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Conserved domains on  [gi|28278121|gb|AAH45265|]
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Dia1 protein [Xenopus laevis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02252 super family cl33442
nitrate reductase [NADPH]
29-301 3.20e-131

nitrate reductase [NADPH]


The actual alignment was detected with superfamily member PLN02252:

Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 393.66  E-value: 3.20e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   29 KPRPAITLeSPDIKYALRLIDREEISHDTRRFRFALPSPEHVLGLPIGQHIYLSARVDGNLVVRPYTPVSSDDNKGYVDL 108
Cdd:PLN02252 622 APGRPVAL-NPREKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFEL 700
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  109 VVKIYFKNVHPKFPEGGKMSQYLDSLRKDETIDFRGPSGLLVYSGKGTFQIrpDKKsppvPKKANHLGMIAGGTGITPML 188
Cdd:PLN02252 701 VIKVYFKNVHPKFPNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFLV--NGK----PKFAKKLAMLAGGTGITPMY 774
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  189 QLIRAILKDKEDKTICYLLFANQTEKDILLRSELEEIRANHPSRFKLWYTLDR-APEDWDYSQGFVNEDMISSFMPPPGD 267
Cdd:PLN02252 775 QVIQAILRDPEDKTEMSLVYANRTEDDILLREELDRWAAEHPDRLKVWYVVSQvKREGWKYSVGRVTEAMLREHLPEGGD 854
                        250       260       270
                 ....*....|....*....|....*....|....
gi 28278121  268 DVLILMCGPPPMVQYAINPSLDKLSYPQDRRFAY 301
Cdd:PLN02252 855 ETLALMCGPPPMIEFACQPNLEKMGYDKDSILVF 888
 
Name Accession Description Interval E-value
PLN02252 PLN02252
nitrate reductase [NADPH]
29-301 3.20e-131

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 393.66  E-value: 3.20e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   29 KPRPAITLeSPDIKYALRLIDREEISHDTRRFRFALPSPEHVLGLPIGQHIYLSARVDGNLVVRPYTPVSSDDNKGYVDL 108
Cdd:PLN02252 622 APGRPVAL-NPREKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFEL 700
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  109 VVKIYFKNVHPKFPEGGKMSQYLDSLRKDETIDFRGPSGLLVYSGKGTFQIrpDKKsppvPKKANHLGMIAGGTGITPML 188
Cdd:PLN02252 701 VIKVYFKNVHPKFPNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFLV--NGK----PKFAKKLAMLAGGTGITPMY 774
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  189 QLIRAILKDKEDKTICYLLFANQTEKDILLRSELEEIRANHPSRFKLWYTLDR-APEDWDYSQGFVNEDMISSFMPPPGD 267
Cdd:PLN02252 775 QVIQAILRDPEDKTEMSLVYANRTEDDILLREELDRWAAEHPDRLKVWYVVSQvKREGWKYSVGRVTEAMLREHLPEGGD 854
                        250       260       270
                 ....*....|....*....|....*....|....
gi 28278121  268 DVLILMCGPPPMVQYAINPSLDKLSYPQDRRFAY 301
Cdd:PLN02252 855 ETLALMCGPPPMIEFACQPNLEKMGYDKDSILVF 888
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
45-301 1.81e-123

Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH.


Pssm-ID: 99780  Cd Length: 234  Bit Score: 352.25  E-value: 1.81e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  45 LRLIDREEISHDTRRFRFALPSPEHVLGLPIGQHIYLSARVDGNLVVRPYTPVSSDDNKGYVDLVVKIYFknvhpkfpeG 124
Cdd:cd06183   1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYP---------G 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 125 GKMSQYLDSLRKDETIDFRGPSGLLVYSGKGtfqirpdkksppvpkKANHLGMIAGGTGITPMLQLIRAILKDKEDKTIC 204
Cdd:cd06183  72 GKMSQYLHSLKPGDTVEIRGPFGKFEYKPNG---------------KVKHIGMIAGGTGITPMLQLIRAILKDPEDKTKI 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 205 YLLFANQTEKDILLRSELEEIRANHPSRFKLWYTLDRAPEDWDYSQGFVNEDMISSFMPP-PGDDVLILMCGPPPMVQYA 283
Cdd:cd06183 137 SLLYANRTEEDILLREELDELAKKHPDRFKVHYVLSRPPEGWKGGVGFITKEMIKEHLPPpPSEDTLVLVCGPPPMIEGA 216
                       250
                ....*....|....*...
gi 28278121 284 INPSLDKLSYPQDRRFAY 301
Cdd:cd06183 217 VKGLLKELGYKKDNVFKF 234
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
44-151 1.10e-46

Oxidoreductase FAD-binding domain;


Pssm-ID: 334332 [Multi-domain]  Cd Length: 99  Bit Score: 151.97  E-value: 1.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121    44 ALRLIDREEISHDTRRFRFALPSPEHVLGLPIGQHIYLSARVDGNLVVRPYTPVSSDDNKGYVDLVVKIYfknvhpkfpE 123
Cdd:pfam00970   1 PLTLVEKEEVSHDTRIFRFALPHPDQVLGLPVGQHVFLRLPIDGELVIRSYTPISSDDDKGFLELLVKVY---------P 71
                          90       100
                  ....*....|....*....|....*...
gi 28278121   124 GGKMSQYLDSLRKDETIDFRGPSGLLVY 151
Cdd:pfam00970  72 GGKMSQYLDELKIGDTIDFKGPLGHFEY 99
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
37-285 1.55e-40

NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];


Pssm-ID: 223617 [Multi-domain]  Cd Length: 252  Bit Score: 141.39  E-value: 1.55e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  37 ESPDIKYALRLIDREEISHDTRRFRFALPSPEhvLGLPIGQhiYLSARVDGnLVVRPYTPVSSDDNKGYVDLVVKIYfkn 116
Cdd:COG0543   2 NPLALLMSYKVVEKEEISPDTFLLRLRLPFVA--LTFKPGQ--FVMLRVPG-GVRRPYSLASAPDDKGELELHIRVY--- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 117 vhpkfpEGGKMSQYLDSLRKDETIDFRGPSGllvySGKgtfqirpdkkspPVPKKANHLGMIAGGTGITPMLQLIRAiLK 196
Cdd:COG0543  74 ------EVGKVTKYIFGLKEGDKIRVRGPLG----NGF------------LREKIGKPVLLIAGGTGIAPLYAIAKE-LK 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 197 DKEDKTICYLLFANQTEKDILLRSELEEIRANHPSrfklwYTLDrapEDWDYSQGFVNEDMISSFMPPPGDDVLIlmCGP 276
Cdd:COG0543 131 EKGDANKVTLLYGARTAKDLLLLDELEELAEKEVH-----PVTD---DGWKGRKGFVTTDVLKELLDLEVDDVYI--CGP 200

                ....*....
gi 28278121 277 PPMVQYAIN 285
Cdd:COG0543 201 PAMVKAVRE 209
PA_CoA_Oxy5 TIGR02160
phenylacetate-CoA oxygenase/reductase, PaaK subunit; Phenylacetate-CoA oxygenase is comprised ...
43-283 1.73e-21

phenylacetate-CoA oxygenase/reductase, PaaK subunit; Phenylacetate-CoA oxygenase is comprised of a five gene complex responsible for the hydroxylation of phenylacetate-CoA (PA-CoA) as the second catabolic step in phenylacetic acid (PA) degradation. Although the exact function of this enzyme has not been determined, it has been shown to be required for phenylacetic acid degradation and has been proposed to function in a multicomponent oxygenase acting on phenylacetate-CoA. [Energy metabolism, Other]


Pssm-ID: 131215 [Multi-domain]  Cd Length: 352  Bit Score: 92.58  E-value: 1.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121    43 YALRLIDREEISHDTRRFRFALPSP--EHVLGLPiGQHIYLSARVDGNLVVRPYTPVSsddnkGYVDLVVKIYFKNVhpk 120
Cdd:TIGR02160   2 HRLTVAEVERLTADAVAISFEIPDElaEDYRFAP-GQHLTLRREVDGEELRRSYSICS-----APAPGEIRVAVKKI--- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   121 fpEGGKMSQYL-DSLRKDETIDFRGPSGLLVYsgkgtfqirpdkksPPVPKKANHLGMIAGGTGITPMLQLIRAILKdKE 199
Cdd:TIGR02160  73 --PGGLFSTWAnDEIRPGDTLEVMAPQGLFTP--------------DLSTPHAGHYVAVAAGSGITPMLSIAETVLA-AE 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   200 DKTICYLLFANQTEKDILLRSELEEIRANHPSRFKLWYTLDRAPEDWDYSQGFVNEDMISSFMpppgdDVLI-------- 271
Cdd:TIGR02160 136 PRSTFTLVYGNRRTASVMFAEELADLKDKHPQRFHLAHVLSREPREAPLLSGRLDGERLAALL-----DSLIdvdradew 210
                         250
                  ....*....|..
gi 28278121   272 LMCGPPPMVQYA 283
Cdd:TIGR02160 211 FLCGPQAMVDDA 222
 
Name Accession Description Interval E-value
PLN02252 PLN02252
nitrate reductase [NADPH]
29-301 3.20e-131

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 393.66  E-value: 3.20e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   29 KPRPAITLeSPDIKYALRLIDREEISHDTRRFRFALPSPEHVLGLPIGQHIYLSARVDGNLVVRPYTPVSSDDNKGYVDL 108
Cdd:PLN02252 622 APGRPVAL-NPREKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFEL 700
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  109 VVKIYFKNVHPKFPEGGKMSQYLDSLRKDETIDFRGPSGLLVYSGKGTFQIrpDKKsppvPKKANHLGMIAGGTGITPML 188
Cdd:PLN02252 701 VIKVYFKNVHPKFPNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFLV--NGK----PKFAKKLAMLAGGTGITPMY 774
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  189 QLIRAILKDKEDKTICYLLFANQTEKDILLRSELEEIRANHPSRFKLWYTLDR-APEDWDYSQGFVNEDMISSFMPPPGD 267
Cdd:PLN02252 775 QVIQAILRDPEDKTEMSLVYANRTEDDILLREELDRWAAEHPDRLKVWYVVSQvKREGWKYSVGRVTEAMLREHLPEGGD 854
                        250       260       270
                 ....*....|....*....|....*....|....
gi 28278121  268 DVLILMCGPPPMVQYAINPSLDKLSYPQDRRFAY 301
Cdd:PLN02252 855 ETLALMCGPPPMIEFACQPNLEKMGYDKDSILVF 888
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
45-301 1.81e-123

Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH.


Pssm-ID: 99780  Cd Length: 234  Bit Score: 352.25  E-value: 1.81e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  45 LRLIDREEISHDTRRFRFALPSPEHVLGLPIGQHIYLSARVDGNLVVRPYTPVSSDDNKGYVDLVVKIYFknvhpkfpeG 124
Cdd:cd06183   1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYP---------G 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 125 GKMSQYLDSLRKDETIDFRGPSGLLVYSGKGtfqirpdkksppvpkKANHLGMIAGGTGITPMLQLIRAILKDKEDKTIC 204
Cdd:cd06183  72 GKMSQYLHSLKPGDTVEIRGPFGKFEYKPNG---------------KVKHIGMIAGGTGITPMLQLIRAILKDPEDKTKI 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 205 YLLFANQTEKDILLRSELEEIRANHPSRFKLWYTLDRAPEDWDYSQGFVNEDMISSFMPP-PGDDVLILMCGPPPMVQYA 283
Cdd:cd06183 137 SLLYANRTEEDILLREELDELAKKHPDRFKVHYVLSRPPEGWKGGVGFITKEMIKEHLPPpPSEDTLVLVCGPPPMIEGA 216
                       250
                ....*....|....*...
gi 28278121 284 INPSLDKLSYPQDRRFAY 301
Cdd:cd06183 217 VKGLLKELGYKKDNVFKF 234
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
23-301 1.81e-120

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521  Cd Length: 300  Bit Score: 347.20  E-value: 1.81e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   23 FQRFFGKPRPAITLEsPDIKYALRLIDREEISHDTRRFRFALPSPEHVLGLPIGQHIYLSARVDGN----LVVRPYTPVS 98
Cdd:PTZ00319  15 FFAFMFSRSPPVALD-PDMFQHFKLIKKTEVTHDTFIFRFALHSPTQRLGLPIGQHIVFRCDCTTPgkpeTVQHSYTPIS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   99 SDDNKGYVDLVVKIYFKNVHPKFPEGGKMSQYLDSLRKDETIDFRGPSGLLVYSGKGTFQIRPDKKSpPVPKKANHLGMI 178
Cdd:PTZ00319  94 SDDEKGYVDFLIKVYFKGVHPSFPNGGRLSQHLYHMKLGDKIEMRGPVGKFEYLGNGTYTVHKGKGG-LKTMHVDAFAMI 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  179 AGGTGITPMLQLIRAILKDKEDKTICYLLFANQTEKDILLRSELEEIrANHPsRFKLWYTLDR-APEDWDYSQGFVNEDM 257
Cdd:PTZ00319 173 AGGTGITPMLQIIHAIKKNKEDRTKVFLVYANQTEDDILLRKELDEA-AKDP-RFHVWYTLDReATPEWKYGTGYVDEEM 250
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 28278121  258 ISSFMPPPG------DDVLILMCGPPPMVQYAINPSLDKLSYPQDRRFAY 301
Cdd:PTZ00319 251 LRAHLPVPDpqnsgiKKVMALMCGPPPMLQMAVKPNLEKIGYTADNMFTF 300
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
51-297 7.56e-47

Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99778 [Multi-domain]  Cd Length: 223  Bit Score: 156.84  E-value: 7.56e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  51 EEISHDTRRFRFALPSPehvLGLPIGQHIYLSARVDGNLVVRPYTPVSSDDNKGYVDLVVKIYfknvhpkfpEGGKMSQY 130
Cdd:cd00322   4 EDVTDDVRLFRLQLPNG---FSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEGELELTVKIV---------PGGPFSAW 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 131 LDSLRKDETIDFRGPsgllvysgKGTFQIRPDKKSPpvpkkanhLGMIAGGTGITPMLQLIRAILKDKEDKTIcYLLFAN 210
Cdd:cd00322  72 LHDLKPGDEVEVSGP--------GGDFFLPLEESGP--------VVLIAGGIGITPFRSMLRHLAADKPGGEI-TLLYGA 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 211 QTEKDILLRSELEEIRANHPsRFKLWYTLDRAPEDWDYSQGFVNEDMISSFMPPPGDDVLILMCGPPPMVQyAINPSLDK 290
Cdd:cd00322 135 RTPADLLFLDELEELAKEGP-NFRLVLALSRESEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAK-AVREALVS 212

                ....*..
gi 28278121 291 LSYPQDR 297
Cdd:cd00322 213 LGVPEER 219
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
44-151 1.10e-46

Oxidoreductase FAD-binding domain;


Pssm-ID: 334332 [Multi-domain]  Cd Length: 99  Bit Score: 151.97  E-value: 1.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121    44 ALRLIDREEISHDTRRFRFALPSPEHVLGLPIGQHIYLSARVDGNLVVRPYTPVSSDDNKGYVDLVVKIYfknvhpkfpE 123
Cdd:pfam00970   1 PLTLVEKEEVSHDTRIFRFALPHPDQVLGLPVGQHVFLRLPIDGELVIRSYTPISSDDDKGFLELLVKVY---------P 71
                          90       100
                  ....*....|....*....|....*...
gi 28278121   124 GGKMSQYLDSLRKDETIDFRGPSGLLVY 151
Cdd:pfam00970  72 GGKMSQYLDELKIGDTIDFKGPLGHFEY 99
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
177-283 2.84e-46

Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.


Pssm-ID: 333901  Cd Length: 108  Bit Score: 151.24  E-value: 2.84e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   177 MIAGGTGITPMLQLIRAILKDKEDKTICYLLFANQTEKDILLRSELEEIRANHPSRFKLWYTLDRAPEDWDYSQGFVNED 256
Cdd:pfam00175   1 MIAGGTGITPVRSVLRAVLEDPDDPTQVWLVFGNRNEDDILYREELDELAAKYPGRLRVVYVVSRPEAGWTGGKGYVQDA 80
                          90       100
                  ....*....|....*....|....*..
gi 28278121   257 MISSFMPPPGDDVLILMCGPPPMVQYA 283
Cdd:pfam00175  81 VLEDHLSLPDEETHVYVCGPPGMIKAV 107
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
37-285 1.55e-40

NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];


Pssm-ID: 223617 [Multi-domain]  Cd Length: 252  Bit Score: 141.39  E-value: 1.55e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  37 ESPDIKYALRLIDREEISHDTRRFRFALPSPEhvLGLPIGQhiYLSARVDGnLVVRPYTPVSSDDNKGYVDLVVKIYfkn 116
Cdd:COG0543   2 NPLALLMSYKVVEKEEISPDTFLLRLRLPFVA--LTFKPGQ--FVMLRVPG-GVRRPYSLASAPDDKGELELHIRVY--- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 117 vhpkfpEGGKMSQYLDSLRKDETIDFRGPSGllvySGKgtfqirpdkkspPVPKKANHLGMIAGGTGITPMLQLIRAiLK 196
Cdd:COG0543  74 ------EVGKVTKYIFGLKEGDKIRVRGPLG----NGF------------LREKIGKPVLLIAGGTGIAPLYAIAKE-LK 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 197 DKEDKTICYLLFANQTEKDILLRSELEEIRANHPSrfklwYTLDrapEDWDYSQGFVNEDMISSFMPPPGDDVLIlmCGP 276
Cdd:COG0543 131 EKGDANKVTLLYGARTAKDLLLLDELEELAEKEVH-----PVTD---DGWKGRKGFVTTDVLKELLDLEVDDVYI--CGP 200

                ....*....
gi 28278121 277 PPMVQYAIN 285
Cdd:COG0543 201 PAMVKAVRE 209
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
55-297 4.42e-38

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99813  Cd Length: 235  Bit Score: 134.32  E-value: 4.42e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  55 HDTRRFRFALPSPEHVLGLPiGQHIYLSARV-DGNLVVRPYTPVSSDDNKGYVDLVVKIYfknvhpkfpEGGKMSQYL-D 132
Cdd:cd06217  14 PTVKTFRLAVPDGVPPPFLA-GQHVDLRLTAiDGYTAQRSYSIASSPTQRGRVELTVKRV---------PGGEVSPYLhD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 133 SLRKDETIDFRGPSGllvysgkgTFQIRPDKKSPPVpkkanhlgMIAGGTGITPMLQLIRAILkDKEDKTICYLLFANQT 212
Cdd:cd06217  84 EVKVGDLLEVRGPIG--------TFTWNPLHGDPVV--------LLAGGSGIVPLMSMIRYRR-DLGWPVPFRLLYSART 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 213 EKDILLRSELEEIRANHPsRFKLWYTLDR-APEDWDYSQGFVNEDMISSFmPPPGDDVLILMCGPPPMVQYAINpSLDKL 291
Cdd:cd06217 147 AEDVIFRDELEQLARRHP-NLHVTEALTRaAPADWLGPAGRITADLIAEL-VPPLAGRRVYVCGPPAFVEAATR-LLLEL 223

                ....*.
gi 28278121 292 SYPQDR 297
Cdd:cd06217 224 GVPRDR 229
PTZ00274 PTZ00274
cytochrome b5 reductase; Provisional
53-282 5.67e-37

cytochrome b5 reductase; Provisional


Pssm-ID: 140300  Cd Length: 325  Bit Score: 133.89  E-value: 5.67e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   53 ISHDTRRFRFALPSPEHVLGLPIG--QHIYLSARVDGNLVVRPYTPVSSDDNKGYVDLVVKiyfknvhpkFPEGGKMSQY 130
Cdd:PTZ00274  63 ITHDTALFRFLLHSEEEFNLKPCStlQACYKYGVQPMDQCQRFYTPVTANHTKGYFDIIVK---------RKKDGLMTNH 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  131 LDSLRKDETIDFRGPSGLLVYSgkgtfqirpdkksppvPKKANHLGMIAGGTGITPMLQLIRAILKDK-----EDKTICY 205
Cdd:PTZ00274 134 LFGMHVGDKLLFRSVTFKIQYR----------------PNRWKHVGMIAGGTGFTPMLQIIRHSLTEPwdsgeVDRTKLS 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  206 LLFANQTEKDILLRSELEEIRANHPSRFKLWYTLDRA--PEDWDYSQGFVNEDMISSFMPPPGDD-VLILMCGPPPMVQY 282
Cdd:PTZ00274 198 FLFCNRTERHILLKGLFDDLARRYSNRFKVYYTIDQAvePDKWNHFLGYVTKEMVRRTMPAPEEKkKIIMLCGPDQLLNH 277
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
45-297 5.87e-32

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal portion of the FAD/NAD binding domain contains most of the NADP(H) binding residues and the N-terminal sub-domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. In this ferredoxin like sub-group, the FAD/NAD sub-domains is typically fused to a C-terminal iron-sulfur binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins which act as electron carriers in photosynthesis and ferredoxins which participate in redox chains from bacteria to mammals. Ferredoxin reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99811  Cd Length: 231  Bit Score: 118.08  E-value: 5.87e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  45 LRLIDREEISHDTRRFRFALPSPEHVLGLPiGQHIYLSARVDGNLVVRPYTPVSSDDNKGYVDLVVKiyfkNVhpkfpEG 124
Cdd:cd06215   1 LRCVKIIQETPDVKTFRFAAPDGSLFAYKP-GQFLTLELEIDGETVYRAYTLSSSPSRPDSLSITVK----RV-----PG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 125 GKMSQYL-DSLRKDETIDFRGPSGLLVYsgkgtfqirpdkksppVPKKANHLGMIAGGTGITPMLQLIRAILKDKEDKTI 203
Cdd:cd06215  71 GLVSNWLhDNLKVGDELWASGPAGEFTL----------------IDHPADKLLLLSAGSGITPMMSMARWLLDTRPDADI 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 204 CYLLFAnQTEKDILLRSELEEIRANHPSrFKLWYTL-DRAPEDWDYSQGFVNEDMISSFMPppgdDVL---ILMCGPPPM 279
Cdd:cd06215 135 VFIHSA-RSPADIIFADELEELARRHPN-FRLHLILeQPAPGAWGGYRGRLNAELLALLVP----DLKertVFVCGPAGF 208
                       250
                ....*....|....*...
gi 28278121 280 VQyAINPSLDKLSYPQDR 297
Cdd:cd06215 209 MK-AVKSLLAELGFPMSR 225
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
57-293 6.95e-32

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 124.89  E-value: 6.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121    57 TRRFRFALPSPEHVLGLPIGQHIYLSARVDGNLVVRPYTPVSSDDNKGYVDLVVKiyfknvhpkfPEGGKMSQYLDSLRK 136
Cdd:PTZ00306  932 SRVLRFNLPGALQRSGLTLGQFIAIRGDWDGQQLIGYYSPITLPDDLGVISILAR----------GDKGTLKEWISALRP 1001
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   137 DETIDFRGPSGLLVysgkgtfQIRPDKKSPPVPK-KANHLGMIAGGTGITPMLQLIRAILKDKEDKTI--CYLLFANQTE 213
Cdd:PTZ00306 1002 GDSVEMKACGGLRI-------ERRPADKQFVFRGhVIRKLALIAGGTGVAPMLQIIRAALKKPYVDSIesIRLIYAAEDV 1074
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   214 KDILLRSELEEIRANHPSRFKLWYTLDRAPEDWDYSQGFVNEDMISSFMPPPGDDVLILMCGPPPMvQYAINPSLDKLSY 293
Cdd:PTZ00306 1075 SELTYRELLESYRKENPGKFKCHFVLNNPPEGWTDGVGFVDRALLQSALQPPSKDLLVAICGPPVM-QRAVKADLLALGY 1153
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
43-281 7.74e-32

NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation oxidoreductase. PA oxidoreductases of E. coli hydroxylate PA-CoA in the second step of PA degradation. Members of this group typically fuse a ferredoxin reductase-like domain with an iron-sulfur binding cluster domain. Ferredoxins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal portion may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria and participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99810  Cd Length: 241  Bit Score: 118.03  E-value: 7.74e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  43 YALRLIDREEISHDTRRFRFALPSP-EHVLGLPIGQHIYLSARVDGNLVVRPY---TPVSSDDnkgyvdlvVKIYFKNVh 118
Cdd:cd06214   2 HPLTVAEVVRETADAVSITFDVPEElRDAFRYRPGQFLTLRVPIDGEEVRRSYsicSSPGDDE--------LRITVKRV- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 119 pkfpEGGKMSQYL-DSLRKDETIDFRGPSGLLVYsgkgtfqirpdkksPPVPKKANHLGmIAGGTGITPMLQLIRAILKD 197
Cdd:cd06214  73 ----PGGRFSNWAnDELKAGDTLEVMPPAGRFTL--------------PPLPGARHYVL-FAAGSGITPVLSILKTALAR 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 198 KEDKTICyLLFANQTEKDILLRSELEEIRANHPSRFKLWYTLDRAPEDWDYSQGFVNEDMISSFMPPPGDDVLI---LMC 274
Cdd:cd06214 134 EPASRVT-LVYGNRTEASVIFREELADLKARYPDRLTVIHVLSREQGDPDLLRGRLDAAKLNALLKNLLDATEFdeaFLC 212

                ....*..
gi 28278121 275 GPPPMVQ 281
Cdd:cd06214 213 GPEPMMD 219
Fpr COG1018
Ferredoxin-NADP reductase [Energy production and conversion];
43-297 8.44e-29

Ferredoxin-NADP reductase [Energy production and conversion];


Pssm-ID: 223949 [Multi-domain]  Cd Length: 266  Bit Score: 110.84  E-value: 8.44e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  43 YALRLIDREEISHDTRRFRFALPSPEHVLGLPiGQHIYLSARVDGNLVVRPYTPVSSDDNKGYVDLVVKIyfknvhpkfP 122
Cdd:COG1018   6 RRVTVTSVEPETDDVFSFTLEPPDGLRLDFEP-GQYITVGLPNGGEPLLRAYSLSSAPDEDSLYRISVKR---------E 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 123 EGGKMSQYL-DSLRKDETIDFRGPSGLLVYsgkgtfqirpdkksPPVPkkANHLGMIAGGTGITPMLQLIRAILKDKEDK 201
Cdd:COG1018  76 DGGGGSNWLhDHLKVGDTLEVSAPAGDFVL--------------DDLP--ERKLLLLAGGIGITPFLSMLRTLLDRGPAD 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 202 TIcyLLFANQTEKDILLRSElEEIRANHPSRFKL-WYTldrapeDWDYSQGFVNEDMISSFMPPPGDDVLIlmCGPPPMV 280
Cdd:COG1018 140 VV--LVHAARTPADLAFRDE-LELAAELPNALLLgLYT------ERGKLQGRIDVSRLLSAAPDGGREVYL--CGPGPFM 208
                       250
                ....*....|....*..
gi 28278121 281 QYAINPsLDKLSYPQDR 297
Cdd:COG1018 209 QAVRLA-LEALGVPDDR 224
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
43-297 1.47e-27

Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal region may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99793  Cd Length: 218  Bit Score: 106.17  E-value: 1.47e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  43 YALRLIDREEISHDTRRFRFALPspeHVLGLPIGQHIYLSARVDG-NLVVRPYTPVSSDDNKgYVDLVVKIYfknvhpkf 121
Cdd:cd06196   1 HTVTLLSIEPVTHDVKRLRFDKP---EGYDFTPGQATEVAIDKPGwRDEKRPFTFTSLPEDD-VLEFVIKSY-------- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 122 PEGGKMSQYLDSLRKDETIDFRGPSGLLVYSGKGTFqirpdkksppvpkkanhlgmIAGGTGITPMLQLIRAILKDKEDK 201
Cdd:cd06196  69 PDHDGVTEQLGRLQPGDTLLIEDPWGAIEYKGPGVF--------------------IAGGAGITPFIAILRDLAAKGKLE 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 202 TiCYLLFANQTEKDILLRSELEEIRANhpsrfKLWYTLDRAPeDWDYSQGFVNEDMISSFMPPPGDDVLIlmCGPPPMVQ 281
Cdd:cd06196 129 G-NTLIFANKTEKDIILKDELEKMLGL-----KFINVVTDEK-DPGYAHGRIDKAFLKQHVTDFNQHFYV--CGPPPMEE 199
                       250
                ....*....|....*.
gi 28278121 282 yAINPSLDKLSYPQDR 297
Cdd:cd06196 200 -AINGALKELGVPEDS 214
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
46-281 8.33e-24

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99812  Cd Length: 243  Bit Score: 96.91  E-value: 8.33e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  46 RLIDREEISHDTRRFRFAlPSPEHVLGLPiGQHIYLSARVDGNLVVRPYTPVSSDDNK-GYVDLVVKIyfknvHPkfpeG 124
Cdd:cd06216  21 RVVAVRPETADMVTLTLR-PNRGWPGHRA-GQHVRLGVEIDGVRHWRSYSLSSSPTQEdGTITLTVKA-----QP----D 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 125 GKMSQYL-DSLRKDETIDFRGPsgllvysgKGTFQIrPDKKSPPvpkkanhLGMIAGGTGITPMLQLIRAILKDKEDKTI 203
Cdd:cd06216  90 GLVSNWLvNHLAPGDVVELSQP--------QGDFVL-PDPLPPR-------LLLIAAGSGITPVMSMLRTLLARGPTADV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 204 CYLLFANQTEkDILLRSELEEIRANHPS-RFKLWYTLDRApedwdysQGFVNEDMISSFMPP-PGDDVLIlmCGPPPMVQ 281
Cdd:cd06216 154 VLLYYARTRE-DVIFADELRALAAQHPNlRLHLLYTREEL-------DGRLSAAHLDAVVPDlADRQVYA--CGPPGFLD 223
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
51-284 8.44e-24

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate, while mono-oxygenases (aka mixed oxygenases) add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.


Pssm-ID: 99784  Cd Length: 224  Bit Score: 96.51  E-value: 8.44e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  51 EEISHDTRRFRFALPSPEHVLGlpiGQhiYLSARVDG-NLVVRPYTPVSSDDNKGYVDLVVKIYfknvhpkfpEGGKMSQ 129
Cdd:cd06187   5 ERLTHDIAVVRLQLDQPLPFWA---GQ--YVNVTVPGrPRTWRAYSPANPPNEDGEIEFHVRAV---------PGGRVSN 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 130 YL-DSLRKDETIDFRGPsgllvysgKGTFQIRPDKKSPPVpkkanhlgMIAGGTGITPMLQLIRAILKDKEDKTIcYLLF 208
Cdd:cd06187  71 ALhDELKVGDRVRLSGP--------YGTFYLRRDHDRPVL--------CIAGGTGLAPLRAIVEDALRRGEPRPV-HLFF 133
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28278121 209 ANQTEKDILLRSELEEIRANHPsRFKLWYTLDRAPEDWDYSQGFVNeDMISSFMPPPGD-DVLIlmCGPPPMVQYAI 284
Cdd:cd06187 134 GARTERDLYDLEGLLALAARHP-WLRVVPVVSHEEGAWTGRRGLVT-DVVGRDGPDWADhDIYI--CGPPAMVDATV 206
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
47-297 2.47e-23

Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+.


Pssm-ID: 99817 [Multi-domain]  Cd Length: 253  Bit Score: 95.75  E-value: 2.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  47 LIDREEISHDTRRFRFALPSPEHVLGLPI-GQHIYLSARVDGNLvvrPYTPVSSDDNKGYVDLVVKiyfkNVhpkfpegG 125
Cdd:cd06221   1 IVEVVDETEDIKTFTLRLEDDDEELFTFKpGQFVMLSLPGVGEA---PISISSDPTRRGPLELTIR----RV-------G 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 126 KMSQYLDSLRKDETIDFRGPSGllvysgkgtfqirpdkKSPPVPKKANH-LGMIAGGTGITPMLQLIRAILKDKEDKTIC 204
Cdd:cd06221  67 RVTEALHELKPGDTVGLRGPFG----------------NGFPVEEMKGKdLLLVAGGLGLAPLRSLINYILDNREDYGKV 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 205 YLLFANQTEKDILLRSELEEIRANhpSRFKLWYTLDRAPEDWDYSQGFVNeDMISSFMPPPGDDVLIlMCGPPPMVQYAI 284
Cdd:cd06221 131 TLLYGARTPEDLLFKEELKEWAKR--SDVEVILTVDRAEEGWTGNVGLVT-DLLPELTLDPDNTVAI-VCGPPIMMRFVA 206
                       250
                ....*....|...
gi 28278121 285 NpSLDKLSYPQDR 297
Cdd:cd06221 207 K-ELLKLGVPEEQ 218
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
51-299 1.17e-22

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. These flavoprotein monooxygenases use molecular oxygen as a substrate and require reduced FAD. One atom of oxygen is incorportated into the aromatic compond, while the other is used to form a molecule of water. In contrast dioxygenases add both atoms of oxygen to the substrate.


Pssm-ID: 99808  Cd Length: 232  Bit Score: 93.55  E-value: 1.17e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  51 EEISHDTRRFRFALPSPEHVLGLPiGQhiYLSARVDGNLVVRPYTPVSSDDNKGYVDLVVKIYfknvhpkfpEGGKMSQY 130
Cdd:cd06212   9 EALTHDIRRLRLRLEEPEPIKFFA-GQ--YVDITVPGTEETRSFSMANTPADPGRLEFIIKKY---------PGGLFSSF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 131 LDS-LRKDETIDFRGPsgllvYsgkGTFQIRPDKKSPPVpkkanhlgMIAGGTGITPMLQLIRAILKDKEDKTICYlLFA 209
Cdd:cd06212  77 LDDgLAVGDPVTVTGP-----Y---GTCTLRESRDRPIV--------LIGGGSGMAPLLSLLRDMAASGSDRPVRF-FYG 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 210 NQTEKDILLRSELEEIRANHPSrFKLWYTLDRAP--EDWDYSQGFVNEDMISSFMPPPGDDVliLMCGPPPMVQyAINPS 287
Cdd:cd06212 140 ARTARDLFYLEEIAALGEKIPD-FTFIPALSESPddEGWSGETGLVTEVVQRNEATLAGCDV--YLCGPPPMID-AALPV 215
                       250
                ....*....|..
gi 28278121 288 LDKLSYPQDRRF 299
Cdd:cd06212 216 LEMSGVPPDQIF 227
PA_CoA_Oxy5 TIGR02160
phenylacetate-CoA oxygenase/reductase, PaaK subunit; Phenylacetate-CoA oxygenase is comprised ...
43-283 1.73e-21

phenylacetate-CoA oxygenase/reductase, PaaK subunit; Phenylacetate-CoA oxygenase is comprised of a five gene complex responsible for the hydroxylation of phenylacetate-CoA (PA-CoA) as the second catabolic step in phenylacetic acid (PA) degradation. Although the exact function of this enzyme has not been determined, it has been shown to be required for phenylacetic acid degradation and has been proposed to function in a multicomponent oxygenase acting on phenylacetate-CoA. [Energy metabolism, Other]


Pssm-ID: 131215 [Multi-domain]  Cd Length: 352  Bit Score: 92.58  E-value: 1.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121    43 YALRLIDREEISHDTRRFRFALPSP--EHVLGLPiGQHIYLSARVDGNLVVRPYTPVSsddnkGYVDLVVKIYFKNVhpk 120
Cdd:TIGR02160   2 HRLTVAEVERLTADAVAISFEIPDElaEDYRFAP-GQHLTLRREVDGEELRRSYSICS-----APAPGEIRVAVKKI--- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   121 fpEGGKMSQYL-DSLRKDETIDFRGPSGLLVYsgkgtfqirpdkksPPVPKKANHLGMIAGGTGITPMLQLIRAILKdKE 199
Cdd:TIGR02160  73 --PGGLFSTWAnDEIRPGDTLEVMAPQGLFTP--------------DLSTPHAGHYVAVAAGSGITPMLSIAETVLA-AE 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   200 DKTICYLLFANQTEKDILLRSELEEIRANHPSRFKLWYTLDRAPEDWDYSQGFVNEDMISSFMpppgdDVLI-------- 271
Cdd:TIGR02160 136 PRSTFTLVYGNRRTASVMFAEELADLKDKHPQRFHLAHVLSREPREAPLLSGRLDGERLAALL-----DSLIdvdradew 210
                         250
                  ....*....|..
gi 28278121   272 LMCGPPPMVQYA 283
Cdd:TIGR02160 211 FLCGPQAMVDDA 222
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
45-297 1.22e-20

Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with a C-terminal iron-sulfur binding cluster domain. FNR was intially identified as a chloroplast reductase activity catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methnae assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99788  Cd Length: 231  Bit Score: 87.97  E-value: 1.22e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  45 LRLIDREEISHDTRRFRFALPSPEHVLGLPiGQHIYLSARVDGNLVVRPYTpVSSDDNKGYVDLVVKIYfknvhpkfpEG 124
Cdd:cd06191   1 LRVAEVRSETPDAVTIVFAVPGPLQYGFRP-GQHVTLKLDFDGEELRRCYS-LCSSPAPDEISITVKRV---------PG 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 125 GKMSQYL-DSLRKDETIDFRGPSGLLVYSgkgtfqirpdkksppvPKKANHLGMIAGGTGITPMLQLIRAILKDKEDKTI 203
Cdd:cd06191  70 GRVSNYLrEHIQPGMTVEVMGPQGHFVYQ----------------PQPPGRYLLVAAGSGITPLMAMIRATLQTAPESDF 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 204 CyLLFANQTEKDILLRSELEEIRANHPS-RFKLWYTLDRAPEDWDYSQGFVNEDMISSFMPPPGDDVlILMCGPPPMVQy 282
Cdd:cd06191 134 T-LIHSARTPADMIFAQELRELADKPQRlRLLCIFTRETLDSDLLHGRIDGEQSLGAALIPDRLERE-AFICGPAGMMD- 210
                       250
                ....*....|....*
gi 28278121 283 AINPSLDKLSYPQDR 297
Cdd:cd06191 211 AVETALKELGMPPER 225
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
42-280 2.66e-20

Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. As a Class I bacterial dioxygenases, benzoate dioxygenase like proteins combine an [2Fe-2S] cluster containing N-terminal ferredoxin at the end fused to an FAD/NADP(P) domain. In dioxygenase FAD/NAD(P) binding domain, the reductase transfers 2 electrons from NAD(P)H to the oxygenase which insert into an aromatic substrate, an initial step in microbial aerobic degradation of aromatic rings. Flavin oxidoreductases use flavins as substrates, unlike flavoenzymes which have a flavin prosthetic group.


Pssm-ID: 99805  Cd Length: 228  Bit Score: 86.88  E-value: 2.66e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  42 KYALRLIDREEISHDTRRFRFALPSPEHVLGLPiGQhiYLSARVDGNLVVRPYTPvSSDDNKGYVDLVVKiyfkNVhpkf 121
Cdd:cd06209   1 TFEATVTEVERLSDSTIGLTLELDEAGALAFLP-GQ--YVNLQVPGTDETRSYSF-SSAPGDPRLEFLIR----LL---- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 122 pEGGKMSQYL-DSLRKDETIDFRGPsgllvysgKGTFQIRPdkksppvpKKANHLgMIAGGTGITPMLQLIRAILKDKED 200
Cdd:cd06209  69 -PGGAMSSYLrDRAQPGDRLTLTGP--------LGSFYLRE--------VKRPLL-MLAGGTGLAPFLSMLDVLAEDGSA 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 201 KTIcYLLFANQTEKDILLRSELEEIRANHPSrFKLWYTLDRaPEDWDYSQGFVNEDMISSFMPPPgdDVLILMCGPPPMV 280
Cdd:cd06209 131 HPV-HLVYGVTRDADLVELDRLEALAERLPG-FSFRTVVAD-PDSWHPRKGYVTDHLEAEDLNDG--DVDVYLCGPPPMV 205
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
47-281 1.26e-19

Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates toluene and forms p-cresol as part of a three component toluene-4-monoxygenase system. Electron transfer is from NADH to an NADH:ferredoxin oxidoreductase (TmoF in P. mendocina) to ferredoxin to an iron-containing oxygenase. TmoF is homologous to other mono- and dioxygenase systems within the ferredoxin reductase family.


Pssm-ID: 99787  Cd Length: 232  Bit Score: 85.38  E-value: 1.26e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  47 LIDREEISHDTRRFRFALPSPEHVLglPiGQHIYLSarVDGNLVVRPYTPVSSDDNKGYVDLVVKiyfknvhpKFPeGGK 126
Cdd:cd06190   1 LVDVRELTHDVAEFRFALDGPADFL--P-GQYALLA--LPGVEGARAYSMANLANASGEWEFIIK--------RKP-GGA 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 127 MSQYL-DSLRKDETIDFRGPSGLLVysgkgtfqIRPDKKSPPVpkkanhlgMIAGGTGITPMLQLIRAILKDK--EDKTI 203
Cdd:cd06190  67 ASNALfDNLEPGDELELDGPYGLAY--------LRPDEDRDIV--------CIAGGSGLAPMLSILRGAARSPylSDRPV 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 204 cYLLFANQTEKDILLrseLEEIRANHPSRFKLWYTLDRAPED------WDYSQGFVNeDMISSFMPPPGDDVLILMCGPP 277
Cdd:cd06190 131 -DLFYGGRTPSDLCA---LDELSALVALGARLRVTPAVSDAGsgsaagWDGPTGFVH-EVVEATLGDRLAEFEFYFAGPP 205

                ....
gi 28278121 278 PMVQ 281
Cdd:cd06190 206 PMVD 209
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
76-297 2.39e-19

FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling.


Pssm-ID: 99781  Cd Length: 247  Bit Score: 84.92  E-value: 2.39e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  76 GQhiYLSARVD----GNLVVRPYTpVSSDDNKGYVDLVVKIyfknvhpkfPEGGKMSQYL-DSLRKDETIDFRGPSGllv 150
Cdd:cd06184  40 GQ--YLSVRVKlpglGYRQIRQYS-LSDAPNGDYYRISVKR---------EPGGLVSNYLhDNVKVGDVLEVSAPAG--- 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 151 ysgkgTFQIRPDKKSPPVpkkanhlgMIAGGTGITPMLQLIRAILKDKEDKTIcYLLFANQTEKDILLRSELEEIRANHP 230
Cdd:cd06184 105 -----DFVLDEASDRPLV--------LISAGVGITPMLSMLEALAAEGPGRPV-TFIHAARNSAVHAFRDELEELAARLP 170
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28278121 231 S-RFKLWY---TLDRAPEDWDYsQGFVNEDMISSFMPPPGDDVLIlmCGPPPMVQyAINPSLDKLSYPQDR 297
Cdd:cd06184 171 NlKLHVFYsepEAGDREEDYDH-AGRIDLALLRELLLPADADFYL--CGPVPFMQ-AVREGLKALGVPAER 237
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
51-283 2.61e-19

NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD.


Pssm-ID: 99786  Cd Length: 224  Bit Score: 84.14  E-value: 2.61e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  51 EEISHDTRRFRfaLPSPEHVLGLPiGQhiYLSARVDGNlVVRPYTPVSSDDNKGYVDLVVKIYfknvhpkfpEGGKMSQY 130
Cdd:cd06189   7 EPLNDDVYRVR--LKPPAPLDFLA-GQ--YLDLLLDDG-DKRPFSIASAPHEDGEIELHIRAV---------PGGSFSDY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 131 -LDSLRKDETIDFRGPsgllvysgKGTFQIRPDKKSPPVpkkanhlgMIAGGTGITPMLQLIRAILKDKEDKTIcYLLFA 209
Cdd:cd06189  72 vFEELKENGLVRIEGP--------LGDFFLREDSDRPLI--------LIAGGTGFAPIKSILEHLLAQGSKRPI-HLYWG 134
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28278121 210 NQTEKDILLRSELEEIRANHPsrfKLWYT--LDRAPEDWDYSQGFVNEDMISSFmpPPGDDVLILMCGPPPMVQYA 283
Cdd:cd06189 135 ARTEEDLYLDELLEAWAEAHP---NFTYVpvLSEPEEGWQGRTGLVHEAVLEDF--PDLSDFDVYACGSPEMVYAA 205
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
51-284 8.50e-18

Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use molecular oxygen as a substrate in the microbial degredation of phenol. This protein is encoded by a single gene and uses a tightly bound FAD cofactor in the NAD(P)H dependent conversion of phenol and O2 to catechol and H2O. This group is related to the NAD binding ferredoxin reductases.


Pssm-ID: 99807  Cd Length: 238  Bit Score: 80.45  E-value: 8.50e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  51 EEISHDTRRFRFALPSPEHVLGLPiGQhiYLSARVDGNLVVRPYTPVSSDDNKGYVDLVVKIYfknvhpkfpEGGKMSQY 130
Cdd:cd06211  15 EDLTPTIKGVRLKLDEPEEIEFQA-GQ--YVNLQAPGYEGTRAFSIASSPSDAGEIELHIRLV---------PGGIATTY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 131 L-DSLRKDETIDFRGPSGLLVYsgkgtfqirpdKKSPPVPkkanhLGMIAGGTGITPMLQLIRAILKDKEDKTIcYLLFA 209
Cdd:cd06211  83 VhKQLKEGDELEISGPYGDFFV-----------RDSDQRP-----IIFIAGGSGLSSPRSMILDLLERGDTRKI-TLFFG 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28278121 210 NQTEKDILLRSELEEIRANHPsRFKLWYTLDRAPE--DWDYSQGFVNeDMISSFMPPPGDDVLILMCGPPPMVQYAI 284
Cdd:cd06211 146 ARTRAELYYLDEFEALEKDHP-NFKYVPALSREPPesNWKGFTGFVH-DAAKKHFKNDFRGHKAYLCGPPPMIDACI 220
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
43-284 4.92e-17

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate while mono-oxygenases add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.


Pssm-ID: 99809  Cd Length: 227  Bit Score: 78.12  E-value: 4.92e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  43 YALRLIDREEISHDTRRFRFALPSPEHVLGlpiGQhiYLSARVDGNLVVRPYTPVSSDDNKGYVDLVVKiyfknvhpKFP 122
Cdd:cd06213   1 IRGTIVAQERLTHDIVRLTVQLDRPIAYKA---GQ--YAELTLPGLPAARSYSFANAPQGDGQLSFHIR--------KVP 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 123 eGGKMSQYL-DSLRKDETIDFRGPSGllvysgkgTFQIRPDKksppvpkkaNHLGMIAGGTGITPmlqlIRAIL---KDK 198
Cdd:cd06213  68 -GGAFSGWLfGADRTGERLTVRGPFG--------DFWLRPGD---------APILCIAGGSGLAP----ILAILeqaRAA 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 199 EDKTICYLLFANQTEKDILLRSELEEIRANHPSRFKLWYTLDRAPE--DWDYSQGFVNEDmISSFMPPPGDDVLilmCGP 276
Cdd:cd06213 126 GTKRDVTLLFGARTQRDLYALDEIAAIAARWRGRFRFIPVLSEEPAdsSWKGARGLVTEH-IAEVLLAATEAYL---CGP 201

                ....*...
gi 28278121 277 PPMVQYAI 284
Cdd:cd06213 202 PAMIDAAI 209
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
51-283 1.32e-16

Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent hydroxylation of methane to methanol. This multicomponent enzyme mediates electron transfer via a hydroxylase (MMOH), a coupling protein, and a reductase which is comprised of an N-terminal [2Fe-2S] ferredoxin domain, an FAD binding subdomain, and an NADH binding subdomain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. Dioxygenases add both atom of oxygen to the substrate, while mono-oxygenases add one atom to the substrate and one atom to water.


Pssm-ID: 99806  Cd Length: 236  Bit Score: 77.00  E-value: 1.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  51 EEISHDTRRFRFAlPSPEHVLGLPI----GQhiYLSARVDGNLVVRPYTPVSSDDNKGYVDLVVKiyfknVHPkfpeGGK 126
Cdd:cd06210  10 DRVSSNVVRLRLQ-PDDAEGAGIAAefvpGQ--FVEIEIPGTDTRRSYSLANTPNWDGRLEFLIR-----LLP----GGA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 127 MSQYLDSLRK-DETIDFRGPSGllvysgkgTFQIRPDKKSPpvpkkanhLGMIAGGTGITPMLQLIRAiLKDKEDKTICY 205
Cdd:cd06210  78 FSTYLETRAKvGQRLNLRGPLG--------AFGLRENGLRP--------RWFVAGGTGLAPLLSMLRR-MAEWGEPQEAR 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 206 LLFANQTEKDILLRSELEEIRANHPSrFKLWYTLDRAPEDWDYSQGFV----NEDMISSFMPPPgddvlILMCGPPPMVQ 281
Cdd:cd06210 141 LFFGVNTEAELFYLDELKRLADSLPN-LTVRICVWRPGGEWEGYRGTVvdalREDLASSDAKPD-----IYLCGPPGMVD 214

                ..
gi 28278121 282 YA 283
Cdd:cd06210 215 AA 216
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
90-297 1.69e-16

Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) provides a means of storing redox reaction energy via the transmembrane translocation of Na2+ ions. The C-terminal domain resembles ferredoxin:NADP+ oxidoreductase, and has NADH and FAD binding sites. (Na+-NQR) is distinct from H+-translocating NADH:quinone oxidoreductases and noncoupled NADH:quinone oxidoreductases. The NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain of this group typically contains an iron-sulfur cluster binding domain.


Pssm-ID: 99785  Cd Length: 283  Bit Score: 77.73  E-value: 1.69e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  90 VVRPYTPVSSDDNKGYVDLVVKIYF-KNVHPKFPEGgKMSQYLDSLRKDETIDFRGPSGllvysgkgtFQIRPDKKSPPV 168
Cdd:cd06188  85 VSRAYSLANYPAEEGELKLNVRIATpPPGNSDIPPG-IGSSYIFNLKPGDKVTASGPFG---------EFFIKDTDREMV 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 169 pkkanhlgMIAGGTGITPMLQLIRAILKDKEDKTICYLLFANQTEKDILLRSELEEIRANHPsRFKLWYTLDR-APED-W 246
Cdd:cd06188 155 --------FIGGGAGMAPLRSHIFHLLKTLKSKRKISFWYGARSLKELFYQEEFEALEKEFP-NFKYHPVLSEpQPEDnW 225
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 28278121 247 DYSQGFVNE---DMISSFMPPPgDDVLILMCGPPPMVQyAINPSLDKLSYPQDR 297
Cdd:cd06188 226 DGYTGFIHQvllENYLKKHPAP-EDIEFYLCGPPPMNS-AVIKMLDDLGVPREN 277
PRK08221 PRK08221
anaerobic sulfite reductase subunit B; Provisional
96-284 1.04e-13

anaerobic sulfite reductase subunit B; Provisional


Pssm-ID: 181300 [Multi-domain]  Cd Length: 263  Bit Score: 69.20  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   96 PVS-SDDNKGYVDLVVKiyfkNVhpkfpegGKMSQYLDSLRKDETIDFRGPSGllvysgkgtfqirpdkKSPPVPK-KAN 173
Cdd:PRK08221  50 PISvSDYGDGYIDLTIR----RV-------GKVTDEIFNLKEGDKLFLRGPYG----------------NGFPVDTyKGK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  174 HLGMIAGGTGITPMLQLIRAILKDKEDKTICYLLFANQTEKDILLRSELEEIRanhpSRFKLWYTLDRAPEDWDYSQGFV 253
Cdd:PRK08221 103 ELIVVAGGTGVAPVKGLMRYFYENPQEIKSLDLILGFKNPDDILFKEDLKRWR----EKINLILTLDEGEEGYRGNVGLV 178
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 28278121  254 ----NEDMISSFmpppgDDVLILMCGPPPMVQYAI 284
Cdd:PRK08221 179 tkyiPELTLKDI-----DNMQVIVVGPPIMMKFTV 208
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
47-280 2.18e-12

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an N-terminal Iron-Sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99791  Cd Length: 222  Bit Score: 64.98  E-value: 2.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  47 LIDREEISHDTRRFRFALPSPehvlgLPI--GQHIYLsARVDGnlVVRPYTPVSSDDNKGYVDLVVKIYfknvhpkfpEG 124
Cdd:cd06194   1 VVSLQRLSPDVLRVRLEPDRP-----LPYlpGQYVNL-RRAGG--LARSYSPTSLPDGDNELEFHIRRK---------PN 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 125 GKMSQYL-DSLRKDETIDFRGPSGLLVYsgkgtfqiRPDKKSPPvpkkanhLGMIAGGTGITPMLQLIRAILKDKEDKTI 203
Cdd:cd06194  64 GAFSGWLgEEARPGHALRLQGPFGQAFY--------RPEYGEGP-------LLLVGAGTGLAPLWGIARAALRQGHQGEI 128
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28278121 204 cYLLFANQTEKDILLRSELEEIRANHPSRFKLWYTLDRAPEDwdysqGFVNEDMISSFMPP-PGDDVLILmCGPPPMV 280
Cdd:cd06194 129 -RLVHGARDPDDLYLHPALLWLAREHPNFRYIPCVSEGSQGD-----PRVRAGRIAAHLPPlTRDDVVYL-CGAPSMV 199
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
46-298 3.95e-12

Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99792  Cd Length: 241  Bit Score: 64.51  E-value: 3.95e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  46 RLIDREEISHDTRRFRFALPSPEH-------VLGLPIGqhiylsarvDGNLVVRPYTPVSSDDNKgyvdlVVKIYFKNVh 118
Cdd:cd06195   1 TVLKRRDWTDDLFSFRVTRDIPFRfqagqftKLGLPND---------DGKLVRRAYSIASAPYEE-----NLEFYIILV- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 119 pkfpEGGKMSQYLDSLRKDETID-FRGPSGllvysgkgTFQIRPDkksPPvpkkANHLGMIAGGTGITPMLQLIRAILKD 197
Cdd:cd06195  66 ----PDGPLTPRLFKLKPGDTIYvGKKPTG--------FLTLDEV---PP----GKRLWLLATGTGIAPFLSMLRDLEIW 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 198 KEDKTIcYLLFANQTEKDILLRSELEEIRANHPSRFKLWYTLDRAPEDWDYSQGFvnEDMISS--------FMPPPGDDV 269
Cdd:cd06195 127 ERFDKI-VLVHGVRYAEELAYQDEIEALAKQYNGKFRYVPIVSREKENGALTGRI--PDLIESgeleehagLPLDPETSH 203
                       250       260
                ....*....|....*....|....*....
gi 28278121 270 lILMCGPPPMVQYAINpSLDKLSYPQDRR 298
Cdd:cd06195 204 -VMLCGNPQMIDDTQE-LLKEKGFSKNHR 230
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
178-297 8.77e-11

NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99795 [Multi-domain]  Cd Length: 216  Bit Score: 60.35  E-value: 8.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 178 IAGGTGITPMLQLIRAILKDKEDKTIcYLLFANQTEKDILLRSELEEIRANHPSRFKLwytLDRAPEDWDYsqgfvnEDM 257
Cdd:cd06198 101 IAGGIGITPFLALLEALAARGDARPV-TLFYCVRDPEDAVFLDELRALAAAAGVVLHV---IDSPSDGRLT------LEQ 170
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 28278121 258 ISSFMPPPGDDVLILMCGPPPMVQyAINPSLDKLSYPQDR 297
Cdd:cd06198 171 LVRALVPDLADADVWFCGPPGMAD-ALEKGLRALGVPARR 209
PRK13289 PRK13289
bifunctional nitric oxide dioxygenase/dihydropteridine reductase 2; Provisional
76-297 1.79e-10

bifunctional nitric oxide dioxygenase/dihydropteridine reductase 2; Provisional


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 60.97  E-value: 1.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   76 GQhiYLSARVD----GNLVVRPYTpVSSDDNKGYVDLVVKiyfknvhpkFPEGGKMSQYL-DSLRKDETIDFRGPSGllv 150
Cdd:PRK13289 188 GQ--YLGVRLDpegeEYQEIRQYS-LSDAPNGKYYRISVK---------REAGGKVSNYLhDHVNVGDVLELAAPAG--- 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  151 ysgkgTFQIRPDKKSPPVpkkanhlgMIAGGTGITPMLQLIRAILKDKEDKTICYLLFAnQTEKDILLRSELEEIRANHP 230
Cdd:PRK13289 253 -----DFFLDVASDTPVV--------LISGGVGITPMLSMLETLAAQQPKRPVHFIHAA-RNGGVHAFRDEVEALAARHP 318
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28278121  231 sRFKL--WYT----LDRAPEDWDYsQGFVNEDMISSFMPPPGDDVLIlmCGPPPMVQyAINPSLDKLSYPQDR 297
Cdd:PRK13289 319 -NLKAhtWYRepteQDRAGEDFDS-EGLMDLEWLEAWLPDPDADFYF--CGPVPFMQ-FVAKQLLELGVPEER 386
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
48-279 9.08e-10

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.


Pssm-ID: 99814 [Multi-domain]  Cd Length: 246  Bit Score: 57.56  E-value: 9.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  48 IDREEISHDTRRFRFALPSPEHVlGLPiGQ--HIYLSARvDGNLVVRPYTPVSSDDNKGYVDLVVKIYfknvhpkfpegG 125
Cdd:cd06218   2 LSNREIADDIYRLVLEAPEIAAA-AKP-GQfvMLRVPDG-SDPLLRRPISIHDVDPEEGTITLLYKVV-----------G 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 126 KMSQYLDSLRKDETIDFRGPsglLvysGKGtFqirpdkkspPVPKKANHLGMIAGGTGITPMLQLIRAILKDKEDKTIcY 205
Cdd:cd06218  68 KGTRLLSELKAGDELDVLGP---L---GNG-F---------DLPDDDGKVLLVGGGIGIAPLLFLAKQLAERGIKVTV-L 130
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28278121 206 LLFAnqTEKDILLRSELEEIRANHpsrfkLWYTldrapEDWDYSQ-GFVnEDMISSFMPPPGDDVlILMCGPPPM 279
Cdd:cd06218 131 LGFR--SADDLFLVEEFEALGAEV-----YVAT-----DDGSAGTkGFV-TDLLKELLAEARPDV-VYACGPEPM 191
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
29-280 5.79e-09

CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 56.03  E-value: 5.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   29 KPRPAITLESPDI---------KYALRLIDREEISHDTRRFRFALPSPEHVLGLPiGQHIYLSARvDGnlVVRPYTPVSS 99
Cdd:PRK07609  80 KPLSDLVLEAREVpalgdipvkKLPCRVASLERVAGDVMRLKLRLPATERLQYLA-GQYIEFILK-DG--KRRSYSIANA 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  100 DDNKGYVDLvvkiyfknvHPKFPEGGKMSQYL-DSLRKDETIDFRGPsgllvysgKGTFQIRPDKKSPPVpkkanhlgMI 178
Cdd:PRK07609 156 PHSGGPLEL---------HIRHMPGGVFTDHVfGALKERDILRIEGP--------LGTFFLREDSDKPIV--------LL 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  179 AGGTGITPMLQLIRAILKDKEDKTIcYLLFANQTEKDILLRSELEEIRANHPSrFKLWYTL-DRAPED-WDYSQGFVNED 256
Cdd:PRK07609 211 ASGTGFAPIKSIVEHLRAKGIQRPV-TLYWGARRPEDLYLSALAEQWAEELPN-FRYVPVVsDALDDDaWTGRTGFVHQA 288
                        250       260
                 ....*....|....*....|....
gi 28278121  257 MISSFmpPPGDDVLILMCGPPPMV 280
Cdd:PRK07609 289 VLEDF--PDLSGHQVYACGSPVMV 310
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
47-279 6.56e-09

FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99789 [Multi-domain]  Cd Length: 243  Bit Score: 55.03  E-value: 6.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  47 LIDREEISHDTRRFRFALPSPEHvLGLPiGQHIYLSARVDGNLVVRPYTPVSSDDNKGYVDLVVKIyfknvhpkfpeGGK 126
Cdd:cd06192   1 IVKKEQLEPNLVLLTIKAPLAAR-LFRP-GQFVFLRNFESPGLERIPLSLAGVDPEEGTISLLVEI-----------RGP 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 127 MSQYLDSLRKDETIDFRGPSGllvysgKGTfqirpdkkspPVPKKANHLGMIAGGTGITPMLQLIRAILKDKEDktiCYL 206
Cdd:cd06192  68 KTKLIAELKPGEKLDVMGPLG------NGF----------EGPKKGGTVLLVAGGIGLAPLLPIAKKLAANGNK---VTV 128
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28278121 207 LFANQTEKDILLRSELEEIRANHPsrfklwYTLDRAPEDWDYSQGFVNEDMissfmpPPGDDVLILMCGPPPM 279
Cdd:cd06192 129 LAGAKKAKEEFLDEYFELPADVEI------WTTDDGELGLEGKVTDSDKPI------PLEDVDRIIVAGSDIM 189
sulfite_red_B TIGR02911
sulfite reductase, subunit B; Members of this protein family include the B subunit, one of ...
96-290 1.29e-08

sulfite reductase, subunit B; Members of this protein family include the B subunit, one of three subunits, of the anaerobic sulfite reductase of Salmonella, and close homologs from various Clostridum species, where the three-gene neighborhood is preserved. Two such gene clusters are found in Clostridium perfringens, but it may be that these sets of genes correspond to the distinct assimilatory and dissimilatory forms as seen in Clostridium pasteurianum. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 131957 [Multi-domain]  Cd Length: 261  Bit Score: 54.41  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121    96 PVS-SDDNKGYVDLVVKiyfkNVhpkfpegGKMSQYLDSLRKDETIDFRGPSGllvysgkGTFQIRPDKKSPPVpkkanh 174
Cdd:TIGR02911  48 PISvSGIGEGYIDLTIR----RV-------GKVTDEVFTLKEGDNLFLRGPYG-------NGFDVDNYKHKELV------ 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   175 lgMIAGGTGITPMLQLIRAILKDKEDKTICYLLFANQTEKDILLRSELEEIRANHpsrfKLWYTLDRAPEDWDYSQGFVN 254
Cdd:TIGR02911 104 --VVAGGTGVAPVKGVVEYFVKNPKEIKSLNLILGFKTPDDILFKEDIAEWKGNI----NLTLTLDEAEEDYKGNIGLVT 177
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 28278121   255 eDMISSFMPPPGDDVLILMCGPPPMVQYAINPSLDK 290
Cdd:TIGR02911 178 -KYIPELTLKDIEEVQAIVVGPPIMMKFTVQELLKK 212
nqrF TIGR01941
NADH:ubiquinone oxidoreductase, Na(+)-translocating, F subunit; This model represents the NqrF ...
90-279 2.30e-08

NADH:ubiquinone oxidoreductase, Na(+)-translocating, F subunit; This model represents the NqrF subunit of the six-protein, Na(+)-pumping NADH-quinone reductase of a number of marine and pathogenic Gram-negative bacteria. This oxidoreductase complex functions primarily as a sodium ion pump. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130996 [Multi-domain]  Cd Length: 405  Bit Score: 54.42  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121    90 VVRPYTPVSSDDNKGYVDLVVKIY---FKNvhPKFPEGgKMSQYLDSLRKDETIDFRGPSGllvysgkgTFQIRpDKKSP 166
Cdd:TIGR01941 205 TVRAYSMANYPAEKGIIKLNVRIAtppFIN--SDIPPG-IMSSYIFSLKPGDKVTISGPFG--------EFFAK-DTDAE 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   167 PVpkkanhlgMIAGGTGITPMLQLIRAILKDKEDKTICYLLFANQTEKDILLRSELEEIRANHPSrFKLWYTL-DRAPED 245
Cdd:TIGR01941 273 MV--------FIGGGAGMAPMRSHIFDQLKRLKSKRKISFWYGARSLREMFYQEDFDQLEAENPN-FVWHVALsDPQPED 343
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 28278121   246 -WDYSQGFV----NEDMISSFMPPpgDDVLILMCGPPPM 279
Cdd:TIGR01941 344 nWTGYTGFIhnvlYENYLKDHDAP--EDCEFYMCGPPMM 380
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
91-243 5.88e-08

These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but lack the FAD-binding region connecting sub-domain. Ferredoxin-NADP+ reductase (FNR) is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins, such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2, which then transfers two electrons and a proton to NADP+ to form NADPH. CYPOR serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases, sulfite reducatase, and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPOR has a C-terminal FNR-like FAD and NAD binding module, an FMN-binding domain, and an additional connecting domain (inserted within the FAD binding region) that orients the FNR and FMN -binding domains. The C-terminal domain contains most of the NADP(H) binding residues, and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule, which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99804 [Multi-domain]  Cd Length: 286  Bit Score: 52.71  E-value: 5.88e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  91 VRPYTPVSSD--DNKGY--VDLVVKIYfKNVHPKFPEG--GKMSQYLDSLRKDETIDFRGPSGllvysgkgtfqirpDKK 164
Cdd:cd06208  64 LRLYSIASSRygDDGDGktLSLCVKRL-VYTDPETDETkkGVCSNYLCDLKPGDDVQITGPVG--------------KTM 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 165 SPPVPKKANHLgMIAGGTGITPMLQLIRAILKDKED----KTICYLLFANQTEKDILLRSELEEIRANHPSRFKLWYTLD 240
Cdd:cd06208 129 LLPEDPNATLI-MIATGTGIAPFRSFLRRLFREKHAdykfTGLAWLFFGVPNSDSLLYDDELEKYPKQYPDNFRIDYAFS 207

                ...
gi 28278121 241 RAP 243
Cdd:cd06208 208 REQ 210
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
45-279 7.41e-08

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 52.18  E-value: 7.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   45 LRLIDREEISHDTRRFRFalpSPEHVLGLPIGQHIYLSARVDGNLVVRPYTpvSSDDNKGYVDLVVKIYfknvhpkfpeg 124
Cdd:PRK00054   7 MKIVENKEIAPNIYTLVL---DGEKVFDMKPGQFVMVWVPGVEPLLERPIS--ISDIDKNEITILYRKV----------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  125 GKMSQYLDSLRKDETIDFRGPSGllvysgKGtFqirpdkkspPVPKKANHLGMIAGGTGITPMLQLIRAILK-DKEDKTI 203
Cdd:PRK00054  71 GEGTKKLSKLKEGDELDIRGPLG------NG-F---------DLEEIGGKVLLVGGGIGVAPLYELAKELKKkGVEVTTV 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  204 CYLlfanQTEKDILLRSELEEIRanhpsrfKLWYTLDrapedwDYS---QGFVNEDMI---SSFmpppgdDVlILMCGPP 277
Cdd:PRK00054 135 LGA----RTKDEVIFEEEFAKVG-------DVYVTTD------DGSygfKGFVTDVLDeldSEY------DA-IYSCGPE 190

                 ..
gi 28278121  278 PM 279
Cdd:PRK00054 191 IM 192
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
39-297 9.59e-08

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 52.12  E-value: 9.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   39 PDIKYALRLIDREEISHDTRRFRFALPSPE---HVLGLPiGQHIYLSARVDGNLvvrPYTPVSSDDNKGYVDLVVKiyfk 115
Cdd:PRK08345   2 PYALHDAKILEVYDLTEREKLFLLRFEDPElaeSFTFKP-GQFVQVTIPGVGEV---PISICSSPTRKGFFELCIR---- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  116 nvhpkfpEGGKMSQYLDSLRKDETIDFRGPSGllvysgkgtfqirpdkKSPPVPKKANH-LGMIAGGTGITPMLQLIRAI 194
Cdd:PRK08345  74 -------RAGRVTTVIHRLKEGDIVGVRGPYG----------------NGFPVDEMEGMdLLLIAGGLGMAPLRSVLLYA 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  195 LKDKEDKTICYLLFANQTEKDILLRSELEEIRAnHPSRFKLWYTLDRAPEDWDY-----------SQGFVNEDMISSFMP 263
Cdd:PRK08345 131 MDNRWKYGNITLIYGAKYYEDLLFYDELIKDLA-EAENVKIIQSVTRDPEWPGChglpqgfiervCKGVVTDLFREANTD 209
                        250       260       270
                 ....*....|....*....|....*....|....
gi 28278121  264 PpgDDVLILMCGPPPMVQYAINPSLDKlSYPQDR 297
Cdd:PRK08345 210 P--KNTYAAICGPPVMYKFVFKELINR-GYRPER 240
antC PRK11872
anthranilate dioxygenase reductase; Provisional
124-281 2.36e-07

anthranilate dioxygenase reductase; Provisional


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 51.28  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  124 GGKMSQYL-DSLRKDETIDFRGPSGllvysgkgTFQIRPDKKSppvpkkanhLGMIAGGTGITPMLQLIRAILKDKEDKT 202
Cdd:PRK11872 177 DGVMSNYLrERCQVGDEILFEAPLG--------AFYLREVERP---------LVFVAGGTGLSAFLGMLDELAEQGCSPP 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  203 IcYLLFANQTEKDIllrSELEEIRAnHPSR---FKLWYTLDRAPEDWDYSQGFVNEDMISSFMPPPGDDvlILMCGPPPM 279
Cdd:PRK11872 240 V-HLYYGVRHAADL---CELQRLAA-YAERlpnFRYHPVVSKASADWQGKRGYIHEHFDKAQLRDQAFD--MYLCGPPPM 312

                 ..
gi 28278121  280 VQ 281
Cdd:PRK11872 313 VE 314
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
42-295 1.22e-06

Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99798 [Multi-domain]  Cd Length: 289  Bit Score: 48.86  E-value: 1.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  42 KYALRLIDR----EEISHDTRRFRFALP-SPEHVLGLPigqhiYLSArvdGNL--VVRPYTPV------SSDDNKGYVDL 108
Cdd:cd06201  45 TKALELVERkdygAAVQAPTAILRFKPAkRKLSGKGLP-----SFEA---GDLlgILPPGSDVprfyslASSSSDGFLEI 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 109 VVKiyfknVHPkfpeGGKMSQYLDSLRKDETID-FRGPSGllvysgkgtfQIRPDKKSPPVPkkanhlgMIAGGTGITPM 187
Cdd:cd06201 117 CVR-----KHP----GGLCSGYLHGLKPGDTIKaFIRPNP----------SFRPAKGAAPVI-------LIGAGTGIAPL 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 188 LQLIRAilkdKEDKTICYLLFANQT-EKDILLRSELEEIRANHPSRfKLWYTLDRAPEDwDYSQGFVNED------MISs 260
Cdd:cd06201 171 AGFIRA----NAARRPMHLYWGGRDpASDFLYEDELDQYLADGRLT-QLHTAFSRTPDG-AYVQDRLRADaerlrrLIE- 243
                       250       260       270
                ....*....|....*....|....*....|....*
gi 28278121 261 fmpppgDDVLILMCGPPPMVQyAINPSLDKLSYPQ 295
Cdd:cd06201 244 ------DGAQIMVCGSRAMAQ-GVAAVLEEILAPQ 271
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
90-285 7.71e-06

Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion];


Pssm-ID: 225426 [Multi-domain]  Cd Length: 410  Bit Score: 46.72  E-value: 7.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  90 VVRPYTPVSSDDNKGYVDLVVKIyfknVHPKFPEG----GKMSQYLDSLRKDETIDFRGPSGLLVYSgkgtfqirpDKKS 165
Cdd:COG2871 210 IIRAYSMASYPEEKGIIKLNVRI----ATPPPRNPdappGQMSSYIWSLKPGDKVTISGPFGEFFAK---------DTDA 276
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 166 PPVpkkanhlgMIAGGTGITPMLQLIRAILKDKEDKTICYLLFANQTEKDILLRSELEEIRANHPSrFKLWYTL-DRAPE 244
Cdd:COG2871 277 EMV--------FIGGGAGMAPMRSHIFDQLKRLHSKRKISFWYGARSLREMFYQEDFDQLQAENPN-FHWHLALsDPLPE 347
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 28278121 245 D-WDYSQGFV----NEDMISSFMPPpgDDVLILMCGPPPMVQYAIN 285
Cdd:COG2871 348 DnWDGYTGFIhnvlYENYLKDHEAP--EDCEYYMCGPPLMNASVIK 391
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
49-281 1.25e-05

Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron transfer from NADH to FMN to an iron sulfur cluster. PDR has an an N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding domain and a C-terminal iron-sulfur [2Fe-2S] cluster domain. Although structurally homologous to FNR, PDR binds FMN rather than FAD in it's FNR-like domain. Electron transfer between pyrimidines and iron-sulfur clusters (Rieske center [2Fe-2S]) or heme groups is mediated by flavins in respiration, photosynthesis, and oxygenase systems. Type I dioxygenase systems, including the hydroxylate phthalate system, have 2 components, a monomeric reductase consisting of a flavin and a 2Fe-2S center and a multimeric oxygenase. In contrast to other Rieske dioxygenases the ferredoxin like domain is C-, not N-terminal.


Pssm-ID: 99782  Cd Length: 211  Bit Score: 45.17  E-value: 1.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  49 DREEISHDTRRFRFALPSPEhvlGLPI---GQHI--YLsarvdGNLVVRPYTPVSSDDNKGYVDLVVKiyfknvhpKFPE 123
Cdd:cd06185   2 RIRDEAPDIRSFELEAPDGA---PLPAfepGAHIdvHL-----PNGLVRQYSLCGDPADRDRYRIAVL--------REPA 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 124 GGKMSQYL-DSLRKDETIDFRGPSGLLvysgkgtfqirpdkksPPVPKKANHLgMIAGGTGITPMLQLIRAILKDKEDKT 202
Cdd:cd06185  66 SRGGSRYMhELLRVGDELEVSAPRNLF----------------PLDEAARRHL-LIAGGIGITPILSMARALAARGADFE 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 203 ICYllFAnqtekdillRSE-----LEEIRANHPSRFKLWYTLDRAPEDwdysqgfvnedmISSFMPPPGDDVLILMCGPP 277
Cdd:cd06185 129 LHY--AG---------RSRedaafLDELAALPGDRVHLHFDDEGGRLD------------LAALLAAPPAGTHVYVCGPE 185

                ....
gi 28278121 278 PMVQ 281
Cdd:cd06185 186 GMMD 189
CyPoR_like cd06207
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
125-284 3.73e-05

NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99803 [Multi-domain]  Cd Length: 382  Bit Score: 44.57  E-value: 3.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 125 GKMSQYLDSLRKDETIDfrgpsgllVYSGKGTFQIRPDKKSPpvpkkanhLGMIAGGTGITPMLQLI--RAILKDKEDKT 202
Cdd:cd06207 199 GLCSSYLAGLKVGQRVT--------VFIKKSSFKLPKDPKKP--------IIMVGPGTGLAPFRAFLqeRAALLAQGPEI 262
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 203 I-CYLLFANQTE-KDILLRSELEE-IRANHPSRFKLWYTldRAPEDWDYSQGFV--NEDMISSFMPPpgDDVLILMCGP- 276
Cdd:cd06207 263 GpVLLYFGCRHEdKDYLYKEELEEyEKSGVLTTLGTAFS--RDQPKKVYVQDLIreNSDLVYQLLEE--GAGVIYVCGSt 338
                       170
                ....*....|.
gi 28278121 277 ---PPMVQYAI 284
Cdd:cd06207 339 wkmPPDVQEAF 349
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
178-279 6.37e-05

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 226582 [Multi-domain]  Cd Length: 438  Bit Score: 44.01  E-value: 6.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 178 IAGGTGITPMLQLIRAILKDKEDKTIcYLLFANQTEKDILLRSELEEIrANHPSRFKLWYtldrapeDWDYSQGFVNEDM 257
Cdd:COG4097 321 IAGGIGITPFISMLFTLAERKSDPPV-HLFYCSRNWEEALYAEELRAL-AQKLPNVVLHI-------IDSSKDGYLDQED 391
                        90       100
                ....*....|....*....|..
gi 28278121 258 ISSFmPPPGDDVLILMCGPPPM 279
Cdd:COG4097 392 LERY-PDRPRTRSVFFCGPIKM 412
CysJ COG0369
Sulfite reductase, alpha subunit (flavoprotein) [Inorganic ion transport and metabolism];
12-224 7.05e-05

Sulfite reductase, alpha subunit (flavoprotein) [Inorganic ion transport and metabolism];


Pssm-ID: 223446 [Multi-domain]  Cd Length: 587  Bit Score: 43.95  E-value: 7.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  12 LTSPFWFIFSIFQRFFGKPRPAITLESPDIKYALRLIDREEISHDTRRFRFALPSPEHVLGLpigqhiylsarvdgnlvV 91
Cdd:COG0369 306 FTSAPKSLLENLAHFAGQEELRRLLEQLDIADLQDYAKRRTLIDVLRDFPPAKLPAEELIDL-----------------L 368
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  92 RPYTP----VSS--DDNKGYVDLVVKIyfknVHPKFPEG---GKMSQYL-DSLRKDETID-FRGPSGllvysgkgTFQIR 160
Cdd:COG0369 369 PPLKPrlysIASspGVSPDEVHLTVGV----VRYQAEGReryGVCSGYLaDLLEEGDTIPvFVQPNK--------NFRLP 436
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28278121 161 PDKKSPPVpkkanhlgMIAGGTGITPMlqliRAILKDKEDKTIC---YLLFANQT-EKDILLRSELEE 224
Cdd:COG0369 437 EDPETPII--------MIGPGTGIAPF----RAFVQERAANGAEgknWLFFGCRHfTEDFLYQEEWEE 492
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
76-224 7.67e-05

NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 42.68  E-value: 7.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  76 GQHIYLSARvdgnLVVR-----PYTPVSS-DDNKGYVDLVVKiyfknvhpkfPEGGKMSQYLDSLRKDETIDFR------ 143
Cdd:cd06186  28 GQHVYLNFP----SLLSfwqshPFTIASSpEDEQDTLSLIIR----------AKKGFTTRLLRKALKSPGGGVSlkvlve 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 144 GPSGllvysgkgtfqirpdkkSPPVP-KKANHLGMIAGGTGITPMLQLIRAILKDKEDKTIC---YLLFANQTEKDIL-L 218
Cdd:cd06186  94 GPYG-----------------SSSEDlLSYDNVLLVAGGSGITFVLPILRDLLRRSSKTSRTrrvKLVWVVRDREDLEwF 156

                ....*.
gi 28278121 219 RSELEE 224
Cdd:cd06186 157 LDELRA 162
DHOD_e_trans_like1 cd06219
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
93-279 1.06e-04

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD, forming FADH2 via a semiquinone intermediate, and then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99815 [Multi-domain]  Cd Length: 248  Bit Score: 42.56  E-value: 1.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  93 PYTPVSSDDNKGYVDLVVKiyfknvhpkfpEGGKMSQYLDSLRKDETI-DFRGPSGllvysgkgtfqirpdkKSPPVPKK 171
Cdd:cd06219  45 PLTIADWDPEKGTITIVVQ-----------VVGKSTRELATLEEGDKIhDVVGPLG----------------KPSEIENY 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 172 ANHLgMIAGGTGITPMLQLIRAiLKDKEDKTIcyLLFANQTEKDILLRSELEEIRANHpsrfklWYTLDrapeDWDYS-Q 250
Cdd:cd06219  98 GTVV-FVGGGVGIAPIYPIAKA-LKEAGNRVI--TIIGARTKDLVILEDEFRAVSDEL------IITTD----DGSYGeK 163
                       170       180       190
                ....*....|....*....|....*....|..
gi 28278121 251 GFVN---EDMISSFMPPPgddvLILMCGPPPM 279
Cdd:cd06219 164 GFVTdplKELIESGEKVD----LVIAIGPPIM 191
FNR_like_2 cd06197
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ...
48-223 1.51e-04

FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and have a variety of physiological functions in a variety of organisms including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99794  Cd Length: 220  Bit Score: 41.99  E-value: 1.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  48 IDREEISHDTRRFRFALPSPEHVLGLPIGQHIYLSArvdGNLVVRPYTPVSSDDNKGYVDLVVKIYFKNVHPkfPEGGKM 127
Cdd:cd06197   1 IKSEVITPTLTRFTFELSPPDVVGKWTPGQYITLDF---SSELDSGYSHMADDDPQSLNDDFVRTFTVSSAP--PHDPAT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 128 SQYLDSLRK------------DETIDFRGPSGLLVYSGKGTFQIRPDKKSPPVPkkanhlgMIAGGTGITPMLQLIRAIL 195
Cdd:cd06197  76 DEFEITVRKkgpvtgflfqvaRRLREQGLEVPVLGVGGEFTLSLPGEGAERKMV-------WIAGGVGITPFLAMLRAIL 148
                       170       180
                ....*....|....*....|....*...
gi 28278121 196 KDKEDKTICYLLFANQTEKDILLRSELE 223
Cdd:cd06197 149 SSRNTTWDITLLWSLREDDLPLVMDTLV 176
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
125-279 1.75e-04

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.


Pssm-ID: 99816 [Multi-domain]  Cd Length: 233  Bit Score: 41.85  E-value: 1.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 125 GKMSQYLDSLRKDETIDFRGPsgllvYsGKGtFQIRPDKKSppvpkkanhlgMIAGGTGITPMLQLIRAiLKDKEDKTIc 204
Cdd:cd06220  59 GEATSALHDLKEGDKLGIRGP-----Y-GNG-FELVGGKVL-----------LIGGGIGIAPLAPLAER-LKKAADVTV- 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121 205 ylLFANQTEKDILLRSELEEIRanhpsrfKLWYTLDrapedwDYSQGF-------VNEDMISSFmpppgdDVlILMCGPP 277
Cdd:cd06220 119 --LLGARTKEELLFLDRLRKSD-------ELIVTTD------DGSYGFkgfvtdlLKELDLEEY------DA-IYVCGPE 176

                ..
gi 28278121 278 PM 279
Cdd:cd06220 177 IM 178
ViuB COG2375
NADPH-dependent ferric siderophore reductase, contains FAD-binding and SIP domains [Inorganic ...
34-147 3.45e-03

NADPH-dependent ferric siderophore reductase, contains FAD-binding and SIP domains [Inorganic ion transport and metabolism];


Pssm-ID: 225250 [Multi-domain]  Cd Length: 265  Bit Score: 38.15  E-value: 3.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  34 ITLESPDikyalrLIDREEISHDTRRFRFALPSP-EHVLGLPIGQHIYLSARVDGNLVVRPYTPVSSDDNKGYVDlvVKI 112
Cdd:COG2375  35 VVLGGEG------LAGFASLGFGDQHIKLFFPPPdGDPPRLPVLEERGAVPPGAQRPPQRTYTIRAVDAAAGELD--VDF 106
                        90       100       110
                ....*....|....*....|....*....|....*
gi 28278121 113 YfknVHpkfPEGGKMSQYLDSLRKDETIDFRGPSG 147
Cdd:COG2375 107 V---LH---GEGGPASRWARTAQPGDTLTIMGPRG 135
PRK05464 PRK05464
Na(+)-translocating NADH-quinone reductase subunit F; Provisional
90-279 3.84e-03

Na(+)-translocating NADH-quinone reductase subunit F; Provisional


Pssm-ID: 235481 [Multi-domain]  Cd Length: 409  Bit Score: 38.31  E-value: 3.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121   90 VVRPYTPVSSDDNKGYVDLVVKI-----YFKNVHPkfpegGKMSQYLDSLRKDETIDFRGPsgllvYsgkGTFQIRPDKk 164
Cdd:PRK05464 209 VIRAYSMANYPEEKGIIMLNVRIatpppGNPDVPP-----GIMSSYIFSLKPGDKVTISGP-----F---GEFFAKDTD- 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  165 sppvpkkaNHLGMIAGGTGITPMLQLIRAILKDKEDKTICYLLFANQTEKDILLRSELEEIRANHPSrFKLWYTLDRA-P 243
Cdd:PRK05464 275 --------AEMVFIGGGAGMAPMRSHIFDQLKRLKSKRKISFWYGARSLREMFYVEDFDQLAAENPN-FKWHVALSDPlP 345
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 28278121  244 ED-WDYSQGFVNEDMISSF---MPPPgDDVLILMCGPPPM 279
Cdd:PRK05464 346 EDnWTGYTGFIHNVLYENYlkdHEAP-EDCEYYMCGPPMM 384
siderophore_interacting cd06193
Siderophore interacting proteins share the domain structure of the ferredoxin reductase like ...
34-151 9.18e-03

Siderophore interacting proteins share the domain structure of the ferredoxin reductase like family. Siderophores are produced in various bacteria (and some plants) to extract iron from hosts. Binding constants are high, so iron can be pilfered from transferrin and lactoferrin for bacterial uptake, contributing to pathogen virulence. Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99790 [Multi-domain]  Cd Length: 235  Bit Score: 36.47  E-value: 9.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  34 ITLESPDikyalrLIDREEiSHDTRRFRFALPSPEHVLGLPIGQHIYLSARVDGNLVVRPYTPVSSDDNKGYVDL-VVki 112
Cdd:cd06193  14 ITLGGPD------LAGFPS-DGPDQHVKLLFPDPGQAPPVLPVLGRRRWPPEEPRPVMRTYTVRRFDPEAGELDIdFV-- 84
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 28278121 113 yfknVHpkfPEGGKMSQYLDSLRKDETIDFRGPSGLLVY 151
Cdd:cd06193  85 ----LH---GDEGPASRWAASAQPGDTLGIAGPGGSFLP 116
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
177-235 9.20e-03

Ferric reductase NAD binding domain;


Pssm-ID: 336906  Cd Length: 152  Bit Score: 35.78  E-value: 9.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28278121   177 MIAGGTGITPMLQLIRAILK--DKEDKTICYLLFANQTEKDI-LLRSELEEIRANHPSRFKL 235
Cdd:pfam08030   6 LVAGGIGITPFISILKDLINksKALKTKKIKFYWVVRDLSSLeWFKDVLNELEELKELNIEI 67
fre PRK08051
FMN reductase; Validated
129-283 9.46e-03

FMN reductase; Validated


Pssm-ID: 236142  Cd Length: 232  Bit Score: 36.76  E-value: 9.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28278121  129 QYLDSLRKDETIDFRGPsgllvysgKGTFQIRPDKKSPpvpkkanhLGMIAGGTGitpmLQLIRAILK---DKEDKTICY 205
Cdd:PRK08051  75 AVMERILKDGEIEVDIP--------HGDAWLREESERP--------LLLIAGGTG----FSYARSILLtalAQGPNRPIT 134
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28278121  206 LLFANQTEKDILLRSELEEIRANHPsRFKLWYTLDRAPEDWDYSQGFVNEDMISSFMPPPGDDvlILMCGPPPMVQYA 283
Cdd:PRK08051 135 LYWGGREEDHLYDLDELEALALKHP-NLHFVPVVEQPEEGWQGKTGTVLTAVMQDFGSLAEYD--IYIAGRFEMAKIA 209
 
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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