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Conserved domains on  [gi|723586612|ref|NP_001289756|]
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NADH-cytochrome b5 reductase 2 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02252 super family cl33442
nitrate reductase [NADPH]
 8-185 1.09e-78

nitrate reductase [NADPH]


The actual alignment was detected with superfamily member PLN02252:

Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 253.06  E-value: 1.09e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612   8 PITLQDPEAKYPLPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKI 87
Cdd:PLN02252 625 RPVALNPREKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFELVIKV 704

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  88 YFKNVHPQYPEGGKMTQYLENMKIGETIFFRGPRGRLFYHGPGNLGIRpdqtSEPKktLADHLGMIAGGTGITPMLQLIR 167
Cdd:PLN02252 705 YFKNVHPKFPNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFLVN----GKPK--FAKKLAMLAGGTGITPMYQVIQ 778

                        170
                 ....*....|....*...
gi 723586612 168 HITKDPSDRTRMSLIFAN 185
Cdd:PLN02252 779 AILRDPEDKTEMSLVYAN 796
 
Name Accession Description Interval E-value
PLN02252 PLN02252
nitrate reductase [NADPH]
 8-185 1.09e-78

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 253.06  E-value: 1.09e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612   8 PITLQDPEAKYPLPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKI 87
Cdd:PLN02252 625 RPVALNPREKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFELVIKV 704

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  88 YFKNVHPQYPEGGKMTQYLENMKIGETIFFRGPRGRLFYHGPGNLGIRpdqtSEPKktLADHLGMIAGGTGITPMLQLIR 167
Cdd:PLN02252 705 YFKNVHPKFPNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFLVN----GKPK--FAKKLAMLAGGTGITPMYQVIQ 778

                        170
                 ....*....|....*...
gi 723586612 168 HITKDPSDRTRMSLIFAN 185
Cdd:PLN02252 779 AILRDPEDKTEMSLVYAN 796
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 20-188 9.43e-74

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: 223.60  E-value: 9.43e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  20 LPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKIYFknvhpqypeG 99
Cdd:cd06183    1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYP---------G 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612 100 GKMTQYLENMKIGETIFFRGPRGRLFYHGPGNlgirpdqtsepkktlADHLGMIAGGTGITPMLQLIRHITKDPSDRTRM 179
Cdd:cd06183   72 GKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGK---------------VKHIGMIAGGTGITPMLQLIRAILKDPEDKTKI 136


                 ....*....
gi 723586612 180 SLIFANQRR 188
Cdd:cd06183  137 SLLYANRTE 145
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
19-126 5.27e-50

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 158.13  E-value: 5.27e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612   19 PLPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypE 98
Cdd:pfam00970   1 PLTLVEKELVSHDTRIFRFALPHPDQVLGLPVGQHLFLRLPIDGELVIRSYTPISSDDDKGYLELLVKVY---------P 71

                          90       100
                  ....*....|....*....|....*...
gi 723586612   99 GGKMTQYLENMKIGETIFFRGPRGRLFY 126
Cdd:pfam00970  72 GGKMSQYLDELKIGDTIDFKGPLGRFEY 99
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
18-188 5.42e-21

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 87.54  E-value: 5.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  18 YPLPLIEKEKISHNTRRFRF----GLPSPDHvlgLPvGNYVQLLAKIDNELVVRAYTPVSSDDDRGfvdliIKIYFKNVh 93
Cdd:COG1018    4 RPLRVVEVRRETPDVVSFTLeppdGAPLPRF---RP-GQFVTLRLPIDGKPLRRAYSLSSAPGDGR-----LEITVKRV- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  94 pqypEGGKMTQYL-ENMKIGETIFFRGPRGRLFYHGPGnlgirpdqtsepkktlADHLGMIAGGTGITPMLQLIRHITKD 172
Cdd:COG1018   74 ----PGGGGSNWLhDHLKVGDTLEVSGPRGDFVLDPEP----------------ARPLLLIAGGIGITPFLSMLRTLLAR 133

                        170
                 ....*....|....*.
gi 723586612 173 PSDRtRMSLIFANQRR 188
Cdd:COG1018  134 GPFR-PVTLVYGARSP 148
 
Name Accession Description Interval E-value
PLN02252 PLN02252
nitrate reductase [NADPH]
 8-185 1.09e-78

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 253.06  E-value: 1.09e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612   8 PITLQDPEAKYPLPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKI 87
Cdd:PLN02252 625 RPVALNPREKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFELVIKV 704

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  88 YFKNVHPQYPEGGKMTQYLENMKIGETIFFRGPRGRLFYHGPGNLGIRpdqtSEPKktLADHLGMIAGGTGITPMLQLIR 167
Cdd:PLN02252 705 YFKNVHPKFPNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFLVN----GKPK--FAKKLAMLAGGTGITPMYQVIQ 778

                        170
                 ....*....|....*...
gi 723586612 168 HITKDPSDRTRMSLIFAN 185
Cdd:PLN02252 779 AILRDPEDKTEMSLVYAN 796
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 20-188 9.43e-74

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: 223.60  E-value: 9.43e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  20 LPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKIYFknvhpqypeG 99
Cdd:cd06183    1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYP---------G 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612 100 GKMTQYLENMKIGETIFFRGPRGRLFYHGPGNlgirpdqtsepkktlADHLGMIAGGTGITPMLQLIRHITKDPSDRTRM 179
Cdd:cd06183   72 GKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGK---------------VKHIGMIAGGTGITPMLQLIRAILKDPEDKTKI 136


                 ....*....
gi 723586612 180 SLIFANQRR 188
Cdd:cd06183  137 SLLYANRTE 145
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
 5-186 2.71e-71

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 219.70  E-value: 2.71e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612   5 RREPITLqDPEAKYPLPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDN----ELVVRAYTPVSSDDDRGF 80
Cdd:PTZ00319  22 RSPPVAL-DPDMFQHFKLIKKTEVTHDTFIFRFALHSPTQRLGLPIGQHIVFRCDCTTpgkpETVQHSYTPISSDDEKGY 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  81 VDLIIKIYFKNVHPQYPEGGKMTQYLENMKIGETIFFRGPRGRLFYHGPGNLGIRPDQtSEPKKTLADHLGMIAGGTGIT 160
Cdd:PTZ00319 101 VDFLIKVYFKGVHPSFPNGGRLSQHLYHMKLGDKIEMRGPVGKFEYLGNGTYTVHKGK-GGLKTMHVDAFAMIAGGTGIT 179

                        170       180
                 ....*....|....*....|....*.
gi 723586612 161 PMLQLIRHITKDPSDRTRMSLIFANQ 186
Cdd:PTZ00319 180 PMLQIIHAIKKNKEDRTKVFLVYANQ 205
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
19-126 5.27e-50

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 158.13  E-value: 5.27e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612   19 PLPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypE 98
Cdd:pfam00970   1 PLTLVEKELVSHDTRIFRFALPHPDQVLGLPVGQHLFLRLPIDGELVIRSYTPISSDDDKGYLELLVKVY---------P 71

                          90       100
                  ....*....|....*....|....*...
gi 723586612   99 GGKMTQYLENMKIGETIFFRGPRGRLFY 126
Cdd:pfam00970  72 GGKMSQYLDELKIGDTIDFKGPLGRFEY 99
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 23-188 1.36e-27

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: 104.84  E-value: 1.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  23 IEKEKISHNTRRFRFGLPSPdhvLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypEGGKM 102
Cdd:cd00322    1 VATEDVTDDVRLFRLQLPNG---FSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEGELELTVKIV---------PGGPF 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612 103 TQYLENMKIGETIFFRGPRGRLFYHGPGNlgirpdqtsepkktlaDHLGMIAGGTGITPMLQLIRHITKDPSDRTrMSLI 182
Cdd:cd00322   69 SAWLHDLKPGDEVEVSGPGGDFFLPLEES----------------GPVVLIAGGIGITPFRSMLRHLAADKPGGE-ITLL 131


                 ....*.
gi 723586612 183 FANQRR 188
Cdd:cd00322  132 YGARTP 137
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
18-188 5.42e-21

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 87.54  E-value: 5.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  18 YPLPLIEKEKISHNTRRFRF----GLPSPDHvlgLPvGNYVQLLAKIDNELVVRAYTPVSSDDDRGfvdliIKIYFKNVh 93
Cdd:COG1018    4 RPLRVVEVRRETPDVVSFTLeppdGAPLPRF---RP-GQFVTLRLPIDGKPLRRAYSLSSAPGDGR-----LEITVKRV- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  94 pqypEGGKMTQYL-ENMKIGETIFFRGPRGRLFYHGPGnlgirpdqtsepkktlADHLGMIAGGTGITPMLQLIRHITKD 172
Cdd:COG1018   74 ----PGGGGSNWLhDHLKVGDTLEVSGPRGDFVLDPEP----------------ARPLLLIAGGIGITPFLSMLRTLLAR 133

                        170
                 ....*....|....*.
gi 723586612 173 PSDRtRMSLIFANQRR 188
Cdd:COG1018  134 GPFR-PVTLVYGARSP 148
PTZ00274 PTZ00274
cytochrome b5 reductase; Provisional
 3-186 8.07e-20

cytochrome b5 reductase; Provisional


Pssm-ID: 140300  Cd Length: 325  Bit Score: 86.13  E-value: 8.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612   3 SRRREPITLQDPeakypLPliekekISHNTRRFRFGLPSPDHvLGLPVGNYVQLLAKID---NELVVRAYTPVSSDDDRG 79
Cdd:PTZ00274  49 SQRYEPYQLGEV-----IP------ITHDTALFRFLLHSEEE-FNLKPCSTLQACYKYGvqpMDQCQRFYTPVTANHTKG 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  80 FVDLIIKiyfknvhpqYPEGGKMTQYLENMKIGETIFFRGPRGRLFYhgpgnlgiRPDQTSepkktladHLGMIAGGTGI 159
Cdd:PTZ00274 117 YFDIIVK---------RKKDGLMTNHLFGMHVGDKLLFRSVTFKIQY--------RPNRWK--------HVGMIAGGTGF 171

                        170       180       190
                 ....*....|....*....|....*....|..
gi 723586612 160 TPMLQLIRHITKDP-----SDRTRMSLIFANQ 186
Cdd:PTZ00274 172 TPMLQIIRHSLTEPwdsgeVDRTKLSFLFCNR 203
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 23-169 9.97e-18

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 79.14  E-value: 9.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  23 IEKEKISHNTRRFRFGLPsPDHVLGLPvGNYVQLlaKIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypegGKM 102
Cdd:COG0543    3 VSVERLAPDVYLLRLEAP-LIALKFKP-GQFVML--RVPGDGLRRPFSIASAPREDGTIELHIRVV-----------GKG 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 723586612 103 TQYLENMKIGETIFFRGPRGRLFyhgpgnlgirpDQTSEPKKTLadhlgMIAGGTGITPMLQLIRHI 169
Cdd:COG0543   68 TRALAELKPGDELDVRGPLGNGF-----------PLEDSGRPVL-----LVAGGTGLAPLRSLAEAL 118
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 20-216 9.16e-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 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: 73.39  E-value: 9.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  20 LPLIEKEKISHNTRRFRFGLPSPDHVLGLPvGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKiyfkNVhpqypEG 99
Cdd:cd06215    1 LRCVKIIQETPDVKTFRFAAPDGSLFAYKP-GQFLTLELEIDGETVYRAYTLSSSPSRPDSLSITVK----RV-----PG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612 100 GKMTQYL-ENMKIGETIFFRGPRGRlFYhgpgnlgirpdqtsePKKTLADHLGMIAGGTGITPMLQLIRHITKDPSD--- 175
Cdd:cd06215   71 GLVSNWLhDNLKVGDELWASGPAGE-FT---------------LIDHPADKLLLLSAGSGITPMMSMARWLLDTRPDadi 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 723586612 176 ------RTRMSLIFANQrrisWSEKSlKKLPGLTQT---SSTCGTPWTGL 216
Cdd:cd06215  135 vfihsaRSPADIIFADE----LEELA-RRHPNFRLHlilEQPAPGAWGGY 179
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 30-187 6.81e-15

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: 71.14  E-value: 6.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  30 HNTRRFRFGLP---SPDHvlgLPvGNYVQL-LAKIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypEGGKMTQY 105
Cdd:cd06217   14 PTVKTFRLAVPdgvPPPF---LA-GQHVDLrLTAIDGYTAQRSYSIASSPTQRGRVELTVKRV---------PGGEVSPY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612 106 L-ENMKIGETIFFRGPRGRlFYHGPGnlgirpdqtsepkktLADHLGMIAGGTGITPMLQLIRHITkDPSDRTRMSLIFA 184
Cdd:cd06217   81 LhDEVKVGDLLEVRGPIGT-FTWNPL---------------HGDPVVLLAGGSGIVPLMSMIRYRR-DLGWPVPFRLLYS 143


                 ...
gi 723586612 185 NQR 187
Cdd:cd06217  144 ART 146
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 22-183 6.38e-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: 68.43  E-value: 6.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  22 LIEKEKISHNTRRFRFGLPSPDHVLglPvGNYVQL-LAKIDnelVVRAYTPVSSDDDRGFVDLIIKiyfknvhpQYPeGG 100
Cdd:cd06190    1 LVDVRELTHDVAEFRFALDGPADFL--P-GQYALLaLPGVE---GARAYSMANLANASGEWEFIIK--------RKP-GG 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612 101 KMTQYL-ENMKIGETIFFRGPRGRLFyhgpgnlgIRPDqtsEPKKTLadhlgMIAGGTGITPMLQLIRHITKDPSDRTRM 179
Cdd:cd06190   66 AASNALfDNLEPGDELELDGPYGLAY--------LRPD---EDRDIV-----CIAGGSGLAPMLSILRGAARSPYLSDRP 129


                 ....
gi 723586612 180 SLIF 183
Cdd:cd06190  130 VDLF 133
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 26-183 2.23e-13

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: 66.85  E-value: 2.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  26 EKISHNTRRFRFGLPSPDHVLGLPvGNYVQLlaKIDNELVVRAYTPVSSDDDRGFVDLIikiyfKNVhpqypEGGKMTQY 105
Cdd:cd06209   10 ERLSDSTIGLTLELDEAGALAFLP-GQYVNL--QVPGTDETRSYSFSSAPGDPRLEFLI-----RLL-----PGGAMSSY 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 723586612 106 LENM-KIGETIFFRGPRGRlFYHGPGNlgiRPdqtsepkktladHLgMIAGGTGITPMLQLIRHITKDPSDRtRMSLIF 183
Cdd:cd06209   77 LRDRaQPGDRLTLTGPLGS-FYLREVK---RP------------LL-MLAGGTGLAPFLSMLDVLAEDGSAH-PVHLVY 137
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 22-177 6.65e-12

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


Pssm-ID: 99807  Cd Length: 238  Bit Score: 62.73  E-value: 6.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  22 LIEKEKISHNTRRFRFGLPSPDHVLGLPvGNYVQLlaKIDNELVVRAYTPVSSDDDRGFVDLIIKiyfknvhpqYPEGGK 101
Cdd:cd06211   11 VVEIEDLTPTIKGVRLKLDEPEEIEFQA-GQYVNL--QAPGYEGTRAFSIASSPSDAGEIELHIR---------LVPGGI 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 723586612 102 MTQYL-ENMKIGETIFFRGPRGRLFYHgpgnlgirpDQTSEPkktladhLGMIAGGTGITPMLQLIRHITKDPSDRT 177
Cdd:cd06211   79 ATTYVhKQLKEGDELEISGPYGDFFVR---------DSDQRP-------IIFIAGGSGLSSPRSMILDLLERGDTRK 139
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 152-186 5.87e-11

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: 57.65  E-value: 5.87e-11
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 723586612  152 MIAGGTGITPMLQLIRHITKDPSDRTRMSLIFANQ 186
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDPKDPTQVVLVFGNR 35
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 51-167 6.31e-11

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: 60.32  E-value: 6.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  51 GNYVQLLAKIDNELVVRAYTPVSSDDDR-GFVDLIIKIyfknvHPqypeGGKMTQYL-ENMKIGETIFFRGPRGRlFYhg 128
Cdd:cd06216   49 GQHVRLGVEIDGVRHWRSYSLSSSPTQEdGTITLTVKA-----QP----DGLVSNWLvNHLAPGDVVELSQPQGD-FV-- 116

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 723586612 129 pgnlgiRPDQTSEPkktladhLGMIAGGTGITPMLQLIR 167
Cdd:cd06216  117 ------LPDPLPPR-------LLLIAAGSGITPVMSMLR 142
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 26-203 2.36e-10

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: 58.51  E-value: 2.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  26 EKISHNTRRFRFGlPSPDHVLGLPV----GNYVQLlaKIDNELVVRAYTPVSSDDDRGFVDLIIKiyfknVHPqypeGGK 101
Cdd:cd06210   10 DRVSSNVVRLRLQ-PDDAEGAGIAAefvpGQFVEI--EIPGTDTRRSYSLANTPNWDGRLEFLIR-----LLP----GGA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612 102 MTQYLEN-MKIGETIFFRGPRGR--LFYHGPgnlgiRPdqtsepkktladhLGMIAGGTGITPMLQLIRHITK--DPSDR 176
Cdd:cd06210   78 FSTYLETrAKVGQRLNLRGPLGAfgLRENGL-----RP-------------RWFVAGGTGLAPLLSMLRRMAEwgEPQEA 139

                        170       180       190
                 ....*....|....*....|....*....|..
gi 723586612 177 TrmsLIF-ANQRRISWSEKSLKKL----PGLT 203
Cdd:cd06210  140 R---LFFgVNTEAELFYLDELKRLadslPNLT 168
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 18-216 2.36e-10

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: 58.41  E-value: 2.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  18 YPLPLIEKEKISHNTRRFRFGLPspdHVLGLPVGNYVQL-LAKIDNELVVRAYTPVSSDDDRgFVDLIIKIYfknvhpqy 96
Cdd:cd06196    1 HTVTLLSIEPVTHDVKRLRFDKP---EGYDFTPGQATEVaIDKPGWRDEKRPFTFTSLPEDD-VLEFVIKSY-------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  97 PEGGKMTQYLENMKIGETIFFRGPRGRLFYHGPGNLgirpdqtsepkktladhlgmIAGGTGITPMLQLIRHITKDP--S 174
Cdd:cd06196   69 PDHDGVTEQLGRLQPGDTLLIEDPWGAIEYKGPGVF--------------------IAGGAGITPFIAILRDLAAKGklE 128

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 723586612 175 DRTrmsLIFANQ--RRISWsEKSLKKLPGLTQTSSTCGTPWTGL 216
Cdd:cd06196  129 GNT---LIFANKteKDIIL-KDELEKMLGLKFINVVTDEKDPGY 168
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 18-188 3.42e-10

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: 57.94  E-value: 3.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  18 YPLPLIEKEKISHNTRRFRFGLPSP-DHVLGLPVGNYVQLLAKIDNELVVRAY---TPVSSDDdrgfvdliIKIYFKNVh 93
Cdd:cd06214    2 HPLTVAEVVRETADAVSITFDVPEElRDAFRYRPGQFLTLRVPIDGEEVRRSYsicSSPGDDE--------LRITVKRV- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  94 pqypEGGKMTQYL-ENMKIGETIFFRGPRGRLFYhgpgnlgirpdqtsePKKTLADHLGMIAGGTGITPMLQLIRHITKD 172
Cdd:cd06214   73 ----PGGRFSNWAnDELKAGDTLEVMPPAGRFTL---------------PPLPGARHYVLFAAGSGITPVLSILKTALAR 133

                        170
                 ....*....|....*.
gi 723586612 173 PSDRtRMSLIFANQRR 188
Cdd:cd06214  134 EPAS-RVTLVYGNRTE 148
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 20-188 2.94e-09

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: 55.23  E-value: 2.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  20 LPLIEKEKISHNTRRFRFGLPSPDHVLGLPvGNYVQLLAKIDNELVVRAYTPVSSD-DDRgfvdliIKIYFKNVhpqypE 98
Cdd:cd06191    1 LRVAEVRSETPDAVTIVFAVPGPLQYGFRP-GQHVTLKLDFDGEELRRCYSLCSSPaPDE------ISITVKRV-----P 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  99 GGKMTQYL-ENMKIGETIFFRGPRGRLFYhgpgnlgirpdQTSEPKKTLAdhlgmIAGGTGITPMLQLIR--HITKDPSD 175
Cdd:cd06191   69 GGRVSNYLrEHIQPGMTVEVMGPQGHFVY-----------QPQPPGRYLL-----VAAGSGITPLMAMIRatLQTAPESD 132

                        170       180
                 ....*....|....*....|
gi 723586612 176 -------RTRMSLIFANQRR 188
Cdd:cd06191  133 ftlihsaRTPADMIFAQELR 152
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 23-169 3.63e-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: 54.91  E-value: 3.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  23 IEKEKISHNTRRFRFGLPSPDHVLGlpvGNYVQLLAkIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypEGGKM 102
Cdd:cd06187    2 VSVERLTHDIAVVRLQLDQPLPFWA---GQYVNVTV-PGRPRTWRAYSPANPPNEDGEIEFHVRAV---------PGGRV 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 723586612 103 TQYLEN-MKIGETIFFRGPRGRLFYHGPGNlgiRPdqtsepkktladhLGMIAGGTGITPMLQLIRHI 169
Cdd:cd06187   69 SNALHDeLKVGDRVRLSGPYGTFYLRRDHD---RP-------------VLCIAGGTGLAPLRAIVEDA 120
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 32-173 1.67e-08

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 54.40  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612   32 TRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKiyfknvhpqyPEGGKMTQYLENMKI 111
Cdd:PTZ00306  932 SRVLRFNLPGALQRSGLTLGQFIAIRGDWDGQQLIGYYSPITLPDDLGVISILAR----------GDKGTLKEWISALRP 1001

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 723586612  112 GETIFFRGPRGRLFYHGPGnlgirpDQTSEPKKTLADHLGMIAGGTGITPMLQLIRHITKDP 173
Cdd:PTZ00306 1002 GDSVEMKACGGLRIERRPA------DKQFVFRGHVIRKLALIAGGTGVAPMLQIIRAALKKP 1057
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 23-175 2.02e-08

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: 52.93  E-value: 2.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  23 IEKEKISHNTRRFRFGLPSPDHVlGLPvGNYVQLLAKIDNELVVRayTPVS---SDDDRGFVDLIIKIYfknvhpqypeg 99
Cdd:cd06218    2 LSNREIADDIYRLVLEAPEIAAA-AKP-GQFVMLRVPDGSDPLLR--RPISihdVDPEEGTITLLYKVV----------- 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 723586612 100 GKMTQYLENMKIGETIFFRGPRGRLFyhgpgnlgirpDQTSEPKKTLadhlgMIAGGTGITPMLQLIRHITKDPSD 175
Cdd:cd06218   67 GKGTRLLSELKAGDELDVLGPLGNGF-----------DLPDDDGKVL-----LVGGGIGIAPLLFLAKQLAERGIK 126
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 17-202 5.24e-08

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 52.18  E-value: 5.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  17 KYPLPLIEKEKISHNTRRFRFGLPSPDHVLGLPvGNYVQLLAKiDNElvVRAYTPVSSDDDRGFVDLiikiyfknvHPQY 96
Cdd:PRK07609 102 KLPCRVASLERVAGDVMRLKLRLPATERLQYLA-GQYIEFILK-DGK--RRSYSIANAPHSGGPLEL---------HIRH 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  97 PEGGKMTQYL-ENMKIGETIFFRGPRGRLFYHgpgnlgirpdqtSEPKKTLAdhlgMIAGGTGITPMLQLIRHITKDPSD 175
Cdd:PRK07609 169 MPGGVFTDHVfGALKERDILRIEGPLGTFFLR------------EDSDKPIV----LLASGTGFAPIKSIVEHLRAKGIQ 232

                        170       180       190
                 ....*....|....*....|....*....|..
gi 723586612 176 RTrMSLIFANQRR-----ISWSEKSLKKLPGL 202
Cdd:PRK07609 233 RP-VTLYWGARRPedlylSALAEQWAEELPNF 263
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 26-177 6.68e-08

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: 51.56  E-value: 6.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  26 EKISHNTRRFRFGLPSPDHVLGLPvGNYVQLLakIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypEGGKMTQY 105
Cdd:cd06212    9 EALTHDIRRLRLRLEEPEPIKFFA-GQYVDIT--VPGTEETRSFSMANTPADPGRLEFIIKKY---------PGGLFSSF 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 723586612 106 LEN-MKIGETIFFRGPRGRLFyhgpgnlgIRPDQTSEpkktladhLGMIAGGTGITPMLQLIRHITKDPSDRT 177
Cdd:cd06212   77 LDDgLAVGDPVTVTGPYGTCT--------LRESRDRP--------IVLIGGGSGMAPLLSLLRDMAASGSDRP 133
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 71-217 1.52e-07

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: 50.68  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  71 PVSSDDDRGFVDLIIKiyfkNVhpqypegGKMTQYLENMKIGETIFFRGPRGRLFyhgpgnlgirpdqtsePKKTLADH- 149
Cdd:cd06221   48 ISSDPTRRGPLELTIR----RV-------GRVTEALHELKPGDTVGLRGPFGNGF----------------PVEEMKGKd 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 723586612 150 LGMIAGGTGITPMLQLIRHITKDPSD----------RTRMSLIFANQRRiSWSEKSLKKLPgLTQTSSTCGTPW-TGLP 217
Cdd:cd06221  101 LLLVAGGLGLAPLRSLINYILDNREDygkvtllygaRTPEDLLFKEELK-EWAKRSDVEVI-LTVDRAEEGWTGnVGLV 177
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 100-183 2.38e-07

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: 49.94  E-value: 2.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612 100 GKMTQYLENMKIGETIFFRGPRGRLFyhgpgnlgirpdqTSEPKKTLAdhlgmIAGGTGITPMLQLIRHITKD------P 173
Cdd:cd06220   59 GEATSALHDLKEGDKLGIRGPYGNGF-------------ELVGGKVLL-----IGGGIGIAPLAPLAERLKKAadvtvlL 120

                         90
                 ....*....|
gi 723586612 174 SDRTRMSLIF 183
Cdd:cd06220  121 GARTKEELLF 130
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
69-188 2.63e-07

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 50.28  E-value: 2.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  69 YTPVSSDDDRGFVDLIIKiyfknvhpqypEGGKMTQYLENMKIGETIFFRGPRGRLFYHGpgnlgiRPDqtsepkktlAD 148
Cdd:COG4097  266 FSISSAPGGDGRLRFTIK-----------ALGDFTRRLGRLKPGTRVYVEGPYGRFTFDR------RDT---------AP 319

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 723586612 149 HLGMIAGGTGITPMLQLIRHITKDPSDRTRMSLIFANQRR 188
Cdd:COG4097  320 RQVWIAGGIGITPFLALLRALAARPGDQRPVDLFYCVRDE 359
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 46-168 7.34e-07

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: 48.33  E-value: 7.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  46 LGLPVGnyvqllakiDNELVVRAYTPVSSDDDRGFVDLIIKIyfknvhpqypEGGKMTQYLENMKIGETIF-FRGPRGRL 124
Cdd:cd06195   33 LGLPND---------DGKLVRRAYSIASAPYEENLEFYIILV----------PDGPLTPRLFKLKPGDTIYvGKKPTGFL 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 723586612 125 FyhgpgnlgIRPDQTSEpkktladHLGMIAGGTGITPMLQLIRH 168
Cdd:cd06195   94 T--------LDEVPPGK-------RLWLLATGTGIAPFLSMLRD 122
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 22-167 2.61e-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: 43.85  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  22 LIEKEKISHNTRRFRFGLPSPDHvLGLPvGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKIyfknvhpqypeGGK 101
Cdd:cd06192    1 IVKKEQLEPNLVLLTIKAPLAAR-LFRP-GQFVFLRNFESPGLERIPLSLAGVDPEEGTISLLVEI-----------RGP 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 723586612 102 MTQYLENMKIGETIFFRGPRGRLFYHGPGNlgirpdqtsepKKTLadhlgMIAGGTGITPMLQLIR 167
Cdd:cd06192   68 KTKLIAELKPGEKLDVMGPLGNGFEGPKKG-----------GTVL-----LVAGGIGLAPLLPIAK 117
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 26-176 2.74e-05

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: 43.69  E-value: 2.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  26 EKISHNTRRFRFGLPSPDHVLGlpvGNYVQLLAKiDNELvvRAYTPVSSDDDRGFVDLIIKIYfknvhpqypEGGKMTQY 105
Cdd:cd06189    7 EPLNDDVYRVRLKPPAPLDFLA---GQYLDLLLD-DGDK--RPFSIASAPHEDGEIELHIRAV---------PGGSFSDY 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 723586612 106 -LENMKIGETIFFRGPRGRLFYHgpgnlgirpDQTSEPkktladhLGMIAGGTGITPMLQLIRHITKDPSDR 176
Cdd:cd06189   72 vFEELKENGLVRIEGPLGDFFLR---------EDSDRP-------LILIAGGTGFAPIKSILEHLLAQGSKR 127
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 98-186 4.03e-05

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: 43.31  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  98 EGGKMTQYL-ENMKIGETIFFRGPRGRLFYhgpgnlgirPDQTSEPkktladhLGMIAGGTGITPMLQLIRHITKDPSDR 176
Cdd:cd06184   79 PGGLVSNYLhDNVKVGDVLEVSAPAGDFVL---------DEASDRP-------LVLISAGVGITPMLSMLEALAAEGPGR 142

                         90
                 ....*....|
gi 723586612 177 tRMSLIFANQ 186
Cdd:cd06184  143 -PVTFIHAAR 151
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 71-183 4.89e-05

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 43.32  E-value: 4.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  71 PVS-SDDDRGFVDLIIKIYfknvhpqypegGKMTQYLENMKIGETIFFRGPRGRLFyhgpgnlgirpDQTSEPKKTLAdh 149
Cdd:PRK00054  52 PISiSDIDKNEITILYRKV-----------GEGTKKLSKLKEGDELDIRGPLGNGF-----------DLEEIGGKVLL-- 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 723586612 150 lgmIAGGTGITPMLQLIRHITK-------DPSDRTRMSLIF 183
Cdd:PRK00054 108 ---VGGGIGVAPLYELAKELKKkgvevttVLGARTKDEVIF 145
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 62-183 5.78e-05

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: 43.06  E-value: 5.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  62 NELVVRAYTPVSSDDDRGFVDLIIKIyfKNVHPQYPEG--GKMTQYLENMKIGETIFFRGPRGrlFYHgpgnlgirpdqT 139
Cdd:cd06188   82 DEPVSRAYSLANYPAEEGELKLNVRI--ATPPPGNSDIppGIGSSYIFNLKPGDKVTASGPFG--EFF-----------I 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 723586612 140 SEPKKTLAdhlgMIAGGTGITPMLQLIRHITKDPSDRTRMSLIF 183
Cdd:cd06188  147 KDTDREMV----FIGGGAGMAPLRSHIFHLLKTLKSKRKISFWY 186
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 15-168 1.28e-04

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: 41.93  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  15 EAKYPLPLIE----KEKISHNTRRFRFGLP-SPDHVLGLP---VGNYVQLLAKidNELVVRAYTPVSSDDDrGFVDLIIK 86
Cdd:cd06201   43 PRTKALELVErkdyGAAVQAPTAILRFKPAkRKLSGKGLPsfeAGDLLGILPP--GSDVPRFYSLASSSSD-GFLEICVR 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  87 iyfknVHPqypeGGKMTQYLENMKIGETI--FFRGprgrlfyhgpgNLGIRPDQTSEPkktladhLGMIAGGTGITPMLQ 164
Cdd:cd06201  120 -----KHP----GGLCSGYLHGLKPGDTIkaFIRP-----------NPSFRPAKGAAP-------VILIGAGTGIAPLAG 172


                 ....
gi 723586612 165 LIRH 168
Cdd:cd06201  173 FIRA 176
PRK05802 PRK05802
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
70-168 1.89e-04

sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;


Pssm-ID: 235613 [Multi-domain]  Cd Length: 320  Bit Score: 41.50  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  70 TPVS---SDDDRGFVDLIIKIYfknvhpqypegGKMTQYLENMKIGETIFFRGPrgrlFYHGPgnLGIRPDQTSEPKKTL 146
Cdd:PRK05802 114 VPISimeADTEENIIKVAIEIR-----------GVKTKKIAKLNKGDEILLRGP----YWNGI--LGLKNIKSTKNGKSL 176

                         90       100
                 ....*....|....*....|..
gi 723586612 147 adhlgMIAGGTGITPMLQLIRH 168
Cdd:PRK05802 177 -----VIARGIGQAPGVPVIKK 193
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 22-168 2.15e-04

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: 41.10  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  22 LIEKEKISHNTRRFRFglpSPDHVLGLPVGNYVQLlakIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypEGGK 101
Cdd:cd06194    1 VVSLQRLSPDVLRVRL---EPDRPLPYLPGQYVNL---RRAGGLARSYSPTSLPDGDNELEFHIRRK---------PNGA 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 723586612 102 MTQYL-ENMKIGETIFFRGPRGRLFYhgpgnlgiRPDQtsepkktLADHLGMIAGGTGITPMLQLIRH 168
Cdd:cd06194   66 FSGWLgEEARPGHALRLQGPFGQAFY--------RPEY-------GEGPLLLVGAGTGLAPLWGIARA 118
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 69-191 5.57e-04

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


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 39.60  E-value: 5.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  69 YTPVSS-DDDRGFVDLIIKiyfknvhpqyPEGGKMT---QYLENMKIGE---TIFFRGPrgrlfYHGPGNLGIRpdqtse 141
Cdd:cd06186   47 FTIASSpEDEQDTLSLIIR----------AKKGFTTrllRKALKSPGGGvslKVLVEGP-----YGSSSEDLLS------ 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 723586612 142 pkktlADHLGMIAGGTGITPMLQLIRHITKDPSDRT---RMSLIFA--NQRRISW 191
Cdd:cd06186  106 -----YDNVLLVAGGSGITFVLPILRDLLRRSSKTSrtrRVKLVWVvrDREDLEW 155
siderophore_interacting cd06193
Siderophore interacting proteins share the domain structure of the ferredoxin reductase like ...
 34-127 1.05e-03

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


Pssm-ID: 99790 [Multi-domain]  Cd Length: 235  Bit Score: 39.17  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  34 RFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKiyfknVHpqyPEGGKMTQYLENMKIGE 113
Cdd:cd06193   32 HVKLLFPDPGQAPPVLPVLGRRRWPPEEPRPVMRTYTVRRFDPEAGELDIDFV-----LH---GDEGPASRWAASAQPGD 103

                         90
                 ....*....|....
gi 723586612 114 TIFFRGPRGRLFYH 127
Cdd:cd06193  104 TLGIAGPGGSFLPP 117
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 148-184 2.10e-03

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 38.67  E-value: 2.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 723586612 148 DHLGMIAGGTGITPMLQLIRHITKDPSDR----TRMSLIFA 184
Cdd:PLN02844 424 DSLLLVAGGIGITPFLSILKEIASQSSSRyrfpKRVQLIYV 464
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
148-199 6.63e-03

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 35.78  E-value: 6.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 723586612  148 DHLGMIAGGTGITPMLQLIRHITKDPS-DRTRM-SLIFA--NQRRISWSEKSLKKL 199
Cdd:pfam08030   2 ENVLLVAGGIGITPFISILKDLGNKSKkLKTKKiKFYWVvrDLSSLEWFKDVLNEL 57
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 7-162 7.25e-03

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 36.71  E-value: 7.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612   7 EPITLQDPEAKYPLPLIEKEKIShntrRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVrayTPVSSDDDRGFVDLIIK 86
Cdd:PRK08345   1 NPYALHDAKILEVYDLTEREKLF----LLRFEDPELAESFTFKPGQFVQVTIPGVGEVPI---SICSSPTRKGFFELCIR 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 723586612  87 iyfknvhpqypEGGKMTQYLENMKIGETIFFRGPRGRLFyhgpgnlgirPDQTSEPKKTLadhlgMIAGGTGITPM 162
Cdd:PRK08345  74 -----------RAGRVTTVIHRLKEGDIVGVRGPYGNGF----------PVDEMEGMDLL-----LIAGGLGMAPL 123
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 58-169 9.95e-03

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: 36.15  E-value: 9.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586612  58 AKIDNELVVRAYTPVSSDD-DRGF---VDLIIKIyfknvHPQY-PEGGKM-----TQYLENMKIGETIFFRGPRGRLFyh 127
Cdd:cd06208   56 AKNGKPHKLRLYSIASSRYgDDGDgktLSLCVKR-----LVYTdPETDETkkgvcSNYLCDLKPGDDVQITGPVGKTM-- 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 723586612 128 gpgnlgIRPDQTSepkktlADHLgMIAGGTGITPMLQLIRHI 169
Cdd:cd06208  129 ------LLPEDPN------ATLI-MIATGTGIAPFRSFLRRL 157
 
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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