEGFSdrivlCTLdrhlpYD-RPKLSKsldtqpeqlALRpkeffraYGI-------EVL-TE 267
Cdd:PRK12771 140 VAVIGGGPAGLSAAYHLRRMGHA-----VTI-----FEaGPKLGG---------MMR-------YGIpayrlprEVLdAE 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  268 AQVVT---VDVRTKKVVFKD--GFKLE--YSKLLLAPG-SSPKTLSCKGKEVENVFT----IRTPEDANRVvrlARGRNV 335
Cdd:PRK12771 194 IQRILdlgVEVRLGVRVGEDitLEQLEgeFDAVFVAIGaQLGKRLPIPGEDAAGVLDavdfLRAVGEGEPP---FLGKRV 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  336 VVVGAGFLGMEVAAylTEK---AHSVSVV-------------ELEE------------TPfRRFLGERVGRALMKMfenn 387
Cdd:PRK12771 271 VVIGGGNTAMDAAR--TARrlgAEEVTIVyrrtredmpahdeEIEEalregveinwlrTP-VEIEGDENGATGLRV---- 343
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  388 rVKFYMQTEVSELRGQEGKLKEVVLKsskvvrADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKM-MQTNVPGVFAAG 466
Cdd:PRK12771 344 -ITVEKMELDEDGRPSPVTGEEETLE------ADLVVLAIGQDIDSAGLESVPGVEVGRGVVQVDPNfMMTGRPGVFAGG 416
                        330       340       350
                 ....*....|....*....|....*....|....
gi 21389617  467 DAVTFPlawrnnRKVNiphwqMAHAQGRVAAQNM 500
Cdd:PRK12771 417 DMVPGP------RTVT-----TAIGHGKKAARNI 439
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
258-466 6.90e-08

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 316275 [Multi-domain]  Cd Length: 290  Bit Score: 54.14  E-value: 6.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   258 RAYGIEVLTEAQVVTVdvrtKKVvfKDGFKLEYSK-------LLLAPG--SSPKTLSCKGKE--VENVFTIRTPEDANrv 326
Cdd:pfam13738  77 DHFELPINTFEEVTSV----KKE--DDGFVVTTSKgtytaryVIIATGefDFPNKPGIPGEEklPKHYHYVKDWHPYA-- 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   327 vrlarGRNVVVVGAGFLGMEVAAYLTEKAHSVSVVEleETPFRRFLGERVGRA--------LMKMFENNRVKFYMQTEVS 398
Cdd:pfam13738 149 -----GQKVVVIGGYNSAVDAALELVRKGARVTVLT--RGSEWEADDSDPSYSlspdtlnrLKELVKNGSIKLYFNAEVK 221
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   399 ELRGQEGKLKeVVLKSSKVVR-ADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKM-MQTNVPGVFAAG 466
Cdd:pfam13738 222 EITEVDVSYK-VHFKDGRKVTsNDDPILATGYHPDLSFLKKSGFELDEDGRPVLTEEtESTNVPGLFLAG 290
PRK05976 PRK05976
dihydrolipoamide dehydrogenase; Validated
293-506 1.25e-07

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235660 [Multi-domain]  Cd Length: 472  Bit Score: 54.14  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  293 LLLAPGSSPKTLSckGKEVENVFTIrTPEDANRVVRLARgrNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEEtpfrRFL 372
Cdd:PRK05976 146 LLIATGSRPVELP--GLPFDGEYVI-SSDEALSLETLPK--SLVIVGGGVIGLEWASMLADFGVEVTVVEAAD----RIL 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  373 ---GERVGRALMKMFENNRVKFYMQTEVSELR-GQEGKLKEVVLKSSKVVR--ADVCVVGIGAVPATgflrqSGIGLDS- 445
Cdd:PRK05976 217 pteDAELSKEVARLLKKLGVRVVTGAKVLGLTlKKDGGVLIVAEHNGEEKTleADKVLVSVGRRPNT-----EGIGLENt 291
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21389617  446 -----RGFIPVNKMMQTNVPGVFAAGDAVTFPlawrnnrkvniphwQMAH---AQGRVAAQNMLAQEAE 506
Cdd:PRK05976 292 didveGGFIQIDDFCQTKERHIYAIGDVIGEP--------------QLAHvamAEGEMAAEHIAGKKPR 346
Rieske_RO_Alpha_VanA_DdmC cd03532
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ...
100-136 2.49e-07

Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and dicamba O-demethylase oxygenase (DdmC) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Vanillate-O-demethylase is a heterodimeric enzyme consisting of a terminal oxygenase (VanA) and reductase (VanB) components. This enzyme reductively catalyzes the conversion of vanillate into protocatechuate and formaldehyde. Protocatechuate and vanillate are important intermediate metabolites in the degradation pathway of lignin-derived compounds such as ferulic acid and vanillin by soil microbes. DDmC is the oxygenase component of a three-component dicamba O-demethylase found in Pseudomonas maltophila, that catalyzes the conversion of a widely used herbicide called herbicide dicamba (2-methoxy-3,6-dichlorobenzoic acid) to DCSA (3,6-dichlorosalicylic acid).


Pssm-ID: 239608 [Multi-domain]  Cd Length: 116  Bit Score: 49.29  E-value: 2.49e-07
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 21389617 100 GEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFN 136
Cdd:cd03532  37 GRVAALEDRCPHRSAPLSKGSVEGGGLVCGYHGLEFD 73
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
228-518 5.25e-07

thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.


Pssm-ID: 273624 [Multi-domain]  Cd Length: 484  Bit Score: 52.16  E-value: 5.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   228 DRHLPYDRPKLSKSLDTQPEQL------ALRPKE--FFRAYGievlteaqvVTVDVRTKKVVFKDGFKLEYS--KLLLAP 297
Cdd:TIGR01438  81 EETVKHDWKRLVEAVQNHIGSLnwgyrvALREKKvkYENAYA---------EFVDKHRIKATNKKGKEKIYSaeRFLIAT 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   298 GSSPKTLSCKG-KEV----ENVFTIrtPEDANRVVrlargrnvvVVGAGFLGMEVAAYLTEKAHSVSVVeLEETPFRRFl 372
Cdd:TIGR01438 152 GERPRYPGIPGaKELcitsDDLFSL--PYCPGKTL---------VVGASYVALECAGFLAGIGLDVTVM-VRSILLRGF- 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   373 GERVGRALMKMFENNRVKFYMQTEVSELRGQEGKLKEVVLKSSKVVRA--DVCVVGIGAVPATgflrqSGIGLDSRGF-- 448
Cdd:TIGR01438 219 DQDCANKVGEHMEEHGVKFKRQFVPIKVEQIEAKVLVEFTDSTNGIEEeyDTVLLAIGRDACT-----RKLNLENVGVki 293
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21389617   449 ------IPVNKMMQTNVPGVFAAGDAVtfplawrNNRKVNIPhwqMAHAQGRVAAQNMLAQEAEMSTVPYLWTAMF 518
Cdd:TIGR01438 294 nkktgkIPADEEEQTNVPYIYAVGDIL-------EDKPELTP---VAIQAGRLLAQRLFKGSTVICDYENVPTTVF 359
PTZ00153 PTZ00153
lipoamide dehydrogenase; Provisional
283-468 6.79e-07

lipoamide dehydrogenase; Provisional


Pssm-ID: 173442 [Multi-domain]  Cd Length: 659  Bit Score: 52.22  E-value: 6.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  283 KDGFKLEYSKLLLAPGSSPKTLSckGKEVENvFTIRTPEDANRVVRLARgrNVVVVGAGFLGMEVAAYLTekAHSVSVVE 362
Cdd:PTZ00153 268 KSGKEFKVKNIIIATGSTPNIPD--NIEVDQ-KSVFTSDTAVKLEGLQN--YMGIVGMGIIGLEFMDIYT--ALGSEVVS 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  363 LEETP-FRRFLGERVGRALMKMFENNR-VKFYMQTEVSELRG----------------QEGKLKEVVLKSSKVVRADVCV 424
Cdd:PTZ00153 341 FEYSPqLLPLLDADVAKYFERVFLKSKpVRVHLNTLIEYVRAgkgnqpviighserqtGESDGPKKNMNDIKETYVDSCL 420
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 21389617  425 VGIGAVPATgflrqSGIGLDS------RGFIPVNKMMQTN------VPGVFAAGDA 468
Cdd:PTZ00153 421 VATGRKPNT-----NNLGLDKlkiqmkRGFVSVDEHLRVLredqevYDNIFCIGDA 471
Rieske_2 pfam13806
Rieske-like [2Fe-2S] domain;
71-166 1.23e-06

Rieske-like [2Fe-2S] domain;


Pssm-ID: 316336 [Multi-domain]  Cd Length: 104  Bit Score: 47.16  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617    71 AVCHVKDLENGQMREVELGWGKVLLVKD-NGEFHALGHKCPHYGAplvkGVLSRGR---------VRCPWHGACFNISTG 140
Cdd:pfam13806   4 PVCPLDDLPPGTGVCALVGGEQVALFRLpDGQVYAIDNIDPFSGA----NVLSRGIvgdlggepvVASPLYKQHFDLKTG 79
                          90       100
                  ....*....|....*....|....*.
gi 21389617   141 DLEDFPGLdSLHKFQVKIEKEKVYVR 166
Cdd:pfam13806  80 ECLEDPEV-SLPVYPVRVEDGNVEVR 104
PRK12778 PRK12778
putative bifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta; ...
187-470 1.69e-06

putative bifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta; Provisional


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 50.90  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  187 PSAGYSSSTNVLIVGAGAAGLVCAETLRQEGFSDRI--VLCTLDRHLPYDRPKLSksldtQPEQLALRPKEFFRAYGIEV 264
Cdd:PRK12778 424 PEVAEKNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVfeALHEIGGVLKYGIPEFR-----LPKKIVDVEIENLKKLGVKF 498
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  265 LTE---AQVVTVDVrtkkvVFKDGFKleysKLLLAPGSS-PKTLSCKGKEVENVFTirTPEDANRV-----------VRL 329
Cdd:PRK12778 499 ETDvivGKTITIEE-----LEEEGFK----GIFIASGAGlPNFMNIPGENSNGVMS--SNEYLTRVnlmdaaspdsdTPI 567
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  330 ARGRNVVVVGAGFLGMEVAAylTEK---AHSVSVV---ELEETPFRRflgERVGRAlmkmfENNRVKFYMQTEVSELRGQ 403
Cdd:PRK12778 568 KFGKKVAVVGGGNTAMDSAR--TAKrlgAERVTIVyrrSEEEMPARL---EEVKHA-----KEEGIEFLTLHNPIEYLAD 637
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  404 E-GKLKEVVLK--------------------SSKVVRADVCVVGIGAVPATGFLRQ-SGIGLDSRGFIPVNKMMQTNVPG 461
Cdd:PRK12778 638 EkGWVKQVVLQkmelgepdasgrrrpvaipgSTFTVDVDLVIVSVGVSPNPLVPSSiPGLELNRKGTIVVDEEMQSSIPG 717

                 ....*....
gi 21389617  462 VFAAGDAVT 470
Cdd:PRK12778 718 IYAGGDIVR 726
PRK13984 PRK13984
putative oxidoreductase; Provisional
197-472 1.77e-06

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 50.54  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  197 VLIVGAGAAGLVCAETLRQEGFsDRIVLCTLDRH---LPYDRPKLSksldtQPEQLALRPKEFFRAYGIEVLTEAQVVtv 273
Cdd:PRK13984 286 VAIVGSGPAGLSAAYFLATMGY-EVTVYESLSKPggvMRYGIPSYR-----LPDEALDKDIAFIEALGVKIHLNTRVG-- 357
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  274 dvrtKKVVFKDgFKLEYSKLLLAPG-SSPKTLSCKGKEVENVFtirtpeDANRVVRLARG------------RNVVVVGA 340
Cdd:PRK13984 358 ----KDIPLEE-LREKHDAVFLSTGfTLGRSTRIPGTDHPDVI------QALPLLREIRDylrgegpkpkipRSLVVIGG 426
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  341 GFLGMEVAAYLTE------KAHSVSVVELEET---------PFRRFLGERV----GRALMK-MFENNRVKFYMQTEVSEL 400
Cdd:PRK13984 427 GNVAMDIARSMARlqkmeyGEVNVKVTSLERTfeempadmeEIEEGLEEGVviypGWGPMEvVIENDKVKGVKFKKCVEV 506
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21389617  401 RGQEGKLKEVVLKSSK-VVRADVCVVGIGAVPATGFLRQSgigLDS-----RGFIPVNKMMQTNVPGVFAAGDAVTFP 472
Cdd:PRK13984 507 FDEEGRFNPKFDESDQiIVEADMVVEAIGQAPDYSYLPEE---LKSklefvRGRILTNEYGQTSIPWLFAGGDIVHGP 581
PRK12831 PRK12831
putative oxidoreductase; Provisional
197-470 2.13e-06

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 50.40  E-value: 2.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  197 VLIVGAGAAGLVCAETLRQEGFSDRI--VLCTLDRHLPYDRP--KLSKSLDTQPEQlalrpkEFFRAYGIEVLTEAQV-- 270
Cdd:PRK12831 143 VAVIGSGPAGLTCAGDLAKMGYDVTIfeALHEPGGVLVYGIPefRLPKETVVKKEI------ENIKKLGVKIETNVVVgk 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  271 -VTVDVRTKKVVFKDGFkleyskllLAPGSS-PKTLSCKGKEVENVFTirtpedAN----RV-----------VRLARGR 333
Cdd:PRK12831 217 tVTIDELLEEEGFDAVF--------IGSGAGlPKFMGIPGENLNGVFS------ANefltRVnlmkaykpeydTPIKVGK 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  334 NVVVVGAGFLGMEVAAY---LTEKAHSVSVVELEETPFRRflgERVGRAL-----MKMF---------ENNRVKfYMQTE 396
Cdd:PRK12831 283 KVAVVGGGNVAMDAARTalrLGAEVHIVYRRSEEELPARV---EEVHHAKeegviFDLLtnpveilgdENGWVK-GMKCI 358
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21389617  397 VSEL--RGQEGKLKEVVLKSSK-VVRADVCVVGIGAVPATGFLRQS-GIGLDSRGFIPVNK-MMQTNVPGVFAAGDAVT 470
Cdd:PRK12831 359 KMELgePDASGRRRPVEIEGSEfVLEVDTVIMSLGTSPNPLISSTTkGLKINKRGCIVADEeTGLTSKEGVFAGGDAVT 437
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
192-501 6.32e-06

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 48.97  E-value: 6.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  192 SSSTNVLIVGAGAAGLVCAETLRQEGFSDRIvlctLDRH------LPYDRP--KLSKSLdtqpeqLALRpKEFFRAYGIE 263
Cdd:PRK12769 325 KSDKRVAIIGAGPAGLACADVLARNGVAVTV----YDRHpeigglLTFGIPafKLDKSL------LARR-REIFSAMGIE 393
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  264 ---------------VLTEAQVVTVDVRTKKVVfKDGFKLEYsklllAPG--SSPKTLSCKGKEVENVftirtPEDANRV 326
Cdd:PRK12769 394 felncevgkdislesLLEDYDAVFVGVGTYRSM-KAGLPNED-----APGvyDALPFLIANTKQVMGL-----EELPEEP 462
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  327 VRLARGRNVVVVGAGFLGME-VAAYLTEKAHSV-------------SVVEL----EETPFRRFLGERVGRALMKMFENNR 388
Cdd:PRK12769 463 FINTAGLNVVVLGGGDTAMDcVRTALRHGASNVtcayrrdeanmpgSKKEVknarEEGANFEFNVQPVALELNEQGHVCG 542
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  389 VKFyMQTEVSELRGQeGKLKEVVLKSSKVVR-ADVCVVGIGAVPAT-GFLRQSGIGLDSRGFI--PVNKMM--QTNVPGV 462
Cdd:PRK12769 543 IRF-LRTRLGEPDAQ-GRRRPVPIPGSEFVMpADAVIMAFGFNPHGmPWLESHGVTVDKWGRIiaDVESQYryQTSNPKI 620
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 21389617  463 FAAGDAVtfplawRNNRKVniphwQMAHAQGRVAAQNML 501
Cdd:PRK12769 621 FAGGDAV------RGADLV-----VTAMAEGRHAAQGII 648
Rieske_NirD cd03529
Assimilatory nitrite reductase (NirD) family, Rieske domain; Assimilatory nitrate and nitrite ...
71-165 1.19e-05

Assimilatory nitrite reductase (NirD) family, Rieske domain; Assimilatory nitrate and nitrite reductases convert nitrate through nitrite to ammonium. Members include bacterial and fungal proteins. The bacterial NirD contains a single Rieske domain while fungal proteins have a C-terminal Rieske domain in addition to several other domains. The fungal NirD is involved in nutrient acquisition, functioning at the soil/fungus interface to control nutrient exchange between the fungus and the host plant. The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. The Rieske [2Fe-2S] cluster is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In this family, only a few members contain these residues. Other members may have lost the ability to bind the Rieske [2Fe-2S] cluster.


Pssm-ID: 239605 [Multi-domain]  Cd Length: 103  Bit Score: 44.04  E-value: 1.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  71 AVCHVKDLENGqmrevelgWGKVLLVKD---------NGEFHALGHKCPHYGAplvkGVLSRG---------RVRCPWHG 132
Cdd:cd03529   3 TVCALDDLPPG--------SGVAALVGDtqiaifrlpGREVYAVQNMDPHSRA----NVLSRGivgdiggepVVASPLYK 70
                        90       100       110
                ....*....|....*....|....*....|....
gi 21389617 133 ACFNISTGD-LEDfPGLdSLHKFQVKIEKEKVYV 165
Cdd:cd03529  71 QHFSLKTGRcLED-EDV-SVATFPVRVEDGEVYV 102
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
71-166 1.22e-05

nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of nitrite reductase [NAD(P)H] (the assimilatory nitrite reductase), which associates with NirB, the large subunit (TIGR02374). In a few bacteria such as Klebsiella pneumoniae and in Fungi, the two regions are fused. [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 131431 [Multi-domain]  Cd Length: 105  Bit Score: 44.23  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617    71 AVCHVKDLENGQMREVELGWGKVLLVKDNG-EFHALGHKCPHYGAplvkGVLSRG---------RVRCPWHGACFNISTG 140
Cdd:TIGR02378   4 DICAIDDIPEETGVCVLLGDTQIAIFRVPGdQVFAIQNMCPHKRA----FVLSRGivgdaqgelWVACPLHKRNFRLEDG 79
                          90       100
                  ....*....|....*....|....*..
gi 21389617   141 D-LEDFPGldSLHKFQVKIEKEKVYVR 166
Cdd:TIGR02378  80 RcLEDDSG--SVRTYEVRVEDGRVYVA 104
mycothione_red TIGR03452
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ...
318-509 1.23e-05

mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and related species, can form a disulfide-linked dimer called mycothione. This enzyme can reduce mycothione to regenerate two mycothiol molecules. The enzyme shows some sequence similarity to glutathione-disulfide reductase, trypanothione-disulfide reductase, and dihydrolipoamide dehydrogenase. The characterized protein from M. tuberculosis, a homodimer, has FAD as a cofactor, one per monomer, and uses NADPH as a substrate.


Pssm-ID: 132493 [Multi-domain]  Cd Length: 452  Bit Score: 47.83  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   318 RTPEDANRVVRLARgrNVVVVGAGFLGMEVAAYLTEKAHSVSVV--------ELEETPFRRFLgervgRALMKMFENNRv 389
Cdd:TIGR03452 157 HTNEDIMRLPELPE--SLVIVGGGYIAAEFAHVFSALGTRVTIVnrstkllrHLDEDISDRFT-----EIAKKKWDIRL- 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   390 kfymQTEVSELRgQEGKLKEVVLKSSKVVRADVCVVGIGAVPATGFL--RQSGIGLDSRGFIPVNKMMQTNVPGVFAAGD 467
Cdd:TIGR03452 229 ----GRNVTAVE-QDGDGVTLTLDDGSTVTADVLLVATGRVPNGDLLdaEAAGVEVDEDGRIKVDEYGRTSARGVWALGD 303
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 21389617   468 aVTFPLAWRNnrkvniphwqMAHAQGRVAAQNMLAQEAEMST 509
Cdd:TIGR03452 304 -VSSPYQLKH----------VANAEARVVKHNLLHPNDLRKM 334
Rieske_RO_Alpha_OMO_CARDO cd03548
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ...
76-144 1.34e-05

Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole 1,9a-dioxygenase (CARDO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. OMO catalyzes the NADH-dependent oxidation of the N-heterocyclic aromatic compound 2-oxoquinoline to 8-hydroxy-2-oxoquinoline, the second step in the bacterial degradation of quinoline. OMO consists of a reductase component (OMR) and an oxygenase component (OMO) that together function to shuttle electrons from the reduced pyridine nucleotide to the active site of OMO, where O2 activation and 2-oxoquinoline hydroxylation occurs. CARDO, which contains oxygenase (CARDO-O), ferredoxin (CARDO-F) and ferredoxin reductase (CARDO-R) components, catalyzes the dihydroxylation at the C1 and C9a positions of carbazole. The oxygenase component of OMO and CARDO contain only alpha subunits arranged in a trimeric structure.


Pssm-ID: 239617 [Multi-domain]  Cd Length: 136  Bit Score: 44.72  E-value: 1.34e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21389617  76 KDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGV--LSRGRVRCPWHGACFNISTGDLED 144
Cdd:cd03548  22 HELEEGEPKGIQLCGEPILLRRVDGKVYALKDRCLHRGVPLSKKPecFTKGTITCWYHGWTYRLDDGKLVT 92
MocE_fam_FeS TIGR02377
Rieske [2Fe-2S] domain protein, MocE subfamily; This model describes a subfamily of the ...
66-165 1.73e-04

Rieske [2Fe-2S] domain protein, MocE subfamily; This model describes a subfamily of the Rieske-like [2Fe-2S] family of ferredoxins that includes MocE, part of the rhizopine (3-O-methyl-scyllo-inosamine) catabolic cluster in Rhizobium. Members of this family are related to, yet distinct from, the small subunit of nitrite reductase [NAD(P)H].


Pssm-ID: 131430 [Multi-domain]  Cd Length: 101  Bit Score: 41.01  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617    66 DCVEAavCHVKDL-ENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLED 144
Cdd:TIGR02377   1 NWVKA--CDADDIgREDVARFDHGGRTFAIYRTPDDQYYATDGLCTHEYAHLADGLVMDTTVECPKHAGCFDYRTGEALN 78
                          90       100
                  ....*....|....*....|.
gi 21389617   145 FPGLDSLHKFQVKIEKEKVYV 165
Cdd:TIGR02377  79 PPVCVNLKTYPVKVVDGAVYV 99
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
196-284 1.94e-04

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 333813 [Multi-domain]  Cd Length: 79  Bit Score: 39.85  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   196 NVLIVGAGAAGLVCAETLRQEGfsdrivlctLDRHLPYDRPKLSKSLDtqpEQLALRPKEFFRAYGIEVLTEAQV--VTV 273
Cdd:pfam00070   1 KVVVVGGGYIGLELAGALARLG---------SKVTVVERRDRLLRGLD---EEIAKILQERLEKNGIEVLLNTTVeaIEG 68
                          90
                  ....*....|.
gi 21389617   274 DVRTKKVVFKD 284
Cdd:pfam00070  69 NGDGVVVVLTD 79
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
337-467 2.12e-04

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 43.85  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  337 VVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRfLGERVGRALMKMFENNRVKFYMQTEVSELRGQEGKLKEVVLKSSK 416
Cdd:PRK08010 163 ILGGGYIGVEFASMFANFGSKVTILEAASLFLPR-EDRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHAQL 241
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 21389617  417 VVraDVCVVGIGAVPATGFL--RQSGIGLDSRGFIPVNKMMQTNVPGVFAAGD 467
Cdd:PRK08010 242 AV--DALLIASGRQPATASLhpENAGIAVNERGAIVVDKYLHTTADNIWAMGD 292
PRK10262 PRK10262
thioredoxin reductase; Provisional
331-469 4.33e-04

thioredoxin reductase; Provisional


Pssm-ID: 182343 [Multi-domain]  Cd Length: 321  Bit Score: 42.36  E-value: 4.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  331 RGRNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETpfrrFLGERVG-RALMKMFENNRVKFYMQTEVSELRGQEGKLKE 409
Cdd:PRK10262 145 RNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDG----FRAEKILiKRLMDKVENGNIILHTNRTLEEVTGDQMGVTG 220
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21389617  410 VVLKSSK----VVRADVC--VVGIGAVPATGFLrQSGIGLDSrGFIPVNKMM-----QTNVPGVFAAGDAV 469
Cdd:PRK10262 221 VRLRDTQnsdnIESLDVAglFVAIGHSPNTAIF-EGQLELEN-GYIKVQSGIhgnatQTSIPGVFAAGDVM 289
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
199-219 8.05e-04

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 316012 [Multi-domain]  Cd Length: 66  Bit Score: 37.88  E-value: 8.05e-04
                          10        20
                  ....*....|....*....|.
gi 21389617   199 IVGAGAAGLVCAETLRQEGFS 219
Cdd:pfam13450   1 IVGAGLAGLVAAYLLAKRGKR 21
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
336-518 8.80e-04

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 42.12  E-value: 8.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  336 VVVGAGFLGMEVAAYLTEKAHSVSVVeLEETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSELRGQEGKLKeVVLKSS 415
Cdd:PTZ00052 186 LIVGASYIGLETAGFLNELGFDVTVA-VRSIPLRGF-DRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDDKIK-VLFSDG 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  416 KVVRADVCVVGIGAVPATGFLRQSGIGL---DSRGFIPVNKMmqTNVPGVFAAGDAVtfplawrnnrkVNIPHWQ-MAHA 491
Cdd:PTZ00052 263 TTELFDTVLYATGRKPDIKGLNLNAIGVhvnKSNKIIAPNDC--TNIPNIFAVGDVV-----------EGRPELTpVAIK 329
                        170       180
                 ....*....|....*....|....*..
gi 21389617  492 QGRVAAQNMLAQEAEMSTVPYLWTAMF 518
Cdd:PTZ00052 330 AGILLARRLFKQSNEFIDYTFIPTTIF 356
Rieske_RO_Alpha_PaO cd03480
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ...
97-146 1.15e-03

Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of a small subfamily of enzymes found in plants as well as oxygenic cyanobacterial photosynthesizers including LLS1 (lethal leaf spot 1, also known as PaO) and ACD1 (accelerated cell death 1). ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. PaO expression increases upon physical wounding of plant leaves and is thought to catalyze a key step in chlorophyll degradation. The Arabidopsis-accelerated cell death gene ACD1 is involved in oxygenation of PaO.


Pssm-ID: 239562 [Multi-domain]  Cd Length: 138  Bit Score: 39.23  E-value: 1.15e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 21389617  97 KDNGEFHALGHKCPHYGAPLVKGVLSR-GRVRCPWHGACFNiSTGDLEDFP 146
Cdd:cd03480  48 RNSQQWRAFDDQCPHRLAPLSEGRIDEeGCLECPYHGWSFD-GSGSCQRIP 97
Rieske_RO_Alpha_Cao cd04337
Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the ...
76-136 1.35e-03

Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the plastid-envelope inner and thylakoid membranes, that catalyzes the conversion of chlorophyllide a to chlorophyllide b. CAO is found not only in plants but also in chlorophytes and prochlorophytes. This domain represents the N-terminal rieske domain of the oxygenase alpha subunit. ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Cao is closely related to several other plant RO's including Tic 55, a 55 kDa protein associated with protein transport through the inner chloroplast membrane; Ptc 52, a novel 52 kDa protein isolated from chloroplasts; and LLS1/Pao (Lethal-leaf spot 1/pheophorbide a oxygenase).


Pssm-ID: 239829 [Multi-domain]  Cd Length: 129  Bit Score: 39.01  E-value: 1.35e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21389617  76 KDLENGQMREVEL---GWgkVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFN 136
Cdd:cd04337  25 KDLKMDTMVPFELfgqPW--VLFRDEDGTPGCIRDECAHRACPLSLGKVIEGRIQCPYHGWEYD 86
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
197-303 1.36e-03

mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]


Pssm-ID: 273944 [Multi-domain]  Cd Length: 463  Bit Score: 41.25  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   197 VLIVGAGAAGLVCAETLRQEGfSDRIVLCTLDRHLPYDRPKLSKSLdtqpeqlalrpKEFFRAYGIEVLTEAQV--VTVD 274
Cdd:TIGR02053 169 LAVIGGGAIGVELAQAFARLG-SEVTILQRSDRLLPREEPEISAAV-----------EEALAEEGIEVVTSAQVkaVSVR 236
                          90       100       110
                  ....*....|....*....|....*....|..
gi 21389617   275 VRTKKVVFK---DGFKLEYSKLLLAPGSSPKT 303
Cdd:TIGR02053 237 GGGKIITVEkpgGQGEVEADELLVATGRRPNT 268
Nterm_to_SelD TIGR03169
pyridine nucleotide-disulfide oxidoreductase family protein; Members of this protein family ...
189-301 1.84e-03

pyridine nucleotide-disulfide oxidoreductase family protein; Members of this protein family include N-terminal sequence regions of (probable) bifunctional proteins whose C-terminal sequences are SelD, or selenide,water dikinase, the selenium donor protein necessary for selenium incorporation into protein (as selenocysteine), tRNA (as 2-selenouridine), or both. However, some members of this family occur in species that do not show selenium incorporation, and the function of this protein family is unknown.


Pssm-ID: 274465 [Multi-domain]  Cd Length: 364  Bit Score: 40.65  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   189 AGYSSSTNVLIVGAGAAG----LVCAETLRQEGFSDRIVLCTLDRHL-PYDRPKLSKSLdtqpeQLALrpkeffRAYGIE 263
Cdd:TIGR03169 139 AKPQQPPRIAVIGGGAAGvelaLAMAHRLRQLGRNAEVTLIDRGNVLlPGHNARVRRRL-----ERAL------QERGVT 207
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 21389617   264 VLTEAQVvtVDVRTKKVVFKDGFKLEYSKLLLAPGSSP 301
Cdd:TIGR03169 208 LHLGATV--AEVTADAVRLEDGQTLPADFTFWATGARP 243
Rieske_RO_Alpha_PhDO_like cd03479
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ...
99-158 1.86e-03

Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of PhDO and similar proteins including 3-chlorobenzoate 3,4-dioxygenase (CBDO), phenoxybenzoate dioxygenase (POB-dioxygenase) and 3-nitrobenzoate oxygenase (MnbA). ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. PhDO and CBDO are two-component RO systems, containing oxygenase and reductase components. PhDO catalyzes the dihydroxylation of phthalate to form the 4,5-dihydro-cis-dihydrodiol of phthalate (DHD). CBDO, together with CbaC dehydrogenase, converts the environmental pollutant 3CBA to protocatechuate (PCA) and 5-Cl-PCA, which are then metabolized by the chromosomal PCA meta (extradiol) ring fission pathway. POB-dioxygenase catalyzes the initial catabolic step in the angular dioxygenation of phenoxybenzoate, converting mono- and dichlorinated phenoxybenzoates to protocatechuate and chlorophenols. These phenoxybenzoates are metabolic products formed during the degradation of pyrethroid insecticides.


Pssm-ID: 239561 [Multi-domain]  Cd Length: 144  Bit Score: 38.77  E-value: 1.86e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21389617  99 NGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNiSTGDLEDFPGL--DSLHKFQVKI 158
Cdd:cd03479  54 SGRVGLLDEHCPHRGASLVFGRVEECGLRCCYHGWKFD-VDGQCLEMPSEppDSQLKQKVRQ 114
mycofact_OYE_2 TIGR03997
mycofactocin system FadH/OYE family oxidoreductase 2; The yeast protein called old yellow ...
302-432 2.30e-03

mycofactocin system FadH/OYE family oxidoreductase 2; The yeast protein called old yellow enzyme and FadH from Escherichia coli (2,4-dienoyl CoA reductase) are enzymes with 4Fe-4S, FMN, and FAD prosthetic groups, and interact with NADPH as well as substrate. Members of this related protein family occur in the vicinity of the putative mycofactocin biosynthesis operon in a number of Actinobacteria such as Frankia sp. and Rhodococcus sp., in Pelotomaculum thermopropionicum SI (Firmicutes), and in Geobacter uraniireducens Rf4 (Deltaproteobacteria). The function of this oxidoreductase is unknown.


Pssm-ID: 274912 [Multi-domain]  Cd Length: 644  Bit Score: 40.83  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617   302 KTLSCkgkeVENVFTIRTPEDANrVVRLARGRNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPfrrflGERVgRALM 381
Cdd:TIGR03997 353 RWLGC----VVNPRAGREFGTVT-LPPPRRPKRVLVVGGGPAGLEAAATAARRGHRVTLFEREDRL-----GGQV-RLAA 421
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 21389617   382 KMFENNRVKFYMQTEVSELRGQEGKLKEVVLKSSKVVRA---DVCVVGIGAVPA 432
Cdd:TIGR03997 422 RLPGRGEFADLIRNLASELRRAGVEVRLGVEADAELVLAekpDAVVVATGSRPV 475
PRK07818 PRK07818
dihydrolipoamide dehydrogenase; Reviewed
197-303 2.74e-03

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 236106 [Multi-domain]  Cd Length: 466  Bit Score: 40.39  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389617  197 VLIVGAGAAGLVCAETLRQEGFSDRIVLcTLDRHLPYDRPKLSKSLDTQpeqlalrpkefFRAYGIEVLTEAQVVTVDVR 276
Cdd:PRK07818 175 IVIAGAGAIGMEFAYVLKNYGVDVTIVE-FLDRALPNEDAEVSKEIAKQ-----------YKKLGVKILTGTKVESIDDN 242
                         90       100       110
                 ....*....|....*....|....*....|...
gi 21389617  277 TKKVVF----KDGFK--LEYSKLLLAPGSSPKT 303
Cdd:PRK07818 243 GSKVTVtvskKDGKAqeLEADKVLQAIGFAPRV 275
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
327-379 4.07e-03

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 39.18  E-value: 4.07e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21389617 327 VRLAR---GRNVVVVGAGFLGMeVAAYLTEKAHSVSVVELEETPFRRFLGERVGRA 379
Cdd:cd08255  90 VRDAEprlGERVAVVGLG