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Conserved domains on  [gi|364517353|gb|AEW60481|]
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NADH oxidoreductase for HCP [Klebsiella pneumoniae subsp. pneumoniae HS11286]

Protein Classification

hybrid-cluster NAD(P)-dependent oxidoreductase( domain architecture ID 11484871)

NAD(P)-dependent oxidoreductase that is a hybrid-cluster protein containing both [2Fe-2S] (or [4Fe-4S]) and [4Fe-2S-2O] clusters, may transfer electrons to carrier proteins such as ferredoxin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 1-322 0e+00

HCP oxidoreductase, NADH-dependent; Provisional


:

Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 676.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353   1 MTMPTSQCPWRMQVHHIHQETPDVWTLSLLCHDYYPYRAGQYALVSVRNSAETLRAYTLSSTPGVSEYITLTVRRIDEGT 80
Cdd:PRK10684   1 MTMPTPQCPNRMQVHSIVQETPDVWTISLICHDFYPYRAGQYALVSIRNSAETLRAYTLSSTPGVSEFITLTVRRIDDGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  81 GSQWLTREVKRGDYLWLSDAMGEFTCDDKAEDKFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVIFAEEW 160
Cdd:PRK10684  81 GSQWLTRDVKRGDYLWLSDAMGEFTCDDKAEDKYLLLAAGCGVTPIMSMRRWLLKNRPQADVQVIFNVRTPQDVIFADEW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 161 RN----YP---VTLVAEHNATHGFVAGRLTRELLQS-VPDLASRTVMTCGPAPYMEKVEQDVAALGVT--RFFKEKFFTP 230
Cdd:PRK10684 161 RQlkqrYPqlnLTLVAENNATEGFIAGRLTRELLQQaVPDLASRTVMTCGPAPYMDWVEQEVKALGVTadRFFKEKFFTP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 231 VAEAATSGLKFTKLQPAREFYAPVGTTLLDALESNKVPVTVACRAGVCGCCKTKVVSGKYSVTSTMTLTDAEIADGYVLA 310
Cdd:PRK10684 241 VAEAATSGLTFTKLQPAREFYAPVGTTLLEALESNKVPVVAACRAGVCGCCKTKVVSGEYTVSSTMTLTPAEIAQGYVLA 320

                        330
                 ....*....|..
gi 364517353 311 CSCHPQSDLVLA 322
Cdd:PRK10684 321 CSCHPQGDLVLA 332
 
Name Accession Description Interval E-value
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 1-322 0e+00

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 676.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353   1 MTMPTSQCPWRMQVHHIHQETPDVWTLSLLCHDYYPYRAGQYALVSVRNSAETLRAYTLSSTPGVSEYITLTVRRIDEGT 80
Cdd:PRK10684   1 MTMPTPQCPNRMQVHSIVQETPDVWTISLICHDFYPYRAGQYALVSIRNSAETLRAYTLSSTPGVSEFITLTVRRIDDGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  81 GSQWLTREVKRGDYLWLSDAMGEFTCDDKAEDKFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVIFAEEW 160
Cdd:PRK10684  81 GSQWLTRDVKRGDYLWLSDAMGEFTCDDKAEDKYLLLAAGCGVTPIMSMRRWLLKNRPQADVQVIFNVRTPQDVIFADEW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 161 RN----YP---VTLVAEHNATHGFVAGRLTRELLQS-VPDLASRTVMTCGPAPYMEKVEQDVAALGVT--RFFKEKFFTP 230
Cdd:PRK10684 161 RQlkqrYPqlnLTLVAENNATEGFIAGRLTRELLQQaVPDLASRTVMTCGPAPYMDWVEQEVKALGVTadRFFKEKFFTP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 231 VAEAATSGLKFTKLQPAREFYAPVGTTLLDALESNKVPVTVACRAGVCGCCKTKVVSGKYSVTSTMTLTDAEIADGYVLA 310
Cdd:PRK10684 241 VAEAATSGLTFTKLQPAREFYAPVGTTLLEALESNKVPVVAACRAGVCGCCKTKVVSGEYTVSSTMTLTPAEIAQGYVLA 320

                        330
                 ....*....|..
gi 364517353 311 CSCHPQSDLVLA 322
Cdd:PRK10684 321 CSCHPQGDLVLA 332
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 12-227 1.12e-95

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 [Multi-domain]  Cd Length: 231  Bit Score: 282.56  E-value: 1.12e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  12 MQVHHIHQETPDVWTLSLLCHDY--YPYRAGQYALVSVRNSAET-LRAYTLSSTPGVSEYITLTVRRIDEGTGSQWLTRE 88
Cdd:cd06215    1 LRCVKIIQETPDVKTFRFAAPDGslFAYKPGQFLTLELEIDGETvYRAYTLSSSPSRPDSLSITVKRVPGGLVSNWLHDN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  89 VKRGDYLWLSDAMGEFTCDDKAEDKFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVIFAEEW----RNYP 164
Cdd:cd06215   81 LKVGDELWASGPAGEFTLIDHPADKLLLLSAGSGITPMMSMARWLLDTRPDADIVFIHSARSPADIIFADELeelaRRHP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 364517353 165 ---VTLVAEHNATH--GFVAGRLTRELLQS-VPDLASRTVMTCGPAPYMEKVEQDVAALGV--TRFFKEKF 227
Cdd:cd06215  161 nfrLHLILEQPAPGawGGYRGRLNAELLALlVPDLKERTVFVCGPAGFMKAVKSLLAELGFpmSRFHQESF 231
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
11-226 4.20e-62

Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 196.93  E-value: 4.20e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  11 RMQVHHIHQETPDVWTLSLLCHD---YYPYRAGQYALVSVR-NSAETLRAYTLSSTPGvSEYITLTVRRIDEGTGSQWLT 86
Cdd:COG1018    5 PLRVVEVRRETPDVVSFTLEPPDgapLPRFRPGQFVTLRLPiDGKPLRRAYSLSSAPG-DGRLEITVKRVPGGGGSNWLH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  87 REVKRGDYLWLSDAMGEFTCDDKAEDKFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVIFAEEWR----N 162
Cdd:COG1018   84 DHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLARGPFRPVTLVYGARSPADLAFRDELEalaaR 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 364517353 163 YP-VTLVAEHNATHGFVAGRLTRELLQS-VPDLASRTVMTCGPAPYMEKVEQDVAALGV--TRFFKEK 226
Cdd:COG1018  164 HPrLRLHPVLSREPAGLQGRLDAELLAAlLPDPADAHVYLCGPPPMMEAVRAALAELGVpeERIHFER 231
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
248-316 2.05e-13

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 64.47  E-value: 2.05e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  248 REFYAPVG-TTLLDALESNKVPVTVACRAGVCGCCKTKVVSGKYSVTSTMTLTDAEIADGYVLACSCHPQ 316
Cdd:pfam00111   8 VTIEVPDGeTTLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSFLEDDELAAGYVVLACQTYPK 77
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
 249-321 1.59e-09

ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ferredoxins. In general, these occur as a single domain proteins or with a chloroplast transit peptide. Species tend to be photosynthetic, but several forms may occur in one species and individually may not be associated with photocynthesis. Halobacterial forms differ somewhat in architecture; they score between trusted and noise cutoffs. Sequences scoring below the noise cutoff tend to be ferredoxin-related domains of larger proteins.


Pssm-ID: 273926 [Multi-domain]  Cd Length: 97  Bit Score: 54.38  E-value: 1.59e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 364517353  249 EFYAPVGTTLLDALESNKVPVTVACRAGVCGCCKTKVVSGKYSVTSTMTLTDAEIADGYVLACSCHPQSDLVL 321
Cdd:TIGR02008  16 TIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDQMEAGYVLTCVAYPTSDCTI 88
 
Name Accession Description Interval E-value
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 1-322 0e+00

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 676.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353   1 MTMPTSQCPWRMQVHHIHQETPDVWTLSLLCHDYYPYRAGQYALVSVRNSAETLRAYTLSSTPGVSEYITLTVRRIDEGT 80
Cdd:PRK10684   1 MTMPTPQCPNRMQVHSIVQETPDVWTISLICHDFYPYRAGQYALVSIRNSAETLRAYTLSSTPGVSEFITLTVRRIDDGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  81 GSQWLTREVKRGDYLWLSDAMGEFTCDDKAEDKFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVIFAEEW 160
Cdd:PRK10684  81 GSQWLTRDVKRGDYLWLSDAMGEFTCDDKAEDKYLLLAAGCGVTPIMSMRRWLLKNRPQADVQVIFNVRTPQDVIFADEW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 161 RN----YP---VTLVAEHNATHGFVAGRLTRELLQS-VPDLASRTVMTCGPAPYMEKVEQDVAALGVT--RFFKEKFFTP 230
Cdd:PRK10684 161 RQlkqrYPqlnLTLVAENNATEGFIAGRLTRELLQQaVPDLASRTVMTCGPAPYMDWVEQEVKALGVTadRFFKEKFFTP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 231 VAEAATSGLKFTKLQPAREFYAPVGTTLLDALESNKVPVTVACRAGVCGCCKTKVVSGKYSVTSTMTLTDAEIADGYVLA 310
Cdd:PRK10684 241 VAEAATSGLTFTKLQPAREFYAPVGTTLLEALESNKVPVVAACRAGVCGCCKTKVVSGEYTVSSTMTLTPAEIAQGYVLA 320

                        330
                 ....*....|..
gi 364517353 311 CSCHPQSDLVLA 322
Cdd:PRK10684 321 CSCHPQGDLVLA 332
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 12-227 1.12e-95

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 [Multi-domain]  Cd Length: 231  Bit Score: 282.56  E-value: 1.12e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  12 MQVHHIHQETPDVWTLSLLCHDY--YPYRAGQYALVSVRNSAET-LRAYTLSSTPGVSEYITLTVRRIDEGTGSQWLTRE 88
Cdd:cd06215    1 LRCVKIIQETPDVKTFRFAAPDGslFAYKPGQFLTLELEIDGETvYRAYTLSSSPSRPDSLSITVKRVPGGLVSNWLHDN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  89 VKRGDYLWLSDAMGEFTCDDKAEDKFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVIFAEEW----RNYP 164
Cdd:cd06215   81 LKVGDELWASGPAGEFTLIDHPADKLLLLSAGSGITPMMSMARWLLDTRPDADIVFIHSARSPADIIFADELeelaRRHP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 364517353 165 ---VTLVAEHNATH--GFVAGRLTRELLQS-VPDLASRTVMTCGPAPYMEKVEQDVAALGV--TRFFKEKF 227
Cdd:cd06215  161 nfrLHLILEQPAPGawGGYRGRLNAELLALlVPDLKERTVFVCGPAGFMKAVKSLLAELGFpmSRFHQESF 231
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
11-226 4.20e-62

Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 196.93  E-value: 4.20e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  11 RMQVHHIHQETPDVWTLSLLCHD---YYPYRAGQYALVSVR-NSAETLRAYTLSSTPGvSEYITLTVRRIDEGTGSQWLT 86
Cdd:COG1018    5 PLRVVEVRRETPDVVSFTLEPPDgapLPRFRPGQFVTLRLPiDGKPLRRAYSLSSAPG-DGRLEITVKRVPGGGGSNWLH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  87 REVKRGDYLWLSDAMGEFTCDDKAEDKFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVIFAEEWR----N 162
Cdd:COG1018   84 DHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLARGPFRPVTLVYGARSPADLAFRDELEalaaR 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 364517353 163 YP-VTLVAEHNATHGFVAGRLTRELLQS-VPDLASRTVMTCGPAPYMEKVEQDVAALGV--TRFFKEK 226
Cdd:COG1018  164 HPrLRLHPVLSREPAGLQGRLDAELLAAlLPDPADAHVYLCGPPPMMEAVRAALAELGVpeERIHFER 231
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 11-227 1.22e-46

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 [Multi-domain]  Cd Length: 243  Bit Score: 157.77  E-value: 1.22e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  11 RMQVHHIHQETPDVWTLSLLC-HDYYPYRAGQYALVSV-RNSAETLRAYTLSSTPGVS-EYITLTVRRIDEGTGSQWLTR 87
Cdd:cd06216   19 RARVVAVRPETADMVTLTLRPnRGWPGHRAGQHVRLGVeIDGVRHWRSYSLSSSPTQEdGTITLTVKAQPDGLVSNWLVN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  88 EVKRGDYLWLSDAMGEFTCDDKAEDKFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVIFAEEWR----NY 163
Cdd:cd06216   99 HLAPGDVVELSQPQGDFVLPDPLPPRLLLIAAGSGITPVMSMLRTLLARGPTADVVLLYYARTREDVIFADELRalaaQH 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 364517353 164 PvTLVAEHNATHGFVAGRLTRELLQSV-PDLASRTVMTCGPAPYMEKVEQDVAALGV-TRFFKEKF 227
Cdd:cd06216  179 P-NLRLHLLYTREELDGRLSAAHLDAVvPDLADRQVYACGPPGFLDAAEELLEAAGLaDRLHTERF 243
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 11-227 8.62e-41

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 [Multi-domain]  Cd Length: 241  Bit Score: 142.30  E-value: 8.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  11 RMQVHHIHQETPDVWTLSL----LCHDYYPYRAGQYalVSVR---NSAETLRAYTLSSTPGvSEYITLTVRRIDEGTGSQ 83
Cdd:cd06214    3 PLTVAEVVRETADAVSITFdvpeELRDAFRYRPGQF--LTLRvpiDGEEVRRSYSICSSPG-DDELRITVKRVPGGRFSN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  84 WLTREVKRGDYLWLSDAMGEFTCDDKAEDK-FLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVIFAEEWRN 162
Cdd:cd06214   80 WANDELKAGDTLEVMPPAGRFTLPPLPGARhYVLFAAGSGITPVLSILKTALAREPASRVTLVYGNRTEASVIFREELAD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 163 ----YPVTLVAEH--NATHGFVA---GRLTRELLQS-----VPDLASRTVMTCGPAPYMEKVEQDVAALGV--TRFFKEK 226
Cdd:cd06214  160 lkarYPDRLTVIHvlSREQGDPDllrGRLDAAKLNAllknlLDATEFDEAFLCGPEPMMDAVEAALLELGVpaERIHREL 239


                 .
gi 364517353 227 F 227
Cdd:cd06214  240 F 240
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 17-221 2.47e-39

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 [Multi-domain]  Cd Length: 235  Bit Score: 138.55  E-value: 2.47e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  17 IHQETPDVWTLSLLCHD--YYPYRAGQYALVSVRNSA--ETLRAYTLSSTPGVSEYITLTVRRIDEGTGSQWLTREVKRG 92
Cdd:cd06217    9 IIQETPTVKTFRLAVPDgvPPPFLAGQHVDLRLTAIDgyTAQRSYSIASSPTQRGRVELTVKRVPGGEVSPYLHDEVKVG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  93 DYLWLSDAMGEFTCDDKAEDKFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVIFAEEWR-------NYPV 165
Cdd:cd06217   89 DLLEVRGPIGTFTWNPLHGDPVVLLAGGSGIVPLMSMIRYRRDLGWPVPFRLLYSARTAEDVIFRDELEqlarrhpNLHV 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 364517353 166 TLVAEHNATHGFV--AGRLTRELLQS-VPDLASRTVMTCGPAPYMEKVEQDVAALGVTR 221
Cdd:cd06217  169 TEALTRAAPADWLgpAGRITADLIAElVPPLAGRRVYVCGPPAFVEAATRLLLELGVPR 227
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 9-230 2.32e-38

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: 136.15  E-value: 2.32e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353   9 PWR-MQVHHIHQETPDVWTLSLLCHDY---YPYRAGQYalVSVR-----NSAETLRAYTLSSTPGvSEYITLTVRRIDEG 79
Cdd:cd06184    5 GFRpFVVARKVAESEDITSFYLEPADGgplPPFLPGQY--LSVRvklpgLGYRQIRQYSLSDAPN-GDYYRISVKREPGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  80 TGSQWLTREVKRGDYLWLSDAMGEFTCDDKAEDKFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVIFAEE 159
Cdd:cd06184   82 LVSNYLHDNVKVGDVLEVSAPAGDFVLDEASDRPLVLISAGVGITPMLSMLEALAAEGPGRPVTFIHAARNSAVHAFRDE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 160 WRNypvtLVAEH-NAT---------------HGFVAGRLTRELLQSVPDLASRTVMTCGPAPYMEKVEQDVAALGV--TR 221
Cdd:cd06184  162 LEE----LAARLpNLKlhvfysepeagdreeDYDHAGRIDLALLRELLLPADADFYLCGPVPFMQAVREGLKALGVpaER 237


                 ....*....
gi 364517353 222 FFKEkFFTP 230
Cdd:cd06184  238 IHYE-VFGP 245
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 16-227 2.36e-36

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 [Multi-domain]  Cd Length: 231  Bit Score: 130.72  E-value: 2.36e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  16 HIHQETPDVWTLSLLC--HDYYPYRAGQYALVSVRNSAETL-RAYTLSSTPGVSEyITLTVRRIDEGTGSQWLTREVKRG 92
Cdd:cd06191    5 EVRSETPDAVTIVFAVpgPLQYGFRPGQHVTLKLDFDGEELrRCYSLCSSPAPDE-ISITVKRVPGGRVSNYLREHIQPG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  93 DYLWLSDAMGEFTCDDKAEDKFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVIFAEEWR-------NYPV 165
Cdd:cd06191   84 MTVEVMGPQGHFVYQPQPPGRYLLVAAGSGITPLMAMIRATLQTAPESDFTLIHSARTPADMIFAQELReladkpqRLRL 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 166 T-----LVAEHNATHGfvAGRLTRELLQS-VPDLASRTVMTCGPAPYMEKVEQDVAALGV--TRFFKEKF 227
Cdd:cd06191  164 LciftrETLDSDLLHG--RIDGEQSLGAAlIPDRLEREAFICGPAGMMDAVETALKELGMppERIHTERF 231
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 17-225 1.25e-35

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: 128.33  E-value: 1.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  17 IHQETPDVWTLSLLCHDYYPYRAGQYALVSVRNSAETL-RAYTLSSTPGVSEYITLTVRRIDEGTGSQWLTREvKRGDYL 95
Cdd:cd00322    3 TEDVTDDVRLFRLQLPNGFSFKPGQYVDLHLPGDGRGLrRAYSIASSPDEEGELELTVKIVPGGPFSAWLHDL-KPGDEV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  96 WLSDAMGEFTCDDKAEDKFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVIFAEEWRNypvtLVAEHNATH 175
Cdd:cd00322   82 EVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGARTPADLLFLDELEE----LAKEGPNFR 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 364517353 176 --------------GFVAGRLTRELLQSVPDLASRTVMTCGPAPYMEKVEQDVAALGVT--RFFKE 225
Cdd:cd00322  158 lvlalsreseaklgPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPeeRIHTE 223
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 13-288 1.97e-31

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 118.04  E-value: 1.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  13 QVHHIHQETPDVWTLSL-LCHDYYPYRAGQYALVSVRNSAETlRAYTLSSTPGVSEYITLTVRRIdeGTGSQWLtREVKR 91
Cdd:COG0543    1 KVVSVERLAPDVYLLRLeAPLIALKFKPGQFVMLRVPGDGLR-RPFSIASAPREDGTIELHIRVV--GKGTRAL-AELKP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  92 GDYLWLSDAMGEFTCDDKAEDKFLLLAAGCGVTPIMAM-RRWLAKYRPqadVQVIYNVRSPEDVIFAEE---WRNYPVTl 167
Cdd:COG0543   77 GDELDVRGPLGNGFPLEDSGRPVLLVAGGTGLAPLRSLaEALLARGRR---VTLYLGARTPEDLYLLDEleaLADFRVV- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 168 VAEHNATHGFVaGRLTRELLQSVPDLASRTVMTCGPAPYMEKVEQDVAALGVtrffkekfftpvaeaatsglkftklqPA 247
Cdd:COG0543  153 VTTDDGWYGRK-GFVTDALKELLAEDSGDDVYACGPPPMMKAVAELLLERGV--------------------------PP 205

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 364517353 248 REFYApvgttlldALESNkvpvtVACRAGVCGCCKTKVVSG 288
Cdd:COG0543  206 ERIYV--------SLERR-----MACGIGMCGGCVVPVGGG 233
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
9-227 5.04e-30

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 118.07  E-value: 5.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353   9 PWRMQVHH-----IHQETPDVW--TLSLLCHDYYPYRAGQYALVSVRNSAETLRA--YTLSSTPGVSEYITLTVRRIdeG 79
Cdd:COG4097  209 PLRSRRHPyrvesVEPEAGDVVelTLRPEGGRWLGHRAGQFAFLRFDGSPFWEEAhpFSISSAPGGDGRLRFTIKAL--G 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  80 TGSQWLTReVKRGDYLWLSDAMGEFTCDDKAE-DKFLLLAAGCGVTPIMAMRRWLA-KYRPQADVQVIYNVRSPEDVIFA 157
Cdd:COG4097  287 DFTRRLGR-LKPGTRVYVEGPYGRFTFDRRDTaPRQVWIAGGIGITPFLALLRALAaRPGDQRPVDLFYCVRDEEDAPFL 365

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 364517353 158 EE-----WRNYPVTLVaEHNATHGfvaGRLTRELL-QSVPDLASRTVMTCGPAPYMEKVEQDVAALGV--TRFFKEKF 227
Cdd:COG4097  366 EElralaARLAGLRLH-LVVSDED---GRLTAERLrRLVPDLAEADVFFCGPPGMMDALRRDLRALGVpaRRIHQERF 439
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 20-227 7.93e-30

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: 112.74  E-value: 7.93e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  20 ETPDVWTLSL-LCHDYYPYRAGQYALVSV-RNSAETLRAYTLSSTPGVSEYITLTVRRIDEGTGSqwLTREVKRGDYLWL 97
Cdd:cd06198    5 EVRPTTTLTLePRGPALGHRAGQFAFLRFdASGWEEPHPFTISSAPDPDGRLRFTIKALGDYTRR--LAERLKPGTRVTV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  98 SDAMGEFTCDDkAEDKFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVIFAEEWRnypvTLVAEHNAT-H- 175
Cdd:cd06198   83 EGPYGRFTFDD-RRARQIWIAGGIGITPFLALLEALAARGDARPVTLFYCVRDPEDAVFLDELR----ALAAAAGVVlHv 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 364517353 176 --GFVAGRLT--RELLQSVPDLASRTVMTCGPAPYMEKVEQDVAALGV--TRFFKEKF 227
Cdd:cd06198  158 idSPSDGRLTleQLVRALVPDLADADVWFCGPPGMADALEKGLRALGVpaRRFHYERF 215
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 14-227 1.27e-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 [Multi-domain]  Cd Length: 224  Bit Score: 99.20  E-value: 1.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  14 VHHIHQETPDVWTLSLLCHDYYPYRAGQYALVSVRNSAETLRAYTLSSTPGVSEYITLTVRRIDEGTGSQWLTREVKRGD 93
Cdd:cd06187    1 VVSVERLTHDIAVVRLQLDQPLPFWAGQYVNVTVPGRPRTWRAYSPANPPNEDGEIEFHVRAVPGGRVSNALHDELKVGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  94 YLWLSDAMGEFTCDDKAEDKFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVI-------FAEEWRNYPVT 166
Cdd:cd06187   81 RVRLSGPYGTFYLRRDHDRPVLCIAGGTGLAPLRAIVEDALRRGEPRPVHLFFGARTERDLYdlegllaLAARHPWLRVV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 364517353 167 LVAEH--NATHGFVaGRLTRELLQSVPDLASRTVMTCGPAPYMEKVEQDVAALGV--TRFFKEKF 227
Cdd:cd06187  161 PVVSHeeGAWTGRR-GLVTDVVGRDGPDWADHDIYICGPPAMVDATVDALLARGAppERIHFDKF 224
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 37-227 1.15e-23

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 [Multi-domain]  Cd Length: 228  Bit Score: 96.89  E-value: 1.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  37 YRAGQYALVSVRNSAETlRAYTLSSTPGVSEyITLTVRRIDEGTGSQWLTREVKRGDYLWLSDAMGEFTCDDKaEDKFLL 116
Cdd:cd06209   31 FLPGQYVNLQVPGTDET-RSYSFSSAPGDPR-LEFLIRLLPGGAMSSYLRDRAQPGDRLTLTGPLGSFYLREV-KRPLLM 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 117 LAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVI-------FAEEWRNYPV-TLVAEHNATH---GFVAGRLTRE 185
Cdd:cd06209  108 LAGGTGLAPFLSMLDVLAEDGSAHPVHLVYGVTRDADLVeldrleaLAERLPGFSFrTVVADPDSWHprkGYVTDHLEAE 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 364517353 186 LLQSvPDlasRTVMTCGPAPYMEKVEQDVAALGVT--RFFKEKF 227
Cdd:cd06209  188 DLND-GD---VDVYLCGPPPMVDAVRSWLDEQGIEpaNFYYEKF 227
Fdx COG0633
Ferredoxin [Energy production and conversion];
248-321 2.12e-23

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 91.83  E-value: 2.12e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 364517353 248 REFYAPVGTTLLDALESNKVPVTVACRAGVCGCCKTKVVSGKYSVTSTMTLTDAEIADGYVLACSCHPQSDLVL 321
Cdd:COG0633   11 HTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARPTSDLVV 84
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 17-219 8.22e-22

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 [Multi-domain]  Cd Length: 211  Bit Score: 91.39  E-value: 8.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  17 IHQETPDVWTLSL-------LChdyyPYRAGQYALVSVRNsaETLRAYTLSSTPGVSEYITLTVRRIDEGT-GSQWLTRE 88
Cdd:cd06185    3 IRDEAPDIRSFELeapdgapLP----AFEPGAHIDVHLPN--GLVRQYSLCGDPADRDRYRIAVLREPASRgGSRYMHEL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  89 VKRGDYLWLSDAMGEFTCDDKAeDKFLLLAAGCGVTPIMAMRRWLAkyRPQADVQVIYNVRSPEDVIFAEEWRNYP---V 165
Cdd:cd06185   77 LRVGDELEVSAPRNLFPLDEAA-RRHLLIAGGIGITPILSMARALA--ARGADFELHYAGRSREDAAFLDELAALPgdrV 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 364517353 166 TLVAEHnathgfVAGRLT-RELLQSVPdlASRTVMTCGPAPYMEKVEQDVAALGV 219
Cdd:cd06185  154 HLHFDD------EGGRLDlAALLAAPP--AGTHVYVCGPEGMMDAVRAAAAALGW 200
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 17-220 3.36e-21

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 [Multi-domain]  Cd Length: 218  Bit Score: 89.99  E-value: 3.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  17 IHQETPDVWTLSLLCHDYYPYRAGQYALVSVRNSA--ETLRAYTLSSTPGvSEYITLTVRRIDEGTGsqwLTREVKR--- 91
Cdd:cd06196    8 IEPVTHDVKRLRFDKPEGYDFTPGQATEVAIDKPGwrDEKRPFTFTSLPE-DDVLEFVIKSYPDHDG---VTEQLGRlqp 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  92 GDYLWLSDAMGEFTcdDKAEDKFLllAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVIFAEEWRNYP---VTLV 168
Cdd:cd06196   84 GDTLLIEDPWGAIE--YKGPGVFI--AGGAGITPFIAILRDLAAKGKLEGNTLIFANKTEKDIILKDELEKMLglkFINV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 364517353 169 AEHNATHGFVAGRLTRELLQSVPDLASRTVMTCGPAPYMEKVEQDVAALGVT 220
Cdd:cd06196  160 VTDEKDPGYAHGRIDKAFLKQHVTDFNQHFYVCGPPPMEEAINGALKELGVP 211
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 248-321 4.70e-21

2Fe-2S iron-sulfur cluster 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). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 85.52  E-value: 4.70e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 364517353 248 REFYAPVGTTLLDALESNKVPVTVACRAGVCGCCKTKVVSGKYSVTSTMTLTDAEIADGYVLACSCHPQSDLVL 321
Cdd:cd00207   10 VEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVTDGLVI 83
PRK13289 PRK13289
NO-inducible flavohemoprotein;
36-235 2.42e-19

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 87.55  E-value: 2.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  36 PYRAGQYALVSVRNSAETL---RAYTLSSTPGVSEY-ITltVRRIDEGTGSQWLTREVKRGDYLWLSDAMGEFTCDDKAE 111
Cdd:PRK13289 184 DFKPGQYLGVRLDPEGEEYqeiRQYSLSDAPNGKYYrIS--VKREAGGKVSNYLHDHVNVGDVLELAAPAGDFFLDVASD 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 112 DKFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVIFAEEWRnypvTLVAEH-----------------NAT 174
Cdd:PRK13289 262 TPVVLISGGVGITPMLSMLETLAAQQPKRPVHFIHAARNGGVHAFRDEVE----ALAARHpnlkahtwyrepteqdrAGE 337

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 364517353 175 HGFVAGRLTRELLQSVPDLASRTVMTCGPAPYMEKVEQDVAALGV--TRFFKEkFFTPVAEAA 235
Cdd:PRK13289 338 DFDSEGLMDLEWLEAWLPDPDADFYFCGPVPFMQFVAKQLLELGVpeERIHYE-FFGPAKVLE 399
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 21-164 5.35e-18

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: 81.53  E-value: 5.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  21 TPDVWTLSLLCHDYYPYRAGQYALVSVrNSAETLRAYTLSSTPGVSEYITLTVRRIDEGTGSQWLTREVKRGDYLWLSDA 100
Cdd:cd06190    8 THDVAEFRFALDGPADFLPGQYALLAL-PGVEGARAYSMANLANASGEWEFIIKRKPGGAASNALFDNLEPGDELELDGP 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 364517353 101 MGEFTCDDKAEDKFLLLAAGCGVTPIMAMRRWLAKYRPQAD--VQVIYNVRSPEDVIFAEEWRNYP 164
Cdd:cd06190   87 YGLAYLRPDEDRDIVCIAGGSGLAPMLSILRGAARSPYLSDrpVDLFYGGRTPSDLCALDELSALV 152
COG3894 COG3894
Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain ...
 248-320 5.18e-16

Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain [Function unknown];


Pssm-ID: 443101 [Multi-domain]  Cd Length: 621  Bit Score: 78.69  E-value: 5.18e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 364517353 248 REFYAPVGTTLLDALESNKVPVTVACR-AGVCGCCKTKVVSGKYS-VTSTMT--LTDAEIADGYVLACSCHPQSDLV 320
Cdd:COG3894   13 KRVEVEAGTTLLDAAREAGVDIDAPCGgRGTCGKCKVKVEEGEFSpVTEEERrlLSPEELAEGYRLACQARVLGDLV 89
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 21-228 8.23e-16

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 [Multi-domain]  Cd Length: 222  Bit Score: 75.00  E-value: 8.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  21 TPDVWTLSLLCHDYYPYRAGQYalVSVRNSAETLRAYTLSSTPGVSEYITLTVRRIDEGTGSQWLTREVKRGDYLWLSDA 100
Cdd:cd06194    8 SPDVLRVRLEPDRPLPYLPGQY--VNLRRAGGLARSYSPTSLPDGDNELEFHIRRKPNGAFSGWLGEEARPGHALRLQGP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 101 MGefTC---DDKAEDKFLLLAAGCGVTPIMAMRRwLAKYR-PQADVQVIYNVRSPEDVIFAEE--W--RNYPVTL----V 168
Cdd:cd06194   86 FG--QAfyrPEYGEGPLLLVGAGTGLAPLWGIAR-AALRQgHQGEIRLVHGARDPDDLYLHPAllWlaREHPNFRyipcV 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 364517353 169 AEHNATHGFV-AGRLTRELLQSVPDlasRTVMTCGPAPYMEKVEQDVAALGV--TRFFKEKFF 228
Cdd:cd06194  163 SEGSQGDPRVrAGRIAAHLPPLTRD---DVVYLCGAPSMVNAVRRRAFLAGApmKRIYADPFE 222
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 12-223 1.06e-15

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 [Multi-domain]  Cd Length: 224  Bit Score: 74.89  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  12 MQVHHIHQETPDVWTLSLLCHDYYPYRAGQYALVSVRNsaETLRAYTLSSTPGVSEYITLTVRRIDEGTGSQWLTREVKR 91
Cdd:cd06189    1 CKVESIEPLNDDVYRVRLKPPAPLDFLAGQYLDLLLDD--GDKRPFSIASAPHEDGEIELHIRAVPGGSFSDYVFEELKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  92 GDYLWLSDAMGEFTCDDKAEDKFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVI-------FAEEWRNY- 163
Cdd:cd06189   79 NGLVRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQGSKRPIHLYWGARTEEDLYldelleaWAEAHPNFt 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 364517353 164 --PVTLVAEHNATH--GFVAgrltRELLQSVPDLASRTVMTCGPaPYMEKVEQDV---AALGVTRFF 223
Cdd:cd06189  159 yvPVLSEPEEGWQGrtGLVH----EAVLEDFPDLSDFDVYACGS-PEMVYAARDDfveKGLPEENFF 220
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 17-220 1.09e-15

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: 75.34  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  17 IHQETPD--VWTLSLLCHDY--YPYRAGQYALVSVRNSAETlrAYTLSSTPGVSEYITLTVRRIdeGTgsqwLTR---EV 89
Cdd:cd06221    4 VVDETEDikTFTLRLEDDDEelFTFKPGQFVMLSLPGVGEA--PISISSDPTRRGPLELTIRRV--GR----VTEalhEL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  90 KRGDYLWLSDAMGEFTCDDKAEDKFLLLAA-GCGVTPIMAMRRWLAKYRP-QADVQVIYNVRSPEDVIFAEE---WRNYP 164
Cdd:cd06221   76 KPGDTVGLRGPFGNGFPVEEMKGKDLLLVAgGLGLAPLRSLINYILDNREdYGKVTLLYGARTPEDLLFKEElkeWAKRS 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 364517353 165 ---VTLVAEHNATH--GFVaGRLTRELLQSVPDLASRTVMTCGPAPYMEKVEQDVAALGVT 220
Cdd:cd06221  156 dveVILTVDRAEEGwtGNV-GLVTDLLPELTLDPDNTVAIVCGPPIMMRFVAKELLKLGVP 215
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 36-227 3.42e-15

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 [Multi-domain]  Cd Length: 232  Bit Score: 73.52  E-value: 3.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  36 PYRAGQYALVSVRNSAETlRAYTLSSTPGVSEYITLTVRRIDEGTGSQWLTREVKRGDYLWLSDAMGEFTCDDKAEDKFL 115
Cdd:cd06212   29 KFFAGQYVDITVPGTEET-RSFSMANTPADPGRLEFIIKKYPGGLFSSFLDDGLAVGDPVTVTGPYGTCTLRESRDRPIV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 116 LLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVIFAEEWRNY----------PVTLVAEHNATHGFVAGRLTRE 185
Cdd:cd06212  108 LIGGGSGMAPLLSLLRDMAASGSDRPVRFFYGARTARDLFYLEEIAALgekipdftfiPALSESPDDEGWSGETGLVTEV 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 364517353 186 LLQSVPDLASRTVMTCGPAPYMEKVEQDVAALGVT--RFFKEKF 227
Cdd:cd06212  188 VQRNEATLAGCDVYLCGPPPMIDAALPVLEMSGVPpdQIFYDKF 231
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 1-212 3.86e-15

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 73.75  E-value: 3.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353   1 MTMPTsqcpwRMQVHHIHQETPDVWTLSLLCHDYYPYRAGQYALVSVRNSAETL-RAYTLSSTPGvsEYITLTVRRidEG 79
Cdd:PRK00054   1 MMKPE-----NMKIVENKEIAPNIYTLVLDGEKVFDMKPGQFVMVWVPGVEPLLeRPISISDIDK--NEITILYRK--VG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  80 TGSQWLTrEVKRGDYLWLsdaMG----EFTCDDKaEDKFLLLAAGCGVTPIMAmrrwLAKY--RPQADVQVIYNVRSPED 153
Cdd:PRK00054  72 EGTKKLS-KLKEGDELDI---RGplgnGFDLEEI-GGKVLLVGGGIGVAPLYE----LAKElkKKGVEVTTVLGARTKDE 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 364517353 154 VIFAEEWRNYPVTLVAEHNAT---HGFVAGRLTREllqsvpDLASRTVMTCGPAPYMEKVEQ 212
Cdd:PRK00054 143 VIFEEEFAKVGDVYVTTDDGSygfKGFVTDVLDEL------DSEYDAIYSCGPEIMMKKVVE 198
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 14-202 9.00e-15

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 [Multi-domain]  Cd Length: 241  Bit Score: 72.60  E-value: 9.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  14 VHHIhqeTPDVWTLSLLCHDYYPYRAGQYALVSVRNSAETL--RAYTLSSTPGvSEYITLTVRRIDEGTGSQWLtREVKR 91
Cdd:cd06195    5 RRDW---TDDLFSFRVTRDIPFRFQAGQFTKLGLPNDDGKLvrRAYSIASAPY-EENLEFYIILVPDGPLTPRL-FKLKP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  92 GDYLWLSD-AMGEFTCDDKAEDK-FLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVIFAEEWRN------- 162
Cdd:cd06195   80 GDTIYVGKkPTGFLTLDEVPPGKrLWLLATGTGIAPFLSMLRDLEIWERFDKIVLVHGVRYAEELAYQDEIEAlakqyng 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 364517353 163 ----YP-VTLVAEHNATHG-----FVAGRLTRELLQSVPDLASRtVMTCG 202
Cdd:cd06195  160 kfryVPiVSREKENGALTGripdlIESGELEEHAGLPLDPETSH-VMLCG 208
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 12-210 1.34e-14

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: 71.90  E-value: 1.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  12 MQVHHIHQETPDVWTLSL-LCHDYYPyraGQYALVSVRNSAEtlRAYTLSSTPGVSEyitLTVRRIDEGTGSQWltrEVK 90
Cdd:cd06220    1 VTIKEVIDETPTVKTFVFdWDFDFKP---GQFVMVWVPGVDE--IPMSLSYIDGPNS---ITVKKVGEATSALH---DLK 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  91 RGDYLWLSDAMGE-FTCDDKaedKFLLLAAGCGVTPIMAMrrwLAKYRPQADVQVIYNVRSPEDVIFAEEWRNYPVTLVA 169
Cdd:cd06220   70 EGDKLGIRGPYGNgFELVGG---KVLLIGGGIGIAPLAPL---AERLKKAADVTVLLGARTKEELLFLDRLRKSDELIVT 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 364517353 170 EHNAT---HGFVAGRLtRELLQSVPDlasrTVMTCGPAPYMEKV 210
Cdd:cd06220  144 TDDGSygfKGFVTDLL-KELDLEEYD----AIYVCGPEIMMYKV 182
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 36-227 4.82e-14

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: 70.45  E-value: 4.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  36 PYRAGQYALVSVRNSAETlRAYTLSSTP---GVSEYItltVRRIDEGTGSQWLTREVKRGDYLWLSDAMGEFTCDDKAED 112
Cdd:cd06210   34 EFVPGQFVEIEIPGTDTR-RSYSLANTPnwdGRLEFL---IRLLPGGAFSTYLETRAKVGQRLNLRGPLGAFGLRENGLR 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 113 KFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSpEDVIF--------AEEWRNYPVTLVAEHNATH-----GFVA 179
Cdd:cd06210  110 PRWFVAGGTGLAPLLSMLRRMAEWGEPQEARLFFGVNT-EAELFyldelkrlADSLPNLTVRICVWRPGGEwegyrGTVV 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 364517353 180 GRLTREL--LQSVPDlasrtVMTCGPAPYMEKVEQDVAALGV--TRFFKEKF 227
Cdd:cd06210  189 DALREDLasSDAKPD-----IYLCGPPGMVDAAFAAAREAGVpdEQVYLEKF 235
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 55-229 7.64e-14

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 [Multi-domain]  Cd Length: 234  Bit Score: 69.90  E-value: 7.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  55 RAYTLSSTPGVSEYITLTVRRIDEGTGSQWLTReVKRGDYLWLSDAMGEFTC-DDKAEDKFLLLAAGCGVTPIM-AMRRW 132
Cdd:cd06183   48 RPYTPISPDDDKGYFDLLIKIYPGGKMSQYLHS-LKPGDTVEIRGPFGKFEYkPNGKVKHIGMIAGGTGITPMLqLIRAI 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 133 LAKYRPQADVQVIYNVRSPEDVIFAEEW----RNYP----VTLV---AEHNATHGfvAGRLTRELLQSV--PDLASRT-V 198
Cdd:cd06183  127 LKDPEDKTKISLLYANRTEEDILLREELdelaKKHPdrfkVHYVlsrPPEGWKGG--VGFITKEMIKEHlpPPPSEDTlV 204

                        170       180       190
                 ....*....|....*....|....*....|..
gi 364517353 199 MTCGPAPYMEK-VEQDVAALGvtrFFKEKFFT 229
Cdd:cd06183  205 LVCGPPPMIEGaVKGLLKELG---YKKDNVFK 233
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
248-316 2.05e-13

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 64.47  E-value: 2.05e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  248 REFYAPVG-TTLLDALESNKVPVTVACRAGVCGCCKTKVVSGKYSVTSTMTLTDAEIADGYVLACSCHPQ 316
Cdd:pfam00111   8 VTIEVPDGeTTLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSFLEDDELAAGYVVLACQTYPK 77
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 243-321 1.63e-12

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 67.20  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 243 KLQPA-REFYAPVGTTLLDALESNKVPVTVACRAGVCGCCKTKVVSGK--YSVTSTMTLTDAEIADGYVLACSCHPQSDL 319
Cdd:PRK07609   6 TLQPSgRQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEveQGPHQASALSGEERAAGEALTCCAKPLSDL 85


                 ..
gi 364517353 320 VL 321
Cdd:PRK07609  86 VL 87
PRK10713 PRK10713
2Fe-2S ferredoxin-like protein;
256-319 4.28e-12

2Fe-2S ferredoxin-like protein;


Pssm-ID: 182668 [Multi-domain]  Cd Length: 84  Bit Score: 61.28  E-value: 4.28e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 364517353 256 TTLLDALESNKVPVTVACRAGVCGCCKTKVVSGKYSVTSTMTltdAEIADGYVLACSCHPQSDL 319
Cdd:PRK10713  20 PSLLAALESHNVAVEYQCREGYCGSCRTRLVAGQVDWIAEPL---AFIQPGEILPCCCRAKGDI 80
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 37-229 9.57e-12

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: 63.88  E-value: 9.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  37 YRAGQYALVSVRNsAETLRAYTLSSTPGVSEYITLTVRRIDEGTGSQWLTREVKRGDYLWLSDAMGEFTCDDKAEDKFLL 116
Cdd:cd06211   36 FQAGQYVNLQAPG-YEGTRAFSIASSPSDAGEIELHIRLVPGGIATTYVHKQLKEGDELEISGPYGDFFVRDSDQRPIIF 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 117 LAAGCGVTPIMAMrrwLAKYRPQAD---VQVIYNVRSPEDVI-------FAEEWRN--YPVTLVAEH-----NATHGFV- 178
Cdd:cd06211  115 IAGGSGLSSPRSM---ILDLLERGDtrkITLFFGARTRAELYyldefeaLEKDHPNfkYVPALSREPpesnwKGFTGFVh 191

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 364517353 179 --AGRLTREllqsvpDLASRTVMTCGPAPYMEKVeqdVAALGVTRFFKEKFFT 229
Cdd:cd06211  192 daAKKHFKN------DFRGHKAYLCGPPPMIDAC---IKTLMQGRLFERDIYY 235
PLN03136 PLN03136
Ferredoxin; Provisional
 231-321 2.83e-11

Ferredoxin; Provisional


Pssm-ID: 178681 [Multi-domain]  Cd Length: 148  Bit Score: 60.53  E-value: 2.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 231 VAEAATSGLKFTKLQPAREFYAPVGTTLLDALESNKVPVTVACRAGVCGCCKTKVVSGKYSVTSTMTLTDAEIADGYVLA 310
Cdd:PLN03136  49 VTAMATYKVKFITPEGEQEVECEEDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSIDQSDQSFLDDEQISEGYVLT 128

                         90
                 ....*....|.
gi 364517353 311 CSCHPQSDLVL 321
Cdd:PLN03136 129 CVAYPTSDVVI 139
petF CHL00134
ferredoxin; Validated
 258-318 1.72e-10

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 57.04  E-value: 1.72e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 364517353 258 LLDALESNKVPVTVACRAGVCGCCKTKVVSGKYSVTSTMTLTDAEIADGYVLACSCHPQSD 318
Cdd:CHL00134  27 ILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQSDQSFLDDDQLEAGFVLTCVAYPTSD 87
PTZ00038 PTZ00038
ferredoxin; Provisional
 258-321 1.44e-09

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 56.77  E-value: 1.44e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 364517353 258 LLDALESNKVPVTVACRAGVCGCCKTKVVSGKYSVTSTMTLTDAEIADGYVLACSCHPQSDLVL 321
Cdd:PTZ00038 117 ILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYLDDEQLKKGYCLLCTCYPKSDCTI 180
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
 249-321 1.59e-09

ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ferredoxins. In general, these occur as a single domain proteins or with a chloroplast transit peptide. Species tend to be photosynthetic, but several forms may occur in one species and individually may not be associated with photocynthesis. Halobacterial forms differ somewhat in architecture; they score between trusted and noise cutoffs. Sequences scoring below the noise cutoff tend to be ferredoxin-related domains of larger proteins.


Pssm-ID: 273926 [Multi-domain]  Cd Length: 97  Bit Score: 54.38  E-value: 1.59e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 364517353  249 EFYAPVGTTLLDALESNKVPVTVACRAGVCGCCKTKVVSGKYSVTSTMTLTDAEIADGYVLACSCHPQSDLVL 321
Cdd:TIGR02008  16 TIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDQMEAGYVLTCVAYPTSDCTI 88
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 38-219 1.75e-09

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: 57.17  E-value: 1.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  38 RAGQYALVSVRNSAETL--RAYTLSSTPGVSEYITLTVRRIDEGTgsQWLTrEVKRGDYLwlsDAMGE----FTcDDKAE 111
Cdd:cd06218   26 KPGQFVMLRVPDGSDPLlrRPISIHDVDPEEGTITLLYKVVGKGT--RLLS-ELKAGDEL---DVLGPlgngFD-LPDDD 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 112 DKFLLLAAGCGVTPIMAMRRWLAKYRpqADVQVIYNVRSPEDVIFAEEWRNYPVTLvaeHNAT-------HGFVAGRLTR 184
Cdd:cd06218   99 GKVLLVGGGIGIAPLLFLAKQLAERG--IKVTVLLGFRSADDLFLVEEFEALGAEV---YVATddgsagtKGFVTDLLKE 173

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 364517353 185 ELLQSVPDLasrtVMTCGPAPYMEKVEQDVAALGV 219
Cdd:cd06218  174 LLAEARPDV----VYACGPEPMLKAVAELAAERGV 204
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 13-207 3.96e-09

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 56.80  E-value: 3.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  13 QVHHIHQETPDVWTLSLL--CHDYYPYRAGQYALVSVRNSAEtlRAYTLSSTPGVSEYITLTVRRIDEGTGSQWLTREVK 90
Cdd:PRK07609 106 RVASLERVAGDVMRLKLRlpATERLQYLAGQYIEFILKDGKR--RSYSIANAPHSGGPLELHIRHMPGGVFTDHVFGALK 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  91 RGDYLWLSDAMGEFTCDDKAEDKFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVI---FAEEW-RNYP-- 164
Cdd:PRK07609 184 ERDILRIEGPLGTFFLREDSDKPIVLLASGTGFAPIKSIVEHLRAKGIQRPVTLYWGARRPEDLYlsaLAEQWaEELPnf 263

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 364517353 165 --VTLVAEHNAT------HGFVAgrltRELLQSVPDLASRTVMTCGpAPYM 207
Cdd:PRK07609 264 ryVPVVSDALDDdawtgrTGFVH----QAVLEDFPDLSGHQVYACG-SPVM 309
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 38-221 1.17e-08

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 [Multi-domain]  Cd Length: 283  Bit Score: 55.39  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  38 RAGQYALVSVrNSAETLRAYTLSSTPGVSEYITLTVR---------RIDEGTGSQWLTrEVKRGDYLWLSDAMGEF-TCD 107
Cdd:cd06188   71 KFGLWQLVFK-HDEPVSRAYSLANYPAEEGELKLNVRiatpppgnsDIPPGIGSSYIF-NLKPGDKVTASGPFGEFfIKD 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 108 DKAEdkFLLLAAGCGVTPIMA-MRRWLAKYRPQADVQVIYNVRSPEDVIFAEEWRN---------YPVTL---VAEHNAT 174
Cdd:cd06188  149 TDRE--MVFIGGGAGMAPLRShIFHLLKTLKSKRKISFWYGARSLKELFYQEEFEAlekefpnfkYHPVLsepQPEDNWD 226

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 364517353 175 --HGFVAGRLTRELLQSVPDLASRTVMTCGPAPYMEKVEQDVAALGVTR 221
Cdd:cd06188  227 gyTGFIHQVLLENYLKKHPAPEDIEFYLCGPPPMNSAVIKMLDDLGVPR 275
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
33-227 5.37e-08

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 53.59  E-value: 5.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  33 DYYPyraGQYALVSVRNSaETLRAYTLSSTPGVSEYITLTVRRIDEGTGSQWLTREVKRGDYLWLSDAMGEFTCDdKAED 112
Cdd:PRK11872 136 DFLP---GQYARLQIPGT-DDWRSYSFANRPNATNQLQFLIRLLPDGVMSNYLRERCQVGDEILFEAPLGAFYLR-EVER 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 113 KFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVI-------FAEEWRNYPVTLV-----AEHNATHGFVAG 180
Cdd:PRK11872 211 PLVFVAGGTGLSAFLGMLDELAEQGCSPPVHLYYGVRHAADLCelqrlaaYAERLPNFRYHPVvskasADWQGKRGYIHE 290

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 364517353 181 RLTRELLQSvpdlASRTVMTCGPAPYMEKVEQ--DVAALGVTRFFKEKF 227
Cdd:PRK11872 291 HFDKAQLRD----QAFDMYLCGPPPMVEAVKQwlDEQALENYRLYYEKF 335
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 21-221 6.77e-08

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: 52.31  E-value: 6.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  21 TPDVWTLSLLCHDYYPYRAGQYALVSVrNSAETLRAYTLSSTPGVSEYITLTVRRIDEGTGSQWLTREVKRGDYLWLSDA 100
Cdd:cd06213   12 THDIVRLTVQLDRPIAYKAGQYAELTL-PGLPAARSYSFANAPQGDGQLSFHIRKVPGGAFSGWLFGADRTGERLTVRGP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 101 MGEFTCDDkAEDKFLLLAAGCGVTPIMAMRRWLAKYRPQADVQVIYNVRSPEDVI-------FAEEWRN----YPVtlVA 169
Cdd:cd06213   91 FGDFWLRP-GDAPILCIAGGSGLAPILAILEQARAAGTKRDVTLLFGARTQRDLYaldeiaaIAARWRGrfrfIPV--LS 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 364517353 170 EHNATH------GFVAGRLTRELLQSVpdlasrTVMTCGPAPYMEKVEQDVAALGVTR 221
Cdd:cd06213  168 EEPADSswkgarGLVTEHIAEVLLAAT------EAYLCGPPAMIDAAIAVLRALGIAR 219
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 36-229 1.34e-07

Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase


Pssm-ID: 442118 [Multi-domain]  Cd Length: 396  Bit Score: 52.56  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  36 PYRAGQYALVSV----------------------RNSAETLRAYTLSSTPGVSEYITLTVR------RIDEGTGSQWLtR 87
Cdd:COG2871  160 DFKAGQYIQIEVppyevdfkdfdipeeekfglfdKNDEEVTRAYSMANYPAEKGIIELNIRiatppmDVPPGIGSSYI-F 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  88 EVKRGDYLWLSDAMGEFTCDDKAEDKfLLLAAGCGVTPIMAM-RRWLAKYRPQADVQVIYNVRSPEDVIFAEEWRnypvT 166
Cdd:COG2871  239 SLKPGDKVTISGPYGEFFLRDSDREM-VFIGGGAGMAPLRSHiFDLLERGKTDRKITFWYGARSLRELFYLEEFR----E 313

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 167 LVAEH----------------NAT--HGFVAGRLTRELLQSVPDLASRTVMTCGPAPYMEKVEQDVAALGVTR---FFkE 225
Cdd:COG2871  314 LEKEHpnfkfhpalseplpedNWDgeTGFIHEVLYENYLKDHPAPEDCEAYLCGPPPMIDAVIKMLDDLGVEEeniYF-D 392


                 ....
gi 364517353 226 KFFT 229
Cdd:COG2871  393 DFGG 396
FNR_like_2 cd06197
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ...
 37-211 3.67e-07

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: 50.08  E-value: 3.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  37 YRAGQYALVS-----------VRNSAETL------RAYTLSSTPGVSEY---ITLTVRRIDEGTGS--QWLTREVKRGDY 94
Cdd:cd06197   26 WTPGQYITLDfsseldsgyshMADDDPQSlnddfvRTFTVSSAPPHDPAtdeFEITVRKKGPVTGFlfQVARRLREQGLE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  95 LWLSDAMGEFTCDDKAED---KFLLLAAGCGVTPIMAMRRWLAKYRPQA-DVQVIYNVRSPEDVIFAEEWRNYPvtlvae 170
Cdd:cd06197  106 VPVLGVGGEFTLSLPGEGaerKMVWIAGGVGITPFLAMLRAILSSRNTTwDITLLWSLREDDLPLVMDTLVRFP------ 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 364517353 171 hnathgfvagrltrELLQSVPDLASRTVMTCGPAPYMEKVE 211
Cdd:cd06197  180 --------------GLPVSTTLFITSEVYLCGPPALEKAVL 206
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
248-322 5.02e-07

iron-sulfur-binding ferredoxin reductase;


Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 50.49  E-value: 5.02e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 364517353 248 REFYAPVGTTLLDALESNKVPVTVACRAGVCGCCKTKVVSGKYSVTSTMTLTDAEIADGYVLACSCHPQSDLVLA 322
Cdd:PRK05713   9 RRWSVPAGSNLLDALNAAGVAVPYSCRAGSCHACLVRCLQGEPEDALPEALAAEKREQGWRLACQCRVVGDLRVE 83
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 37-210 6.85e-07

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: 49.63  E-value: 6.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  37 YRAGQYALVSVRNSAETLR-AYTLSSTPGVSEYITLTVRRIDEGTGsqWLTrEVKRGDYLWLsdaMGEF---TCDDKAED 112
Cdd:cd06192   25 FRPGQFVFLRNFESPGLERiPLSLAGVDPEEGTISLLVEIRGPKTK--LIA-ELKPGEKLDV---MGPLgngFEGPKKGG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 113 KFLLLAAGCGVTPIMAMRRwlAKYRPQADVQVIYNVRSPEDVIFAEEWRNYPVTLVAEHNATHGFVAGRLTRELLQSvPD 192
Cdd:cd06192   99 TVLLVAGGIGLAPLLPIAK--KLAANGNKVTVLAGAKKAKEEFLDEYFELPADVEIWTTDDGELGLEGKVTDSDKPI-PL 175

                        170
                 ....*....|....*...
gi 364517353 193 LASRTVMTCGPAPYMEKV 210
Cdd:cd06192  176 EDVDRIIVAGSDIMMKAV 193
PLN02252 PLN02252
nitrate reductase [NADPH]
 48-209 4.20e-06

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 48.52  E-value: 4.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  48 RNSAETLRAYTLSSTPGVSEYITLTVRRI---------DEGTGSQWLTrEVKRGDYLWLSDAMGE--------FTCDDKA 110
Cdd:PLN02252 677 INGKLCMRAYTPTSSDDEVGHFELVIKVYfknvhpkfpNGGLMSQYLD-SLPIGDTIDVKGPLGHieyagrgsFLVNGKP 755

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353 111 E--DKFLLLAAGCGVTPIMAMRRWLAKyRPQADVQ--VIYNVRSPEDVIFAEE---W-RNYP----VTLVAEHNATHG-- 176
Cdd:PLN02252 756 KfaKKLAMLAGGTGITPMYQVIQAILR-DPEDKTEmsLVYANRTEDDILLREEldrWaAEHPdrlkVWYVVSQVKREGwk 834

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 364517353 177 FVAGRLTRELL-QSVPDLASRTV-MTCGPAPYMEK 209
Cdd:PLN02252 835 YSVGRVTEAMLrEHLPEGGDETLaLMCGPPPMIEF 869
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 116-212 1.59e-05

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


Pssm-ID: 425503 [Multi-domain]  Cd Length: 109  Bit Score: 43.40  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517353  116 LLAAGCGVTPIMAM-RRWLAKYRPQADVQVIYNVRSPEDVIFAEEWRnypvTLVAEHNATHGFVA-------------GR 181
Cdd:pfam00175   1 MIAGGTGIAPVRSMlRAILEDPKDPTQVVLVFGNRNEDDILYREELD----ELAEKHPGRLTVVYvvsrpeagwtggkGR 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 364517353  182 LTRELLQSVPDLASRTVMT--CGPAPYMEKVEQ 212
Cdd:pfam00175  77 VQDALLEDHLSLPDEETHVyvCGPPGMIKAVRK 109
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
250-318 2.98e-05

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 45.12  E-value: 2.98e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 364517353 250 FYAPVGTT--LLDALESNKVPVTVACRAGVCGCCKTKVVSGKYS--VTSTMTLTDAEIADGYVLACSCHPQSD 318
Cdd:PRK11872  15 LFFPVGKDelLLDAALRNGINLPLDCREGVCGTCQGRCESGIYSqdYVDEDALSERDLAQRKMLACQTRVKSD 87
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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