NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|6322699|ref|NP_012772|]
View 

cytochrome-b5 reductase [Saccharomyces cerevisiae S288C]

Protein Classification

cytochrome b5 reductase family protein( domain architecture ID 10153046)

cytochrome b5 reductase family protein such as NADH-cytochrome b5 reductase that catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor; the cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes

CATH:  3.40.50.80
EC:  1.-.-.-
Gene Ontology:  GO:0016491
PubMed:  19997042

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
56-302 5.29e-101

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: 295.63  E-value: 5.29e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   56 LPISKIEEESHDTRRFTFKLPTEDSEMGLVLASALFAKFVTPkGSNVVRPYTPVSDLSQKGHFQLVVKHYEGGKMTSHLF 135
Cdd:cd06183   1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDD-GEQVVRPYTPISPDDDKGYFDLLIKIYPGGKMSQYLH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  136 GLKPNDTVSFKGPIMKWKWQPNQ-FKSITLLGAGTGINPLYQLAHHIVENPNDKTKVNLLYGNKTPQDILLRKELDALKE 214
Cdd:cd06183  80 SLKPGDTVEIRGPFGKFEYKPNGkVKHIGMIAGGTGITPMLQLIRAILKDPEDKTKISLLYANRTEEDILLREELDELAK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  215 KYPDKFNVTYFVddKQDDQDFDGEISFISKDFIQEHVP-GPKESTHLFVCGPPPFMNaysgekkspkdqGELIGILNNLG 293
Cdd:cd06183 160 KHPDRFKVHYVL--SRPPEGWKGGVGFITKEMIKEHLPpPPSEDTLVLVCGPPPMIE------------GAVKGLLKELG 225

                ....*....
gi 6322699  294 YSKDQVFKF 302
Cdd:cd06183 226 YKKDNVFKF 234
 
Name Accession Description Interval E-value
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
56-302 5.29e-101

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: 295.63  E-value: 5.29e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   56 LPISKIEEESHDTRRFTFKLPTEDSEMGLVLASALFAKFVTPkGSNVVRPYTPVSDLSQKGHFQLVVKHYEGGKMTSHLF 135
Cdd:cd06183   1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDD-GEQVVRPYTPISPDDDKGYFDLLIKIYPGGKMSQYLH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  136 GLKPNDTVSFKGPIMKWKWQPNQ-FKSITLLGAGTGINPLYQLAHHIVENPNDKTKVNLLYGNKTPQDILLRKELDALKE 214
Cdd:cd06183  80 SLKPGDTVEIRGPFGKFEYKPNGkVKHIGMIAGGTGITPMLQLIRAILKDPEDKTKISLLYANRTEEDILLREELDELAK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  215 KYPDKFNVTYFVddKQDDQDFDGEISFISKDFIQEHVP-GPKESTHLFVCGPPPFMNaysgekkspkdqGELIGILNNLG 293
Cdd:cd06183 160 KHPDRFKVHYVL--SRPPEGWKGGVGFITKEMIKEHLPpPPSEDTLVLVCGPPPMIE------------GAVKGLLKELG 225

                ....*....
gi 6322699  294 YSKDQVFKF 302
Cdd:cd06183 226 YKKDNVFKF 234
PLN02252 PLN02252
nitrate reductase [NADPH]
52-302 4.31e-54

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 188.73  E-value: 4.31e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699    52 KWIDLPISKIEEESHDTRRFTFKLPTEDSEMGL-----VLASAlfakfvTPKGSNVVRPYTPVSDLSQKGHFQLVVKHY- 125
Cdd:PLN02252 633 EKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLpvgkhVFLCA------TINGKLCMRAYTPTSSDDEVGHFELVIKVYf 706
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   126 --------EGGKMTSHLFGLKPNDTVSFKGPIMKWKW----------QPNQFKSITLLGAGTGINPLYQLAHHIVENPND 187
Cdd:PLN02252 707 knvhpkfpNGGLMSQYLDSLPIGDTIDVKGPLGHIEYagrgsflvngKPKFAKKLAMLAGGTGITPMYQVIQAILRDPED 786
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   188 KTKVNLLYGNKTPQDILLRKELDALKEKYPDKFNVTYFVDDKQDDQDFDGeISFISKDFIQEHVPGPKESTHLFVCGPPP 267
Cdd:PLN02252 787 KTEMSLVYANRTEDDILLREELDRWAAEHPDRLKVWYVVSQVKREGWKYS-VGRVTEAMLREHLPEGGDETLALMCGPPP 865
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 6322699   268 FMnaysgekkspkdQGELIGILNNLGYSKDQVFKF 302
Cdd:PLN02252 866 MI------------EFACQPNLEKMGYDKDSILVF 888
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
55-154 2.17e-41

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 138.87  E-value: 2.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699     55 DLPISKIEEESHDTRRFTFKLPTEDSEMGLVLASALFAKfVTPKGSNVVRPYTPVSDLSQKGHFQLVVKHYEGGKMTSHL 134
Cdd:pfam00970   1 PLTLVEKELVSHDTRIFRFALPHPDQVLGLPVGQHLFLR-LPIDGELVIRSYTPISSDDDKGYLELLVKVYPGGKMSQYL 79
                          90       100
                  ....*....|....*....|
gi 6322699    135 FGLKPNDTVSFKGPIMKWKW 154
Cdd:pfam00970  80 DELKIGDTIDFKGPLGRFEY 99
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
51-300 1.54e-31

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 117.20  E-value: 1.54e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   51 DKWIDLPISKIEEESHDTRRFTFKLPTedsemGLVLASAL---FAKF-VTPKGSNVVRPYTPVSDLSQkGHFQLVVKHYE 126
Cdd:COG1018   1 AGFRPLRVVEVRRETPDVVSFTLEPPD-----GAPLPRFRpgqFVTLrLPIDGKPLRRAYSLSSAPGD-GRLEITVKRVP 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  127 GGKMTSHLF-GLKPNDTVSFKGPIMKWKWQPNQFKSITLLGAGTGINPLYQLAHHIVENpNDKTKVNLLYGNKTPQDILL 205
Cdd:COG1018  75 GGGGSNWLHdHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLAR-GPFRPVTLVYGARSPADLAF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  206 RKELDALKEKYPdkfNVTYFVDDKQDDQDFDGeisFISKDFIQEHVPGPKEsTHLFVCGPPPFMNAysgekkspkdqgeL 285
Cdd:COG1018 154 RDELEALAARHP---RLRLHPVLSREPAGLQG---RLDAELLAALLPDPAD-AHVYLCGPPPMMEA-------------V 213
                       250
                ....*....|....*
gi 6322699  286 IGILNNLGYSKDQVF 300
Cdd:COG1018 214 RAALAELGVPEERIH 228
 
Name Accession Description Interval E-value
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
56-302 5.29e-101

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: 295.63  E-value: 5.29e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   56 LPISKIEEESHDTRRFTFKLPTEDSEMGLVLASALFAKFVTPkGSNVVRPYTPVSDLSQKGHFQLVVKHYEGGKMTSHLF 135
Cdd:cd06183   1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDD-GEQVVRPYTPISPDDDKGYFDLLIKIYPGGKMSQYLH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  136 GLKPNDTVSFKGPIMKWKWQPNQ-FKSITLLGAGTGINPLYQLAHHIVENPNDKTKVNLLYGNKTPQDILLRKELDALKE 214
Cdd:cd06183  80 SLKPGDTVEIRGPFGKFEYKPNGkVKHIGMIAGGTGITPMLQLIRAILKDPEDKTKISLLYANRTEEDILLREELDELAK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  215 KYPDKFNVTYFVddKQDDQDFDGEISFISKDFIQEHVP-GPKESTHLFVCGPPPFMNaysgekkspkdqGELIGILNNLG 293
Cdd:cd06183 160 KHPDRFKVHYVL--SRPPEGWKGGVGFITKEMIKEHLPpPPSEDTLVLVCGPPPMIE------------GAVKGLLKELG 225

                ....*....
gi 6322699  294 YSKDQVFKF 302
Cdd:cd06183 226 YKKDNVFKF 234
PLN02252 PLN02252
nitrate reductase [NADPH]
52-302 4.31e-54

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 188.73  E-value: 4.31e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699    52 KWIDLPISKIEEESHDTRRFTFKLPTEDSEMGL-----VLASAlfakfvTPKGSNVVRPYTPVSDLSQKGHFQLVVKHY- 125
Cdd:PLN02252 633 EKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLpvgkhVFLCA------TINGKLCMRAYTPTSSDDEVGHFELVIKVYf 706
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   126 --------EGGKMTSHLFGLKPNDTVSFKGPIMKWKW----------QPNQFKSITLLGAGTGINPLYQLAHHIVENPND 187
Cdd:PLN02252 707 knvhpkfpNGGLMSQYLDSLPIGDTIDVKGPLGHIEYagrgsflvngKPKFAKKLAMLAGGTGITPMYQVIQAILRDPED 786
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   188 KTKVNLLYGNKTPQDILLRKELDALKEKYPDKFNVTYFVDDKQDDQDFDGeISFISKDFIQEHVPGPKESTHLFVCGPPP 267
Cdd:PLN02252 787 KTEMSLVYANRTEDDILLREELDRWAAEHPDRLKVWYVVSQVKREGWKYS-VGRVTEAMLREHLPEGGDETLALMCGPPP 865
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 6322699   268 FMnaysgekkspkdQGELIGILNNLGYSKDQVFKF 302
Cdd:PLN02252 866 MI------------EFACQPNLEKMGYDKDSILVF 888
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
18-302 7.68e-42

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 146.52  E-value: 7.68e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699    18 GTVAIAAATAFYFAnrnqhsFVFNESNKVFKGDDKWIDLPISKIEEESHDTRRFTFKLPTEDSEMGLVLASAL-FAKFVT 96
Cdd:PTZ00319   4 LAVIIALGVAAFFA------FMFSRSPPVALDPDMFQHFKLIKKTEVTHDTFIFRFALHSPTQRLGLPIGQHIvFRCDCT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699    97 PKGSN--VVRPYTPVSDLSQKGHFQLVVKHY---------EGGKMTSHLFGLKPNDTVSFKGPIMKWKWQPNQFKSI--- 162
Cdd:PTZ00319  78 TPGKPetVQHSYTPISSDDEKGYVDFLIKVYfkgvhpsfpNGGRLSQHLYHMKLGDKIEMRGPVGKFEYLGNGTYTVhkg 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   163 ------------TLLGAGTGINPLYQLAHHIVENPNDKTKVNLLYGNKTPQDILLRKELDALKEKypDKFNVTYFVDDKQ 230
Cdd:PTZ00319 158 kgglktmhvdafAMIAGGTGITPMLQIIHAIKKNKEDRTKVFLVYANQTEDDILLRKELDEAAKD--PRFHVWYTLDREA 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322699   231 DDQDFDGEiSFISKDFIQEHVPGPK------ESTHLFVCGPPPFMnaysgekkspkdQGELIGILNNLGYSKDQVFKF 302
Cdd:PTZ00319 236 TPEWKYGT-GYVDEEMLRAHLPVPDpqnsgiKKVMALMCGPPPML------------QMAVKPNLEKIGYTADNMFTF 300
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
55-154 2.17e-41

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 138.87  E-value: 2.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699     55 DLPISKIEEESHDTRRFTFKLPTEDSEMGLVLASALFAKfVTPKGSNVVRPYTPVSDLSQKGHFQLVVKHYEGGKMTSHL 134
Cdd:pfam00970   1 PLTLVEKELVSHDTRIFRFALPHPDQVLGLPVGQHLFLR-LPIDGELVIRSYTPISSDDDKGYLELLVKVYPGGKMSQYL 79
                          90       100
                  ....*....|....*....|
gi 6322699    135 FGLKPNDTVSFKGPIMKWKW 154
Cdd:pfam00970  80 DELKIGDTIDFKGPLGRFEY 99
PTZ00274 PTZ00274
cytochrome b5 reductase; Provisional
27-302 3.93e-41

cytochrome b5 reductase; Provisional


Pssm-ID: 140300  Cd Length: 325  Bit Score: 145.06  E-value: 3.93e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699    27 AFYFANRNQHSFVFNESNKVFKGDDKwidLPISkieeesHDTRRFTFKLPTEDsEMGLVLASALFAKF---VTPKgSNVV 103
Cdd:PTZ00274  35 ALHFRNKPRPGRVFSQRYEPYQLGEV---IPIT------HDTALFRFLLHSEE-EFNLKPCSTLQACYkygVQPM-DQCQ 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   104 RPYTPVSDLSQKGHFQLVVKHYEGGKMTSHLFGLKPNDTVSFKGPIMKWKWQPNQFKSITLLGAGTGINPLYQLAHHIVE 183
Cdd:PTZ00274 104 RFYTPVTANHTKGYFDIIVKRKKDGLMTNHLFGMHVGDKLLFRSVTFKIQYRPNRWKHVGMIAGGTGFTPMLQIIRHSLT 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   184 NP-----NDKTKVNLLYGNKTPQDILLRKELDALKEKYPDKFNVTYFVDDKQDDQDFDGEISFISKDFIQEHVPGPKEST 258
Cdd:PTZ00274 184 EPwdsgeVDRTKLSFLFCNRTERHILLKGLFDDLARRYSNRFKVYYTIDQAVEPDKWNHFLGYVTKEMVRRTMPAPEEKK 263
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322699   259 H-LFVCGPPPFMNAYSGEKKS--------------PKDQGELI---GILNNLGYSKDQVFKF 302
Cdd:PTZ00274 264 KiIMLCGPDQLLNHVAGTPMGtmssmssgmniqpmAPDLNNLVslgGILGELGYDNDDVYRF 325
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
164-273 1.62e-35

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: 123.91  E-value: 1.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699    164 LLGAGTGINPLYQLAHHIVENPNDKTKVNLLYGNKTPQDILLRKELDALKEKYPDKFNVTYFVddKQDDQDFDGEISFIS 243
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDPKDPTQVVLVFGNRNEDDILYREELDELAEKHPGRLTVVYVV--SRPEAGWTGGKGRVQ 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 6322699    244 KDFIQEHVPGPKESTHLFVCGPPPFMNAYS 273
Cdd:pfam00175  79 DALLEDHLSLPDEETHVYVCGPPGMIKAVR 108
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
59-271 9.78e-34

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: 122.94  E-value: 9.78e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   59 SKIEEESHDTRRFTFKLPTEdsemglvlASAL---FAKFVTP-KGSNVVRPYTPVSDLSQKGHFQLVVKHYEGGKMTSHL 134
Cdd:cd00322   1 VATEDVTDDVRLFRLQLPNG--------FSFKpgqYVDLHLPgDGRGLRRAYSIASSPDEEGELELTVKIVPGGPFSAWL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  135 FGLKPNDTVSFKGPIMKWKWQPNQFKSITLLGAGTGINPLYQLAHHIVENPNdKTKVNLLYGNKTPQDILLRKELDALKE 214
Cdd:cd00322  73 HDLKPGDEVEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKP-GGEITLLYGARTPADLLFLDELEELAK 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6322699  215 KypdKFNVTYFVDDKQDDQDFDGEISFISKDFIQEHVPGPKESTHLFVCGPPPFMNA 271
Cdd:cd00322 152 E---GPNFRLVLALSRESEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAKA 205
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
51-300 1.54e-31

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 117.20  E-value: 1.54e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   51 DKWIDLPISKIEEESHDTRRFTFKLPTedsemGLVLASAL---FAKF-VTPKGSNVVRPYTPVSDLSQkGHFQLVVKHYE 126
Cdd:COG1018   1 AGFRPLRVVEVRRETPDVVSFTLEPPD-----GAPLPRFRpgqFVTLrLPIDGKPLRRAYSLSSAPGD-GRLEITVKRVP 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  127 GGKMTSHLF-GLKPNDTVSFKGPIMKWKWQPNQFKSITLLGAGTGINPLYQLAHHIVENpNDKTKVNLLYGNKTPQDILL 205
Cdd:COG1018  75 GGGGSNWLHdHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLAR-GPFRPVTLVYGARSPADLAF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  206 RKELDALKEKYPdkfNVTYFVDDKQDDQDFDGeisFISKDFIQEHVPGPKEsTHLFVCGPPPFMNAysgekkspkdqgeL 285
Cdd:COG1018 154 RDELEALAARHP---RLRLHPVLSREPAGLQG---RLDAELLAALLPDPAD-AHVYLCGPPPMMEA-------------V 213
                       250
                ....*....|....*
gi 6322699  286 IGILNNLGYSKDQVF 300
Cdd:COG1018 214 RAALAELGVPEERIH 228
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
53-275 6.24e-31

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: 115.83  E-value: 6.24e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   53 WIDLPISKIEEESHDTRRFTFKLPTEDsemglvLASALFAKFVT-----PKGSNVVRPYTPVSDLSQKGHFQLVVKHYEG 127
Cdd:cd06217   1 WRVLRVTEIIQETPTVKTFRLAVPDGV------PPPFLAGQHVDlrltaIDGYTAQRSYSIASSPTQRGRVELTVKRVPG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  128 GKMTSHLFG-LKPNDTVSFKGPIMKWKWQPNQFKSITLLGAGTGINPLYQLAHHIVENpNDKTKVNLLYGNKTPQDILLR 206
Cdd:cd06217  75 GEVSPYLHDeVKVGDLLEVRGPIGTFTWNPLHGDPVVLLAGGSGIVPLMSMIRYRRDL-GWPVPFRLLYSARTAEDVIFR 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322699  207 KELDALKEKYPDkFNVTYfVDDKQDDQDFDGEISFISKDFIQEHVPgPKESTHLFVCGPPPFMNAYSGE 275
Cdd:cd06217 154 DELEQLARRHPN-LHVTE-ALTRAAPADWLGPAGRITADLIAELVP-PLAGRRVYVCGPPAFVEAATRL 219
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
60-301 3.42e-25

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: 100.36  E-value: 3.42e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   60 KIEEESHDTRRFTFKLPTEdsemglvlasALFA----KFVTPK----GSNVVRPYTPVSDLSQKGHFQLVVKHYEGGKMT 131
Cdd:cd06215   5 KIIQETPDVKTFRFAAPDG----------SLFAykpgQFLTLEleidGETVYRAYTLSSSPSRPDSLSITVKRVPGGLVS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  132 SHLF-GLKPNDTVSFKGPIMKWKWQPNQFKSITLLGAGTGINPLYQLAHHIVENpNDKTKVNLLYGNKTPQDILLRKELD 210
Cdd:cd06215  75 NWLHdNLKVGDELWASGPAGEFTLIDHPADKLLLLSAGSGITPMMSMARWLLDT-RPDADIVFIHSARSPADIIFADELE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  211 ALKEKYPDkFNVTyFVDDKQDDQDFDGEISFISKDFIQEHVPGPKESThLFVCGPPPFMNAysgekkspkdqgeLIGILN 290
Cdd:cd06215 154 ELARRHPN-FRLH-LILEQPAPGAWGGYRGRLNAELLALLVPDLKERT-VFVCGPAGFMKA-------------VKSLLA 217
                       250
                ....*....|.
gi 6322699  291 NLGYSKDQVFK 301
Cdd:cd06215 218 ELGFPMSRFHQ 228
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
58-300 6.48e-25

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: 100.37  E-value: 6.48e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   58 ISKIEEESHDTRRFTFKLPTEDSEmGLVLASALFAkFVTPKGSNVVrPYTPVSDLSQKGHFQLVVKHYegGKMTSHLFGL 137
Cdd:cd06221   1 IVEVVDETEDIKTFTLRLEDDDEE-LFTFKPGQFV-MLSLPGVGEA-PISISSDPTRRGPLELTIRRV--GRVTEALHEL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  138 KPNDTVSFKGPIMKWkWQPNQF--KSITLLGAGTGINPLYQLAHHIVENPNDKTKVNLLYGNKTPQDILLRKELDALKEK 215
Cdd:cd06221  76 KPGDTVGLRGPFGNG-FPVEEMkgKDLLLVAGGLGLAPLRSLINYILDNREDYGKVTLLYGARTPEDLLFKEELKEWAKR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  216 ypDKFNVTYFVddKQDDQDFDGEISFISkDFIQEHVPGPKESThLFVCGPPPFMNAysgekkspkdqgeLIGILNNLGYS 295
Cdd:cd06221 155 --SDVEVILTV--DRAEEGWTGNVGLVT-DLLPELTLDPDNTV-AIVCGPPIMMRF-------------VAKELLKLGVP 215

                ....*
gi 6322699  296 KDQVF 300
Cdd:cd06221 216 EEQIW 220
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
58-271 3.96e-24

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 98.01  E-value: 3.96e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   58 ISKIEEESHDTRRFTFKLPtedsemgLVLASAL---FAkFVTPKGSNVVRPYTPVSDLSQKGHFQLVVKHYegGKMTSHL 134
Cdd:COG0543   2 VVSVERLAPDVYLLRLEAP-------LIALKFKpgqFV-MLRVPGDGLRRPFSIASAPREDGTIELHIRVV--GKGTRAL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  135 FGLKPNDTVSFKGPIMKWKWQPNQFKSITLLGAGTGINPLYQLAHHIVENPNdktKVNLLYGNKTPQDILLRKELDALKE 214
Cdd:COG0543  72 AELKPGDELDVRGPLGNGFPLEDSGRPVLLVAGGTGLAPLRSLAEALLARGR---RVTLYLGARTPEDLYLLDELEALAD 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  215 kypdkFNVTYFVDdkqddqdfdgEISFISKDFIQEHVP---GPKESTHLFVCGPPPFMNA 271
Cdd:COG0543 149 -----FRVVVTTD----------DGWYGRKGFVTDALKellAEDSGDDVYACGPPPMMKA 193
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
56-271 1.20e-22

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: 93.76  E-value: 1.20e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   56 LPISKIEEESHDTRRFTFKLPTEDSEmglvlasaLFA----KFVTPK----GSNVVRPY---TPVSDlsqkGHFQLVVKH 124
Cdd:cd06214   4 LTVAEVVRETADAVSITFDVPEELRD--------AFRyrpgQFLTLRvpidGEEVRRSYsicSSPGD----DELRITVKR 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  125 YEGGKMTSHLFG-LKPNDTVSFKGPIMKWKWQPNQF-KSITLLGAGTGINPLYQLAHHIVENPnDKTKVNLLYGNKTPQD 202
Cdd:cd06214  72 VPGGRFSNWANDeLKAGDTLEVMPPAGRFTLPPLPGaRHYVLFAAGSGITPVLSILKTALARE-PASRVTLVYGNRTEAS 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322699  203 ILLRKELDALKEKYPDKFNVTY-FVDDKQDDQDFDGEI--SFIskDFIQEHVPGPKESTHLFVCGPPPFMNA 271
Cdd:cd06214 151 VIFREELADLKARYPDRLTVIHvLSREQGDPDLLRGRLdaAKL--NALLKNLLDATEFDEAFLCGPEPMMDA 220
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
58-302 7.97e-21

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: 88.93  E-value: 7.97e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   58 ISKIEEESHDTRRFTFKLpTEDSEMGLVlaSALFAKFVTPkGSNVVRPYTPVSDLSQKGHFQLVVKHYEGGKMTSHLF-G 136
Cdd:cd06212   5 VVAVEALTHDIRRLRLRL-EEPEPIKFF--AGQYVDITVP-GTEETRSFSMANTPADPGRLEFIIKKYPGGLFSSFLDdG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  137 LKPNDTVSFKGPIMKWKWQPNQFKSITLLGAGTGINPLYQLAHHIVENPNDKTkVNLLYGNKTPQDILLRKELDALKEKY 216
Cdd:cd06212  81 LAVGDPVTVTGPYGTCTLRESRDRPIVLIGGGSGMAPLLSLLRDMAASGSDRP-VRFFYGARTARDLFYLEEIAALGEKI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  217 PDkFNVTYFVDDKQDDQDFDGEISFISkDFIQEHVPGpKESTHLFVCGPPPFMNAysgekkspkdqgeLIGILNNLGYSK 296
Cdd:cd06212 160 PD-FTFIPALSESPDDEGWSGETGLVT-EVVQRNEAT-LAGCDVYLCGPPPMIDA-------------ALPVLEMSGVPP 223

                ....*...
gi 6322699  297 DQVF--KF 302
Cdd:cd06212 224 DQIFydKF 231
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
56-299 3.90e-19

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: 83.83  E-value: 3.90e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   56 LPISKIEEESHDTRRFTFKLPtEDSEMGLVLASALFAKfvTPKGSNVVRPYTPVSdLSQKGHFQLVVKHYEG-GKMTSHL 134
Cdd:cd06196   3 VTLLSIEPVTHDVKRLRFDKP-EGYDFTPGQATEVAID--KPGWRDEKRPFTFTS-LPEDDVLEFVIKSYPDhDGVTEQL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  135 FGLKPNDTVsfkgpIMKWKWQPNQFKSI-TLLGAGTGINP----LYQLAHhivenpNDKTKVN-LLYGNKTPQDILLRKE 208
Cdd:cd06196  79 GRLQPGDTL-----LIEDPWGAIEYKGPgVFIAGGAGITPfiaiLRDLAA------KGKLEGNtLIFANKTEKDIILKDE 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  209 LDALKEkypDKFnvTYFVDDKQDDQDFDGEisfISKDFIQEHVpgPKESTHLFVCGPPPFMNAysgekkspkdqgeLIGI 288
Cdd:cd06196 148 LEKMLG---LKF--INVVTDEKDPGYAHGR---IDKAFLKQHV--TDFNQHFYVCGPPPMEEA-------------INGA 204
                       250
                ....*....|.
gi 6322699  289 LNNLGYSKDQV 299
Cdd:cd06196 205 LKELGVPEDSI 215
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
56-274 7.48e-18

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: 80.65  E-value: 7.48e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   56 LPISKIEEESHDTRRFTFKLPTEDSEMGL----VLASALFAKFVTPKGSNVVRPYTPvsdlsqkGHFQLVVKHYEGGKMT 131
Cdd:cd06191   1 LRVAEVRSETPDAVTIVFAVPGPLQYGFRpgqhVTLKLDFDGEELRRCYSLCSSPAP-------DEISITVKRVPGGRVS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  132 SHLF-GLKPNDTVSFKGPIMKWKWQPNQFKSITLLGAGTGINPLYQL--AHHIVENPNDktkVNLLYGNKTPQDILLRKE 208
Cdd:cd06191  74 NYLReHIQPGMTVEVMGPQGHFVYQPQPPGRYLLVAAGSGITPLMAMirATLQTAPESD---FTLIHSARTPADMIFAQE 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322699  209 LDALKEKYPdKFNVTYFVDDKQDDQDFDGEISFISKDFIQEHVPGPKESThLFVCGPPPFMNAYSG 274
Cdd:cd06191 151 LRELADKPQ-RLRLLCIFTRETLDSDLLHGRIDGEQSLGAALIPDRLERE-AFICGPAGMMDAVET 214
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
99-271 2.82e-17

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: 79.19  E-value: 2.82e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   99 GSNVVRPYTPVSDLSQK-GHFQLVVKHYEGGKMTSHLFG-LKPNDTVSFKGPIMKWKWQPNQFKSITLLGAGTGINPLYQ 176
Cdd:cd06216  60 GVRHWRSYSLSSSPTQEdGTITLTVKAQPDGLVSNWLVNhLAPGDVVELSQPQGDFVLPDPLPPRLLLIAAGSGITPVMS 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  177 LAHHIVENpNDKTKVNLLYGNKTPQDILLRKELDALKEKYPdkfNVTYFVDDKQDdqdfdGEISFISKDFIQEHVPgPKE 256
Cdd:cd06216 140 MLRTLLAR-GPTADVVLLYYARTREDVIFADELRALAAQHP---NLRLHLLYTRE-----ELDGRLSAAHLDAVVP-DLA 209
                       170
                ....*....|....*
gi 6322699  257 STHLFVCGPPPFMNA 271
Cdd:cd06216 210 DRQVYACGPPGFLDA 224
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
91-271 2.83e-17

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 81.48  E-value: 2.83e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   91 FAkFVTPKGSNVVR---PYTPVSDLSQKGHFQLVVKhyEGGKMTSHLFGLKPNDTVSFKGP-----IMKWKWQPNQFksi 162
Cdd:COG4097 249 FA-FLRFDGSPFWEeahPFSISSAPGGDGRLRFTIK--ALGDFTRRLGRLKPGTRVYVEGPygrftFDRRDTAPRQV--- 322
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  163 tLLGAGTGINPLYQLAHHIVENPNDKTKVNLLYGNKTPQDILLRKELDALKEKYPDkFNVTYFVDdkqddqdfdGEISFI 242
Cdd:COG4097 323 -WIAGGIGITPFLALLRALAARPGDQRPVDLFYCVRDEEDAPFLEELRALAARLAG-LRLHLVVS---------DEDGRL 391
                       170       180
                ....*....|....*....|....*....
gi 6322699  243 SKDFIQEHVPGPKEStHLFVCGPPPFMNA 271
Cdd:COG4097 392 TAERLRRLVPDLAEA-DVFFCGPPGMMDA 419
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
58-271 2.61e-16

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: 76.09  E-value: 2.61e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   58 ISKIEEESHDTRRFTFKLpteDSEMGLVLASALFAKfVTPKGSNVVRPYTPvSDLSQKGHFQLVVKHYEGGKMTSHLFGL 137
Cdd:cd06209   6 VTEVERLSDSTIGLTLEL---DEAGALAFLPGQYVN-LQVPGTDETRSYSF-SSAPGDPRLEFLIRLLPGGAMSSYLRDR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  138 -KPNDTVSFKGPIMKWKWQPNQfKSITLLGAGTGINPLYQLAHHIVENPNDKtKVNLLYGNKTPQDILLRKELDALKEKY 216
Cdd:cd06209  81 aQPGDRLTLTGPLGSFYLREVK-RPLLMLAGGTGLAPFLSMLDVLAEDGSAH-PVHLVYGVTRDADLVELDRLEALAERL 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6322699  217 PDkFNVTYFVDDKQDDQDFDGeisFISKDFIQEHVPGPkeSTHLFVCGPPPFMNA 271
Cdd:cd06209 159 PG-FSFRTVVADPDSWHPRKG---YVTDHLEAEDLNDG--DVDVYLCGPPPMVDA 207
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
53-300 4.02e-16

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: 76.06  E-value: 4.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   53 WIDLPISKIEEESHDTRRFTFKlPTEDSEmglvLASALFAKFVTPK------GSNVVRPYTpVSDLSQKGHFQLVVKHYE 126
Cdd:cd06184   6 FRPFVVARKVAESEDITSFYLE-PADGGP----LPPFLPGQYLSVRvklpglGYRQIRQYS-LSDAPNGDYYRISVKREP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  127 GGKMTSHLFG-LKPNDTVSFKGPIMKWKWQPNQFKSITLLGAGTGINPLYQLAHHIVENpNDKTKVNLLYGNKTPQDILL 205
Cdd:cd06184  80 GGLVSNYLHDnVKVGDVLEVSAPAGDFVLDEASDRPLVLISAGVGITPMLSMLEALAAE-GPGRPVTFIHAARNSAVHAF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  206 RKELDALKEKYPD-KFNVTYFVDDKQDDQDFDGEISFISKDFIQEHVPGPKesTHLFVCGPPPFMNAysgekkspkdqge 284
Cdd:cd06184 159 RDELEELAARLPNlKLHVFYSEPEAGDREEDYDHAGRIDLALLRELLLPAD--ADFYLCGPVPFMQA------------- 223
                       250
                ....*....|....*.
gi 6322699  285 LIGILNNLGYSKDQVF 300
Cdd:cd06184 224 VREGLKALGVPAERIH 239
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
58-302 3.67e-15

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: 74.90  E-value: 3.67e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   58 ISKIEEESHDTRRFTFKLPtEDSEM-------------GLVLASALFAKFVTPK-------GSNVVRPYTPVSDLSQKGH 117
Cdd:COG2871 136 VVSNENVTTFIKELVLELP-EGEEIdfkagqyiqievpPYEVDFKDFDIPEEEKfglfdknDEEVTRAYSMANYPAEKGI 214
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  118 FQLVVKH------YEGGKMTSHLFGLKPNDTVSFKGPIMKWKWQPNQfKSITLLGAGTGINPLYQLAHHIVENPNDKTKV 191
Cdd:COG2871 215 IELNIRIatppmdVPPGIGSSYIFSLKPGDKVTISGPYGEFFLRDSD-REMVFIGGGAGMAPLRSHIFDLLERGKTDRKI 293
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  192 NLLYGNKTPQDILLRKELDALKEKYPdkfNVTYFVD--DKQDDQDFDGEISFI----SKDFIQEHvPGPkESTHLFVCGP 265
Cdd:COG2871 294 TFWYGARSLRELFYLEEFRELEKEHP---NFKFHPAlsEPLPEDNWDGETGFIhevlYENYLKDH-PAP-EDCEAYLCGP 368
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 6322699  266 PPFMNAysgekkspkdqgeLIGILNNLGYSKDQVF--KF 302
Cdd:COG2871 369 PPMIDA-------------VIKMLDDLGVEEENIYfdDF 394
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
58-271 1.76e-14

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: 71.20  E-value: 1.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   58 ISKIEEESHDTRRFTFKLpteDSEMGLVLASALFAKFVTPKGSnVVRPYTPVSDLSQKGHFQLVVKHYEGGKMTSHLFG- 136
Cdd:cd06211  11 VVEIEDLTPTIKGVRLKL---DEPEEIEFQAGQYVNLQAPGYE-GTRAFSIASSPSDAGEIELHIRLVPGGIATTYVHKq 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  137 LKPNDTVSFKGPIMKWKWQPNQFKSITLLGAGTGINPLYQLAHHIVENpNDKTKVNLLYGNKTPQDILLRKELDALKEKY 216
Cdd:cd06211  87 LKEGDELEISGPYGDFFVRDSDQRPIIFIAGGSGLSSPRSMILDLLER-GDTRKITLFFGARTRAELYYLDEFEALEKDH 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6322699  217 PDkFNVTYFVDDKQDDQDFDGEISFISkDFIQEHVPGPKESTHLFVCGPPPFMNA 271
Cdd:cd06211 166 PN-FKYVPALSREPPESNWKGFTGFVH-DAAKKHFKNDFRGHKAYLCGPPPMIDA 218
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
128-301 2.41e-14

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: 71.57  E-value: 2.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  128 GKMTSHLFGLKPNDTVSFKGPIMKWkWQPNQFKSITLLGAGTGINPLYQLAHHIVENPNDKTKVNLLYGNKTPQDILLRK 207
Cdd:cd06188 120 GIGSSYIFNLKPGDKVTASGPFGEF-FIKDTDREMVFIGGGAGMAPLRSHIFHLLKTLKSKRKISFWYGARSLKELFYQE 198
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  208 ELDALKEKYPdkfNVTYFVD--DKQDDQDFDGEISFISKDFIQ---EHVPGPkESTHLFVCGPPPFMNAysgekkspkdq 282
Cdd:cd06188 199 EFEALEKEFP---NFKYHPVlsEPQPEDNWDGYTGFIHQVLLEnylKKHPAP-EDIEFYLCGPPPMNSA----------- 263
                       170
                ....*....|....*....
gi 6322699  283 geLIGILNNLGYSKDQVFK 301
Cdd:cd06188 264 --VIKMLDDLGVPRENIAF 280
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
65-282 6.56e-14

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: 69.59  E-value: 6.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   65 SHDTRRFTFKlpTEDSemglvlASALFAKF--VTPKGSNVVRPYTpVSDLSQ-KGHFQLVVKHYEGGKMTSHLFG-LKPN 140
Cdd:cd06190   8 THDVAEFRFA--LDGP------ADFLPGQYalLALPGVEGARAYS-MANLANaSGEWEFIIKRKPGGAASNALFDnLEPG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  141 DTVSFKGPIMKWKWQPNQFKSITLLGAGTGINPLYQLAHHIVENP-NDKTKVNLLYGNKTPQDILLRKELDALKEkYPDK 219
Cdd:cd06190  79 DELELDGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILRGAARSPyLSDRPVDLFYGGRTPSDLCALDELSALVA-LGAR 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322699  220 FNVTYFV--DDKQDDQDFDGEISFISkDFIQEHVPGPKESTHLFVCGPPPFMNAYS----GEKKSPKDQ 282
Cdd:cd06190 158 LRVTPAVsdAGSGSAAGWDGPTGFVH-EVVEATLGDRLAEFEFYFAGPPPMVDAVQrmlmIEGVVPFDQ 225
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
91-297 1.28e-13

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: 69.13  E-value: 1.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   91 FAK--FVTPKGSNVVRPYTPVSdLSQKGHFQLVVKHYEGGKMTSHLFGLKPNDTVSfkgpIMKwkwQPNQF--------- 159
Cdd:cd06195  30 FTKlgLPNDDGKLVRRAYSIAS-APYEENLEFYIILVPDGPLTPRLFKLKPGDTIY----VGK---KPTGFltldevppg 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  160 KSITLLGAGTGINP-LYQLAHHIVENPNDKtkVNLLYGNKTPQDILLRKELDALKEKYPDKFNVTYFVDDKQDDQDFDGE 238
Cdd:cd06195 102 KRLWLLATGTGIAPfLSMLRDLEIWERFDK--IVLVHGVRYAEELAYQDEIEALAKQYNGKFRYVPIVSREKENGALTGR 179
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322699  239 IS-FISKDFIQEHV--PGPKESTHLFVCGpppfmnaysgekkSPKDQGELIGILNNLGYSKD 297
Cdd:cd06195 180 IPdLIESGELEEHAglPLDPETSHVMLCG-------------NPQMIDDTQELLKEKGFSKN 228
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
104-271 5.99e-13

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: 66.91  E-value: 5.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  104 RPYTPVSDLSQKGHFQLVVKHYEGGKMTSHLFG-LKPNDTVSFKGP----IMKWKWQPNQfksITLLGAGTGINPLYQLA 178
Cdd:cd06194  40 RSYSPTSLPDGDNELEFHIRRKPNGAFSGWLGEeARPGHALRLQGPfgqaFYRPEYGEGP---LLLVGAGTGLAPLWGIA 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  179 HH-IVENPndKTKVNLLYGNKTPQDILLRKELDALKEKYPdkfNVTYfVDDKQDDQDFDGEisfISKDFIQEHVPGPKES 257
Cdd:cd06194 117 RAaLRQGH--QGEIRLVHGARDPDDLYLHPALLWLAREHP---NFRY-IPCVSEGSQGDPR---VRAGRIAAHLPPLTRD 187
                       170
                ....*....|....
gi 6322699  258 THLFVCGPPPFMNA 271
Cdd:cd06194 188 DVVYLCGAPSMVNA 201
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
105-266 1.63e-12

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 66.37  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   105 PYTPVSDLSQKGHFQLVVKhyEGGKMTSHLFGLKPNDTVSFKGPIMKW----KWQPNqfkSITLLGAGTGINPLYQLAHH 180
Cdd:PRK08345  55 PISICSSPTRKGFFELCIR--RAGRVTTVIHRLKEGDIVGVRGPYGNGfpvdEMEGM---DLLLIAGGLGMAPLRSVLLY 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   181 IVENPNDKTKVNLLYGNKTPQDILLRKELDALKeKYPDKFN----VTYFVDDKQDDQDFDGEISFISKDFIQEHVPGPK- 255
Cdd:PRK08345 130 AMDNRWKYGNITLIYGAKYYEDLLFYDELIKDL-AEAENVKiiqsVTRDPEWPGCHGLPQGFIERVCKGVVTDLFREANt 208
                        170
                 ....*....|...
gi 6322699   256 --ESTHLFVCGPP 266
Cdd:PRK08345 209 dpKNTYAAICGPP 221
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
61-271 1.77e-11

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: 62.61  E-value: 1.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   61 IEEESHDTRRFTFKLPTedsemGLVLASALFAKFVTPKGSNVVRPYTPVSDLSQKGHFQLVVKHYEGGKMTSHLFG-LKP 139
Cdd:cd06187   4 VERLTHDIAVVRLQLDQ-----PLPFWAGQYVNVTVPGRPRTWRAYSPANPPNEDGEIEFHVRAVPGGRVSNALHDeLKV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  140 NDTVSFKGP----IMKwkwqPNQFKSITLLGAGTGINPLYQLAHHIVENpNDKTKVNLLYGNKTPQDILLRKELDALKEK 215
Cdd:cd06187  79 GDRVRLSGPygtfYLR----RDHDRPVLCIAGGTGLAPLRAIVEDALRR-GEPRPVHLFFGARTERDLYDLEGLLALAAR 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6322699  216 YPdkfNVTYFVDDKQDDQDFDGEISFISkDFIQEHVPGPKESThLFVCGPPPFMNA 271
Cdd:cd06187 154 HP---WLRVVPVVSHEEGAWTGRRGLVT-DVVGRDGPDWADHD-IYICGPPAMVDA 204
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
133-224 2.44e-09

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


Pssm-ID: 99804 [Multi-domain]  Cd Length: 286  Bit Score: 56.95  E-value: 2.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  133 HLFGLKPNDTVSFKGPIMKWKWQPNQFKS-ITLLGAGTGINP----LYQLAHHIVENPNDKTKVNLLYGNKTPQDILLRK 207
Cdd:cd06208 108 YLCDLKPGDDVQITGPVGKTMLLPEDPNAtLIMIATGTGIAPfrsfLRRLFREKHADYKFTGLAWLFFGVPNSDSLLYDD 187
                        90
                ....*....|....*..
gi 6322699  208 ELDALKEKYPDKFNVTY 224
Cdd:cd06208 188 ELEKYPKQYPDNFRIDY 204
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
95-210 3.79e-09

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


Pssm-ID: 99798 [Multi-domain]  Cd Length: 289  Bit Score: 56.57  E-value: 3.79e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   95 VTPKGSNVVRPYTPVSdLSQKGHFQLVVKHYEGGKMTSHLFGLKPNDTVsfKGPImkwkwQPN-QF------KSITLLGA 167
Cdd:cd06201  92 ILPPGSDVPRFYSLAS-SSSDGFLEICVRKHPGGLCSGYLHGLKPGDTI--KAFI-----RPNpSFrpakgaAPVILIGA 163
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 6322699  168 GTGINPLYQLAHHivenpNDK-TKVNLLYGNKTPQ-DILLRKELD 210
Cdd:cd06201 164 GTGIAPLAGFIRA-----NAArRPMHLYWGGRDPAsDFLYEDELD 203
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
128-264 1.87e-08

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 55.01  E-value: 1.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   128 GKMTSHLFGLKPNDTVSFKGPIMKWKWQP-NQFKSITLLGAGTGINPLYQLAHHIVENPNDKTKVN----LLYGNKTPQD 202
Cdd:PLN03115 183 GVCSNFLCDLKPGAEVKITGPVGKEMLMPkDPNATIIMLATGTGIAPFRSFLWKMFFEKHDDYKFNglawLFLGVPTSSS 262
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322699   203 ILLRKELDALKEKYPDKFNVTYFVddKQDDQDFDGEisfisKDFIQEHVPG---------PKESTHLFVCG 264
Cdd:PLN03115 263 LLYKEEFEKMKEKAPENFRLDFAV--SREQTNAKGE-----KMYIQTRMAEyaeelwellKKDNTYVYMCG 326
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
65-271 1.32e-07

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: 51.57  E-value: 1.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   65 SHDTRRFTFK-LPTEDSEMGLVLASALFAKFVTPkGSNVVRPYTPVSDLSQKGHFQLVVKHYEGGKMTSHL-FGLKPNDT 142
Cdd:cd06210  13 SSNVVRLRLQpDDAEGAGIAAEFVPGQFVEIEIP-GTDTRRSYSLANTPNWDGRLEFLIRLLPGGAFSTYLeTRAKVGQR 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  143 VSFKGPIMKWKWQPNQFKSITLLGAGTGINPLYQLAHHIVE--NPNDKTkvnLLYGNKTPQDILLRKELDALKEKYPdkf 220
Cdd:cd06210  92 LNLRGPLGAFGLRENGLRPRWFVAGGTGLAPLLSMLRRMAEwgEPQEAR---LFFGVNTEAELFYLDELKRLADSLP--- 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 6322699  221 NVTYFVDDKQDDQDFDGEISfISKDFIQEHVPGPKESTHLFVCGPPPFMNA 271
Cdd:cd06210 166 NLTVRICVWRPGGEWEGYRG-TVVDALREDLASSDAKPDIYLCGPPGMVDA 215
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
58-224 1.61e-07

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 51.80  E-value: 1.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699    58 ISKIEEESHDTRRFTFKLPtedsemglvlASALFA-------KFVTPKGSNvvRPYTPVSDLSQKGHFQLVVKHYEGGKM 130
Cdd:PRK07609 107 VASLERVAGDVMRLKLRLP----------ATERLQylagqyiEFILKDGKR--RSYSIANAPHSGGPLELHIRHMPGGVF 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   131 TSHLFG-LKPNDTVSFKGPIMKWKWQPNQFKSITLLGAGTGINPLYQLAHHIVENpNDKTKVNLLYGNKTPQDILLRKEL 209
Cdd:PRK07609 175 TDHVFGaLKERDILRIEGPLGTFFLREDSDKPIVLLASGTGFAPIKSIVEHLRAK-GIQRPVTLYWGARRPEDLYLSALA 253
                        170
                 ....*....|....*
gi 6322699   210 DALKEKYPdkfNVTY 224
Cdd:PRK07609 254 EQWAEELP---NFRY 265
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
122-271 2.97e-07

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: 50.39  E-value: 2.97e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  122 VKHYEGGKMTSHLFG-LKPNDTVSFKGPIMKWKWQPNQFKsITLLGAGTGINPLYQLAHHIVENpNDKTKVNLLYGNKTP 200
Cdd:cd06213  63 IRKVPGGAFSGWLFGaDRTGERLTVRGPFGDFWLRPGDAP-ILCIAGGSGLAPILAILEQARAA-GTKRDVTLLFGARTQ 140
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322699  201 QDILLRKELDALKEKYPDKFNVTYFVDDKQDDQDFDGEisfisKDFIQEHVPG-PKESTHLFVCGPPPFMNA 271
Cdd:cd06213 141 RDLYALDEIAAIAARWRGRFRFIPVLSEEPADSSWKGA-----RGLVTEHIAEvLLAATEAYLCGPPAMIDA 207
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
164-301 3.20e-07

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 50.86  E-value: 3.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   164 LLGAGTGINPLYQLAHHIVENpNDKTKVNLLYGNKTPQDILLRKELDALKEKYPdKFNVTYFVDDKQDDQDFDGEisfIS 243
Cdd:PRK10684 116 LLAAGCGVTPIMSMRRWLLKN-RPQADVQVIFNVRTPQDVIFADEWRQLKQRYP-QLNLTLVAENNATEGFIAGR---LT 190
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6322699   244 KDFIQEHVPGPKESThLFVCGPPPFMNAYSGEKKspkdqgeligilnNLGYSKDQVFK 301
Cdd:PRK10684 191 RELLQQAVPDLASRT-VMTCGPAPYMDWVEQEVK-------------ALGVTADRFFK 234
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
58-291 5.43e-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: 5.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   58 ISKIEEESHDTRRFTFKLPtedsemglvLASALF--AKFV---TPKGSNVVR-PYTPVSDLSQKGHFQLVVKhyEGGKMT 131
Cdd:cd06192   1 IVKKEQLEPNLVLLTIKAP---------LAARLFrpGQFVflrNFESPGLERiPLSLAGVDPEEGTISLLVE--IRGPKT 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  132 SHLFGLKPNDTVSFKGP----IMKwkwqPNQFKSITLLGAGTGINPLYQLAHHIVENPNdktKVNLLYGNKTPQDILLRK 207
Cdd:cd06192  70 KLIAELKPGEKLDVMGPlgngFEG----PKKGGTVLLVAGGIGLAPLLPIAKKLAANGN---KVTVLAGAKKAKEEFLDE 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  208 ELdalkEKYPDKFNVTyfvddkqddqDFDGEISFISKDFIQeHVPGPKES-THLFVCGPPPFMNAYSGEKKSPKDQGELI 286
Cdd:cd06192 143 YF----ELPADVEIWT----------TDDGELGLEGKVTDS-DKPIPLEDvDRIIVAGSDIMMKAVVEALDEWLQLIKAS 207

                ....*
gi 6322699  287 GILNN 291
Cdd:cd06192 208 VSNNS 212
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
68-299 6.31e-07

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 50.93  E-value: 6.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699     68 TRRFTFKLPTEDSEMGLVLAsalfaKFVTPKG----SNVVRPYTPVSDLSQKGHFQLVVKHyEGGKMTSHLFGLKPNDTV 143
Cdd:PTZ00306  932 SRVLRFNLPGALQRSGLTLG-----QFIAIRGdwdgQQLIGYYSPITLPDDLGVISILARG-DKGTLKEWISALRPGDSV 1005
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699    144 SFK---GPIMKWKWQPNQF-------KSITLLGAGTGINPLYQLAHHIVENPNDKT--KVNLLYGNKTPQDILLRKELDA 211
Cdd:PTZ00306 1006 EMKacgGLRIERRPADKQFvfrghviRKLALIAGGTGVAPMLQIIRAALKKPYVDSieSIRLIYAAEDVSELTYRELLES 1085
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699    212 LKEKYPDKFNVTyFVDDKQDDQDFDGeISFISKDFIQEHVPGPKESTHLFVCGPPPFMNAYSGEKKSpkdqgeligilnn 291
Cdd:PTZ00306 1086 YRKENPGKFKCH-FVLNNPPEGWTDG-VGFVDRALLQSALQPPSKDLLVAICGPPVMQRAVKADLLA------------- 1150

                  ....*...
gi 6322699    292 LGYSKDQV 299
Cdd:PTZ00306 1151 LGYNMELV 1158
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
105-271 1.28e-06

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: 48.41  E-value: 1.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  105 PYTPVSDLSQKGHFQLVVKHYegGKMTSHLFG-LKPNDTVSFKGPIMKWKWQPNQFKSItLLGAGTGINPLYQLAHHIVE 183
Cdd:cd06198  43 PFTISSAPDPDGRLRFTIKAL--GDYTRRLAErLKPGTRVTVEGPYGRFTFDDRRARQI-WIAGGIGITPFLALLEALAA 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  184 NPNDKtKVNLLYGNKTPQDILLRKELDALKEKYpdkfNVTYFVDDKQDDQDFDGEisfiskDFIQEHVPGPKEsTHLFVC 263
Cdd:cd06198 120 RGDAR-PVTLFYCVRDPEDAVFLDELRALAAAA----GVVLHVIDSPSDGRLTLE------QLVRALVPDLAD-ADVWFC 187

                ....*...
gi 6322699  264 GPPPFMNA 271
Cdd:cd06198 188 GPPGMADA 195
PRK13289 PRK13289
NO-inducible flavohemoprotein;
110-271 3.15e-06

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 48.26  E-value: 3.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   110 SDLSQKGHFQLVVKHYEGGKMTSHLF-GLKPNDTVSFKGPIMKWKWQPNQFKSITLLGAGTGINPLYQLAHHIVENPNDK 188
Cdd:PRK13289 211 SDAPNGKYYRISVKREAGGKVSNYLHdHVNVGDVLELAAPAGDFFLDVASDTPVVLISGGVGITPMLSMLETLAAQQPKR 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   189 tKVNLLYGNKTPQDILLRKELDALKEKYPDkFNVTYF---VDDKQDDQDFDGEISFISKDFIQEHVPGPKesTHLFVCGP 265
Cdd:PRK13289 291 -PVHFIHAARNGGVHAFRDEVEALAARHPN-LKAHTWyrePTEQDRAGEDFDSEGLMDLEWLEAWLPDPD--ADFYFCGP 366

                 ....*.
gi 6322699   266 PPFMNA 271
Cdd:PRK13289 367 VPFMQF 372
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
128-271 1.79e-05

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: 45.23  E-value: 1.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  128 GKMTSHLFGLKPNDTVSFKGPI-----MKWKWQPnqfksITLLGAGTGINPLYQLAHHIVENPNdktKVNLLYGNKTPQD 202
Cdd:cd06218  67 GKGTRLLSELKAGDELDVLGPLgngfdLPDDDGK-----VLLVGGGIGIAPLLFLAKQLAERGI---KVTVLLGFRSADD 138
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322699  203 ILLRKELdalkEKYPDKFNVTyfvddkqddqDFDGEISF------ISKDFIQEHVPGpkestHLFVCGPPPFMNA 271
Cdd:cd06218 139 LFLVEEF----EALGAEVYVA----------TDDGSAGTkgfvtdLLKELLAEARPD-----VVYACGPEPMLKA 194
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
91-271 4.63e-05

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 44.35  E-value: 4.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699    91 FAKFVTPkGSNVVRPYTPVSDLSQKGHFQLVVKHYEGGKMTSHLF-GLKPNDTVSFKGPIMKWKWQPNQfKSITLLGAGT 169
Cdd:PRK11872 142 YARLQIP-GTDDWRSYSFANRPNATNQLQFLIRLLPDGVMSNYLReRCQVGDEILFEAPLGAFYLREVE-RPLVFVAGGT 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   170 GINPLYQLAHHIVENPNDKTkVNLLYGNKTPQDILLRKELDALKEKYPdkfNVTYFVDDKQDDQDFDGEISFISKDFIQE 249
Cdd:PRK11872 220 GLSAFLGMLDELAEQGCSPP-VHLYYGVRHAADLCELQRLAAYAERLP---NFRYHPVVSKASADWQGKRGYIHEHFDKA 295
                        170       180
                 ....*....|....*....|..
gi 6322699   250 HVPgpKESTHLFVCGPPPFMNA 271
Cdd:PRK11872 296 QLR--DQAFDMYLCGPPPMVEA 315
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
108-214 5.00e-05

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: 43.78  E-value: 5.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  108 PVSDLSQKGHFQLVVKHYegGKMTSHLFGLKPNDTVSFKGPIMKwKWQPNQFKsITLLGAGTGINPLYQLAHHIVEnpnd 187
Cdd:cd06220  41 PMSLSYIDGPNSITVKKV--GEATSALHDLKEGDKLGIRGPYGN-GFELVGGK-VLLIGGGIGIAPLAPLAERLKK---- 112
                        90       100
                ....*....|....*....|....*..
gi 6322699  188 KTKVNLLYGNKTPQDILLRKELDALKE 214
Cdd:cd06220 113 AADVTVLLGARTKEELLFLDRLRKSDE 139
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
58-271 1.98e-04

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 42.17  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699    58 ISKIEEESHDTRRFTFKLP-TEDSEMGlvlasalfaKFV---TPKGSNVVRpyTPVSdLSQKGHFQL--VVKHYegGKMT 131
Cdd:PRK00054   9 IVENKEIAPNIYTLVLDGEkVFDMKPG---------QFVmvwVPGVEPLLE--RPIS-ISDIDKNEItiLYRKV--GEGT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699   132 SHLFGLKPNDTVSFKGPimkwkwQPNQF------KSITLLGAGTGINPLYQLAHHIVENpndKTKVNLLYGNKTPQDILL 205
Cdd:PRK00054  75 KKLSKLKEGDELDIRGP------LGNGFdleeigGKVLLVGGGIGVAPLYELAKELKKK---GVEVTTVLGARTKDEVIF 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322699   206 RKELDALKEKYPDKFNVTYfvddkqddqdfdGEISFISkDFIQEHvpgpKES-THLFVCGPPPFMNA 271
Cdd:PRK00054 146 EEEFAKVGDVYVTTDDGSY------------GFKGFVT-DVLDEL----DSEyDAIYSCGPEIMMKK 195
DHOD_e_trans_like1 cd06219
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
105-277 8.78e-04

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


Pssm-ID: 99815 [Multi-domain]  Cd Length: 248  Bit Score: 39.87  E-value: 8.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  105 PYTPVSDLSQKGHFQLVVkhYEGGKMTSHLFGLKPNDTVS-FKGPIMKWKWQPNqFKSITLLGAGTGINPLYQLAHHIVE 183
Cdd:cd06219  45 PLTIADWDPEKGTITIVV--QVVGKSTRELATLEEGDKIHdVVGPLGKPSEIEN-YGTVVFVGGGVGIAPIYPIAKALKE 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322699  184 NPNdktKVNLLYGNKTPQDILLRKELdalkEKYPDKFNVTyfvddkqddqdfDGEISFISK----DFIQEHVPGPKESTH 259
Cdd:cd06219 122 AGN---RVITIIGARTKDLVILEDEF----RAVSDELIIT------------TDDGSYGEKgfvtDPLKELIESGEKVDL 182
                       170
                ....*....|....*...
gi 6322699  260 LFVCGPPPFMNAYSGEKK 277
Cdd:cd06219 183 VIAIGPPIMMKAVSELTR 200
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
247-271 7.06e-03

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: 37.08  E-value: 7.06e-03
                        10        20
                ....*....|....*....|....*
gi 6322699  247 IQEHVPGPKESTHLFVCGPPPFMNA 271
Cdd:cd06185 166 LAALLAAPPAGTHVYVCGPEGMMDA 190
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH
HHS Vulnerability Disclosure