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Conserved domains on  [gi|134133308|ref|NP_001026842|]
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NADH-cytochrome b5 reductase-like isoform 1 [Homo sapiens]

Protein Classification

Oxidored-like and cyt_b5_reduct_like domain-containing protein( domain architecture ID 10298874)

Oxidored-like and cyt_b5_reduct_like domain-containing protein

Graphical summary

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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 ...
 80-315 6.80e-64

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: 201.64  E-value: 6.80e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  80 FCIIAMDRLTKDTYRVRFALPGNSQ-LGLRPGQHLILRGIVDDLEIQRAYTPISPANAEGYFEVLIKCYQMGLMSRYVES 158
Cdd:cd06183    1 FKLVSKEDISHDTRIFRFELPSPDQvLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYPGGKMSQYLHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 159 WRVGDTAFWRGPFGDFFYKPNQY-----------GellllaagtgLAPMVPILQSITDNENDETFVTLVGCFKTFESIYL 227
Cdd:cd06183   81 LKPGDTVEIRGPFGKFEYKPNGKvkhigmiaggtG----------ITPMLQLIRAILKDPEDKTKISLLYANRTEEDILL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 228 KTFLQE--QARFWNVRTFFVLSQESSseqlPWSYqektHFGHLGQDLIKELVS-CCRRKPFALVCGSAEFTK-DIARCLL 303
Cdd:cd06183  151 REELDElaKKHPDRFKVHYVLSRPPE----GWKG----GVGFITKEMIKEHLPpPPSEDTLVLVCGPPPMIEgAVKGLLK 222

                        250
                 ....*....|..
gi 134133308 304 CAGLTEDSYFLF 315
Cdd:cd06183  223 ELGYKKDNVFKF 234
Oxidored-like super family cl10765
Oxidoreductase-like protein, N-terminal; Members of this family are found in the N terminal ...
 19-51 8.60e-07

Oxidoreductase-like protein, N-terminal; Members of this family are found in the N terminal region of various oxidoreductase like proteins. Their exact function is, as yet, unknown.


The actual alignment was detected with superfamily member pfam09791:

Pssm-ID: 462904  Cd Length: 45  Bit Score: 44.86  E-value: 8.60e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 134133308   19 RPTEPlpSQCCGSGCSPCVFDLYHRDLARWEAA 51
Cdd:pfam09791   9 KPEEP--DNCCMSGCVNCVWDLYREDLEEWAEA 39
 
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 ...
 80-315 6.80e-64

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: 201.64  E-value: 6.80e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  80 FCIIAMDRLTKDTYRVRFALPGNSQ-LGLRPGQHLILRGIVDDLEIQRAYTPISPANAEGYFEVLIKCYQMGLMSRYVES 158
Cdd:cd06183    1 FKLVSKEDISHDTRIFRFELPSPDQvLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYPGGKMSQYLHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 159 WRVGDTAFWRGPFGDFFYKPNQY-----------GellllaagtgLAPMVPILQSITDNENDETFVTLVGCFKTFESIYL 227
Cdd:cd06183   81 LKPGDTVEIRGPFGKFEYKPNGKvkhigmiaggtG----------ITPMLQLIRAILKDPEDKTKISLLYANRTEEDILL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 228 KTFLQE--QARFWNVRTFFVLSQESSseqlPWSYqektHFGHLGQDLIKELVS-CCRRKPFALVCGSAEFTK-DIARCLL 303
Cdd:cd06183  151 REELDElaKKHPDRFKVHYVLSRPPE----GWKG----GVGFITKEMIKEHLPpPPSEDTLVLVCGPPPMIEgAVKGLLK 222

                        250
                 ....*....|..
gi 134133308 304 CAGLTEDSYFLF 315
Cdd:cd06183  223 ELGYKKDNVFKF 234
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
87-176 4.05e-26

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 99.19  E-value: 4.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308   87 RLTKDTYRVRFALPGNSQ-LGLRPGQHLILRGIVDDLEIQRAYTPISPANAEGYFEVLIKCYQMGLMSRYVESWRVGDTA 165
Cdd:pfam00970   9 LVSHDTRIFRFALPHPDQvLGLPVGQHLFLRLPIDGELVIRSYTPISSDDDKGYLELLVKVYPGGKMSQYLDELKIGDTI 88

                          90
                  ....*....|.
gi 134133308  166 FWRGPFGDFFY 176
Cdd:pfam00970  89 DFKGPLGRFEY 99
PLN02252 PLN02252
nitrate reductase [NADPH]
 69-315 6.14e-26

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 108.23  E-value: 6.14e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  69 PSKLNPETFVAFCIIAMDRLTKDTYRVRFALPG-NSQLGLRPGQHLILRGIVDDLEIQRAYTPISPANAEGYFEVLIKCY 147
Cdd:PLN02252 626 PVALNPREKIPCRLVEKISLSHDVRLFRFALPSeDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFELVIKVY 705

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 148 ---------QMGLMSRYVESWRVGDTAFWRGPFGDFFY----------KPNQYGELLLLAAGTGLAPMVPILQSITDNEN 208
Cdd:PLN02252 706 fknvhpkfpNGGLMSQYLDSLPIGDTIDVKGPLGHIEYagrgsflvngKPKFAKKLAMLAGGTGITPMYQVIQAILRDPE 785

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 209 DETFVTLVGCFKTFESIYLKTFLQEQA-----RFwnvRTFFVLSQESSSEqlpWSYQekthFGHLGQDLIKELVSCCRRK 283
Cdd:PLN02252 786 DKTEMSLVYANRTEDDILLREELDRWAaehpdRL---KVWYVVSQVKREG---WKYS----VGRVTEAMLREHLPEGGDE 855

                        250       260       270
                 ....*....|....*....|....*....|...
gi 134133308 284 PFALVCGSAEFTKDIAR-CLLCAGLTEDSYFLF 315
Cdd:PLN02252 856 TLALMCGPPPMIEFACQpNLEKMGYDKDSILVF 888
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
75-313 2.05e-20

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 87.92  E-value: 2.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  75 ETFVAFCIIAMDRLTKDTYRVRFALP-GNSQLGLRPGQHLILRGIVDDLEIQRAYTpISPANAEGYFEVLIKCYQMGLMS 153
Cdd:COG1018    1 AGFRPLRVVEVRRETPDVVSFTLEPPdGAPLPRFRPGQFVTLRLPIDGKPLRRAYS-LSSAPGDGRLEITVKRVPGGGGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 154 RYV-ESWRVGDTAFWRGPFGDFFYKPNQY--------GellllaagTGLAPMVPILQSITDNENDETfVTLVGCFKTFES 224
Cdd:COG1018   80 NWLhDHLKVGDTLEVSGPRGDFVLDPEPArpllliagG--------IGITPFLSMLRTLLARGPFRP-VTLVYGARSPAD 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 225 IYLKTFLQE-QARFWNVRTFFVLSQESSSEQlpwsyqekthfGHLGQDLIKELVsccrrKPFA----LVCGSAEFTKDIA 299
Cdd:COG1018  151 LAFRDELEAlAARHPRLRLHPVLSREPAGLQ-----------GRLDAELLAALL-----PDPAdahvYLCGPPPMMEAVR 214

                        250
                 ....*....|....
gi 134133308 300 RCLLCAGLTEDSYF 313
Cdd:COG1018  215 AALAELGVPEERIH 228
Oxidored-like pfam09791
Oxidoreductase-like protein, N-terminal; Members of this family are found in the N terminal ...
 19-51 8.60e-07

Oxidoreductase-like protein, N-terminal; Members of this family are found in the N terminal region of various oxidoreductase like proteins. Their exact function is, as yet, unknown.


Pssm-ID: 462904  Cd Length: 45  Bit Score: 44.86  E-value: 8.60e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 134133308   19 RPTEPlpSQCCGSGCSPCVFDLYHRDLARWEAA 51
Cdd:pfam09791   9 KPEEP--DNCCMSGCVNCVWDLYREDLEEWAEA 39
 
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 ...
 80-315 6.80e-64

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: 201.64  E-value: 6.80e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  80 FCIIAMDRLTKDTYRVRFALPGNSQ-LGLRPGQHLILRGIVDDLEIQRAYTPISPANAEGYFEVLIKCYQMGLMSRYVES 158
Cdd:cd06183    1 FKLVSKEDISHDTRIFRFELPSPDQvLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYPGGKMSQYLHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 159 WRVGDTAFWRGPFGDFFYKPNQY-----------GellllaagtgLAPMVPILQSITDNENDETFVTLVGCFKTFESIYL 227
Cdd:cd06183   81 LKPGDTVEIRGPFGKFEYKPNGKvkhigmiaggtG----------ITPMLQLIRAILKDPEDKTKISLLYANRTEEDILL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 228 KTFLQE--QARFWNVRTFFVLSQESSseqlPWSYqektHFGHLGQDLIKELVS-CCRRKPFALVCGSAEFTK-DIARCLL 303
Cdd:cd06183  151 REELDElaKKHPDRFKVHYVLSRPPE----GWKG----GVGFITKEMIKEHLPpPPSEDTLVLVCGPPPMIEgAVKGLLK 222

                        250
                 ....*....|..
gi 134133308 304 CAGLTEDSYFLF 315
Cdd:cd06183  223 ELGYKKDNVFKF 234
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
87-176 4.05e-26

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 99.19  E-value: 4.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308   87 RLTKDTYRVRFALPGNSQ-LGLRPGQHLILRGIVDDLEIQRAYTPISPANAEGYFEVLIKCYQMGLMSRYVESWRVGDTA 165
Cdd:pfam00970   9 LVSHDTRIFRFALPHPDQvLGLPVGQHLFLRLPIDGELVIRSYTPISSDDDKGYLELLVKVYPGGKMSQYLDELKIGDTI 88

                          90
                  ....*....|.
gi 134133308  166 FWRGPFGDFFY 176
Cdd:pfam00970  89 DFKGPLGRFEY 99
PLN02252 PLN02252
nitrate reductase [NADPH]
 69-315 6.14e-26

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 108.23  E-value: 6.14e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  69 PSKLNPETFVAFCIIAMDRLTKDTYRVRFALPG-NSQLGLRPGQHLILRGIVDDLEIQRAYTPISPANAEGYFEVLIKCY 147
Cdd:PLN02252 626 PVALNPREKIPCRLVEKISLSHDVRLFRFALPSeDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFELVIKVY 705

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 148 ---------QMGLMSRYVESWRVGDTAFWRGPFGDFFY----------KPNQYGELLLLAAGTGLAPMVPILQSITDNEN 208
Cdd:PLN02252 706 fknvhpkfpNGGLMSQYLDSLPIGDTIDVKGPLGHIEYagrgsflvngKPKFAKKLAMLAGGTGITPMYQVIQAILRDPE 785

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 209 DETFVTLVGCFKTFESIYLKTFLQEQA-----RFwnvRTFFVLSQESSSEqlpWSYQekthFGHLGQDLIKELVSCCRRK 283
Cdd:PLN02252 786 DKTEMSLVYANRTEDDILLREELDRWAaehpdRL---KVWYVVSQVKREG---WKYS----VGRVTEAMLREHLPEGGDE 855

                        250       260       270
                 ....*....|....*....|....*....|...
gi 134133308 284 PFALVCGSAEFTKDIAR-CLLCAGLTEDSYFLF 315
Cdd:PLN02252 856 TLALMCGPPPMIEFACQpNLEKMGYDKDSILVF 888
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
 65-315 8.34e-25

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 101.45  E-value: 8.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  65 SQSCPSKLNPETFVAFCIIAMDRLTKDTYRVRFALPGNSQ-LGLRPGQHLILRGIVDD----LEIQRAYTPISPANAEGY 139
Cdd:PTZ00319  21 SRSPPVALDPDMFQHFKLIKKTEVTHDTFIFRFALHSPTQrLGLPIGQHIVFRCDCTTpgkpETVQHSYTPISSDDEKGY 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 140 FEVLIKCYQMGL---------MSRYVESWRVGDTAFWRGPFGDFFYKPN-----QYGELLLLAAG----------TGLAP 195
Cdd:PTZ00319 101 VDFLIKVYFKGVhpsfpnggrLSQHLYHMKLGDKIEMRGPVGKFEYLGNgtytvHKGKGGLKTMHvdafamiaggTGITP 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 196 MVPILQSITDNENDETFVTLVGCFKTFESIYLKTFLQEQARFWNVRTFFVLSQESSSEqlpWSYQEkthfGHLGQDLIKE 275
Cdd:PTZ00319 181 MLQIIHAIKKNKEDRTKVFLVYANQTEDDILLRKELDEAAKDPRFHVWYTLDREATPE---WKYGT----GYVDEEMLRA 253

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 134133308 276 LV------SCCRRKPFALVCGSAEFTKD-IARCLLCAGLTEDSYFLF 315
Cdd:PTZ00319 254 HLpvpdpqNSGIKKVMALMCGPPPMLQMaVKPNLEKIGYTADNMFTF 300
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
75-313 2.05e-20

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 87.92  E-value: 2.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  75 ETFVAFCIIAMDRLTKDTYRVRFALP-GNSQLGLRPGQHLILRGIVDDLEIQRAYTpISPANAEGYFEVLIKCYQMGLMS 153
Cdd:COG1018    1 AGFRPLRVVEVRRETPDVVSFTLEPPdGAPLPRFRPGQFVTLRLPIDGKPLRRAYS-LSSAPGDGRLEITVKRVPGGGGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 154 RYV-ESWRVGDTAFWRGPFGDFFYKPNQY--------GellllaagTGLAPMVPILQSITDNENDETfVTLVGCFKTFES 224
Cdd:COG1018   80 NWLhDHLKVGDTLEVSGPRGDFVLDPEPArpllliagG--------IGITPFLSMLRTLLARGPFRP-VTLVYGARSPAD 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 225 IYLKTFLQE-QARFWNVRTFFVLSQESSSEQlpwsyqekthfGHLGQDLIKELVsccrrKPFA----LVCGSAEFTKDIA 299
Cdd:COG1018  151 LAFRDELEAlAARHPRLRLHPVLSREPAGLQ-----------GRLDAELLAALL-----PDPAdahvYLCGPPPMMEAVR 214

                        250
                 ....*....|....
gi 134133308 300 RCLLCAGLTEDSYF 313
Cdd:COG1018  215 AALAELGVPEERIH 228
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 87-313 1.96e-19

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: 85.19  E-value: 1.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  87 RLTKDTYRVRFALPgnSQLGLRPGQHLILRGIVDDLEIQRAYTPISPANAEGYFEVLIKCYQMGLMSRYVESWRVGDTAF 166
Cdd:cd00322    5 DVTDDVRLFRLQLP--NGFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEGELELTVKIVPGGPFSAWLHDLKPGDEVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 167 WRGPFGDFFYKPNQYGELLLLAAGTGLAPMVPILQSITDNENDETFVTLVGCfKTFESI-YLKTFLQEQARFWNVRTFFV 245
Cdd:cd00322   83 VSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGA-RTPADLlFLDELEELAKEGPNFRLVLA 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134133308 246 LSQESSSEQLPWsyqektHFGHLGQDLIKELVSccRRKPFALVCGSAEFTKDIARCLLCAGLTEDSYF 313
Cdd:cd00322  162 LSRESEAKLGPG------GRIDREAEILALLPD--DSGALVYICGPPAMAKAVREALVSLGVPEERIH 221
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 89-312 3.26e-17

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: 79.11  E-value: 3.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  89 TKDTYRVRFALPGNSQLGLRPGQHLILRGIVDDLEIQRAYTpISPANAEGYFEVLIKCYQMGLMSRY-VESWRVGDTAFW 167
Cdd:cd06191   10 TPDAVTIVFAVPGPLQYGFRPGQHVTLKLDFDGEELRRCYS-LCSSPAPDEISITVKRVPGGRVSNYlREHIQPGMTVEV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 168 RGPFGDFFYKPNQYGELLLLAAGTGLAPMVPILQSITDNENDETFvTLVGCFKTFESIYLKTFLQEQARF-WNVRTFFVL 246
Cdd:cd06191   89 MGPQGHFVYQPQPPGRYLLVAAGSGITPLMAMIRATLQTAPESDF-TLIHSARTPADMIFAQELRELADKpQRLRLLCIF 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134133308 247 SQESSseQLPWSYQEkthfGHLGQDLIKELVScCRRKPFALVCGSAEFTKDIARCLLCAGLTEDSY 312
Cdd:cd06191  168 TRETL--DSDLLHGR----IDGEQSLGAALIP-DRLEREAFICGPAGMMDAVETALKELGMPPERI 226
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 89-310 2.03e-16

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: 76.92  E-value: 2.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  89 TKDTYRVRFALPGNSQLGLRPGQHLILR-GIVDDLEIQRAYTPISPANAEGYFEVLIKCYQMGLMSRY-VESWRVGDTAF 166
Cdd:cd06217   13 TPTVKTFRLAVPDGVPPPFLAGQHVDLRlTAIDGYTAQRSYSIASSPTQRGRVELTVKRVPGGEVSPYlHDEVKVGDLLE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 167 WRGPFGDFFYKPNQYGELLLLAAGTGLAPMVPILQSITDNENDETFVTLVGCFKTFESIYLKTFLQEQARFWNVRTFFVL 246
Cdd:cd06217   93 VRGPIGTFTWNPLHGDPVVLLAGGSGIVPLMSMIRYRRDLGWPVPFRLLYSARTAEDVIFRDELEQLARRHPNLHVTEAL 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134133308 247 SQESSSEqlpWSyqekthfGHLGQ---DLIKELVSCCRRKPFaLVCGSAEFTKDIARCLLCAGLTED 310
Cdd:cd06217  173 TRAAPAD---WL-------GPAGRitaDLIAELVPPLAGRRV-YVCGPPAFVEAATRLLLELGVPRD 228
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 82-310 7.13e-16

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 75.67  E-value: 7.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  82 IIAMDRLTKDTYRVRFALPGnSQLGLRPGQHLILRgiVDDLEIQRAYTPISPANAEGYFEVLIKcyQMGLMSRYVESWRV 161
Cdd:COG0543    2 VVSVERLAPDVYLLRLEAPL-IALKFKPGQFVMLR--VPGDGLRRPFSIASAPREDGTIELHIR--VVGKGTRALAELKP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 162 GDTAFWRGPFGDFFYKPNQY----------GellllaagtgLAPMVPILQSITDNENDetfVTLV-GcFKTFESIYLKTF 230
Cdd:COG0543   77 GDELDVRGPLGNGFPLEDSGrpvllvaggtG----------LAPLRSLAEALLARGRR---VTLYlG-ARTPEDLYLLDE 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 231 LQEqarfWNVRTFFVLSQESSseqlpwsyqekthFGHLG--QDLIKELVSccRRKPF-ALVCGSAEFTKDIARCLLCAGL 307
Cdd:COG0543  143 LEA----LADFRVVVTTDDGW-------------YGRKGfvTDALKELLA--EDSGDdVYACGPPPMMKAVAELLLERGV 203


                 ...
gi 134133308 308 TED 310
Cdd:COG0543  204 PPE 206
PTZ00274 PTZ00274
cytochrome b5 reductase; Provisional
 88-299 4.73e-14

cytochrome b5 reductase; Provisional


Pssm-ID: 140300  Cd Length: 325  Bit Score: 71.49  E-value: 4.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  88 LTKDTYRVRFALPGNSQLGLRPG---QHLILRGIVDDLEIQRAYTPISPANAEGYFEVLIKCYQMGLMSRYVESWRVGDT 164
Cdd:PTZ00274  63 ITHDTALFRFLLHSEEEFNLKPCstlQACYKYGVQPMDQCQRFYTPVTANHTKGYFDIIVKRKKDGLMTNHLFGMHVGDK 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 165 AFWRGPFGDFFYKPNQYGELLLLAAGTGLAPMVPIL-----QSITDNENDETFVTLVGCFKTFESIYLKTFLQEQA-RFW 238
Cdd:PTZ00274 143 LLFRSVTFKIQYRPNRWKHVGMIAGGTGFTPMLQIIrhsltEPWDSGEVDRTKLSFLFCNRTERHILLKGLFDDLArRYS 222

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134133308 239 N-VRTFFVLSQESSSEQLPwsyqektHF-GHLGQDLIKELVSCC-RRKPFALVCGSAEFTKDIA 299
Cdd:PTZ00274 223 NrFKVYYTIDQAVEPDKWN-------HFlGYVTKEMVRRTMPAPeEKKKIIMLCGPDQLLNHVA 279
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 82-310 3.83e-12

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: 64.87  E-value: 3.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  82 IIAMDRLTKDTYRVRFALP--GNSQLGLRPGQHLILRGIVDDLEIQRAYTpISPANAEGYFEVLIKCYQMGLMSRYV-ES 158
Cdd:cd06214    6 VAEVVRETADAVSITFDVPeeLRDAFRYRPGQFLTLRVPIDGEEVRRSYS-ICSSPGDDELRITVKRVPGGRFSNWAnDE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 159 WRVGDTAFWRGPFGDFFYKPNQY-----------GellllaagtgLAPMVPILQSITDNENDETFvTLVGCFKTFESIYL 227
Cdd:cd06214   85 LKAGDTLEVMPPAGRFTLPPLPGarhyvlfaagsG----------ITPVLSILKTALAREPASRV-TLVYGNRTEASVIF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 228 K---TFLQEQ--ARFwnvRTFFVLSQESSSEQLPwsyqekthFGHLGQDLIKELV-SCCRRKPFALV--CGSAEFTKDIA 299
Cdd:cd06214  154 ReelADLKARypDRL---TVIHVLSREQGDPDLL--------RGRLDAAKLNALLkNLLDATEFDEAflCGPEPMMDAVE 222

                        250
                 ....*....|.
gi 134133308 300 RCLLCAGLTED 310
Cdd:cd06214  223 AALLELGVPAE 233
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 88-310 3.02e-11

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: 62.34  E-value: 3.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  88 LTKDTYRVRFALPGNSQLGLRPGQHLILRgiVDDLEIQRAYTPISPANAEGYFEVLIKCYQMGLMSRYV-ESWRVGDTAF 166
Cdd:cd06211   17 LTPTIKGVRLKLDEPEEIEFQAGQYVNLQ--APGYEGTRAFSIASSPSDAGEIELHIRLVPGGIATTYVhKQLKEGDELE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 167 WRGPFGDFFYKPNQygellllaagtgLAPMV---------PILQSITD--NENDETFVTLVGCFKTFESIY-LKTFLQEQ 234
Cdd:cd06211   95 ISGPYGDFFVRDSD------------QRPIIfiaggsglsSPRSMILDllERGDTRKITLFFGARTRAELYyLDEFEALE 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134133308 235 ARFWNVRTFFVLSQEssSEQLPWsyQEKTHFGHlgqDLIKELVSCCRRKPFALVCGSAEFTKDIARCLLCAGLTED 310
Cdd:cd06211  163 KDHPNFKYVPALSRE--PPESNW--KGFTGFVH---DAAKKHFKNDFRGHKAYLCGPPPMIDACIKTLMQGRLFER 231
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 89-313 5.54e-09

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: 55.67  E-value: 5.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  89 TKDTYRVRFALPGNSQLGLRPGQHLILRGIVDDLEIQRAYTPISPANAEGYFEVLIKCYQMGLMSRY-VESWRVGDTAFW 167
Cdd:cd06215   10 TPDVKTFRFAAPDGSLFAYKPGQFLTLELEIDGETVYRAYTLSSSPSRPDSLSITVKRVPGGLVSNWlHDNLKVGDELWA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 168 RGPFGDFFYKPNQYGELLLLAAGTGLAPMVPILQSITDNENDeTFVTLVGCFKTFESIYLKTFLQE-QARFWNVRTFFVL 246
Cdd:cd06215   90 SGPAGEFTLIDHPADKLLLLSAGSGITPMMSMARWLLDTRPD-ADIVFIHSARSPADIIFADELEElARRHPNFRLHLIL 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134133308 247 SQESSSeqlPWSYQEkthfGHLGQDLIKELVSCCRRKPfALVCGSAEFTKDIARCLLCAGLTEDSYF 313
Cdd:cd06215  169 EQPAPG---AWGGYR----GRLNAELLALLVPDLKERT-VFVCGPAGFMKAVKSLLAELGFPMSRFH 227
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 82-310 6.62e-09

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: 55.29  E-value: 6.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  82 IIAMDRLTKDTYRVRFALPGnsQLGLRPGQHLILRgiVDDLEIQ-RAYTPISPANAEGYFEVLIKCYQMGLMSRYVESW- 159
Cdd:cd06187    1 VVSVERLTHDIAVVRLQLDQ--PLPFWAGQYVNVT--VPGRPRTwRAYSPANPPNEDGEIEFHVRAVPGGRVSNALHDEl 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 160 RVGDTAFWRGPFGDFFYKPNQYGELLLLAAGTGLAPMVPIL-QSITDNENDEtfVTLVGCFKTFESIY-LKTFLQEQARF 237
Cdd:cd06187   77 KVGDRVRLSGPYGTFYLRRDHDRPVLCIAGGTGLAPLRAIVeDALRRGEPRP--VHLFFGARTERDLYdLEGLLALAARH 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134133308 238 WNVRTFFVLSQESSseqlPWSYQEKTHFGHLGQDlikeLVSCCRRKpfALVCGSAEFTKDIARCLLCAGLTED 310
Cdd:cd06187  155 PWLRVVPVVSHEEG----AWTGRRGLVTDVVGRD----GPDWADHD--IYICGPPAMVDATVDALLARGAPPE 217
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 82-307 3.45e-08

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: 53.04  E-value: 3.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  82 IIAMDRLTKDTYRVRFALPgnSQLGLRPGQHLILRGiVDDLeiQRAYTPISPANAEGYFEVLIKCYQMGLMSRY-VESWR 160
Cdd:cd06194    1 VVSLQRLSPDVLRVRLEPD--RPLPYLPGQYVNLRR-AGGL--ARSYSPTSLPDGDNELEFHIRRKPNGAFSGWlGEEAR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 161 VGDTAFWRGPFGDFFYKP-NQYGELLLLAAGTGLAPMVPILQSITDNENDETFVTLVGCfKTFESIYLKTFLQEQAR-FW 238
Cdd:cd06194   76 PGHALRLQGPFGQAFYRPeYGEGPLLLVGAGTGLAPLWGIARAALRQGHQGEIRLVHGA-RDPDDLYLHPALLWLAReHP 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134133308 239 NVRTFFVLSQESSSEQLPWSYQEKTHFGHLGQDlikelvscCRrkpfALVCGSAEFTKDIARCLLCAGL 307
Cdd:cd06194  155 NFRYIPCVSEGSQGDPRVRAGRIAAHLPPLTRD--------DV----VYLCGAPSMVNAVRRRAFLAGA 211
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 82-174 9.16e-08

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: 52.23  E-value: 9.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  82 IIAMDRLTKDTYRVRFAlPGNSQLGLRPGQHLILRGIVDDLEIQRAYTPIS-PANAEGYFEVLIKCYQMGLMSRY-VESW 159
Cdd:cd06216   22 VVAVRPETADMVTLTLR-PNRGWPGHRAGQHVRLGVEIDGVRHWRSYSLSSsPTQEDGTITLTVKAQPDGLVSNWlVNHL 100

                         90
                 ....*....|....*
gi 134133308 160 RVGDTAFWRGPFGDF 174
Cdd:cd06216  101 APGDVVELSQPQGDF 115
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 82-258 2.53e-07

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: 50.79  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  82 IIAMDRLTKDTYRVRFALPGNSQLGLRPGQHLILrgIVDDLEIQRAYTPISPANAEGYFEVLIKCYQMGLMSRYVES-WR 160
Cdd:cd06212    5 VVAVEALTHDIRRLRLRLEEPEPIKFFAGQYVDI--TVPGTEETRSFSMANTPADPGRLEFIIKKYPGGLFSSFLDDgLA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 161 VGDTAFWRGPFGDFFYKPNQYGELLLLAAGTGLAPMVPILQSITDNENDETFVTLVGCFKTFESIYLKTFLQEQARFWNV 240
Cdd:cd06212   83 VGDPVTVTGPYGTCTLRESRDRPIVLIGGGSGMAPLLSLLRDMAASGSDRPVRFFYGARTARDLFYLEEIAALGEKIPDF 162

                        170
                 ....*....|....*...
gi 134133308 241 RTFFVLSQESSSEqlPWS 258
Cdd:cd06212  163 TFIPALSESPDDE--GWS 178
Oxidored-like pfam09791
Oxidoreductase-like protein, N-terminal; Members of this family are found in the N terminal ...
 19-51 8.60e-07

Oxidoreductase-like protein, N-terminal; Members of this family are found in the N terminal region of various oxidoreductase like proteins. Their exact function is, as yet, unknown.


Pssm-ID: 462904  Cd Length: 45  Bit Score: 44.86  E-value: 8.60e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 134133308   19 RPTEPlpSQCCGSGCSPCVFDLYHRDLARWEAA 51
Cdd:pfam09791   9 KPEEP--DNCCMSGCVNCVWDLYREDLEEWAEA 39
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 76-218 2.75e-06

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: 47.59  E-value: 2.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  76 TFVAFcIIAMDRLTKDTYRVRFALPGNSQLGLRPGQHLILRgiVDDLEIQRAYTPISPANaEGYFEVLIKCYQMGLMSRY 155
Cdd:cd06209    1 TFEAT-VTEVERLSDSTIGLTLELDEAGALAFLPGQYVNLQ--VPGTDETRSYSFSSAPG-DPRLEFLIRLLPGGAMSSY 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134133308 156 VESW-RVGDTAFWRGPFGDFFYKPNQyGELLLLAAGTGLAPMVPILQSITDNENDETFVTLVGC 218
Cdd:cd06209   77 LRDRaQPGDRLTLTGPLGSFYLREVK-RPLLMLAGGTGLAPFLSMLDVLAEDGSAHPVHLVYGV 139
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 192-300 4.87e-06

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: 44.56  E-value: 4.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  192 GLAPMVPILQSITDNENDETFVTLVGCFKTFESIYLKTFLQE--QARFWNVRTFFVLSQESSSeqlpWSYQEkthfGHLG 269
Cdd:pfam00175   7 GIAPVRSMLRAILEDPKDPTQVVLVFGNRNEDDILYREELDElaEKHPGRLTVVYVVSRPEAG----WTGGK----GRVQ 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 134133308  270 QDLIKELVSCCRRKPFALVCGSAEFTKDIAR 300
Cdd:pfam00175  79 DALLEDHLSLPDEETHVYVCGPPGMIKAVRK 109
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 82-200 8.29e-06

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: 46.18  E-value: 8.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  82 IIAMDRLTKDTYRVRF----ALPGNSQLGLRPGQHLILRgiVDDLEIQRAYTPISPANAEGYFEVLIKCYQMGLMSRYVE 157
Cdd:cd06210    6 IVAVDRVSSNVVRLRLqpddAEGAGIAAEFVPGQFVEIE--IPGTDTRRSYSLANTPNWDGRLEFLIRLLPGGAFSTYLE 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 134133308 158 SW-RVGDTAFWRGPFGDFFYKPNQYGELLLLAAGTGLAPMVPIL 200
Cdd:cd06210   84 TRaKVGQRLNLRGPLGAFGLRENGLRPRWFVAGGTGLAPLLSML 127
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 86-311 1.74e-05

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: 44.92  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  86 DRLTKDTYRVRFALPGNsqLGLRPGQ--HLILR--GIVDDleiQRAYTPISpANAEGYFEVLIKCY--QMGLMSRyVESW 159
Cdd:cd06196    9 EPVTHDVKRLRFDKPEG--YDFTPGQatEVAIDkpGWRDE---KRPFTFTS-LPEDDVLEFVIKSYpdHDGVTEQ-LGRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 160 RVGDTAFWRGPFGDFFYKpnqyGELLLLAAGTGLAPMVPILQSITDNENDETFvTLVGCFKTFESIYLKtflQEQARFWN 239
Cdd:cd06196   82 QPGDTLLIEDPWGAIEYK----GPGVFIAGGAGITPFIAILRDLAAKGKLEGN-TLIFANKTEKDIILK---DELEKMLG 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134133308 240 VRTFFVLSQESSSeqlpwsyqeKTHFGHLGQDLIKELVSCCRRKPFalVCGSAEFTKDIARCLLCAGLTEDS 311
Cdd:cd06196  154 LKFINVVTDEKDP---------GYAHGRIDKAFLKQHVTDFNQHFY--VCGPPPMEEAINGALKELGVPEDS 214
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 82-228 2.57e-05

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: 44.62  E-value: 2.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  82 IIAMDRLTKDTYRVRFALPGNSQLgLRPGQHLILRGivdDLEIQRAYTPISPANA---EGYFEVLIKcyQMGLMSRYVES 158
Cdd:cd06192    1 IVKKEQLEPNLVLLTIKAPLAARL-FRPGQFVFLRN---FESPGLERIPLSLAGVdpeEGTISLLVE--IRGPKTKLIAE 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 159 WRVGDTAFWRGPFGDFFYKPNQYGELLLLAAGTGLAPMVPILQSITDNENDetfVTLVGCFKTFESIYLK 228
Cdd:cd06192   75 LKPGEKLDVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIAKKLAANGNK---VTVLAGAKKAKEEFLD 141
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 87-260 1.06e-04

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: 42.63  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  87 RLTKDTYRVRFALPGnsQLGLRPGQHLILRgiVDDLEIQRAYTPISPANAEGYFEVLIKCYQMGLMSRYV-ESWRVGDTA 165
Cdd:cd06190    6 ELTHDVAEFRFALDG--PADFLPGQYALLA--LPGVEGARAYSMANLANASGEWEFIIKRKPGGAASNALfDNLEPGDEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 166 FWRGPFGDFFYKPNQYGELLLLAAGTGLAPMVPILQ-SITDNENDETFVTLV-GCFKTFESIYLKTFLQEQARFWNVRTF 243
Cdd:cd06190   82 ELDGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILRgAARSPYLSDRPVDLFyGGRTPSDLCALDELSALVALGARLRVT 161

                        170
                 ....*....|....*..
gi 134133308 244 FVLSQESSSEQLPWSYQ 260
Cdd:cd06190  162 PAVSDAGSGSAAGWDGP 178
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 108-306 1.38e-04

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: 42.54  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 108 RPGQHLILRGIVDDLE--IQRAYTpISPANAEGYFEVLIKCYQMGLMSRYV-ESWRVGDTAFWRGPFGDFFYKPNQ---- 180
Cdd:cd06184   38 LPGQYLSVRVKLPGLGyrQIRQYS-LSDAPNGDYYRISVKREPGGLVSNYLhDNVKVGDVLEVSAPAGDFVLDEASdrpl 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 181 ------YGellllaagtgLAPMVPILQSITDNENDETfVTLVGCFKTFESIYLKTFLQE-QARFWNVRTFFVLSQESSSE 253
Cdd:cd06184  117 vlisagVG----------ITPMLSMLEALAAEGPGRP-VTFIHAARNSAVHAFRDELEElAARLPNLKLHVFYSEPEAGD 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 134133308 254 QLpwsyQEKTHFGHLGQDLIKELVsccrrkPFA----LVCGSAEFTKDIARCLLCAG 306
Cdd:cd06184  186 RE----EDYDHAGRIDLALLRELL------LPAdadfYLCGPVPFMQAVREGLKALG 232
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 82-258 1.82e-04

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: 41.91  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  82 IIAMDRLTKDTYRVRFALpgNSQLGLRPGQHLILRgiVDDLEIQRAYTPISPANAEGYFEVLIKCYQMGLMSRYV-ESWR 160
Cdd:cd06213    5 IVAQERLTHDIVRLTVQL--DRPIAYKAGQYAELT--LPGLPAARSYSFANAPQGDGQLSFHIRKVPGGAFSGWLfGADR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 161 VGDTAFWRGPFGDFFYKPNQY-------GellllaagTGLAPMVPILQSITDNENDETFVTLVGCfKTFESIYLKTFLQE 233
Cdd:cd06213   81 TGERLTVRGPFGDFWLRPGDApilciagG--------SGLAPILAILEQARAAGTKRDVTLLFGA-RTQRDLYALDEIAA 151

                        170       180
                 ....*....|....*....|....*..
gi 134133308 234 QARFWNVRTFF--VLSQESSSEqlPWS 258
Cdd:cd06213  152 IAARWRGRFRFipVLSEEPADS--SWK 176
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 82-314 2.46e-04

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 42.10  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  82 IIAMDRLT--KDTYRVRFALPG-NSQLGLRPGQHLIL--RGiVDDLEIQRAYTPISPanaeGYFEVLIKcyQMGLMSRYV 156
Cdd:PRK08345  10 ILEVYDLTerEKLFLLRFEDPElAESFTFKPGQFVQVtiPG-VGEVPISICSSPTRK----GFFELCIR--RAGRVTTVI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 157 ESWRVGDTAFWRGPFGDFFykPNQYGELLLLAAGTGLAPMVP---ILQSITDNENDETFVTLVGCFKTFESI-YLKTFLQ 232
Cdd:PRK08345  83 HRLKEGDIVGVRGPYGNGF--PVDEMEGMDLLLIAGGLGMAPlrsVLLYAMDNRWKYGNITLIYGAKYYEDLlFYDELIK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 233 EQARFWNVRTFFVLSQE---SSSEQLPWSYQEKTHFGHLGQDLIKELVSCcrRKPFALVCGSAEFTKDIARCLLCAGLTE 309
Cdd:PRK08345 161 DLAEAENVKIIQSVTRDpewPGCHGLPQGFIERVCKGVVTDLFREANTDP--KNTYAAICGPPVMYKFVFKELINRGYRP 238


                 ....*
gi 134133308 310 DSYFL 314
Cdd:PRK08345 239 ERIYV 243
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 88-180 6.43e-04

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: 41.00  E-value: 6.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  88 LTKDTYRVRFALPGNSQLGLRPGQ----------------------HLILRGIVDDlEIQRAYTPISPANAEGYFEVLIK 145
Cdd:COG2871  142 VTTFIKELVLELPEGEEIDFKAGQyiqievppyevdfkdfdipeeeKFGLFDKNDE-EVTRAYSMANYPAEKGIIELNIR 220

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 134133308 146 ------CYQMGLMSRYVESWRVGDTAFWRGPFGDFFYKPNQ 180
Cdd:COG2871  221 iatppmDVPPGIGSSYIFSLKPGDKVTISGPYGEFFLRDSD 261
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 82-313 7.78e-04

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: 40.22  E-value: 7.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  82 IIAMDRLTKDTYRVRFALPGNsqLGLRPGQHLILrgIVDDlEIQRAYTPISPANAEGYFEVLIKCYQMGLMSRYV-ESWR 160
Cdd:cd06189    3 VESIEPLNDDVYRVRLKPPAP--LDFLAGQYLDL--LLDD-GDKRPFSIASAPHEDGEIELHIRAVPGGSFSDYVfEELK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 161 VGDTAFWRGPFGDFFYKPNQYGELLLLAAGTGLAPMVPILQSITDNENDETfVTLV-GCfKTFESIYLKTFLQEQARFW- 238
Cdd:cd06189   78 ENGLVRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQGSKRP-IHLYwGA-RTEEDLYLDELLEAWAEAHp 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 239 NVRTFFVLSQESSSeqlpWSYqektHFGHLGQDLIKELVSccrrkpfaL------VCGSAEFTKDIARCLLCAGLTEDSY 312
Cdd:cd06189  156 NFTYVPVLSEPEEG----WQG----RTGLVHEAVLEDFPD--------LsdfdvyACGSPEMVYAARDDFVEKGLPEENF 219


                 .
gi 134133308 313 F 313
Cdd:cd06189  220 F 220
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 82-314 1.93e-03

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: 39.13  E-value: 1.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308  82 IIAMDRLTKD--TYRVRFALPGNSQLGLRPGQHLILrGIVDDLEIqraytPISPANA---EGYFEVLIKcyQMGLMSRYV 156
Cdd:cd06221    1 IVEVVDETEDikTFTLRLEDDDEELFTFKPGQFVML-SLPGVGEA-----PISISSDptrRGPLELTIR--RVGRVTEAL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 157 ESWRVGDTAFWRGPFGDFFyKPNQY----------GellllaagTGLAPMVPILQSITDNENDETFVTLVGCFKTFESIY 226
Cdd:cd06221   73 HELKPGDTVGLRGPFGNGF-PVEEMkgkdlllvagG--------LGLAPLRSLINYILDNREDYGKVTLLYGARTPEDLL 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133308 227 LKTFLQEQARFWNVRTFfvLSQESSSEQlpWSyqekthfGHLG--QDLIKELvsccRRKP---FALVCGSAEFTKDIARC 301
Cdd:cd06221  144 FKEELKEWAKRSDVEVI--LTVDRAEEG--WT-------GNVGlvTDLLPEL----TLDPdntVAIVCGPPIMMRFVAKE 208

                        250
                 ....*....|...
gi 134133308 302 LLCAGLTEDSYFL 314
Cdd:cd06221  209 LLKLGVPEEQIWV 221
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
104-175 7.07e-03

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 37.80  E-value: 7.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134133308 104 QLGLRPGQHLILRgiVDDLEIQRAYTPISPANAEGYFEVLIKCYQMGLMSRYV-ESWRVGDTAFWRGPFGDFF 175
Cdd:PRK11872 134 QLDFLPGQYARLQ--IPGTDDWRSYSFANRPNATNQLQFLIRLLPDGVMSNYLrERCQVGDEILFEAPLGAFY 204
 
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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