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Conserved domains on  [gi|2443331|dbj|BAA22375|]
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Nfrl [Xenopus laevis]

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 1.17e-73

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: 237.60  E-value: 1.17e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    195 TNILIIGAGPAGLVCAETLRQEGFsdRIVMCTSEKNLPYDRSKLSKSMDSQAEQ--IFLRSKEFFHTY---------DIE 263
Cdd:pfam07992   1 YDVVIIGGGPAGLAAALTLARAGG--KVTLIEDEGTCPYGGCVLSKALLGAAEApeIASLWAELYERKeevvkklnnGIE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    264 VLTETQVVSVDTKNKIVMFK-----DGFRMEYNKLLIATGSTPKTLTCKGKELDNVITIRTPEDANKVVRLASSKNAVIV 338
Cdd:pfam07992  79 VLLGTEVVSIDPGAKKVVLEnlvdgDGETITYDRLVIATGARPRLPPIPGVELNVGKLVRTLDSAEALRLKLLPKRLVVV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    339 GASFLGMEVAAYLCEKAHSVSVVELENIPFKKFlGEKVGLAIMKMFENNRVKFYMQTEVSELrEQEGKLKEVVLKSGKVL 418
Cdd:pfam07992 159 GGGYIGVELAAALAKLGKEVTLIEALDRLLRAF-DEEISAILEKALKKNGVEVRLGTSVKEI-IGDGDVVKVILKDGTEI 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2443331    419 RADVCVIGIGASPTTGFLKQSGVALDSRGYIPVNKMMQTNIPGVFAAGDVvtfplafrnnKKMNVPHWQMAHMQG 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 3.37e-57

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: 186.67  E-value: 3.37e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   70 ASVCHVKDLENGQMREVDLGCGKALLVKQNGEYYAMGHKCPHYGAPLVKGVLSKGRVRCPWHGACFNIATGDIEDFPGLD 149
Cdd:cd03478   1 AVVCRLSDLGDGEMKEVDVGDGKVLLVRQGGEVHAIGAKCPHYGAPLAKGVLTDGRIRCPWHGACFNLRTGDIEDAPALD 80
                        90
                ....*....|....*
gi 2443331  150 GLPKFQVKIEKERVY 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 7.04e-09

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: 52.93  E-value: 7.04e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2443331    512 YLWTAMFGKSIRYAGHGEGFDDVIIQGDIDELKFVAFYTRNDEVIAVASMN 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 1.17e-73

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: 237.60  E-value: 1.17e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    195 TNILIIGAGPAGLVCAETLRQEGFsdRIVMCTSEKNLPYDRSKLSKSMDSQAEQ--IFLRSKEFFHTY---------DIE 263
Cdd:pfam07992   1 YDVVIIGGGPAGLAAALTLARAGG--KVTLIEDEGTCPYGGCVLSKALLGAAEApeIASLWAELYERKeevvkklnnGIE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    264 VLTETQVVSVDTKNKIVMFK-----DGFRMEYNKLLIATGSTPKTLTCKGKELDNVITIRTPEDANKVVRLASSKNAVIV 338
Cdd:pfam07992  79 VLLGTEVVSIDPGAKKVVLEnlvdgDGETITYDRLVIATGARPRLPPIPGVELNVGKLVRTLDSAEALRLKLLPKRLVVV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    339 GASFLGMEVAAYLCEKAHSVSVVELENIPFKKFlGEKVGLAIMKMFENNRVKFYMQTEVSELrEQEGKLKEVVLKSGKVL 418
Cdd:pfam07992 159 GGGYIGVELAAALAKLGKEVTLIEALDRLLRAF-DEEISAILEKALKKNGVEVRLGTSVKEI-IGDGDVVKVILKDGTEI 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2443331    419 RADVCVIGIGASPTTGFLKQSGVALDSRGYIPVNKMMQTNIPGVFAAGDVvtfplafrnnKKMNVPHWQMAHMQG 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 3.37e-57

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: 186.67  E-value: 3.37e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   70 ASVCHVKDLENGQMREVDLGCGKALLVKQNGEYYAMGHKCPHYGAPLVKGVLSKGRVRCPWHGACFNIATGDIEDFPGLD 149
Cdd:cd03478   1 AVVCRLSDLGDGEMKEVDVGDGKVLLVRQGGEVHAIGAKCPHYGAPLAKGVLTDGRIRCPWHGACFNLRTGDIEDAPALD 80
                        90
                ....*....|....*
gi 2443331  150 GLPKFQVKIEKERVY 164
Cdd:cd03478  81 SLPCYEVEVEDGRVY 95
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
197-597 2.77e-56

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: 195.13  E-value: 2.77e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  197 ILIIGAGPAGLVCAETLRQEGFSDRIVMCTSEKNLPYDRSKLSK--SMDSQAEQIFLRSKEFFHTYDIEVLTETQVVSVD 274
Cdd:COG0446   1 IVIVGGGAAGLSAATTLRRLLLAAEITLIGREPKYSYYRCPLSLyvGGGIASLEDLRYPPRFNRATGIDVRTGTEVTSID 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  275 TKNKIVMFKDGfRMEYNKLLIATGSTPKTLtcKGKELDNVITIRTPEDANKVV-RLASSKNAVIVGASFLGMEVAAYLCE 353
Cdd:COG0446  81 PENKVVLLDDG-EIEYDYLVLATGARPRPP--PISDWEGVVTLRLREDAEALKgGAEPPKDVVVVGAGPIGLEAAEAAAK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  354 KAHSVSVVELENIPFKKFLGEKVGLAIMKMFENNRVKFYMQTEVSELREQEGKL--KEVVLKSGKVLRADVCVIGIGASP 431
Cdd:COG0446 158 RGKKVTLIEAADRLGGQLLDPEVAEELAELLEKYGVELLLGTKVVGVEGKGNTLvvERVVGIDGEEIKADLVIIGPGERP 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  432 TTGFLKQSGVALDSR-GYIPVNKMMQT-NIPGVFAAGDVVTFPlAFRNNKKMNVPHWQMAHMQGRIAALNMLAQGTEINT 509
Cdd:COG0446 238 NVVLANDALPGLALAgGAVLVDERGGTsKDPDVYAAGDVAEIP-AAETGKGGRIALWAIAVAAGRIAAENIAGALRIPGL 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  510 VPYLWTAMFGKSIRYAGHGEGFDDVIiqgdIDELKFVAFYTRNDEVIAVASMNYDPIVSKVAEIMASGKTIRKRDVETGD 589
Cdd:COG0446 317 LGTVISDVGDLCAASTGLTEGKERGI----DVVLVVSGGKDPRAHLYPGAELVGIKLVGDADTGRILGGQELEVLKRIGA 392

                ....*...
gi 2443331  590 ISWLTGKG 597
Cdd:COG0446 393 LALAIGLG 400
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
197-592 4.57e-47

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 169.72  E-value: 4.57e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   197 ILIIGAGPAGLVCAETLRQEGFSDRIVMCTSEKNLPYDRSKLSKSM--DSQAEQIFLRSKEFFHTYDIEVLTETQVVSVD 274
Cdd:PRK09754   6 IIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMllEDSPQLQQVLPANWWQENNVHLHSGVTIKTLG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   275 TKNKIVMFKDGFRMEYNKLLIATGSTPKTLTCKGKELDNVITIRTPEDANKVVR-LASSKNAVIVGASFLGMEVAAYLCE 353
Cdd:PRK09754  86 RDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREvLQPERSVVIVGAGTIGLELAASATQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   354 KAHSVSVVELENIPFKKFLGEKVGLAIMKMFENNRVKFYMQTEVSELreQEGKLKEVVLKSGKVLRADVCVIGIGASPTT 433
Cdd:PRK09754 166 RRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHV--VDGEKVELTLQSGETLQADVVIYGIGISAND 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   434 GFLKQSGvaLDSRGYIPVNKMMQTNIPGVFAAGDVVTFPLAfrNNKKMNVPHWQMAHMQGRIAALNMLAQGTEINTVPYL 513
Cdd:PRK09754 244 QLAREAN--LDTANGIVIDEACRTCDPAIFAGGDVAITRLD--NGALHRCESWENANNQAQIAAAAMLGLPLPLLPPPWF 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2443331   514 WTAMFGKSIRYAGHGEGfDDVIIQGDIDELKFVAFYTRNDEVIAVASMNYDPIVSKVAEIMASGKTIRKRDVEtgDISW 592
Cdd:PRK09754 320 WSDQYSDNLQFIGDMRG-DDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLLI--DENI 395
CoA_CoA_reduc TIGR03385
CoA-disulfide reductase; Members of this protein family are CoA-disulfide reductase (EC 1.8.1. ...
255-500 1.62e-38

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: 146.81  E-value: 1.62e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    255 EFFHTYDIEVLTETQVVSVDTKNKIVMFKDG-----FRMEYNKLLIATGSTPKTLTCKGKELDNVITIRTPEDANKVVRL 329
Cdd:TIGR03385  52 VFIKKRGIDVKTNHEVIEVNDERQTVVVRNNktnetYEESYDYLILSPGASPIVPNIEGINLDIVFTLRNLEDTDAIKQY 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    330 A---SSKNAVIVGASFLGMEVAAYLCEKAHSVSVVELENIPFKKFLGEKVGLAIMKMFENNRVKFYMQTEVSELREQEgk 406
Cdd:TIGR03385 132 IdknKVENVVIIGGGYIGIEMAEALRERGKNVTLIHRSERILNKLFDEEMNQIVEEELKKHEINLRLNEEVDSIEGEE-- 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    407 lKEVVLKSGKVLRADVCVIGIGASPTTGFLKQSGVALDSRGYIPVNKMMQTNIPGVFAAGDVVTfPLAFRNNKKMNVPHW 486
Cdd:TIGR03385 210 -RVKVFTSGGVYQADMVILATGIKPNSELAKDSGLKLGETGAIWVNEKFQTSVPNIYAAGDVAE-SHNIITKKPAWVPLA 287
                         250
                  ....*....|....
gi 2443331    487 QMAHMQGRIAALNM 500
Cdd:TIGR03385 288 WGANKMGRIAGENI 301
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
72-154 1.89e-26

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: 102.78  E-value: 1.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331     72 VCHVKDLENGQMREVDLGCGKALLVK-QNGEYYAMGHKCPHYGAPLVKGVLSKGRVRCPWHGACFNiATGDIEDFPGLDG 150
Cdd:pfam00355   4 VCASSELPEGDPLGVEVGGEPLVVFRdEDGELYALEDRCPHRGAPLSEGKVDGDRIECPYHGWRFD-GTGKVKKVPALRP 82

                  ....
gi 2443331    151 LPKF 154
Cdd:pfam00355  83 LKTY 86
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
65-166 2.80e-22

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: 91.64  E-value: 2.80e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   65 KDVVEASVCHVKDLENGQMREVDLGCGK-ALLVKQNGEYYAMGHKCPHYGAPLVKGVLS-KGRVRCPWHGACFNIATGDI 142
Cdd:COG2146   1 MMMNWIRICKVDDLPEGGGVRVLVGGGRfALVVRADGEVFAIDNRCPHAGAPLSRGLVEgDETVVCPLHGARFDLRTGEC 80
                        90       100
                ....*....|....*....|....
gi 2443331  143 EDFPGLDGLPKFQVKIEKERVYIR 166
Cdd:COG2146  81 LEPPAGKTLKTYPVRVEGGRVFVD 104
PRK09965 PRK09965
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
72-165 3.74e-09

3-phenylpropionate dioxygenase ferredoxin subunit; Provisional


Pssm-ID: 170182 [Multi-domain]  Cd Length: 106  Bit Score: 54.40  E-value: 3.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    72 VCHVKDLENGQMREVDLGCGKALLvKQNGEYYAMGHKCPHYGAPLVKGVLSKG-RVRCPWHGACFNIATGDIEDFPGLDG 150
Cdd:PRK09965   6 ACPVADLPEGEALRVDTSPVIALF-NVGGEFYAIDDRCSHGNASLSEGYLEDDaTVECPLHAASFCLRTGKALCLPATDP 84
                         90
                 ....*....|....*
gi 2443331   151 LPKFQVKIEKERVYI 165
Cdd:PRK09965  85 LRTYPVHVEGGDIFI 99
Reductase_C pfam14759
Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, ...
512-562 7.04e-09

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: 52.93  E-value: 7.04e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2443331    512 YLWTAMFGKSIRYAGHGEGFDDVIIQGDIDELKFVAFYTRNDEVIAVASMN 562
Cdd:pfam14759   1 WFWSDQYDLKLQIAGLPTGADEVVVRGDPEDGSFSVFYLRDGRLVAVDAVN 51
MocE_fam_FeS TIGR02377
Rieske [2Fe-2S] domain protein, MocE subfamily; This model describes a subfamily of the ...
71-165 3.58e-06

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: 45.63  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331     71 SVCHVKDL-ENGQMREVDLGCGKALLVKQNGEYYAMGHKCPHYGAPLVKGVLSKGRVRCPWHGACFNIATGDIEDFPGLD 149
Cdd:TIGR02377   4 KACDADDIgREDVARFDHGGRTFAIYRTPDDQYYATDGLCTHEYAHLADGLVMDTTVECPKHAGCFDYRTGEALNPPVCV 83
                          90
                  ....*....|....*.
gi 2443331    150 GLPKFQVKIEKERVYI 165
Cdd:TIGR02377  84 NLKTYPVKVVDGAVYV 99
 
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 1.17e-73

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: 237.60  E-value: 1.17e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    195 TNILIIGAGPAGLVCAETLRQEGFsdRIVMCTSEKNLPYDRSKLSKSMDSQAEQ--IFLRSKEFFHTY---------DIE 263
Cdd:pfam07992   1 YDVVIIGGGPAGLAAALTLARAGG--KVTLIEDEGTCPYGGCVLSKALLGAAEApeIASLWAELYERKeevvkklnnGIE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    264 VLTETQVVSVDTKNKIVMFK-----DGFRMEYNKLLIATGSTPKTLTCKGKELDNVITIRTPEDANKVVRLASSKNAVIV 338
Cdd:pfam07992  79 VLLGTEVVSIDPGAKKVVLEnlvdgDGETITYDRLVIATGARPRLPPIPGVELNVGKLVRTLDSAEALRLKLLPKRLVVV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    339 GASFLGMEVAAYLCEKAHSVSVVELENIPFKKFlGEKVGLAIMKMFENNRVKFYMQTEVSELrEQEGKLKEVVLKSGKVL 418
Cdd:pfam07992 159 GGGYIGVELAAALAKLGKEVTLIEALDRLLRAF-DEEISAILEKALKKNGVEVRLGTSVKEI-IGDGDVVKVILKDGTEI 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2443331    419 RADVCVIGIGASPTTGFLKQSGVALDSRGYIPVNKMMQTNIPGVFAAGDVvtfplafrnnKKMNVPHWQMAHMQG 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 3.37e-57

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: 186.67  E-value: 3.37e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   70 ASVCHVKDLENGQMREVDLGCGKALLVKQNGEYYAMGHKCPHYGAPLVKGVLSKGRVRCPWHGACFNIATGDIEDFPGLD 149
Cdd:cd03478   1 AVVCRLSDLGDGEMKEVDVGDGKVLLVRQGGEVHAIGAKCPHYGAPLAKGVLTDGRIRCPWHGACFNLRTGDIEDAPALD 80
                        90
                ....*....|....*
gi 2443331  150 GLPKFQVKIEKERVY 164
Cdd:cd03478  81 SLPCYEVEVEDGRVY 95
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
197-597 2.77e-56

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: 195.13  E-value: 2.77e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  197 ILIIGAGPAGLVCAETLRQEGFSDRIVMCTSEKNLPYDRSKLSK--SMDSQAEQIFLRSKEFFHTYDIEVLTETQVVSVD 274
Cdd:COG0446   1 IVIVGGGAAGLSAATTLRRLLLAAEITLIGREPKYSYYRCPLSLyvGGGIASLEDLRYPPRFNRATGIDVRTGTEVTSID 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  275 TKNKIVMFKDGfRMEYNKLLIATGSTPKTLtcKGKELDNVITIRTPEDANKVV-RLASSKNAVIVGASFLGMEVAAYLCE 353
Cdd:COG0446  81 PENKVVLLDDG-EIEYDYLVLATGARPRPP--PISDWEGVVTLRLREDAEALKgGAEPPKDVVVVGAGPIGLEAAEAAAK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  354 KAHSVSVVELENIPFKKFLGEKVGLAIMKMFENNRVKFYMQTEVSELREQEGKL--KEVVLKSGKVLRADVCVIGIGASP 431
Cdd:COG0446 158 RGKKVTLIEAADRLGGQLLDPEVAEELAELLEKYGVELLLGTKVVGVEGKGNTLvvERVVGIDGEEIKADLVIIGPGERP 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  432 TTGFLKQSGVALDSR-GYIPVNKMMQT-NIPGVFAAGDVVTFPlAFRNNKKMNVPHWQMAHMQGRIAALNMLAQGTEINT 509
Cdd:COG0446 238 NVVLANDALPGLALAgGAVLVDERGGTsKDPDVYAAGDVAEIP-AAETGKGGRIALWAIAVAAGRIAAENIAGALRIPGL 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  510 VPYLWTAMFGKSIRYAGHGEGFDDVIiqgdIDELKFVAFYTRNDEVIAVASMNYDPIVSKVAEIMASGKTIRKRDVETGD 589
Cdd:COG0446 317 LGTVISDVGDLCAASTGLTEGKERGI----DVVLVVSGGKDPRAHLYPGAELVGIKLVGDADTGRILGGQELEVLKRIGA 392

                ....*...
gi 2443331  590 ISWLTGKG 597
Cdd:COG0446 393 LALAIGLG 400
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
197-592 4.57e-47

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 169.72  E-value: 4.57e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   197 ILIIGAGPAGLVCAETLRQEGFSDRIVMCTSEKNLPYDRSKLSKSM--DSQAEQIFLRSKEFFHTYDIEVLTETQVVSVD 274
Cdd:PRK09754   6 IIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMllEDSPQLQQVLPANWWQENNVHLHSGVTIKTLG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   275 TKNKIVMFKDGFRMEYNKLLIATGSTPKTLTCKGKELDNVITIRTPEDANKVVR-LASSKNAVIVGASFLGMEVAAYLCE 353
Cdd:PRK09754  86 RDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREvLQPERSVVIVGAGTIGLELAASATQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   354 KAHSVSVVELENIPFKKFLGEKVGLAIMKMFENNRVKFYMQTEVSELreQEGKLKEVVLKSGKVLRADVCVIGIGASPTT 433
Cdd:PRK09754 166 RRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHV--VDGEKVELTLQSGETLQADVVIYGIGISAND 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   434 GFLKQSGvaLDSRGYIPVNKMMQTNIPGVFAAGDVVTFPLAfrNNKKMNVPHWQMAHMQGRIAALNMLAQGTEINTVPYL 513
Cdd:PRK09754 244 QLAREAN--LDTANGIVIDEACRTCDPAIFAGGDVAITRLD--NGALHRCESWENANNQAQIAAAAMLGLPLPLLPPPWF 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2443331   514 WTAMFGKSIRYAGHGEGfDDVIIQGDIDELKFVAFYTRNDEVIAVASMNYDPIVSKVAEIMASGKTIRKRDVEtgDISW 592
Cdd:PRK09754 320 WSDQYSDNLQFIGDMRG-DDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLLI--DENI 395
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
192-506 1.82e-45

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


Pssm-ID: 224171 [Multi-domain]  Cd Length: 793  Bit Score: 172.12  E-value: 1.82e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  192 TAITNILIIGAGPAGLVCAET-LRQEGFSDRIVMCTSEKNLPYDRSKLSK--SMDSQAEQIFLRSKEFFHTYDIEVLTET 268
Cdd:COG1251   1 MKKQKLVIIGNGMAGHRTIEElLESAPDLYDITVFGEEPRPNYNRILLSSvlAGEKTAEDISLNRNDWYEENGITLYTGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  269 QVVSVDTKNKIVMFKDGFRMEYNKLLIATGSTPKTLTCKGKELDNVITIRTPEDANKVVRLA-SSKNAVIVGASFLGMEV 347
Cdd:COG1251  81 KVIQIDRANKVVTTDAGRTVSYDKLIIATGSYPFILPIPGSDLPGVFVYRTIDDVEAMLDCArNKKKAVVIGGGLLGLEA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  348 AAYLCEKAHSVSVVELENIPFKKFLGEKVGLAIMKMFENNRVKFYMQTEVSELReQEGKLKEVVLKSGKVLRADVCVIGI 427
Cdd:COG1251 161 ARGLKDLGMEVTVVHIAPTLMERQLDRTAGRLLRRKLEDLGIKVLLEKNTEEIV-GEDKVEGVRFADGTEIPADLVVMAV 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  428 GASPTTGFLKQSGVALDsRGyIPVNKMMQTNIPGVFAAGDVVTFplafrNNKKMNV--PHWQMAhmqgRIAALNMLAQGT 505
Cdd:COG1251 240 GIRPNDELAKEAGLAVN-RG-IVVNDYMQTSDPDIYAVGECAEH-----RGKVYGLvaPLYEQA----KVLADHLCGGEA 308

                .
gi 2443331  506 E 506
Cdd:COG1251 309 E 309
CoA_CoA_reduc TIGR03385
CoA-disulfide reductase; Members of this protein family are CoA-disulfide reductase (EC 1.8.1. ...
255-500 1.62e-38

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: 146.81  E-value: 1.62e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    255 EFFHTYDIEVLTETQVVSVDTKNKIVMFKDG-----FRMEYNKLLIATGSTPKTLTCKGKELDNVITIRTPEDANKVVRL 329
Cdd:TIGR03385  52 VFIKKRGIDVKTNHEVIEVNDERQTVVVRNNktnetYEESYDYLILSPGASPIVPNIEGINLDIVFTLRNLEDTDAIKQY 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    330 A---SSKNAVIVGASFLGMEVAAYLCEKAHSVSVVELENIPFKKFLGEKVGLAIMKMFENNRVKFYMQTEVSELREQEgk 406
Cdd:TIGR03385 132 IdknKVENVVIIGGGYIGIEMAEALRERGKNVTLIHRSERILNKLFDEEMNQIVEEELKKHEINLRLNEEVDSIEGEE-- 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    407 lKEVVLKSGKVLRADVCVIGIGASPTTGFLKQSGVALDSRGYIPVNKMMQTNIPGVFAAGDVVTfPLAFRNNKKMNVPHW 486
Cdd:TIGR03385 210 -RVKVFTSGGVYQADMVILATGIKPNSELAKDSGLKLGETGAIWVNEKFQTSVPNIYAAGDVAE-SHNIITKKPAWVPLA 287
                         250
                  ....*....|....
gi 2443331    487 QMAHMQGRIAALNM 500
Cdd:TIGR03385 288 WGANKMGRIAGENI 301
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
197-468 1.24e-33

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 136.50  E-value: 1.24e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    197 ILIIGAGPAGLVCAETLRQEGFSD-RIVMCTSEKNLPYDRSKLSK--SMDSQAEQIFLRSKEFFHTYDIEVLTETQVVSV 273
Cdd:TIGR02374   1 LVLVGNGMAGHRCIEEVLKLNRHMfEITIFGEEPHPNYNRILLSSvlQGEADLDDITLNSKDWYEKHGITLYTGETVIQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    274 DTKNKIVMFKDGFRMEYNKLLIATGSTPKTLTCKGKELDNVITIRTPEDANKVVRLAS-SKNAVIVGASFLGMEVAAYLC 352
Cdd:TIGR02374  81 DTDQKQVITDAGRTLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQrFKKAAVIGGGLLGLEAAVGLQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    353 EKAHSVSVVELENIPFKKFLGEKVGLAIMKMFENNRVKFYMQTEVSELrEQEGKLKEVVLKSGKVLRADVCVIGIGASPT 432
Cdd:TIGR02374 161 NLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEI-VGATKADRIRFKDGSSLEADLIVMAAGIRPN 239
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2443331    433 TGFLKQSGVALdSRGYIpVNKMMQTNIPGVFAAGDV 468
Cdd:TIGR02374 240 DELAVSAGIKV-NRGII-VNDSMQTSDPDIYAVGEC 273
Lpd COG1249
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase (E3) component ...
197-512 6.67e-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: 128.48  E-value: 6.67e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  197 ILIIGAGPAGLVCAETLRQEGFSDRIVmctsEKNLPY-----------------------------------------DR 235
Cdd:COG1249   7 VVVIGAGPAGYVAAIRAAQLGLKVALV----EKGERLggtclnvgcipskallhaaevieearhaakeygisaevpkiDF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  236 SKLSKSMDSQAEQIFLRSKEFFHTYDIEVLTETQVVsVDTKNKIVMFKDGFRMEYNKLLIATGSTPKTLTCKGKELDNVI 315
Cdd:COG1249  83 EKLLARKDKVVRLLTGGVEGLLKKNGVDVIRGEARF-VDPHTVEVTGEDKETITADNIIIATGSRPRIPPGPGIDGARIL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  316 TIRTPEDANKVvrlasSKNAVIVGASFLGMEVAAYLCEKAHSVSVVELENIPFKKFLGEkVGLAIMKMFENNRVKFYMQT 395
Cdd:COG1249 162 DSSDALFLLEL-----PKSLVIVGGGYIGLEFASVFAALGSKVTVVERGDRILPGEDPE-ISKELTKQLEKGGVKILLNT 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  396 EVSELREQEGKLkEVVLKSGK--VLRADVCVIGIGASPTTGF--LKQSGVALDSRGYIPVNKMMQTNIPGVFAAGDVVTF 471
Cdd:COG1249 236 KVTAVEKKDDGV-LVTLEDGEggTIEADAVLVAIGRKPNTDGlgLENAGVELDDRGFIKVDDQMTTNVPGIYAIGDVIGG 314
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 2443331  472 PlafrnnkkmnvphwQMAH---MQGRIAALNMLAQGTEI---NTVPY 512
Cdd:COG1249 315 P--------------MLAHvamAEGRIAAENIAGGKRTPidyRLIPS 347
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
194-500 2.18e-31

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 126.82  E-value: 2.18e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   194 ITNILIIGAGPAGLVCAETLRQ-EGFSDRIV------MCTSEKNLPYdrsKLSKSMDSQAEQIFLRSKEFFHTYDIEVLT 266
Cdd:PRK13512   1 MPKIIVVGAVAGGATCASQIRRlDKESDIIIfekdrdMSFANCALPY---YIGEVVEDRKYALAYTPEKFYDRKQITVKT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   267 ETQVVSVDTKNKIVMFKD-----GFRMEYNKLLIATGSTPKTLtckGKELDNVITIRTPEDANKV---VRLASSKNAVIV 338
Cdd:PRK13512  78 YHEVIAINDERQTVTVLNrktneQFEESYDKLILSPGASANSL---GFESDITFTLRNLEDTDAIdqfIKANQVDKALVV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   339 GASFLGMEVAAYLCEKAHSVSVVElENIPFKKFLGEKVGLAIMKMFENNRVKFYMQTEVSELREQEgklkeVVLKSGKVL 418
Cdd:PRK13512 155 GAGYISLEVLENLYERGLHPTLIH-RSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGNE-----VTFKSGKVE 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   419 RADVCVIGIGASPTTGFLKQSGVALDSRGYIPVNKMMQTNIPGVFAAGDVVTfpLAFRN-NKKMNVPHWQMAHMQGRIAA 497
Cdd:PRK13512 229 HYDMIIEGVGTHPNSKFIESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIIT--SHYRHvDLPASVPLAWGAHRAASIVA 306

                 ...
gi 2443331   498 LNM 500
Cdd:PRK13512 307 EQI 309
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
197-500 2.09e-30

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 124.00  E-value: 2.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   197 ILIIGAGPAGLVCAETLRQEGFSDRIVMctSEKN---------LPYdrskLSKSMDSQAEQIFLRSKEFFHTYDIEVLTE 267
Cdd:PRK09564   3 IIIIGGTAAGMSAAAKAKRLNKELEITV--YEKTdivsfgacgLPY----FVGGFFDDPNTMIARTPEEFIKSGIDVKTE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   268 TQVVSVDTKNKIVMFKDG-----FRMEYNKLLIATGSTPKTLTCKGKELDNVITIRTPEDANKVVRLASS---KNAVIVG 339
Cdd:PRK09564  77 HEVVKVDAKNKTITVKNLktgsiFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKELLKDeeiKNIVIIG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   340 ASFLGMEVAAYLCEKAHSVSVVELEN-IPFKKFLGEKVGLAIMKMFENNrVKFYMQTEVSELrEQEGKLKEVVLKSGKVl 418
Cdd:PRK09564 157 AGFIGLEAVEAAKHLGKNVRIIQLEDrILPDSFDKEITDVMEEELRENG-VELHLNEFVKSL-IGEDKVEGVVTDKGEY- 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   419 RADVCVIGIGASPTTGFLKQSGVALDSRGYIPVNKMMQTNIPGVFAAGDVVTFpLAFRNNKKMNVPHWQMAHMQGRIAAL 498
Cdd:PRK09564 234 EADVVIVATGVKPNTEFLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDCATI-YNIVSNKNVYVPLATTANKLGRMVGE 312

                 ..
gi 2443331   499 NM 500
Cdd:PRK09564 313 NL 314
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
72-154 1.89e-26

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: 102.78  E-value: 1.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331     72 VCHVKDLENGQMREVDLGCGKALLVK-QNGEYYAMGHKCPHYGAPLVKGVLSKGRVRCPWHGACFNiATGDIEDFPGLDG 150
Cdd:pfam00355   4 VCASSELPEGDPLGVEVGGEPLVVFRdEDGELYALEDRCPHRGAPLSEGKVDGDRIECPYHGWRFD-GTGKVKKVPALRP 82

                  ....
gi 2443331    151 LPKF 154
Cdd:pfam00355  83 LKTY 86
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
196-512 4.79e-24

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


Pssm-ID: 224172 [Multi-domain]  Cd Length: 405  Bit Score: 104.64  E-value: 4.79e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  196 NILIIGAGPAGLVCAETLRQEGFSDRIVM----------------CTSEKNLPYDRSKLsksmdsqaEQIFLRSKEFFHT 259
Cdd:COG1252   5 RIVILGGGFGGLSAAKRLARKLPDVEITLvdrrdyhlftpllyevATGTLSESEIAIPL--------RALLRKSGNVQFV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  260 YDievltetQVVSVDTKNKIVMFKDGFRMEYNKLLIATGSTPKTLTCKGKElDNVITIRTPEDANKV-------VRLASS 332
Cdd:COG1252  77 QG-------EVTDIDRDAKKVTLADLGEISYDYLVVALGSETNYFGIPGAA-EYAFGLKTLEDALRLrrhlleaFEKASQ 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  333 KNA-------VIVGASFLGMEVAAYLCEKAHS-------------VSVVELENIPFKKFlGEKVGLAIMKMFENNRVKFY 392
Cdd:COG1252 149 EEDdralltiVIVGGGPTGVELAGELAERLHRllkkfrvdpselrVILVEAGPRILPMF-PPKLSKYAERALEKLGVEVL 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  393 MQTEVSELrEQEGklkeVVLKSG-KVLRADvCVI---GIGASPttgFLKQ-SGVALDSRGYIPVNKMMQ-TNIPGVFAAG 466
Cdd:COG1252 228 LGTPVTEV-TPDG----VTLKDGeEEIPAD-TVVwaaGVRASP---LLKDlSGLETDRRGRLVVNPTLQvPGHPDIFAAG 298
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 2443331  467 DVVTFPlafrnNKKMNVPHWQMAHMQGRIAALNMLAQGTEINTVPY 512
Cdd:COG1252 299 DCAAVI-----DPRPVPPTAQAAHQQGEYAAKNIKARLKGKPLKPF 339
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
72-161 2.82e-23

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: 94.09  E-value: 2.82e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   72 VCHVKDLENGQMREVDLGCGKALLV-KQNGEYYAMGHKCPHYGAPLVKGVLSKGRVRCPWHGACFNIATGDIEDFPGLDG 150
Cdd:cd03467   4 VGALSELPPGGGRVVVVGGGPVVVVrREGGEVYALSNRCTHQGCPLSEGEGEDGCIVCPCHGSRFDLRTGEVVSGPAPRP 83
                        90
                ....*....|.
gi 2443331  151 LPKFQVKIEKE 161
Cdd:cd03467  84 LPKYPVKVEGD 94
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
197-475 7.91e-23

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


Pssm-ID: 223566 [Multi-domain]  Cd Length: 305  Bit Score: 98.90  E-value: 7.91e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  197 ILIIGAGPAGLVCAETLRQEGFSDRIVMctsEKNLPydRSKLSKSMDS----------QAEQIFLRSKEFFHTYDIEVLT 266
Cdd:COG0492   6 VIIIGGGPAGLTAAIYAARAGLKVVLIL---EGGEP--GGQLTKTTDVenypgfpggiLGPELMEQMKEQAEKFGVEIVE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  267 ETqVVSVDT--KNKIVMFKDG-FRMEYnkLLIATGSTPKTLTCKGkeldnvitirTPEDANKVV-------RLASSKNAV 336
Cdd:COG0492  81 DE-VEKVELegGPFKVKTDKGtYEAKA--VIIATGAGARKLGVPG----------EEEFEGKGVsycatcdGFFKGKDVV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  337 IVGASFLGMEVAAYLCEKAHSVSVVelenIPFKKFLGEKVglAIMKMFENNRVKFYMQTEVSELREQEgkLKEVVLKSGK 416
Cdd:COG0492 148 VIGGGDSAVEEALYLSKIAKKVTLV----HRRDEFRAEEI--LVERLKKNVKIEVLTNTVVKEILGDD--VEGVVLKNVK 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2443331  417 ----VLRADVCVIGIGASPTTGFLKQSGVaLDSRGYIPVNKMMQTNIPGVFAAGDVVTFPLAF 475
Cdd:COG0492 220 geekELPVDGVFIAIGHLPNTELLKGLGV-LDENGYIVVDEEMETSVPGIFAAGDVADKNGRQ 281
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
65-166 2.80e-22

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: 91.64  E-value: 2.80e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   65 KDVVEASVCHVKDLENGQMREVDLGCGK-ALLVKQNGEYYAMGHKCPHYGAPLVKGVLS-KGRVRCPWHGACFNIATGDI 142
Cdd:COG2146   1 MMMNWIRICKVDDLPEGGGVRVLVGGGRfALVVRADGEVFAIDNRCPHAGAPLSRGLVEgDETVVCPLHGARFDLRTGEC 80
                        90       100
                ....*....|....*....|....
gi 2443331  143 EDFPGLDGLPKFQVKIEKERVYIR 166
Cdd:COG2146  81 LEPPAGKTLKTYPVRVEGGRVFVD 104
PRK04965 PRK04965
NADH:flavorubredoxin oxidoreductase; Provisional
196-467 4.55e-21

NADH:flavorubredoxin oxidoreductase; Provisional


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 94.98  E-value: 4.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   196 NILIIGAGPAGLVCAETLRQEGFSDRIVMCTSEKNLPYDRSKLSKSMDSQ---AEQIFLRSKEFFHTYDIEVLTETQVVS 272
Cdd:PRK04965   4 GIVIIGSGFAARQLVKNIRKQDAHIPITLITADSGDEYNKPDLSHVFSQGqraDDLTRQSAGEFAEQFNLRLFPHTWVTD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   273 VDTKNKIVMFKDGfRMEYNKLLIATGSTPKTLTCKGKELdnVITI------RTPEDankvvRLASSKNAVIVGASFLGME 346
Cdd:PRK04965  84 IDAEAQVVKSQGN-QWQYDKLVLATGASAFVPPIPGREL--MLTLnsqqeyRAAET-----QLRDAQRVLVVGGGLIGTE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   347 VAAYLCEKAHSVSVVELENIPFKKFLGEKVGLAIMKMFENNRVKFYMQTEVSELREQEGKLKeVVLKSGKVLRADVCVIG 426
Cdd:PRK04965 156 LAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIR-ATLDSGRSIEVDAVIAA 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 2443331   427 IGASPTTGFLKQSGVALDsRGyIPVNKMMQTNIPGVFAAGD 467
Cdd:PRK04965 235 AGLRPNTALARRAGLAVN-RG-IVVDSYLQTSAPDIYALGD 273
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
194-512 5.10e-21

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: 96.17  E-value: 5.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    194 ITNILIIGAGPAGLVCAETLRQEGFSDRIV-------MCTSEKNLPydrsklSKSMDSQAEqIFLRSKEfFHTYDIEVLT 266
Cdd:TIGR01350   1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVekeylggTCLNVGCIP------TKALLHSAE-VYDEIKH-AKDLGIEVEN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    267 etqvVSVD-----------------------TKNKI----------------VMFKDGFRM-EYNKLLIATGSTPKTLTC 306
Cdd:TIGR01350  73 ----VSVDwekmqkrknkvvkklvggvsgllKKNKVtvikgeakfldpgtvsVTGENGEETlEAKNIIIATGSRPRSLPG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    307 KGKELDNVITIRTPEDANKVVrlasSKNAVIVGASFLGMEVAAYLCEKAHSVSVVE-LENIPFkkFLGEKVGLAIMKMFE 385
Cdd:TIGR01350 149 PFDFDGKVVITSTGALNLEEV----PESLVIIGGGVIGIEFASIFASLGSKVTVIEmLDRILP--GEDAEVSKVLQKALK 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    386 NNRVKFYMQTEVSELREQEGKLK-EVVLKSGKVLRADVCVIGIGASPTTGF--LKQSGVALDSRGYIPVNKMMQTNIPGV 462
Cdd:TIGR01350 223 KKGVKILTNTKVTAVEKNDDQVTyENKGGETETLTGEKVLVAVGRKPNTEGlgLEKLGVELDERGRIVVDEYMRTNVPGI 302
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2443331    463 FAAGDVVTfplafrnnkkmnvpHWQMAHM---QGRIAALNMLAQ-GTEIN--TVPY 512
Cdd:TIGR01350 303 YAIGDVIG--------------GPMLAHVashEGIVAAENIAGKePAHIDydAVPS 344
TRX_reduct TIGR01292
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ...
197-468 9.63e-21

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: 92.69  E-value: 9.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    197 ILIIGAGPAGLVCA--------ETLRQEGFS--DRIVMCTSEKNLPYDR-----SKLSKSMDSQAEQiflrskeffhtYD 261
Cdd:TIGR01292   2 VIIIGAGPAGLTAAiyaaranlKPLLIEGMEpgGQLTTTTEVENYPGFPegisgPELMEKMKEQAVK-----------FG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    262 IEVLTETqVVSVDTKN--KIVMFKDGFRMEYNKLLIATGSTPKTLTCKGKEldnvitirtpEDANKVVrlasSKNAVIVG 339
Cdd:TIGR01292  71 AEIIYEE-VIKVDKSDrpFKVYTGDGKEYTAKAVIIATGASARKLGIPGED----------EFWGRGV----SYCATCDG 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    340 ASFLGMEV------------AAYLCEKAHSVSVVELENipfkKFLGEKVglAIMKMFENNRVKFYMQTEVSELREQEG-- 405
Cdd:TIGR01292 136 PFFKNKEVavvgggdsaieeALYLTRIAKKVTLVHRRD----KFRAEKI--LLDRLKKNPKIEFLWNSTVEEIVGDNKve 209
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2443331    406 --KLKEVVLKSGKVLRADVCVIGIGASPTTGFLKQSgVALDSRGYIPVNKMMQTNIPGVFAAGDV 468
Cdd:TIGR01292 210 gvKIKNTVTGEEEELEVDGVFIAIGHEPNTELLKGL-LELDENGYIVTDEGMRTSVPGVFAAGDV 273
Rieske_RO_ferredoxin cd03528
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ...
72-166 5.00e-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: 5.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   72 VCHVKDLENGQMREVDLGCGKALLVKQNGEYYAMGHKCPHYGAPLVKGVLSKGRVRCPWHGACFNIATGDIEDFPGLDGL 151
Cdd:cd03528   4 VCAVDELPEGEPKRVDVGGRPIAVYRVDGEFYATDDLCTHGDASLSEGYVEGGVIECPLHGGRFDLRTGKALSLPATEPL 83
                        90
                ....*....|....*
gi 2443331  152 PKFQVKIEKERVYIR 166
Cdd:cd03528  84 KTYPVKVEDGDVYVD 98
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
197-467 1.80e-18

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 89.41  E-value: 1.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   197 ILIIGAGPAGLVCAETLRQEGFSDRI---VMCtSEKNLPYDRSKLSKSMDSQ-AEQIFLRSKEFFHTYDIEVLTETQVVS 272
Cdd:PRK14989   6 LAIIGNGMVGHRFIEDLLDKADAANFditVFC-EEPRIAYDRVHLSSYFSHHtAEELSLVREGFYEKHGIKVLVGERAIT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   273 VDTKNKIVMFKDGFRMEYNKLLIATGSTPKTLTCKGKELDNVITIRTPEDANKVVRLA-SSKNAVIVGASFLGMEVAAYL 351
Cdd:PRK14989  85 INRQEKVIHSSAGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACArRSKRGAVVGGGLLGLEAAGAL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   352 CEKAHSVSVVELENIPFKKFLGEKVGLAIMKMFENNRVKFYMQTEVSELrEQEGK--LKEVVLKSGKVLRADVCVIGIGA 429
Cdd:PRK14989 165 KNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEI-VQEGVeaRKTMRFADGSELEVDFIVFSTGI 243
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 2443331   430 SPTTGFLKQSGVALDSRGYIPVNKMMQTNIPGVFAAGD 467
Cdd:PRK14989 244 RPQDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
197-521 3.65e-17

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 84.07  E-value: 3.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   197 ILIIGAGPAGLVCAETLRQEGfsDRIVM---------CTSEKNLPydrsklSKSMDSQAEQI--FLRSKEFF-HTYDIEV 264
Cdd:PRK06292   6 VIVIGAGPAGYVAARRAAKLG--KKVALiekgplggtCLNVGCIP------SKALIAAAEAFheAKHAEEFGiHADGPKI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   265 ---------------LTETQVVSVDTKNKIVMFK-------------DGFRMEYNKLLIATGST----PKTLTCKGKELd 312
Cdd:PRK06292  78 dfkkvmarvrrerdrFVGGVVEGLEKKPKIDKIKgtarfvdpntvevNGERIEAKNIVIATGSRvppiPGVWLILGDRL- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   313 nvITIRTPEDANKVvrlasSKNAVIVGASFLGMEVAAYLcekaHS----VSVVE-LENIpfkkfLG---EKVGLAIMKMF 384
Cdd:PRK06292 157 --LTSDDAFELDKL-----PKSLAVIGGGVIGLELGQAL----SRlgvkVTVFErGDRI-----LPledPEVSKQAQKIL 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   385 ENnRVKFYMQTEVSELREQEGKLKEVVLKSGKV--LRADVCVIGIGASPTT---GfLKQSGVALDSRGYIPVNKMMQTNI 459
Cdd:PRK06292 221 SK-EFKIKLGAKVTSVEKSGDEKVEELEKGGKTetIEADYVLVATGRRPNTdglG-LENTGIELDERGRPVVDEHTQTSV 298
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2443331   460 PGVFAAGDVvtfplafrNNKKMnvphwqMAHM---QGRIAALNMLA-QGTEINTVPYLWT-------AMFGKS 521
Cdd:PRK06292 299 PGIYAAGDV--------NGKPP------LLHEaadEGRIAAENAAGdVAGGVRYHPIPSVvftdpqiASVGLT 357
PRK05249 PRK05249
soluble pyridine nucleotide transhydrogenase; Provisional
276-512 3.76e-17

soluble pyridine nucleotide transhydrogenase; Provisional


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 84.05  E-value: 3.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   276 KNKI-VMFKDGFRMEY--NKLLIATGSTPktltckgkeldnvitiRTPE----------DANKVVRLASS-KNAVIVGAS 341
Cdd:PRK05249 121 PHTVeVECPDGEVETLtaDKIVIATGSRP----------------YRPPdvdfdhpriyDSDSILSLDHLpRSLIIYGAG 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   342 FLGMEVAAYLCEKAHSVSVVE-----LEnipfkkFLGEKVGLAIMKMFENNRVKFYMQTEVSELREQEGKlKEVVLKSGK 416
Cdd:PRK05249 185 VIGCEYASIFAALGVKVTLINtrdrlLS------FLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDG-VIVHLKSGK 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   417 VLRADVCVIGIGASPTTGFL--KQSGVALDSRGYIPVNKMMQTNIPGVFAAGDVVTFP-LAfrnnkkmnvphwqMAHM-Q 492
Cdd:PRK05249 258 KIKADCLLYANGRTGNTDGLnlENAGLEADSRGQLKVNENYQTAVPHIYAVGDVIGFPsLA-------------SASMdQ 324
                        250       260
                 ....*....|....*....|..
gi 2443331   493 GRIAALNML--AQGTEINTVPY 512
Cdd:PRK05249 325 GRIAAQHAVgeATAHLIEDIPT 346
PRK07818 PRK07818
dihydrolipoamide dehydrogenase; Reviewed
196-497 4.63e-17

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 236106 [Multi-domain]  Cd Length: 466  Bit Score: 83.92  E-value: 4.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   196 NILIIGAGPAGLVCAETLRQEGFSDRIV-------MCTSEKNLPydrsklSKSMDSQAE--QIFLRSKEFFH-----TYD 261
Cdd:PRK07818   6 DVVVLGAGPGGYVAAIRAAQLGLKTAVVekkywggVCLNVGCIP------SKALLRNAElaHIFTKEAKTFGisgevTFD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   262 IEV-------LTETQVVSVD---TKNKIV------MFKDGFRME------------YNKLLIATGSTPKTLtcKGKEL-D 312
Cdd:PRK07818  80 YGAafdrsrkVAEGRVKGVHflmKKNKITeihgygTFTDANTLEvdlndggtetvtFDNAIIATGSSTRLL--PGTSLsE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   313 NVIT----IRTPEdankvvrlaSSKNAVIVGASFLGMEVAAYLCEKAHSVSVVElenipfkkFL-------GEKVGLAIM 381
Cdd:PRK07818 158 NVVTyeeqILSRE---------LPKSIVIAGAGAIGMEFAYVLKNYGVDVTIVE--------FLdralpneDAEVSKEIA 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   382 KMFENNRVKFYMQTEVSELREQEGKLK-EVVLKSGK--VLRADVCVIGIGASP-TTGF-LKQSGVALDSRGYIPVNKMMQ 456
Cdd:PRK07818 221 KQYKKLGVKILTGTKVESIDDNGSKVTvTVSKKDGKaqELEADKVLQAIGFAPrVEGYgLEKTGVALTDRGAIAIDDYMR 300
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 2443331   457 TNIPGVFAAGDVvtfplafrnNKKMNVPHwqMAHMQGRIAA 497
Cdd:PRK07818 301 TNVPHIYAIGDV---------TAKLQLAH--VAEAQGVVAA 330
gltD PRK12810
glutamate synthase subunit beta; Reviewed
199-469 1.56e-16

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 82.13  E-value: 1.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   199 IIGAGPAGLVCAETLRQEGFSdrIVMctseknlpYDRS--------------KLSKS-MDSQAEQIflrSKEffhtyDIE 263
Cdd:PRK12810 148 VVGSGPAGLAAADQLARAGHK--VTV--------FERAdriggllrygipdfKLEKEvIDRRIELM---EAE-----GIE 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   264 VLTETQVvSVDTKnkivmfKDGFRMEYNKLLIATGST-PKTLTCKGKELDNV------ITirtpeDANKVVR-------- 328
Cdd:PRK12810 210 FRTNVEV-GKDIT------AEELLAEYDAVFLGTGAYkPRDLGIPGRDLDGVhfamdfLI-----QNTRRVLgdetepfi 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   329 LASSKNAVIVGASFLGME-VAAYLCEKAHSVSVVELENIPFKKFLGEKVGLAIMKMFE--------NNRVkFYMQT---- 395
Cdd:PRK12810 278 SAKGKHVVVIGGGDTGMDcVGTAIRQGAKSVTQRDIMPMPPSRRNKNNPWPYWPMKLEvsnaheegVERE-FNVQTkefe 356
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   396 ---------EVSELREQEGKLkEVVLKSGKVLRADVCVIGIG-ASPTTGFLKQSGVALDSRGYIPVNKM-MQTNIPGVFA 464
Cdd:PRK12810 357 gengkvtgvKVVRTELGEGDF-EPVEGSEFVLPADLVLLAMGfTGPEAGLLAQFGVELDERGRVAAPDNaYQTSNPKVFA 435

                 ....*
gi 2443331   465 AGDVV 469
Cdd:PRK12810 436 AGDMR 440
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
197-507 3.21e-16

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 81.35  E-value: 3.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   197 ILIIGAGPAGLVCAETLRQEGFSDRIVmctseknlpyDRSKL-----------SKSMDSQAE--QIFLRSKEF-----FH 258
Cdd:PRK06416   7 VIVIGAGPGGYVAAIRAAQLGLKVAIV----------EKEKLggtclnrgcipSKALLHAAEraDEARHSEDFgikaeNV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   259 TYDIEVLTE--TQVVSVDT--------KNKI----------------VMFKDGFR-MEYNKLLIATGSTPKTLtcKGKEL 311
Cdd:PRK06416  77 GIDFKKVQEwkNGVVNRLTggvegllkKNKVdiirgeaklvdpntvrVMTEDGEQtYTAKNIILATGSRPREL--PGIEI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   312 DNViTIRTPEDANKVVRLASSknAVIVGASFLGMEVA-AYL---CEkahsVSVVE-LENI-P-FKKflgEKVGLAiMKMF 384
Cdd:PRK06416 155 DGR-VIWTSDEALNLDEVPKS--LVVIGGGYIGVEFAsAYAslgAE----VTIVEaLPRIlPgEDK---EISKLA-ERAL 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   385 ENNRVKFYMQTEVSELREQEGKLKEVVLKSGKV--LRADVCVIGIGASPTT---GfLKQSGVALDsRGYIPVNKMMQTNI 459
Cdd:PRK06416 224 KKRGIKIKTGAKAKKVEQTDDGVTVTLEDGGKEetLEADYVLVAVGRRPNTenlG-LEELGVKTD-RGFIEVDEQLRTNV 301
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 2443331   460 PGVFAAGDVVTFPlafrnnkkmnvphwQMAH---MQGRIAALNMLAQGTEI 507
Cdd:PRK06416 302 PNIYAIGDIVGGP--------------MLAHkasAEGIIAAEAIAGNPHPI 338
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
234-501 3.29e-16

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: 81.31  E-value: 3.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    234 DRSKLSKSMDSQAEQifLRSKEF---FHTYDIEVL------TETQVVSVDTKNKIVmfkdgfrmEYNKLLIATGSTPKTL 304
Cdd:TIGR02053  74 DFGELLEGKREVVEE--LRHEKYedvLSSYGVDYLrgrarfKDPKTVKVDLGREVR--------GAKRFLIATGARPAIP 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    305 TCKG-KELDnvitIRTPEDANKVVRLASSknAVIVGASFLGMEVAAYLCEKAHSVSVVELENIPFKKFlGEKVGLAIMKM 383
Cdd:TIGR02053 144 PIPGlKEAG----YLTSEEALALDRIPES--LAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPRE-EPEISAAVEEA 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    384 FENNRVKFYMQTEVSELREQEGKLKEVVLKSGK--VLRADVCVIGIGASPTTGFL--KQSGVALDSRGYIPVNKMMQTNI 459
Cdd:TIGR02053 217 LAEEGIEVVTSAQVKAVSVRGGGKIITVEKPGGqgEVEADELLVATGRRPNTDGLglEKAGVKLDERGGILVDETLRTSN 296
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2443331    460 PGVFAAGDVVTFPlafrnnkkMNVPhwqMAHMQGRIAALNML 501
Cdd:TIGR02053 297 PGIYAAGDVTGGL--------QLEY---VAAKEGVVAAENAL 327
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
199-470 9.57e-16

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 79.84  E-value: 9.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   199 IIGAGPAGLVCAETLRQEGFSDRIvmctseknlpYDRS--------------KLSKSMdSQAEQIFLRSKeffhtyDIEV 264
Cdd:PRK11749 145 VIGAGPAGLTAAHRLARKGYDVTI----------FEARdkaggllrygipefRLPKDI-VDREVERLLKL------GVEI 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   265 LTETQV---VSVDtknkivmfkdGFRMEYNKLLIATG-STPKTLTCKGKELDNVitirtpEDAN---KVVRLASS----- 332
Cdd:PRK11749 208 RTNTEVgrdITLD----------ELRAGYDAVFIGTGaGLPRFLGIPGENLGGV------YSAVdflTRVNQAVAdydlp 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   333 --KNAVIVGASFLGMEVA--AYLcEKAHSVSVV------------------ELENIPF------KKFLGEKVGLAIMKmf 384
Cdd:PRK11749 272 vgKRVVVIGGGNTAMDAArtAKR-LGAESVTIVyrrgreempaseeevehaKEEGVEFewlaapVEILGDEGRVTGVE-- 348
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   385 ennrvkfYMQTEVSELREQeGKLKEVVLKSGKVLRADVCVIGIGASPTTGFLK-QSGVALDSRGY-IPVNKMMQTNIPGV 462
Cdd:PRK11749 349 -------FVRMELGEPDAS-GRRRVPIEGSEFTLPADLVIKAIGQTPNPLILStTPGLELNRWGTiIADDETGRTSLPGV 420

                 ....*...
gi 2443331   463 FAAGDVVT 470
Cdd:PRK11749 421 FAGGDIVT 428
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
197-521 3.16e-15

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 78.04  E-value: 3.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   197 ILIIGAGPAGLVCAETLRQEGFSdriVMCTSEKNLPYDRSKL-----------SKSMDSQAEQiFLRSKEFFHTYDIEVl 265
Cdd:PRK06327   7 VVVIGAGPGGYVAAIRAAQLGLK---VACIEAWKNPKGKPALggtclnvgcipSKALLASSEE-FENAGHHFADHGIHV- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   266 tetQVVSVDT-----------------------KNKIVMFK----------DGFRMEY----------NKLLIATGSTPK 302
Cdd:PRK06327  82 ---DGVKIDVakmiarkdkvvkkmtggieglfkKNKITVLKgrgsfvgktdAGYEIKVtgedetvitaKHVIIATGSEPR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   303 TLTckGKELDNVITIrtpeDANKVVRLAS-SKNAVIVGASFLGMEVAAYLCEKAHSVSVveLENIPfkKFLG---EKVGL 378
Cdd:PRK06327 159 HLP--GVPFDNKIIL----DNTGALNFTEvPKKLAVIGAGVIGLELGSVWRRLGAEVTI--LEALP--AFLAaadEQVAK 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   379 AIMKMFENNRVKFYMQTEVSELREQEgklKEVVLK------SGKVLRADVCVIGIGASPTTGFL--KQSGVALDSRGYIP 450
Cdd:PRK06327 229 EAAKAFTKQGLDIHLGVKIGEIKTGG---KGVSVAytdadgEAQTLEVDKLIVSIGRVPNTDGLglEAVGLKLDERGFIP 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   451 VNKMMQTNIPGVFAAGDVVTfplafrnnkkmnvpHWQMAHM---QGRIAALNMLAQGTEIN--TVPY-LWT----AMFGK 520
Cdd:PRK06327 306 VDDHCRTNVPNVYAIGDVVR--------------GPMLAHKaeeEGVAVAERIAGQKGHIDynTIPWvIYTspeiAWVGK 371

                 .
gi 2443331   521 S 521
Cdd:PRK06327 372 T 372
PRK06370 PRK06370
mercuric reductase; Validated
196-518 5.77e-15

mercuric reductase; Validated


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 77.16  E-value: 5.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   196 NILIIGAGPAGLVCAETLRQEGFSDRIVmctsEKNL-----------PydrsklSKSMDSQAEQIFL--RSKEFFhtydi 262
Cdd:PRK06370   7 DAIVIGAGQAGPPLAARAAGLGMKVALI----ERGLlggtcvntgcvP------TKTLIASARAAHLarRAAEYG----- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   263 evLTETQVVSVDT------KNKIVM---------FK----------------------DGFRMEYNKLLIATGSTPKTLT 305
Cdd:PRK06370  72 --VSVGGPVSVDFkavmarKRRIRArsrhgseqwLRglegvdvfrgharfespntvrvGGETLRAKRIFINTGARAAIPP 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   306 CKGkeLDNV--IT-------IRTPEdankvvRLassknaVIVGASFLGMEVAAYLCEKAHSVSVVELENipfkKFLG--- 373
Cdd:PRK06370 150 IPG--LDEVgyLTnetifslDELPE------HL------VIIGGGYIGLEFAQMFRRFGSEVTVIERGP----RLLPred 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   374 EKVGLAIMKMFENNRVKFYMQTEVSEL-REQEGKLKEVVLKSGK-VLRADVCVIGIGASP-TTGF-LKQSGVALDSRGYI 449
Cdd:PRK06370 212 EDVAAAVREILEREGIDVRLNAECIRVeRDGDGIAVGLDCNGGApEITGSHILVAVGRVPnTDDLgLEAAGVETDARGYI 291
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2443331   450 PVNKMMQTNIPGVFAAGDvVTFPLAFRNnkkmnvphwqMAHMQGRIAALNMLAQG---TEINTVPYlwtAMF 518
Cdd:PRK06370 292 KVDDQLRTTNPGIYAAGD-CNGRGAFTH----------TAYNDARIVAANLLDGGrrkVSDRIVPY---ATY 349
PLN02507 PLN02507
glutathione reductase
284-468 1.35e-14

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 76.39  E-value: 1.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   284 DGFRMEYN--KLLIATGSTPKTLTCKGKELdnviTIrTPEDANKVVRLAssKNAVIVGASFLGMEVAAYLCEKAHSVSVV 361
Cdd:PLN02507 160 DGTKLRYTakHILIATGSRAQRPNIPGKEL----AI-TSDEALSLEELP--KRAVVLGGGYIAVEFASIWRGMGATVDLF 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   362 ELENIPFKKFLGEKVGLaIMKMFENNRVKFYMQTEVSELREQEGKLKeVVLKSGKVLRADVCVIGIGASPTTGF--LKQS 439
Cdd:PLN02507 233 FRKELPLRGFDDEMRAV-VARNLEGRGINLHPRTNLTQLTKTEGGIK-VITDHGEEFVADVVLFATGRAPNTKRlnLEAV 310
                        170       180
                 ....*....|....*....|....*....
gi 2443331   440 GVALDSRGYIPVNKMMQTNIPGVFAAGDV 468
Cdd:PLN02507 311 GVELDKAGAVKVDEYSRTNIPSIWAIGDV 339
AhpF_homolog TIGR03143
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ...
194-468 5.91e-14

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: 74.43  E-value: 5.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    194 ITNILIIGAGPAGLVCA--------ETLRQEgfSDRI---VMCTSE-KNLPYDR----SKLSKSMDSQAEqiflrskeff 257
Cdd:TIGR03143   4 IYDLIIIGGGPAGLSAGiyagraklDTLIIE--KDDFggqITITSEvVNYPGILnttgPELMQEMRQQAQ---------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    258 htyDIEV-LTETQVVSVDTKNKIVMFKDGfRMEYNKL--LIATGSTPKTLTCKGKEldnvitirtpEDANKVVRLASS-- 332
Cdd:TIGR03143  72 ---DFGVkFLQAEVLDVDFDGDIKTIKTA-RGDYKTLavLIATGASPRKLGFPGEE----------EFTGRGVAYCATcd 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    333 ------KNAVIVGASFLGMEVAAYLCEKAHSVSVVELE-NIPFKKFLGEKVglaimkmFENNRVKFYMQTEVSELREQeG 405
Cdd:TIGR03143 138 gefftgMDVFVIGGGFAAAEEAVFLTRYASKVTVIVREpDFTCAKLIAEKV-------KNHPKIEVKFNTELKEATGD-D 209
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2443331    406 KLKEVVLK---SGKV----LRADVCVIGI----GASPTTGFLKQSgVALDSRGYIPVNKMMQTNIPGVFAAGDV 468
Cdd:TIGR03143 210 GLRYAKFVnnvTGEIteykAPKDAGTFGVfvfvGYAPSSELFKGV-VELDKRGYIPTNEDMETNVPGVYAAGDL 282
gltA TIGR01316
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ...
197-469 1.68e-13

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: 72.60  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    197 ILIIGAGPAGLVCAETLRQEGFSDRI---------VMCTSEKNLPYDRSKLsksmDSQAEQIFLRSKEFFHTYDIevlte 267
Cdd:TIGR01316 136 VAVIGAGPAGLACASELAKAGHSVTVfealhkpggVVTYGIPEFRLPKEIV----VTEIKTLKKLGVTFRMNFLV----- 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    268 tqvvsvdtkNKIVMFkDGFRMEYNKLLIATGS-TPKTLTCKGKELDNVIT----------IRTPEDANKVVRLASSKNAV 336
Cdd:TIGR01316 207 ---------GKTATL-EELFSQYDAVFIGTGAgLPKLMNIPGEELCGVYSandfltranlMKAYEFPHADTPVYAGKSVV 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    337 IVGASF-----------LGMEV-AAYLCEKAHSVSVVEL------ENIPFK------KFLGEkvglaimkmfENNRVK-- 390
Cdd:TIGR01316 277 VIGGGNtavdsartalrLGAEVhCLYRRTREDMTARVEEiahaeeEGVKFHflcqpvEIIGD----------EEGNVRav 346
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2443331    391 FYMQTEVSELREQEGKLKEVVLKSGKVLRADVCVIGIGASPTTGFLKQSGVALDSRGYIPVNKMMQTNIPGVFAAGDVV 469
Cdd:TIGR01316 347 KFRKMDCQEQIDSGERRFLPCGDAECKLEADAVIVAIGNGSNPIMAETTRLKTSERGTIVVDEDQRTSIPGVFAGGDII 425
acoL PRK06912
dihydrolipoamide dehydrogenase; Validated
196-469 1.73e-13

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 180743 [Multi-domain]  Cd Length: 458  Bit Score: 72.82  E-value: 1.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   196 NILIIGAGPAGLVCAETLRQEGfsdRIVM----------CTSEKNLP----------YDRSKLS---------------- 239
Cdd:PRK06912   2 KLVVIGGGPAGYVAAITAAQNG---KNVTlideadlggtCLNEGCMPtksllesaevHDKVKKAnhfgitlpngsisidw 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   240 KSMDSQAEQI---------FLRSKEffhtyDIEVLTETqvVSVDTKNKIVMFKDGFR--MEYNKLLIATGSTPKTL---T 305
Cdd:PRK06912  79 KQMQARKSQIvtqlvqgiqYLMKKN-----KIKVIQGK--ASFETDHRVRVEYGDKEevVDAEQFIIAAGSEPTELpfaP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   306 CKGKeldnviTIRTPEDANKVVRLASSknAVIVGASFLGMEVAAYLCEKAHSVSVVELEN--IPfkkflGEKVGLA--IM 381
Cdd:PRK06912 152 FDGK------WIINSKHAMSLPSIPSS--LLIVGGGVIGCEFASIYSRLGTKVTIVEMAPqlLP-----GEDEDIAhiLR 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   382 KMFENNRVKFYMQTEVSELREQEgklKEVVLKSG---KVLRADVCVIGIGASPTTGFLK--QSGVALDSRGyIPVNKMMQ 456
Cdd:PRK06912 219 EKLENDGVKIFTGAALKGLNSYK---KQALFEYEgsiQEVNAEFVLVSVGRKPRVQQLNleKAGVQFSNKG-ISVNEHMQ 294
                        330
                 ....*....|...
gi 2443331   457 TNIPGVFAAGDVV 469
Cdd:PRK06912 295 TNVPHIYACGDVI 307
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
197-472 2.34e-13

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 71.56  E-value: 2.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   197 ILIIGAGPAGLVCAETLRQEGFS----DR-------IVMCTSEKNLPYDRSKLS-KSMDSQAEQIFLRSKEFfhtYDIEV 264
Cdd:PRK12770  21 VAIIGAGPAGLAAAGYLACLGYEvhvyDKlpepgglMLFGIPEFRIPIERVREGvKELEEAGVVFHTRTKVC---CGEPL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   265 LTETQVVSVDtknKIVMFKDGFRmEYNKLLIATGS-TPKTLTCKGKELDNVIT-------IRTPEDA---NKVVRLASSK 333
Cdd:PRK12770  98 HEEEGDEFVE---RIVSLEELVK-KYDAVLIATGTwKSRKLGIPGEDLPGVYSaleylfrIRAAKLGylpWEKVPPVEGK 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   334 NAVIVGASFLGMEVA--AYLcEKAHSVSVV---ELENIPFKKFLGEKVGLAIMKMFEN-NRVKFYMQTEVSELREQEGKL 407
Cdd:PRK12770 174 KVVVVGAGLTAVDAAleAVL-LGAEKVYLAyrrTINEAPAGKYEIERLIARGVEFLELvTPVRIIGEGRVEGVELAKMRL 252
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2443331   408 K----------EVVLKSGKVLRADVCVIGIGASPTTGFLKQS-GVALDSRGYIPVNKMMQTNIPGVFAAGDVVTFP 472
Cdd:PRK12770 253 GepdesgrprpVPIPGSEFVLEADTVVFAIGEIPTPPFAKEClGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGP 328
AhpF TIGR03140
alkyl hydroperoxide reductase subunit F; This enzyme is the partner of the peroxiredoxin ...
196-472 4.22e-13

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: 71.63  E-value: 4.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    196 NILIIGAGPAGLVCA-----ETLRQEGFSDRI---VMCT-SEKNL---PYDR-SKLSKSMDSQAEQiflrskeffhtYDI 262
Cdd:TIGR03140 214 DVLVVGGGPAGAAAAiyaarKGLRTAMVAERIggqVKDTvGIENLisvPYTTgSQLAANLEEHIKQ-----------YPI 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    263 EVLTETQVVSVDT--KNKIVMFKDGFRMEYNKLLIATGSTPKTLTCKGKEldnvitirtpEDANKVVR--------LASS 332
Cdd:TIGR03140 283 DLMENQRAKKIETedGLIVVTLESGEVLKAKSVIVATGARWRKLGVPGEK----------EYIGKGVAycphcdgpFFKG 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    333 KNAVIVGASFLGMEVA---AYLCEKahsVSVVE-LENIPFKKFLGEKvglaiMKMFENNRVKFYMQTE--------VSEL 400
Cdd:TIGR03140 353 KDVAVIGGGNSGIEAAidlAGIVRH---VTVLEfADELKADKVLQDK-----LKSLPNVDILTSAQTTeivgdgdkVTGI 424
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2443331    401 REQEGKLKEVvlksgKVLRADVCVIGIGASPTTGFLKQSgVALDSRGYIPVNKMMQTNIPGVFAAGDVVTFP 472
Cdd:TIGR03140 425 RYQDRNSGEE-----KQLDLDGVFVQIGLVPNTEWLKDA-VELNRRGEIVIDERGRTSVPGIFAAGDVTTVP 490
PRK06116 PRK06116
glutathione reductase; Validated
292-468 2.15e-12

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 69.03  E-value: 2.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   292 KLLIATGSTPKTLTCKGKELdnviTIrtpeDANKVVRL-ASSKNAVIVGASFLGMEVAAYLcekaHSvsvvelenipfkk 370
Cdd:PRK06116 134 HILIATGGRPSIPDIPGAEY----GI----TSDGFFALeELPKRVAVVGAGYIAVEFAGVL----NG------------- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   371 fLGEKVGL-----AIMKMF------------ENNRVKFYMQTEVSEL-REQEGKLKeVVLKSGKVLRADVCVIGIGASP- 431
Cdd:PRK06116 189 -LGSETHLfvrgdAPLRGFdpdiretlveemEKKGIRLHTNAVPKAVeKNADGSLT-LTLEDGETLTVDCLIWAIGREPn 266
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 2443331   432 TTGF-LKQSGVALDSRGYIPVNKMMQTNIPGVFAAGDV 468
Cdd:PRK06116 267 TDGLgLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDV 304
PRK13748 PRK13748
putative mercuric reductase; Provisional
274-472 2.18e-12

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 69.41  E-value: 2.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   274 DTKNKIVMFKDGFRME--YNKLLIATGSTPKTLTCKG-KE------LDNVITIRTPEdankvvRLAssknavIVGASFLG 344
Cdd:PRK13748 215 DDQTLIVRLNDGGERVvaFDRCLIATGASPAVPPIPGlKEtpywtsTEALVSDTIPE------RLA------VIGSSVVA 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   345 MEVAAYLCEKAHSVSVVELENIPFKK--FLGEKVGLAimkmFENNRVKFYMQTEVSELREQEGklkEVVLKSGK-VLRAD 421
Cdd:PRK13748 283 LELAQAFARLGSKVTILARSTLFFREdpAIGEAVTAA----FRAEGIEVLEHTQASQVAHVDG---EFVLTTGHgELRAD 355
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 2443331   422 VCVIGIGASPTTGFL--KQSGVALDSRGYIPVNKMMQTNIPGVFAAGDVVTFP 472
Cdd:PRK13748 356 KLLVATGRAPNTRSLalDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQP 408
Nterm_to_SelD TIGR03169
pyridine nucleotide-disulfide oxidoreductase family protein; Members of this protein family ...
269-471 2.48e-12

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: 68.38  E-value: 2.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    269 QVVSVDTKNKIVMFKDGFRMEYNKLLIATGSTPKTLTCKG--------KELDNVIT----IRTPEDANKVVRLAssknav 336
Cdd:TIGR03169  75 RAIGLDLAAKQVICAGRPPIAYDVLSIDIGSTPALPDVPGfaehaipaKPLGQFAQrwqrFLERAKPQQPPRIA------ 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    337 IVGASFLGMEVA---AY-LCEKAHSVSVVELENIP-FKKFLGEKVGLAIMKMFENNRVKFYMQTEVSELREqegklKEVV 411
Cdd:TIGR03169 149 VIGGGAAGVELAlamAHrLRQLGRNAEVTLIDRGNvLLPGHNARVRRRLERALQERGVTLHLGATVAEVTA-----DAVR 223
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2443331    412 LKSGKVLRADVCVIGIGASPTtGFLKQSGVALDSRGYIPVNKMMQT-NIPGVFAAGDVVTF 471
Cdd:TIGR03169 224 LEDGQTLPADFTFWATGARPP-GWLAESGLALDEDGFIRVGPTLQSlSHPDIFAAGDCAHL 283
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
409-496 3.70e-12

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 68.35  E-value: 3.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   409 EVVLKSGKVLRADVCVIGIGASPTT---GfLKQSGVALDSRGYIPVNKMMQTNIPGVFAAGDVVT-FPLAfrnnkkmnvp 484
Cdd:PRK07845 252 VVTLTDGRTVEGSHALMAVGSVPNTaglG-LEEAGVELTPSGHITVDRVSRTSVPGIYAAGDCTGvLPLA---------- 320
                         90
                 ....*....|..
gi 2443331   485 hwQMAHMQGRIA 496
Cdd:PRK07845 321 --SVAAMQGRIA 330
Rieske_NirD_small_Bacillus cd03530
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ...
72-165 4.43e-12

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: 62.24  E-value: 4.43e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   72 VCHVKDLENGQMREVDLGCGK-ALLVKQNGEYYAMGHKCPHYGAPLVKGVLSKGRVRCPWHGACFNIATGDIEdfpGLDG 150
Cdd:cd03530   4 IGALEDIPPRGARKVQTGGGEiAVFRTADDEVFALENRCPHKGGPLSEGIVHGEYVTCPLHNWVIDLETGEAQ---GPDE 80
                        90
                ....*....|....*..
gi 2443331  151 --LPKFQVKIEKERVYI 165
Cdd:cd03530  81 gcVRTFPVKVEDGRVYL 97
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
260-466 4.67e-12

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 316275 [Multi-domain]  Cd Length: 290  Bit Score: 66.85  E-value: 4.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    260 YDIEVLTETQVVSVDtKNKivmfkDGFRMEYNK-------LLIATG--STPKTLTCKGKElDNVITIRTPEDANKVvrla 330
Cdd:pfam13738  79 FELPINTFEEVTSVK-KED-----DGFVVTTSKgtytaryVIIATGefDFPNKPGIPGEE-KLPKHYHYVKDWHPY---- 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    331 SSKNAVIVGASFLGMEVAAYLCEKAHSVSVV----ELENIPFKKflgeKVGLA------IMKMFENNRVKFYMQTEVSEL 400
Cdd:pfam13738 148 AGQKVVVIGGYNSAVDAALELVRKGARVTVLtrgsEWEADDSDP----SYSLSpdtlnrLKELVKNGSIKLYFNAEVKEI 223
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2443331    401 REQEGKLKeVVLKSGKVLR-ADVCVIGIGASPTTGFLKQSGVALDSRGYIPVNKM-MQTNIPGVFAAG 466
Cdd:pfam13738 224 TEVDVSYK-VHFKDGRKVTsNDDPILATGYHPDLSFLKKSGFELDEDGRPVLTEEtESTNVPGLFLAG 290
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
334-411 7.17e-12

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: 61.04  E-value: 7.17e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2443331    334 NAVIVGASFLGMEVAAYLCEKAHSVSVVELENIPFKKFlGEKVGLAIMKMFENNRVKFYMQTEVSELREQEGKLKEVV 411
Cdd:pfam00070   1 KVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLRGL-DEEIAKILQERLEKNGIEVLLNTTVEAIEGNGDGVVVVL 77
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
267-497 7.24e-12

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 67.48  E-value: 7.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   267 ETQVVSVDTKNKIVMFKDG----------FRMEYNKLLIATGSTPKTLTCKG--------KELDNVITIRTP-----EDA 323
Cdd:PTZ00318  81 RAVVYDVDFEEKRVKCGVVsksnnanvntFSVPYDKLVVAHGARPNTFNIPGveerafflKEVNHARGIRKRivqciERA 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   324 N-KVVRLASSK---NAVIVGASFLGMEVAAYLCE-KAHSVSVVELENIPFKKFLGEKVGLAIMKMFE------------N 386
Cdd:PTZ00318 161 SlPTTSVEERKrllHFVVVGGGPTGVEFAAELADfFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDqalrkygqrrlrR 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   387 NRVKFYMQTEVSELREqegklKEVVLKSGKVLRADVCV--IGIGASPTTgflKQSGVALDSRGYIPVNKMMQT-NIPGVF 463
Cdd:PTZ00318 241 LGVDIRTKTAVKEVLD-----KEVVLKDGEVIPTGLVVwsTGVGPGPLT---KQLKVDKTSRGRISVDDHLRVkPIPNVF 312
                        250       260       270
                 ....*....|....*....|....*....|....
gi 2443331   464 AAGDVVTfplafrNNKKMNVPHWQMAHMQGRIAA 497
Cdd:PTZ00318 313 ALGDCAA------NEERPLPTLAQVASQQGVYLA 340
gluta_reduc_1 TIGR01421
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ...
196-469 8.30e-12

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: 67.17  E-value: 8.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    196 NILIIGAGPAGLVCAETLRQEGFSDRI------------VMCTSEKNLPYDrSKLSKSMDSQAEQIFLRSKEffHTYDIE 263
Cdd:TIGR01421   4 DYLVIGGGSGGIASARRAAEHGAKALLveakklggtcvnVGCVPKKVMWYA-SDLAERMHDAADYGFYQNDE--NTFNWP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    264 VLTETQVVSVD----------TKNKI------VMFKDGFRMEYNK-------LLIATGSTPKTLT-CKGKELDNvitirt 319
Cdd:TIGR01421  81 ELKEKRDAYVDrlngiyqknlEKNKVdvifghARFTKDGTVEVNGrdytaphILIATGGKPSFPEnIPGAELGT------ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    320 peDANKVVRLAS-SKNAVIVGASFLGMEVAAYLCEKAHSVSVVELENIPFKKFlGEKVGLAIMKMFENNRVKFYMQTEVS 398
Cdd:TIGR01421 155 --DSDGFFALEElPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRHERVLRSF-DSMISETITEEYEKEGINVHKLSKPV 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2443331    399 ELREQ-EGKLKEVVLKSGKVLRADVCVIGIGASPTTG--FLKQSGVALDSRGYIPVNKMMQTNIPGVFAAGDVV 469
Cdd:TIGR01421 232 KVEKTvEGKLVIHFEDGKSIDDVDELIWAIGRKPNTKglGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVV 305
GOGAT_sm_gam TIGR01317
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ...
199-467 4.16e-11

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: 65.24  E-value: 4.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    199 IIGAGPAGLVCAETLRQEGFSdrivMCTSEKNlpyDRS-----------KLSKSmdsqaeqIFLRSKEFFHTYDIEVLTE 267
Cdd:TIGR01317 148 VVGSGPAGLAAADQLNRAGHT----VTVFERE---DRCggllmygipnmKLDKA-------IVDRRIDLLSAEGIDFVTN 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    268 TQV---VSVDTknkivmfkdgFRMEYNKLLIATGST-PKTLTCKGKELDNV------ITIRTPEDANKVVR-----LASS 332
Cdd:TIGR01317 214 TEIgvdISADE----------LKEQFDAVVLAGGATkPRDLPIPGRELKGIhyamefLPSATKALLGKDFKdiifiKAKG 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    333 KNAVIVGASFLGME-VAAYLCEKAHSVSVVEL---------ENIPF-------------------------------KKF 371
Cdd:TIGR01317 284 KKVVVIGGGDTGADcVGTSLRHGAASVHQFEImpkppearaKDNPWpewprvyrvdyaheeaaahygrdpreysiltKEF 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    372 LGEKVGlaimkmfennRVKFYMQTEVSELREQEGKLKEV-VLKSGKVLRADVCVIGIG-ASPTTGFLKQSGVALDSRGYI 449
Cdd:TIGR01317 364 IGDDEG----------KVTALRTVRVEWKKSQDGKWQFVeIPGSEEVFEADLVLLAMGfVGPEQILLDDFGVKKTRRGNI 433
                         330
                  ....*....|....*....
gi 2443331    450 PVN-KMMQTNIPGVFAAGD 467
Cdd:TIGR01317 434 SAGyDDYSTSIPGVFAAGD 452
PRK09853 PRK09853
putative selenate reductase subunit YgfK; Provisional
161-472 6.63e-11

putative selenate reductase subunit YgfK; Provisional


Pssm-ID: 236630 [Multi-domain]  Cd Length: 1019  Bit Score: 65.38  E-value: 6.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    161 ERVYIRASKQALLSQRRTKVMAKCIALSNYSTAiTNILIIGAGPAGLVCAETLRQEGFsDRIVMctsEKnlpydRSKLSK 240
Cdd:PRK09853  507 EAVNIRELKKVALEKGWDEYKQRWHKPAGIGSR-KKVAVIGAGPAGLAAAYFLARAGH-PVTVF---ER-----EENAGG 576
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    241 SMDSQAEQIFLRSKEFFHtyDIEVLTETQVVSVDTKNKIVMFKDGFRMEYNKLLIATG-STPKTLTCKGKElDNVIT--- 316
Cdd:PRK09853  577 VVKNIIPQFRIPAELIQH--DIEFVKAHGVKFEFGCSPDLTVEQLKNEGYDYVVVAIGaDKNGGLKLEGGN-QNVIKalp 653
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    317 -IRTPEDANKVVRLAssKNAVIVGASFLGMEVA--AYLCEKAHSVSVV---ELENIP-----FKKFLGEKVGLaimkMFE 385
Cdd:PRK09853  654 fLEEYKNKGTALKLG--KHVVVVGGGNTAMDAAraALRVPGVEKVTVVyrrTKQEMPawreeYEEALEDGVEF----KEL 727
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    386 NNRVKFYMQ----TEVSELREQEGKLKEVVLKSGK--VLRADVCVIGIGASPTTGFLKQSGVALDSRGYIPVNKMMQTNI 459
Cdd:PRK09853  728 LNPESFDADgtltCRVMKLGEPDESGRRRPVETGEtvTLEADTVITAIGEQVDTELLKANGIPLDKKGWPVVDANGETSL 807
                         330
                  ....*....|...
gi 2443331    460 PGVFAAGDVVTFP 472
Cdd:PRK09853  808 TNVYMIGDVQRGP 820
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
197-470 8.21e-11

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: 64.23  E-value: 8.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  197 ILIIGAGPAGLVCAETLRQEGfsdriVMCTSEKNLPYD---------RSKLSKSMDSQAEQIFLRSKEFFHTydievlte 267
Cdd:COG0493 126 VAVIGAGPAGLAAADDLSRAG-----HDVTVFERVALDgglllygipDFKLPKDILDRRLELLERSGVEFKL-------- 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  268 tqVVSVDtknKIVMFKDgFRMEYNKLLIATGS-TPKTLTCKGKELDNV---------ITIRTPEDANKV-VRLASSKNAV 336
Cdd:COG0493 193 --NVRVG---RDITLEE-LLKEYDAVFLATGAgKPRPLDIPGEDAKGVafaldfltrLNKEVLGDFAEDrTPPAKGKRVV 266
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  337 IVGASFLGMEVAA----YLCEKAHSVSV--VELENIPFKKF--------LGEKvglAIMKMFENNRVKF--YMQTEVSEL 400
Cdd:COG0493 267 VIGGGDTAMDCAGtalrLGAKSVTCFYRedRDDETNEWPTWaaqlevrsAGEE---GVERLPFVQPKAFigNEGGRVTGV 343
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  401 REQEGKLKEVVLKSGK-----------VLRADVCVIGIGASP--TTGFLKQSGVALDSRGYIPVNKMM-QTNIPGVFAAG 466
Cdd:COG0493 344 KFGRVEPGEYVDGWGRrgpvgvigtekTDAADTVILAIGFEGdaTDGLLLEFGLKLDKRGRIKVDENLqQTSIPGVFAGG 423

                ....
gi 2443331  467 DVVT 470
Cdd:COG0493 424 DAVR 427
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
292-518 8.61e-11

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: 64.10  E-value: 8.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    292 KLLIATGSTPKTLTCKG-KEL----DNVITIrtPEDANKVVrlassknavIVGASFLGMEVAAYLCEKAHSVSVVeLENI 366
Cdd:TIGR01438 146 RFLIATGERPRYPGIPGaKELcitsDDLFSL--PYCPGKTL---------VVGASYVALECAGFLAGIGLDVTVM-VRSI 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    367 PFKKFlGEKVGLAIMKMFENNRVKFYMQTEVSELREQEGKLKEVVLKS--GKVLRADVCVIGIGASPTTGF--LKQSGVA 442
Cdd:TIGR01438 214 LLRGF-DQDCANKVGEHMEEHGVKFKRQFVPIKVEQIEAKVLVEFTDStnGIEEEYDTVLLAIGRDACTRKlnLENVGVK 292
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2443331    443 LDSR-GYIPVNKMMQTNIPGVFAAGDVVtfplafrNNKKMNVPhwqMAHMQGRIAALNMLAQGTEINTVPYLWTAMF 518
Cdd:TIGR01438 293 INKKtGKIPADEEEQTNVPYIYAVGDIL-------EDKPELTP---VAIQAGRLLAQRLFKGSTVICDYENVPTTVF 359
PRK14694 PRK14694
putative mercuric reductase; Provisional
213-472 1.61e-10

putative mercuric reductase; Provisional


Pssm-ID: 237790 [Multi-domain]  Cd Length: 468  Bit Score: 63.42  E-value: 1.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   213 LRQEG-FSDRIvmctSEKNLPYDRSKLSKSMDSQAEQifLRSKEFfhtydIEVLTETQVVSV--------DTKNKIVMFK 283
Cdd:PRK14694  64 LRRESpFDDGL----SAQAPVVDRSALLAQQQARVEE--LRESKY-----QSILRENAAITVlngearfvDERTLTVTLN 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   284 DGFR--MEYNKLLIATGSTPKTLTCKGKELDNVITIRTPEDANKVvrlasSKNAVIVGASFLGMEVAAYLCEKAHSVSVV 361
Cdd:PRK14694 133 DGGEqtVHFDRAFIGTGARPAEPPVPGLAETPYLTSTSALELDHI-----PERLLVIGASVVALELAQAFARLGSRVTVL 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   362 ELENIPFKKflGEKVGLAIMKMFENNRVKFYMQTEVSELREQEgklKEVVLKS-GKVLRADVCVIGIGASPTTGFLKQSG 440
Cdd:PRK14694 208 ARSRVLSQE--DPAVGEAIEAAFRREGIEVLKQTQASEVDYNG---REFILETnAGTLRAEQLLVATGRTPNTENLNLES 282
                        250       260       270
                 ....*....|....*....|....*....|...
gi 2443331   441 VALD-SRGYIPVNKMMQTNIPGVFAAGDVVTFP 472
Cdd:PRK14694 283 IGVEtERGAIRIDEHLQTTVSGIYAAGDCTDQP 315
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
287-468 1.73e-10

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: 63.45  E-value: 1.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    287 RMEYNKLLIATGSTPKTLTCKGKELdnVITirtpedANKVVRLASS-KNAVIVGASFLGMEVAAYLCEKAHSVSVVEL-- 363
Cdd:TIGR01423 149 RLQAEHILLATGSWPQMLGIPGIEH--CIS------SNEAFYLDEPpRRVLTVGGGFISVEFAGIFNAYKPRGGKVTLcy 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    364 ENIPFKKFLGEKVGLAIMKMFENNRVKFYMQTEVSELREQEGKLKEVVLKSGKVLRADVCVIGIGASPTTGFLK--QSGV 441
Cdd:TIGR01423 221 RNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTLNADGSKHVTFESGKTLDVDVVMMAIGRVPRTQTLQldKVGV 300
                         170       180
                  ....*....|....*....|....*..
gi 2443331    442 ALDSRGYIPVNKMMQTNIPGVFAAGDV 468
Cdd:TIGR01423 301 ELTKKGAIQVDEFSRTNVPNIYAIGDV 327
PTZ00058 PTZ00058
glutathione reductase; Provisional
228-469 2.67e-10

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 62.71  E-value: 2.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   228 EKNLPYDRSKlsKSMDSQAEQIFLRSKEFFHTYDIEVLTETQVVSVDTKNKivmfKDGFRMEYNKLLIATGSTPKTLTCK 307
Cdd:PTZ00058 147 KDNVEYFEGK--GSLLSENQVLIKKVSQVDGEADESDDDEVTIVSAGVSQL----DDGQVIEGKNILIAVGNKPIFPDVK 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   308 GKEldNVItirtpeDANKVVRLASSKNAVIVGASFLGMEVAAYLCEKAHSVSVVELENIPFKKFlGEKVGLAIMKMFENN 387
Cdd:PTZ00058 221 GKE--FTI------SSDDFFKIKEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKF-DETIINELENDMKKN 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   388 RVKFYMQTEVSELREQEGK-LKEVVLKSGKVLRADVCVIGIGASPTTGFLKQSGVA-LDSRGYIPVNKMMQTNIPGVFAA 465
Cdd:PTZ00058 292 NINIITHANVEEIEKVKEKnLTIYLSDGRKYEHFDYVIYCVGRSPNTEDLNLKALNiKTPKGYIKVDDNQRTSVKHIYAV 371

                 ....
gi 2443331   466 GDVV 469
Cdd:PTZ00058 372 GDCC 375
Bthiol_YpdA TIGR04018
putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, ...
197-469 2.73e-10

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: 61.81  E-value: 2.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    197 ILIIGAGPAGLVCAETLRQEGFSDRIV---------------M---CTSEK----NLPYdRSKLSKSMDSQAEQIFLRSK 254
Cdd:TIGR04018   2 VIIIGAGPCGLACAIEAQKAGLSYLIIekgnlvnsiyryptnMtffSTSERleigGIPF-ISENPKPTRNEALEYYRRVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    255 EFFHtydIEVLTETQVVSVD-TKNKIVMFKDGFRMEYNKLLIATG--STPKTLTCKGKELDNVITIRtpEDANKVVRLas 331
Cdd:TIGR04018  81 ERFK---LNIRLYEEVLKVKkTDGGFEVTTEKGTYQAKNVIVATGyyDIPNLLNVPGEDLPKVSHYY--KEAHPYFGQ-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    332 skNAVIVGASFLGMEVAAYLCEKAHSVSVVELENipfkkFLGEKVGLAIMKMFEN----NRVKFYMQTEVSELREQEgkl 407
Cdd:TIGR04018 154 --KVVVVGGSNSAVDAALELYRKGAEVTMVHRGD-----EVSSSVKYWVRPDIENrikeGSIKAYFNSRVKEITEDS--- 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2443331    408 keVVLKS--GKV--LRADVCVIGIGASPTTGFLKQSGVALDSRGYIPV-NK-MMQTNIPGVFAAGDVV 469
Cdd:TIGR04018 224 --VTLETpdGEVhtIPNDFVFALTGYRPDFEFLESLGVELDEDTGIPVyNPeTMETNVPGLYLAGVIA 289
PRK14727 PRK14727
putative mercuric reductase; Provisional
290-472 4.71e-10

putative mercuric reductase; Provisional


Pssm-ID: 237806 [Multi-domain]  Cd Length: 479  Bit Score: 61.88  E-value: 4.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   290 YNKLLIATGSTPKTLTCKGkeLDNVITIRTPEDANKVvrlASSKNAVIVGASFLGMEVAAYLCEKAHSVSVVELENIPFK 369
Cdd:PRK14727 151 ADRCLIATGSTPTIPPIPG--LMDTPYWTSTEALFSD---ELPASLTVIGSSVVAAEIAQAYARLGSRVTILARSTLLFR 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   370 K--FLGEKvglaIMKMFENNRVKFYMQTEVSELREQEgklKEVVLKSGK-VLRADVCVIGIGASPTTG--FLKQSGVALD 444
Cdd:PRK14727 226 EdpLLGET----LTACFEKEGIEVLNNTQASLVEHDD---NGFVLTTGHgELRAEKLLISTGRHANTHdlNLEAVGVTTD 298
                        170       180
                 ....*....|....*....|....*...
gi 2443331   445 SRGYIPVNKMMQTNIPGVFAAGDVVTFP 472
Cdd:PRK14727 299 TSGAIVVNPAMETSAPDIYAAGDCSDLP 326
gluta_reduc_2 TIGR01424
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ...
292-468 1.30e-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: 60.21  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    292 KLLIATGSTPKTLTCKGKELdnVITirtpedANKVVRL-ASSKNAVIVGASFLGMEVAAYLCEKAHSVSVVELENIPFKK 370
Cdd:TIGR01424 133 KILIAVGGRPPKPALPGHEL--GIT------SNEAFHLpTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRGKEILRG 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    371 FlGEKVGLAIMKMFENNRVKFYMQTEVSEL-REQEGKLKeVVLKSGKVLRADVCVIGIGASPTT-GF-LKQSGVALDSRG 447
Cdd:TIGR01424 205 F-DDDMRRGLAAALEERGIRILPEDSITSIsKDDDGRLK-ATLSKHEEIVADVVLFATGRSPNTnGLgLEAAGVRLNDLG 282
                         170       180
                  ....*....|....*....|.
gi 2443331    448 YIPVNKMMQTNIPGVFAAGDV 468
Cdd:TIGR01424 283 AIAVDEYSRTSTPSIYAVGDV 303
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
198-468 1.35e-09

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 60.41  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   198 LIIGAGPAGLVCAETLRQEGFSDRIVM--------------CTSEKNLPYDRSK---LSKSMDSQAEQI-FLRSKEFFHT 259
Cdd:PRK08010   7 VIIGFGKAGKTLAVTLAKAGWRVALIEqsnamyggtcinigCIPTKTLVHDAQQhtdFVRAIQRKNEVVnFLRNKNFHNL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   260 YD---IEVLtETQVVSVDTKNKIVMFKDGFR-MEYNKLLIATGSTPKTLTCKGkeldnVITIRTPEDANKVVRLASSKNA 335
Cdd:PRK08010  87 ADmpnIDVI-DGQAEFINNHSLRVHRPEGNLeIHGEKIFINTGAQTVVPPIPG-----ITTTPGVYDSTGLLNLKELPGH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   336 V-IVGASFLGMEVAAYLCEKAHSVSVVELENIpFKKFLGEKVGLAIMKMFENNRVKFYMQTEVSELREQEGKLKevVLKS 414
Cdd:PRK08010 161 LgILGGGYIGVEFASMFANFGSKVTILEAASL-FLPREDRDIADNIATILRDQGVDIILNAHVERISHHENQVQ--VHSE 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 2443331   415 GKVLRADVCVIGIGASPTTGFL--KQSGVALDSRGYIPVNKMMQTNIPGVFAAGDV 468
Cdd:PRK08010 238 HAQLAVDALLIASGRQPATASLhpENAGIAVNERGAIVVDKYLHTTADNIWAMGDV 293
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
72-171 1.67e-09

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: 55.67  E-value: 1.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   72 VCHVKDL-ENGQMREVDLGcGKALLV--KQNGEYYAMGHKCPHYGAPLVKG-VLSKGRVRCPWHGACFN-----IATGDI 142
Cdd:cd03469   4 VGHSSELpEPGDYVTLELG-GEPLVLvrDRDGEVRAFHNVCPHRGARLCEGrGGNAGRLVCPYHGWTYDldgklVGVPRE 82
                        90       100       110
                ....*....|....*....|....*....|...
gi 2443331  143 EDFPGLD----GLPKFQVKIEKERVYIRASKQA 171
Cdd:cd03469  83 EGFPGFDkeklGLRTVPVEEWGGLIFVNLDPDA 115
PRK09965 PRK09965
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
72-165 3.74e-09

3-phenylpropionate dioxygenase ferredoxin subunit; Provisional


Pssm-ID: 170182 [Multi-domain]  Cd Length: 106  Bit Score: 54.40  E-value: 3.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    72 VCHVKDLENGQMREVDLGCGKALLvKQNGEYYAMGHKCPHYGAPLVKGVLSKG-RVRCPWHGACFNIATGDIEDFPGLDG 150
Cdd:PRK09965   6 ACPVADLPEGEALRVDTSPVIALF-NVGGEFYAIDDRCSHGNASLSEGYLEDDaTVECPLHAASFCLRTGKALCLPATDP 84
                         90
                 ....*....|....*
gi 2443331   151 LPKFQVKIEKERVYI 165
Cdd:PRK09965  85 LRTYPVHVEGGDIFI 99
Se_ygfK TIGR03315
putative selenate reductase, YgfK subunit; Members of this protein family are YgfK, predicted ...
161-472 4.16e-09

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: 59.42  E-value: 4.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331     161 ERVYIRASKQALLSQRRTKVMAKCIAlSNYSTAITNILIIGAGPAGLVCAETLRQEGFSDRIvmctseknlpYDRSKLSK 240
Cdd:TIGR03315  505 ESVNIREMKKVAAEKGYDEYKTRWHK-PQGKSSAHKVAVIGAGPAGLSAGYFLARAGHPVTV----------FEKKEKPG 573
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331     241 SMDSQAEQIFLRSKEFFHtYDIEvLTETQVVSVDTKNKIVMFKDGFRME-YNKLLIATG---STPKTLTCKG-KELDNVI 315
Cdd:TIGR03315  574 GVVKNIIPEFRISAESIQ-KDIE-LVKFHGVEFKYGCSPDLTVAELKNQgYKYVILAIGawkHGPLRLEGGGeRVLKSLE 651
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331     316 TIRTPEDANKVVRLAssKNAVIVGASFLGMEVA--AYLCEKAHSVSVV---ELENIP-FKKFLGEKVGLAIMKMFENNRV 389
Cdd:TIGR03315  652 FLRAFKEGPTINPLG--KHVVVVGGGNTAMDAAraALRVPGVEKVTVVyrrTKRYMPaSREELEEALEDGVDFKELLSPE 729
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331     390 KFYMQT---EVSELREQEGKLKEVVLKSGKV--LRADVCVIGIGASPTTGFLKQSGVALDSRGYIPVNK-MMQTNIPGVF 463
Cdd:TIGR03315  730 SFEDGTltcEVMKLGEPDASGRRRPVGTGETvdLPADTVIAAVGEQVDTDLLQKNGIPLDEYGWPVVNQaTGETNITNVF 809

                   ....*....
gi 2443331     464 AAGDVVTFP 472
Cdd:TIGR03315  810 VIGDANRGP 818
Reductase_C pfam14759
Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, ...
512-562 7.04e-09

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: 52.93  E-value: 7.04e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2443331    512 YLWTAMFGKSIRYAGHGEGFDDVIIQGDIDELKFVAFYTRNDEVIAVASMN 562
Cdd:pfam14759   1 WFWSDQYDLKLQIAGLPTGADEVVVRGDPEDGSFSVFYLRDGRLVAVDAVN 51
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
427-472 3.00e-08

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 56.32  E-value: 3.00e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 2443331   427 IGASPTTGFLKQSgVALDSRGYIPVNKMMQTNIPGVFAAGDVVTFP 472
Cdd:PRK15317 445 IGLVPNTEWLKGT-VELNRRGEIIVDARGATSVPGVFAAGDCTTVP 489
PRK06467 PRK06467
dihydrolipoamide dehydrogenase; Reviewed
419-473 3.36e-08

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 180579 [Multi-domain]  Cd Length: 471  Bit Score: 56.12  E-value: 3.36e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 2443331   419 RADVCVIGIGASPTTGFL--KQSGVALDSRGYIPVNKMMQTNIPGVFAAGDVVTFPL 473
Cdd:PRK06467 262 RYDAVLVAVGRVPNGKLLdaEKAGVEVDERGFIRVDKQCRTNVPHIFAIGDIVGQPM 318
PRK12831 PRK12831
putative oxidoreductase; Provisional
199-470 5.95e-08

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 55.02  E-value: 5.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   199 IIGAGPAGLVCAETLRQEGFSDRIVMCTSEKN--LPYD--RSKLSKSMDSQAEQIFLRSkeffhtydIEVLTETQVVSvd 274
Cdd:PRK12831 145 VIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGgvLVYGipEFRLPKETVVKKEIENIKK--------LGVKIETNVVV-- 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   275 tkNKIVMFKDGFRME-YNKLLIATGS-TPKTLTCKGKELDNVITirtpedANKVVR---------------LASSKNAVI 337
Cdd:PRK12831 215 --GKTVTIDELLEEEgFDAVFIGSGAgLPKFMGIPGENLNGVFS------ANEFLTrvnlmkaykpeydtpIKVGKKVAV 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   338 VGASFLGMEVA------------AY------LCEKAHSVSVVELENIPF------KKFLGEkvglaimkmfENNRVKfYM 393
Cdd:PRK12831 287 VGGGNVAMDAArtalrlgaevhiVYrrseeeLPARVEEVHHAKEEGVIFdlltnpVEILGD----------ENGWVK-GM 355
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   394 QTEVSELRE--QEGKLKEVVLK-SGKVLRADVCVIGIGASPTTGFLKQS-GVALDSRGYIPVNK-MMQTNIPGVFAAGDV 468
Cdd:PRK12831 356 KCIKMELGEpdASGRRRPVEIEgSEFVLEVDTVIMSLGTSPNPLISSTTkGLKINKRGCIVADEeTGLTSKEGVFAGGDA 435

                 ..
gi 2443331   469 VT 470
Cdd:PRK12831 436 VT 437
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
336-518 7.76e-08

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 54.83  E-value: 7.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   336 VIVGASFLGMEVAAYLCEKAHSVSVVeLENIPFKKFlGEKVGLAIMKMFENNRVKFYMQTEVSELREQEGKLKeVVLKSG 415
Cdd:PTZ00052 186 LIVGASYIGLETAGFLNELGFDVTVA-VRSIPLRGF-DRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDDKIK-VLFSDG 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   416 KVLRADVCVIGIGASPTTGFLK--QSGVALDSRGYIPVNKMMqTNIPGVFAAGDVVTfplafrnnkkmNVPHWQ-MAHMQ 492
Cdd:PTZ00052 263 TTELFDTVLYATGRKPDIKGLNlnAIGVHVNKSNKIIAPNDC-TNIPNIFAVGDVVE-----------GRPELTpVAIKA 330
                        170       180
                 ....*....|....*....|....*.
gi 2443331   493 GRIAALNMLAQGTEINTVPYLWTAMF 518
Cdd:PTZ00052 331 GILLARRLFKQSNEFIDYTFIPTTIF 356
PRK06115 PRK06115
dihydrolipoamide dehydrogenase; Reviewed
279-473 7.94e-08

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 180409 [Multi-domain]  Cd Length: 466  Bit Score: 54.86  E-value: 7.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   279 IVMFKDGFR--MEYNKLLIATGSTPKTLtcKGKELDNVITIrtpeDANKVVRLAS-SKNAVIVGASFLGMEVAAYLCEKA 355
Cdd:PRK06115 124 VVKAEDGSEtqLEAKDIVIATGSEPTPL--PGVTIDNQRII----DSTGALSLPEvPKHLVVIGAGVIGLELGSVWRRLG 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   356 HSVSVVE-LENIPfkKFLGEKVGLAIMKMFENNRVKFYMQTEVSELREQEG----KLKEVVLKSGKVLRADVCVIGIGAS 430
Cdd:PRK06115 198 AQVTVVEyLDRIC--PGTDTETAKTLQKALTKQGMKFKLGSKVTGATAGADgvslTLEPAAGGAAETLQADYVLVAIGRR 275
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 2443331   431 P-TTGF-LKQSGVALDSRGYIpVNKMMQTNIPGVFAAGDVVTFPL 473
Cdd:PRK06115 276 PyTQGLgLETVGLETDKRGML-ANDHHRTSVPGVWVIGDVTSGPM 319
Rieske_RO_Alpha_VanA_DdmC cd03532
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ...
90-154 8.54e-08

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: 50.83  E-value: 8.54e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2443331   90 CGK--ALLVKQNGEYYAMGHKCPHYGAPLVKGVLSKGRVRCPWHGACFNIAtGDIEDFPGLDGLPKF 154
Cdd:cd03532  25 LGEpvVLYRTQDGRVAALEDRCPHRSAPLSKGSVEGGGLVCGYHGLEFDSD-GRCVHMPGQERVPAK 90
PRK05976 PRK05976
dihydrolipoamide dehydrogenase; Validated
195-497 1.10e-07

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235660 [Multi-domain]  Cd Length: 472  Bit Score: 54.53  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   195 TNILIIGAGPAGLVCAETLRQEGFSDRIVmctseknlpyDRSKL-----------SKSMdsqaeqifLRSKEFFHT---- 259
Cdd:PRK05976   5 YDLVIIGGGPGGYVAAIRAGQLGLKTALV----------EKGKLggtclhkgcipSKAL--------LHSAEVFQTakka 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   260 --YDIEV----LTETQVVS-----VD----------TKNKIVMFK-------------------------DGFRMEYNKL 293
Cdd:PRK05976  67 spFGISVsgpaLDFAKVQErkdgiVDrltkgvaallKKGKIDVFHgigrilgpsifspmpgtvsvetetgENEMIIPENL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   294 LIATGSTPKTLtcKGKELD--NVITirtPEDANKVVRLASSknAVIVGASFLGMEVAAYLCEKAHSVSVVE-LENI-PFK 369
Cdd:PRK05976 147 LIATGSRPVEL--PGLPFDgeYVIS---SDEALSLETLPKS--LVIVGGGVIGLEWASMLADFGVEVTVVEaADRIlPTE 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   370 KflgEKVGLAIMKMFENNRVKFYMQTEVSELR-EQEGKLKEVVLKSGKVLR--ADVCVIGIGASPTTGFLKQSGVALD-S 445
Cdd:PRK05976 220 D---AELSKEVARLLKKLGVRVVTGAKVLGLTlKKDGGVLIVAEHNGEEKTleADKVLVSVGRRPNTEGIGLENTDIDvE 296
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 2443331   446 RGYIPVNKMMQTNIPGVFAAGDVVTFPlafrnnkkmnvphwQMAHM---QGRIAA 497
Cdd:PRK05976 297 GGFIQIDDFCQTKERHIYAIGDVIGEP--------------QLAHVamaEGEMAA 337
PRK07251 PRK07251
pyridine nucleotide-disulfide oxidoreductase; Provisional
337-468 1.67e-07

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 53.60  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   337 IVGASFLGMEVAAYLCEKAHSVSVVELENIPFKKFLGEKVGLAIMKMfENNRVKFYMQTEVSELREQEGKLkeVVLKSGK 416
Cdd:PRK07251 162 IIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYM-EEDGITFLLNAHTTEVKNDGDQV--LVVTEDE 238
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 2443331   417 VLRADVCVIGIGASPTTG--FLKQSGVALDSRGYIPVNKMMQTNIPGVFAAGDV 468
Cdd:PRK07251 239 TYRFDALLYATGRKPNTEplGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDV 292
Rieske_2 pfam13806
Rieske-like [2Fe-2S] domain;
72-166 2.62e-07

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


Pssm-ID: 316336 [Multi-domain]  Cd Length: 104  Bit Score: 48.70  E-value: 2.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331     72 VCHVKDLENGQMREVDLGcGK--ALLVKQNGEYYAMGHKCPHYGAplvkGVLSKGR---------VRCPWHGACFNIATG 140
Cdd:pfam13806   5 VCPLDDLPPGTGVCALVG-GEqvALFRLPDGQVYAIDNIDPFSGA----NVLSRGIvgdlggepvVASPLYKQHFDLKTG 79
                          90       100
                  ....*....|....*....|....*.
gi 2443331    141 DIEDFPGLdGLPKFQVKIEKERVYIR 166
Cdd:pfam13806  80 ECLEDPEV-SLPVYPVRVEDGNVEVR 104
PRK07846 PRK07846
mycothione reductase; Reviewed
284-468 2.63e-07

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 53.03  E-value: 2.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   284 DGFRMEYNKLLIATGSTPktlTCKGKELDNVITIRTPEDankVVRLAS-SKNAVIVGASFLGMEVAAYLCEKAHSVSVVE 362
Cdd:PRK07846 123 DGEEITADQVVIAAGSRP---VIPPVIADSGVRYHTSDT---IMRLPElPESLVIVGGGFIAAEFAHVFSALGVRVTVVN 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   363 LenipfKKFLGEKVGLAIMKMFEN---NRVKFYMQTEVSELREQEGKLkEVVLKSGKVLRADVCVIGIGASPTTGFL--K 437
Cdd:PRK07846 197 R-----SGRLLRHLDDDISERFTElasKRWDVRLGRNVVGVSQDGSGV-TLRLDDGSTVEADVLLVATGRVPNGDLLdaA 270
                        170       180       190
                 ....*....|....*....|....*....|.
gi 2443331   438 QSGVALDSRGYIPVNKMMQTNIPGVFAAGDV 468
Cdd:PRK07846 271 AAGVDVDEDGRVVVDEYQRTSAEGVFALGDV 301
Rieske_T4moC cd03474
Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske ...
72-166 6.76e-07

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: 47.72  E-value: 6.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   72 VCHVKDLENGQMREVDLGCGKALLV-KQNGEYYAMGHKCPHYGAPLVKGVLSKGRVRCPWHGACFNIATGDIEDfPGLDG 150
Cdd:cd03474   4 VCSLDDVWEGEMELVDVDGEEVLLVaPEGGEFRAFQGICPHQEIPLAEGGFDGGVLTCRAHLWQFDADTGEGLN-PRDCR 82
                        90
                ....*....|....*.
gi 2443331  151 LPKFQVKIEKERVYIR 166
Cdd:cd03474  83 LARYPVKVEGGDILVD 98
AhpF COG3634
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
196-472 7.20e-07

Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];


Pssm-ID: 226160 [Multi-domain]  Cd Length: 520  Bit Score: 51.68  E-value: 7.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  196 NILIIGAGPAGLVCA-----ETLRQEGFSDRI---VMCT-SEKNL---PY-DRSKLSKSMDSQAEQiflrskeffhtYDI 262
Cdd:COG3634 213 DVLVVGGGPAGAAAAiyaarKGIRTGLVAERFggqVLDTmGIENFisvPEtEGPKLAAALEAHVKQ-----------YDV 281
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  263 EVLTETQVVSVDTKNKI-----VMFKDGFRMEYNKLLIATGSTPKTLTCKGKEldnvitirtpEDANKVVR--------L 329
Cdd:COG3634 282 DVMNLQRASKLEPAAVEgglieVELANGAVLKARTVILATGARWRNMNVPGED----------EYRNKGVAycphcdgpL 351
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  330 ASSKNAVIVGASFLGMEVAAYLCEKAHSVSVVElenipfkkFLGEKVGLAIM--KMFENNRVKFYMQTEVSELREQEGK- 406
Cdd:COG3634 352 FKGKRVAVIGGGNSGVEAAIDLAGIVEHVTLLE--------FAPELKADAVLqdKLRSLPNVTIITNAQTTEVKGDGDKv 423
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331  407 --LKEVVLKSG--KVLRADVCVIGIGASPTTGFLKQSgVALDSRGYIPVNKMMQTNIPGVFAAGDVVTFP 472
Cdd:COG3634 424 tgLEYRDRVSGeeHHLELEGVFVQIGLLPNTEWLKGA-VELNRRGEIIVDARGETNVPGVFAAGDCTTVP 492
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
197-498 9.62e-07

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 51.65  E-value: 9.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   197 ILIIGAGPAGLVCAETLRQEGFSDRIvmctseknlpYDRSKLSKSMDSQAEQIFlRSKEFFHTYDIEVLTEtqvVSVDTK 276
Cdd:PRK12814 196 VAIIGAGPAGLTAAYYLLRKGHDVTI----------FDANEQAGGMMRYGIPRF-RLPESVIDADIAPLRA---MGAEFR 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   277 NKIVMFKD----GFRMEYNKLLIATG-STPKTLTCKGKELDNVIT-IRTPEDANKVVRLASSKNAVIVGASFLGMEVA-A 349
Cdd:PRK12814 262 FNTVFGRDitleELQKEFDAVLLAVGaQKASKMGIPGEELPGVISgIDFLRNVALGTALHPGKKVVVIGGGNTAIDAArT 341
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   350 YLCEKAHSVSVV---ELENIP-----FKKFLGEKVGL-------AIMKMfeNNRVKfyMQTEVSELRE--QEGKLKEV-V 411
Cdd:PRK12814 342 ALRLGAESVTILyrrTREEMPanraeIEEALAEGVSLrelaapvSIERS--EGGLE--LTAIKMQQGEpdESGRRRPVpV 417
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   412 LKSGKVLRADVCVIGIGASPTTGFLKQSGVALDSRGYIPVNK-MMQTNIPGVFAAGDVVTFP-LAFRnnkkmnvphwqmA 489
Cdd:PRK12814 418 EGSEFTLQADTVISAIGQQVDPPIAEAAGIGTSRNGTVKVDPeTLQTSVAGVFAGGDCVTGAdIAIN------------A 485

                 ....*....
gi 2443331   490 HMQGRIAAL 498
Cdd:PRK12814 486 VEQGKRAAH 494
PRK13984 PRK13984
putative oxidoreductase; Provisional
199-472 2.26e-06

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 50.54  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   199 IIGAGPAGLVCAETLRQEGFSDRIVMCTS-----------EKNLPYDrsklskSMDsqaeqiflRSKEFFHTYDIEVLTE 267
Cdd:PRK13984 288 IVGSGPAGLSAAYFLATMGYEVTVYESLSkpggvmrygipSYRLPDE------ALD--------KDIAFIEALGVKIHLN 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   268 TQVVsvdtknKIVMFKDgFRMEYNKLLIATGST-PKTLTCKGKELDNVIT-------IRT--------PEDANKVVRLAS 331
Cdd:PRK13984 354 TRVG------KDIPLEE-LREKHDAVFLSTGFTlGRSTRIPGTDHPDVIQalpllreIRDylrgegpkPKIPRSLVVIGG 426
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   332 SKNAVIVGASFLGMEVAAYlceKAHSVSVVELENIpFKKFL--------GEKVGLAIMK-------MFENNRVKFYMQTE 396
Cdd:PRK13984 427 GNVAMDIARSMARLQKMEY---GEVNVKVTSLERT-FEEMPadmeeieeGLEEGVVIYPgwgpmevVIENDKVKGVKFKK 502
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2443331   397 VSELREQEGKLKEVVLKSGK-VLRADVCVIGIGASPTTGFLKQS-GVALD-SRGYIPVNKMMQTNIPGVFAAGDVVTFP 472
Cdd:PRK13984 503 CVEVFDEEGRFNPKFDESDQiIVEADMVVEAIGQAPDYSYLPEElKSKLEfVRGRILTNEYGQTSIPWLFAGGDIVHGP 581
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
72-136 3.02e-06

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: 49.41  E-value: 3.02e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2443331   72 VCHVKDLENGQMREVDLGcGKALLV--KQNGEYYAMGHKCPHYGAPLVKG-VLSKGRVRCPWHGACFN 136
Cdd:COG4638  31 VAHSSELPKPDPLTVRIG-GEPLVVvrDKDGQVHALADVCPHRGARLSEGrVGGKGRLTCPYHGWTYD 97
MocE_fam_FeS TIGR02377
Rieske [2Fe-2S] domain protein, MocE subfamily; This model describes a subfamily of the ...
71-165 3.58e-06

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: 45.63  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331     71 SVCHVKDL-ENGQMREVDLGCGKALLVKQNGEYYAMGHKCPHYGAPLVKGVLSKGRVRCPWHGACFNIATGDIEDFPGLD 149
Cdd:TIGR02377   4 KACDADDIgREDVARFDHGGRTFAIYRTPDDQYYATDGLCTHEYAHLADGLVMDTTVECPKHAGCFDYRTGEALNPPVCV 83
                          90
                  ....*....|....*.
gi 2443331    150 GLPKFQVKIEKERVYI 165
Cdd:TIGR02377  84 NLKTYPVKVVDGAVYV 99
gltD_gamma_fam TIGR01318
glutamate synthase small subunit family protein, proteobacterial; This model represents one of ...
199-469 3.84e-06

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: 49.42  E-value: 3.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    199 IIGAGPAGLVCAETLRQEGFsdrivmctseKNLPYDRS--------------KLSKSMDSQAEQIFLRSKEFFHtYDIEV 264
Cdd:TIGR01318 146 VIGAGPAGLACADILARAGV----------QVVVFDRHpeigglltfgipsfKLDKAVLSRRREIFTAMGIEFR-LNCEV 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    265 LTETQVvsvdtknkivmfkDGFRMEYNKLLIATGS-TPKTLTCKGKELDNVI------------TIRTPEDANKVVRLAS 331
Cdd:TIGR01318 215 GRDISL-------------DDLLEDYDAVFLGVGTyRSMRGGLPGEDAPGVLpalpfliantrqLMGLPEEPEEPLIDVE 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    332 SKNAVIVGASFLGME-VAAYLCEKAHSVSVV---ELENIPfkkflGEKVGLAIMK----MFENNRVKFYMQ--------- 394
Cdd:TIGR01318 282 GKRVVVLGGGDTAMDcVRTAIRLGATKVTCAyrrDEANMP-----GSRREVANAReegvEFLFNVQPVSIEsdedgqvig 356
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    395 -----TEVSELREQEGKLKEVVLKSGKVLRADVCVIGIGASPTTG-FLKQSGVALDSRGYIPVNKM----MQTNIPGVFA 464
Cdd:TIGR01318 357 vtvvrTKLGEPDANGRRRPVPVAGSEFVLPADVVIMAFGFSPHLMpWLAAHGITLDSWGRIITALSsgltYQTTNPKIFA 436

                  ....*
gi 2443331    465 AGDVV 469
Cdd:TIGR01318 437 GGDAV 441
PRK10262 PRK10262
thioredoxin reductase; Provisional
191-469 1.58e-05

thioredoxin reductase; Provisional


Pssm-ID: 182343 [Multi-domain]  Cd Length: 321  Bit Score: 46.98  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   191 STAITNILIIGAGPAGLVCAETLRQEGFS----------DRIVMCTSEKNLPYDRSKLSKSMdsqaeqIFLRSKEFFHTY 260
Cdd:PRK10262   3 TTKHSKLLILGSGPAGYTAAVYAARANLQpvlitgmekgGQLTTTTEVENWPGDPNDLTGPL------LMERMHEHATKF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   261 DIEVLTEtQVVSVDTKNK-IVMFKDGFRMEYNKLLIATGSTPKTLTCKGKELDNVITIRTPEDANKVvrLASSKNAVIVG 339
Cdd:PRK10262  77 ETEIIFD-HINKVDLQNRpFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGF--FYRNQKVAVIG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   340 ASFLGMEVAAYLCEKAHSVSVVELENipfkKFLGEKVGLA-IMKMFENNRVKFYMQTEVSELREQEGKLKEVVLKSGK-- 416
Cdd:PRK10262 154 GGNTAVEEALYLSNIASEVHLIHRRD----GFRAEKILIKrLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQns 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2443331   417 ----VLRADVCVIGIGASPTTGFLKqsGVALDSRGYIPVNKMM-----QTNIPGVFAAGDVV 469
Cdd:PRK10262 230 dnieSLDVAGLFVAIGHSPNTAIFE--GQLELENGYIKVQSGIhgnatQTSIPGVFAAGDVM 289
Rieske_RO_Alpha_PhDO_like cd03479
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ...
99-167 2.87e-05

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: 44.16  E-value: 2.87e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2443331   99 NGEYYAMGHKCPHYGAPLVKGVLSKGRVRCPWHGACFNiATGDIEDFPGldGLPKFQVkieKERVYIRA 167
Cdd:cd03479  54 SGRVGLLDEHCPHRGASLVFGRVEECGLRCCYHGWKFD-VDGQCLEMPS--EPPDSQL---KQKVRQPA 116
Rieske_RO_Alpha_PaO cd03480
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ...
97-146 5.01e-05

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: 43.08  E-value: 5.01e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 2443331   97 KQNGEYYAMGHKCPHYGAPLVKGVLS-KGRVRCPWHGACFNiATGDIEDFP 146
Cdd:cd03480  48 RNSQQWRAFDDQCPHRLAPLSEGRIDeEGCLECPYHGWSFD-GSGSCQRIP 97
Rieske_RO_Alpha_OMO_CARDO cd03548
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ...
76-144 6.75e-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: 42.79  E-value: 6.75e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2443331   76 KDLENGQMREVDLgCG-KALLVKQNGEYYAMGHKCPHYGAPLVKGV--LSKGRVRCPWHGACFNIATGDIED 144
Cdd:cd03548  22 HELEEGEPKGIQL-CGePILLRRVDGKVYALKDRCLHRGVPLSKKPecFTKGTITCWYHGWTYRLDDGKLVT 92
PRK12778 PRK12778
putative bifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta; ...
418-470 1.82e-04

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 44.35  E-value: 1.82e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 2443331   418 LRADVCVIGIGASPTTGFLKQ-SGVALDSRGYIPVNKMMQTNIPGVFAAGDVVT 470
Cdd:PRK12778 673 VDVDLVIVSVGVSPNPLVPSSiPGLELNRKGTIVVDEEMQSSIPGIYAGGDIVR 726
PTZ00153 PTZ00153
lipoamide dehydrogenase; Provisional
276-467 5.62e-04

lipoamide dehydrogenase; Provisional


Pssm-ID: 173442 [Multi-domain]  Cd Length: 659  Bit Score: 42.59  E-value: 5.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   276 KNKIVMFKDGFRMEYNKLLIATGSTPKTLTckGKELDNvITIRTPEDANKVVRLASSKNavIVGASFLGMEVAAYLCEKA 355
Cdd:PTZ00153 261 KNTIKSEKSGKEFKVKNIIIATGSTPNIPD--NIEVDQ-KSVFTSDTAVKLEGLQNYMG--IVGMGIIGLEFMDIYTALG 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   356 HSVSVVEL--ENIPFkkfLGEKVGLAIMKMFENNR-VKFYMQTEVSELR----------------EQEGKLKEVVLKSGK 416
Cdd:PTZ00153 336 SEVVSFEYspQLLPL---LDADVAKYFERVFLKSKpVRVHLNTLIEYVRagkgnqpviighserqTGESDGPKKNMNDIK 412
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2443331   417 VLRADVCVIGIGASPTTgflkqSGVALDS------RGYIPVNKMMQTN------IPGVFAAGD 467
Cdd:PTZ00153 413 ETYVDSCLVATGRKPNT-----NNLGLDKlkiqmkRGFVSVDEHLRVLredqevYDNIFCIGD 470
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
197-219 7.01e-04

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 223717 [Multi-domain]  Cd Length: 396  Bit Score: 42.06  E-value: 7.01e-04
                        10        20
                ....*....|....*....|...
gi 2443331  197 ILIIGAGPAGLVCAETLRQEGFS 219
Cdd:COG0644   6 VVIVGAGPAGSSAARRLAKAGLD 28
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
199-219 7.57e-04

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 316012 [Multi-domain]  Cd Length: 66  Bit Score: 37.88  E-value: 7.57e-04
                          10        20
                  ....*....|....*....|.
gi 2443331    199 IIGAGPAGLVCAETLRQEGFS 219
Cdd:pfam13450   1 IVGAGLAGLVAAYLLAKRGKR 21
Rieske_NirD cd03529
Assimilatory nitrite reductase (NirD) family, Rieske domain; Assimilatory nitrate and nitrite ...
71-165 1.32e-03

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: 38.26  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331   71 SVCHVKDLENGQmrevdlgcGKALLVKQ---------NGEYYAMGHKCPHYGAplvkGVLSKG---------RVRCPWHG 132
Cdd:cd03529   3 TVCALDDLPPGS--------GVAALVGDtqiaifrlpGREVYAVQNMDPHSRA----NVLSRGivgdiggepVVASPLYK 70
                        90       100       110
                ....*....|....*....|....*....|...
gi 2443331  133 ACFNIATGDIEDFPGLDgLPKFQVKIEKERVYI 165
Cdd:cd03529  71 QHFSLKTGRCLEDEDVS-VATFPVRVEDGEVYV 102
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
393-470 2.84e-03

putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 40.69  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331    393 MQTEVSELRE--QEGKLKEVVLKSGKVLRADVCVIGIGASPTTgFLKQS--GVALDSRGYI-----PVNKMMQTNIPGVF 463
Cdd:PRK12775  646 MKVEEMELGEpdEKGRRKPMPTGEFKDLECDTVIYALGTKANP-IITQStpGLALNKWGNIaaddgKLESTQSTNLPGVF 724

                  ....*..
gi 2443331    464 AAGDVVT 470
Cdd:PRK12775  725 AGGDIVT 731
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
71-166 3.35e-03

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: 37.30  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443331     71 SVCHVKDLENGQMREVDLGCGKALLVKQNG-EYYAMGHKCPHYGAplvkGVLSKG---------RVRCPWH--------G 132
Cdd:TIGR02378   4 DICAIDDIPEETGVCVLLGDTQIAIFRVPGdQVFAIQNMCPHKRA----FVLSRGivgdaqgelWVACPLHkrnfrledG 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2443331    133 ACFNIATGDIEDFPgldglpkfqVKIEKERVYIR 166
Cdd:TIGR02378  80 RCLEDDSGSVRTYE---------VRVEDGRVYVA 104
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
197-219 3.71e-03

Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];


Pssm-ID: 225915 [Multi-domain]  Cd Length: 331  Bit Score: 39.79  E-value: 3.71e-03
                        10        20
                ....*....|....*....|...
gi 2443331  197 ILIIGAGPAGLVCAETLRQEGFS 219
Cdd:COG3380   4 IAIVGAGIAGLAAAYALREAGRE 26
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
418-472 7.44e-03

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 39.09  E-value: 7.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 2443331   418 LRADVCVIGIGASPTTGFLKQSGVALDSRGYIPVNKM-MQTNIPGVFAAGDVVTFP 472
Cdd:PRK12771 367 LEADLVVLAIGQDIDSAGLESVPGVEVGRGVVQVDPNfMMTGRPGVFAGGDMVPGP 422
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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