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Conserved domains on  [gi|723586615|ref|NP_001289755|]
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NADH-cytochrome b5 reductase 2 isoform 1 [Homo sapiens]

Protein Classification

electron transport protein( domain architecture ID 1000686)

electron transport protein is involved in electron transfer reactions within the cell; similar to NADH-cytochrome b5 reductase which catalyzes the transfer of electrons from NADH to cytochrome b5, and to nitrate reductase which catalyzes NAD(P)H reaction of nitrate to nitrite

Gene Ontology:  GO:0050464|GO:0004128

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02252 super family cl33442
nitrate reductase [NADPH]
8-276 6.18e-124

nitrate reductase [NADPH]


The actual alignment was detected with superfamily member PLN02252:

Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 374.01  E-value: 6.18e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615   8 PITLQDPEAKYPLPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKI 87
Cdd:PLN02252 625 RPVALNPREKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFELVIKV 704
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  88 YFKNVHPQYPEGGKMTQYLENMKIGETIFFRGPRGRLFYHGPGNLGIRpdqtSEPKktLADHLGMIAGGTGITPMLQLIR 167
Cdd:PLN02252 705 YFKNVHPKFPNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFLVN----GKPK--FAKKLAMLAGGTGITPMYQVIQ 778
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 168 HITKDPSDRTRMSLIFANQTEEDILVRKELEEIARTHPDQFNLWYTLDRP-PIGWKYSSGFVTADMIKEHLPPPAKSTLI 246
Cdd:PLN02252 779 AILRDPEDKTEMSLVYANRTEDDILLREELDRWAAEHPDRLKVWYVVSQVkREGWKYSVGRVTEAMLREHLPEGGDETLA 858
                        250       260       270
                 ....*....|....*....|....*....|
gi 723586615 247 LVCGPPPLIQTAAHPNLEKLGYTQDMIFTY 276
Cdd:PLN02252 859 LMCGPPPMIEFACQPNLEKMGYDKDSILVF 888
 
Name Accession Description Interval E-value
PLN02252 PLN02252
nitrate reductase [NADPH]
8-276 6.18e-124

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 374.01  E-value: 6.18e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615   8 PITLQDPEAKYPLPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKI 87
Cdd:PLN02252 625 RPVALNPREKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFELVIKV 704
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  88 YFKNVHPQYPEGGKMTQYLENMKIGETIFFRGPRGRLFYHGPGNLGIRpdqtSEPKktLADHLGMIAGGTGITPMLQLIR 167
Cdd:PLN02252 705 YFKNVHPKFPNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFLVN----GKPK--FAKKLAMLAGGTGITPMYQVIQ 778
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 168 HITKDPSDRTRMSLIFANQTEEDILVRKELEEIARTHPDQFNLWYTLDRP-PIGWKYSSGFVTADMIKEHLPPPAKSTLI 246
Cdd:PLN02252 779 AILRDPEDKTEMSLVYANRTEDDILLREELDRWAAEHPDRLKVWYVVSQVkREGWKYSVGRVTEAMLREHLPEGGDETLA 858
                        250       260       270
                 ....*....|....*....|....*....|
gi 723586615 247 LVCGPPPLIQTAAHPNLEKLGYTQDMIFTY 276
Cdd:PLN02252 859 LMCGPPPMIEFACQPNLEKMGYDKDSILVF 888
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
20-276 5.05e-123

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


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 350.33  E-value: 5.05e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  20 LPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKIYFknvhpqypeG 99
Cdd:cd06183    1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYP---------G 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 100 GKMTQYLENMKIGETIFFRGPRGRLFYHGPGNlgirpdqtsepkktlADHLGMIAGGTGITPMLQLIRHITKDPSDRTRM 179
Cdd:cd06183   72 GKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGK---------------VKHIGMIAGGTGITPMLQLIRAILKDPEDKTKI 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 180 SLIFANQTEEDILVRKELEEIARTHPDQFNLWYTLDRPPIGWKYSSGFVTADMIKEHLPP-PAKSTLILVCGPPPLIQTA 258
Cdd:cd06183  137 SLLYANRTEEDILLREELDELAKKHPDRFKVHYVLSRPPEGWKGGVGFITKEMIKEHLPPpPSEDTLVLVCGPPPMIEGA 216
                        250
                 ....*....|....*...
gi 723586615 259 AHPNLEKLGYTQDMIFTY 276
Cdd:cd06183  217 VKGLLKELGYKKDNVFKF 234
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
19-126 3.25e-49

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 157.74  E-value: 3.25e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615   19 PLPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypE 98
Cdd:pfam00970   1 PLTLVEKELVSHDTRIFRFALPHPDQVLGLPVGQHLFLRLPIDGELVIRSYTPISSDDDKGYLELLVKVY---------P 71
                          90       100
                  ....*....|....*....|....*...
gi 723586615   99 GGKMTQYLENMKIGETIFFRGPRGRLFY 126
Cdd:pfam00970  72 GGKMSQYLDELKIGDTIDFKGPLGRFEY 99
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
18-275 1.08e-40

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 140.31  E-value: 1.08e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  18 YPLPLIEKEKISHNTRRFRF----GLPSPDHvlgLPvGNYVQLLAKIDNELVVRAYTPVSSDDDRGfvdliIKIYFKNVh 93
Cdd:COG1018    4 RPLRVVEVRRETPDVVSFTLeppdGAPLPRF---RP-GQFVTLRLPIDGKPLRRAYSLSSAPGDGR-----LEITVKRV- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  94 pqypEGGKMTQYL-ENMKIGETIFFRGPRGRLFYHGPGnlgirpdqtsepkktlADHLGMIAGGTGITPMLQLIRHITKD 172
Cdd:COG1018   74 ----PGGGGSNWLhDHLKVGDTLEVSGPRGDFVLDPEP----------------ARPLLLIAGGIGITPFLSMLRTLLAR 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 173 PSDRtRMSLIFANQTEEDILVRKELEEIARTHPdQFNLWYTLDRPPIGWkysSGFVTADMIKEHLPPPAkSTLILVCGPP 252
Cdd:COG1018  134 GPFR-PVTLVYGARSPADLAFRDELEALAARHP-RLRLHPVLSREPAGL---QGRLDAELLAALLPDPA-DAHVYLCGPP 207
                        250       260
                 ....*....|....*....|...
gi 723586615 253 PLIQTAAHpNLEKLGYTQDMIFT 275
Cdd:COG1018  208 PMMEAVRA-ALAELGVPEERIHF 229
 
Name Accession Description Interval E-value
PLN02252 PLN02252
nitrate reductase [NADPH]
8-276 6.18e-124

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 374.01  E-value: 6.18e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615   8 PITLQDPEAKYPLPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKI 87
Cdd:PLN02252 625 RPVALNPREKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFELVIKV 704
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  88 YFKNVHPQYPEGGKMTQYLENMKIGETIFFRGPRGRLFYHGPGNLGIRpdqtSEPKktLADHLGMIAGGTGITPMLQLIR 167
Cdd:PLN02252 705 YFKNVHPKFPNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFLVN----GKPK--FAKKLAMLAGGTGITPMYQVIQ 778
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 168 HITKDPSDRTRMSLIFANQTEEDILVRKELEEIARTHPDQFNLWYTLDRP-PIGWKYSSGFVTADMIKEHLPPPAKSTLI 246
Cdd:PLN02252 779 AILRDPEDKTEMSLVYANRTEDDILLREELDRWAAEHPDRLKVWYVVSQVkREGWKYSVGRVTEAMLREHLPEGGDETLA 858
                        250       260       270
                 ....*....|....*....|....*....|
gi 723586615 247 LVCGPPPLIQTAAHPNLEKLGYTQDMIFTY 276
Cdd:PLN02252 859 LMCGPPPMIEFACQPNLEKMGYDKDSILVF 888
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
20-276 5.05e-123

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


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 350.33  E-value: 5.05e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  20 LPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKIYFknvhpqypeG 99
Cdd:cd06183    1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYP---------G 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 100 GKMTQYLENMKIGETIFFRGPRGRLFYHGPGNlgirpdqtsepkktlADHLGMIAGGTGITPMLQLIRHITKDPSDRTRM 179
Cdd:cd06183   72 GKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGK---------------VKHIGMIAGGTGITPMLQLIRAILKDPEDKTKI 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 180 SLIFANQTEEDILVRKELEEIARTHPDQFNLWYTLDRPPIGWKYSSGFVTADMIKEHLPP-PAKSTLILVCGPPPLIQTA 258
Cdd:cd06183  137 SLLYANRTEEDILLREELDELAKKHPDRFKVHYVLSRPPEGWKGGVGFITKEMIKEHLPPpPSEDTLVLVCGPPPMIEGA 216
                        250
                 ....*....|....*...
gi 723586615 259 AHPNLEKLGYTQDMIFTY 276
Cdd:cd06183  217 VKGLLKELGYKKDNVFKF 234
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
5-276 8.56e-113

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 326.79  E-value: 8.56e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615   5 RREPITLqDPEAKYPLPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDN----ELVVRAYTPVSSDDDRGF 80
Cdd:PTZ00319  22 RSPPVAL-DPDMFQHFKLIKKTEVTHDTFIFRFALHSPTQRLGLPIGQHIVFRCDCTTpgkpETVQHSYTPISSDDEKGY 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  81 VDLIIKIYFKNVHPQYPEGGKMTQYLENMKIGETIFFRGPRGRLFYHGPGNLGIRPDQtSEPKKTLADHLGMIAGGTGIT 160
Cdd:PTZ00319 101 VDFLIKVYFKGVHPSFPNGGRLSQHLYHMKLGDKIEMRGPVGKFEYLGNGTYTVHKGK-GGLKTMHVDAFAMIAGGTGIT 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 161 PMLQLIRHITKDPSDRTRMSLIFANQTEEDILVRKELEEIARThpDQFNLWYTLDRP-PIGWKYSSGFVTADMIKEHLPP 239
Cdd:PTZ00319 180 PMLQIIHAIKKNKEDRTKVFLVYANQTEDDILLRKELDEAAKD--PRFHVWYTLDREaTPEWKYGTGYVDEEMLRAHLPV 257
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 723586615 240 PA------KSTLILVCGPPPLIQTAAHPNLEKLGYTQDMIFTY 276
Cdd:PTZ00319 258 PDpqnsgiKKVMALMCGPPPMLQMAVKPNLEKIGYTADNMFTF 300
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
19-126 3.25e-49

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 157.74  E-value: 3.25e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615   19 PLPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypE 98
Cdd:pfam00970   1 PLTLVEKELVSHDTRIFRFALPHPDQVLGLPVGQHLFLRLPIDGELVIRSYTPISSDDDKGYLELLVKVY---------P 71
                          90       100
                  ....*....|....*....|....*...
gi 723586615   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 ...
23-275 1.85e-45

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: 152.60  E-value: 1.85e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  23 IEKEKISHNTRRFRFGLPSPdhvLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypEGGKM 102
Cdd:cd00322    1 VATEDVTDDVRLFRLQLPNG---FSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEGELELTVKIV---------PGGPF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 103 TQYLENMKIGETIFFRGPRGRLFYHGPGNlgirpdqtsepkktlaDHLGMIAGGTGITPMLQLIRHITKDPSDRTrMSLI 182
Cdd:cd00322   69 SAWLHDLKPGDEVEVSGPGGDFFLPLEES----------------GPVVLIAGGIGITPFRSMLRHLAADKPGGE-ITLL 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 183 FANQTEEDILVRKELEEIARTHPDQFnLWYTLDRPPIGWKYSSGFVTADMIKEHLPPPAKSTLILVCGPPPLIQTAAHpN 262
Cdd:cd00322  132 YGARTPADLLFLDELEELAKEGPNFR-LVLALSRESEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVRE-A 209
                        250
                 ....*....|...
gi 723586615 263 LEKLGYTQDMIFT 275
Cdd:cd00322  210 LVSLGVPEERIHT 222
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
152-260 3.30e-43

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: 142.78  E-value: 3.30e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  152 MIAGGTGITPMLQLIRHITKDPSDRTRMSLIFANQTEEDILVRKELEEIARTHPDQFNLWYTLDRPPIGWKYSSGFVTAD 231
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDPKDPTQVVLVFGNRNEDDILYREELDELAEKHPGRLTVVYVVSRPEAGWTGGKGRVQDA 80
                          90       100
                  ....*....|....*....|....*....
gi 723586615  232 MIKEHLPPPAKSTLILVCGPPPLIQTAAH 260
Cdd:pfam00175  81 LLEDHLSLPDEETHVYVCGPPGMIKAVRK 109
PTZ00274 PTZ00274
cytochrome b5 reductase; Provisional
3-259 3.27e-42

cytochrome b5 reductase; Provisional


Pssm-ID: 140300  Cd Length: 325  Bit Score: 146.99  E-value: 3.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615   3 SRRREPITLQDPeakypLPliekekISHNTRRFRFGLPSPDHvLGLPVGNYVQLLAKID---NELVVRAYTPVSSDDDRG 79
Cdd:PTZ00274  49 SQRYEPYQLGEV-----IP------ITHDTALFRFLLHSEEE-FNLKPCSTLQACYKYGvqpMDQCQRFYTPVTANHTKG 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  80 FVDLIIKiyfknvhpqYPEGGKMTQYLENMKIGETIFFRGPRGRLFYhgpgnlgiRPDQTSepkktladHLGMIAGGTGI 159
Cdd:PTZ00274 117 YFDIIVK---------RKKDGLMTNHLFGMHVGDKLLFRSVTFKIQY--------RPNRWK--------HVGMIAGGTGF 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 160 TPMLQLIRHITKDP-----SDRTRMSLIFANQTEEDILVRKELEEIARTHPDQFNLWYTLDRP--PIGWKYSSGFVTADM 232
Cdd:PTZ00274 172 TPMLQIIRHSLTEPwdsgeVDRTKLSFLFCNRTERHILLKGLFDDLARRYSNRFKVYYTIDQAvePDKWNHFLGYVTKEM 251
                        250       260
                 ....*....|....*....|....*...
gi 723586615 233 IKEHLPPP-AKSTLILVCGPPPLIQTAA 259
Cdd:PTZ00274 252 VRRTMPAPeEKKKIIMLCGPDQLLNHVA 279
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
18-275 1.08e-40

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 140.31  E-value: 1.08e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  18 YPLPLIEKEKISHNTRRFRF----GLPSPDHvlgLPvGNYVQLLAKIDNELVVRAYTPVSSDDDRGfvdliIKIYFKNVh 93
Cdd:COG1018    4 RPLRVVEVRRETPDVVSFTLeppdGAPLPRF---RP-GQFVTLRLPIDGKPLRRAYSLSSAPGDGR-----LEITVKRV- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  94 pqypEGGKMTQYL-ENMKIGETIFFRGPRGRLFYHGPGnlgirpdqtsepkktlADHLGMIAGGTGITPMLQLIRHITKD 172
Cdd:COG1018   74 ----PGGGGSNWLhDHLKVGDTLEVSGPRGDFVLDPEP----------------ARPLLLIAGGIGITPFLSMLRTLLAR 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 173 PSDRtRMSLIFANQTEEDILVRKELEEIARTHPdQFNLWYTLDRPPIGWkysSGFVTADMIKEHLPPPAkSTLILVCGPP 252
Cdd:COG1018  134 GPFR-PVTLVYGARSPADLAFRDELEALAARHP-RLRLHPVLSREPAGL---QGRLDAELLAALLPDPA-DAHVYLCGPP 207
                        250       260
                 ....*....|....*....|...
gi 723586615 253 PLIQTAAHpNLEKLGYTQDMIFT 275
Cdd:COG1018  208 PMMEAVRA-ALAELGVPEERIHF 229
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
30-275 5.81e-38

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


Pssm-ID: 99813 [Multi-domain]  Cd Length: 235  Bit Score: 133.55  E-value: 5.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  30 HNTRRFRFGLP---SPDHvlgLPvGNYVQL-LAKIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypEGGKMTQY 105
Cdd:cd06217   14 PTVKTFRLAVPdgvPPPF---LA-GQHVDLrLTAIDGYTAQRSYSIASSPTQRGRVELTVKRV---------PGGEVSPY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 106 L-ENMKIGETIFFRGPRGRlFYHGPGnlgirpdqtsepkktLADHLGMIAGGTGITPMLQLIRHITkDPSDRTRMSLIFA 184
Cdd:cd06217   81 LhDEVKVGDLLEVRGPIGT-FTWNPL---------------HGDPVVLLAGGSGIVPLMSMIRYRR-DLGWPVPFRLLYS 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 185 NQTEEDILVRKELEEIARTHPDqFNLWYTLDRP-PIGWKYSSGFVTADMIkEHLPPPAKSTLILVCGPPPLIQTAAhPNL 263
Cdd:cd06217  144 ARTAEDVIFRDELEQLARRHPN-LHVTEALTRAaPADWLGPAGRITADLI-AELVPPLAGRRVYVCGPPAFVEAAT-RLL 220
                        250
                 ....*....|..
gi 723586615 264 EKLGYTQDMIFT 275
Cdd:cd06217  221 LELGVPRDRIRT 232
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
23-274 9.82e-32

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 117.66  E-value: 9.82e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  23 IEKEKISHNTRRFRFGLPsPDHVLGLPvGNYVQLlaKIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypegGKM 102
Cdd:COG0543    3 VSVERLAPDVYLLRLEAP-LIALKFKP-GQFVML--RVPGDGLRRPFSIASAPREDGTIELHIRVV-----------GKG 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 103 TQYLENMKIGETIFFRGPRGRLFyhgpgnlgirpDQTSEPKKTLadhlgMIAGGTGITPMLQLIRHITKDPSdrtRMSLI 182
Cdd:COG0543   68 TRALAELKPGDELDVRGPLGNGF-----------PLEDSGRPVL-----LVAGGTGLAPLRSLAEALLARGR---RVTLY 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 183 FANQTEEDILVRKELEEIArthpdQFNLWYTLDRppiGWKYSSGFVTaDMIKEHLpPPAKSTLILVCGPPPLIQtAAHPN 262
Cdd:COG0543  129 LGARTPEDLYLLDELEALA-----DFRVVVTTDD---GWYGRKGFVT-DALKELL-AEDSGDDVYACGPPPMMK-AVAEL 197
                        250
                 ....*....|..
gi 723586615 263 LEKLGYTQDMIF 274
Cdd:COG0543  198 LLERGVPPERIY 209
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
71-275 3.67e-31

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: 116.17  E-value: 3.67e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  71 PVSSDDDRGFVDLIIKiyfkNVhpqypegGKMTQYLENMKIGETIFFRGPRGRLFyhgpgnlgirpdqtsePKKTLADH- 149
Cdd:cd06221   48 ISSDPTRRGPLELTIR----RV-------GRVTEALHELKPGDTVGLRGPFGNGF----------------PVEEMKGKd 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 150 LGMIAGGTGITPMLQLIRHITKDPSDRTRMSLIFANQTEEDILVRKELEEIARtHPDqFNLWYTLDRPPIGWKYSSGFVT 229
Cdd:cd06221  101 LLLVAGGLGLAPLRSLINYILDNREDYGKVTLLYGARTPEDLLFKEELKEWAK-RSD-VEVILTVDRAEEGWTGNVGLVT 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 723586615 230 aDMIKEHLPPPAKSTLIlVCGPPPLIQTAAhPNLEKLGYTQDMIFT 275
Cdd:cd06221  179 -DLLPELTLDPDNTVAI-VCGPPIMMRFVA-KELLKLGVPEEQIWV 221
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
20-275 8.14e-30

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: 111.91  E-value: 8.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  20 LPLIEKEKISHNTRRFRFGLPSPDHVLGLPvGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKiyfkNVhpqypEG 99
Cdd:cd06215    1 LRCVKIIQETPDVKTFRFAAPDGSLFAYKP-GQFLTLELEIDGETVYRAYTLSSSPSRPDSLSITVK----RV-----PG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 100 GKMTQYL-ENMKIGETIFFRGPRGRlFYhgpgnlgirpdqtsePKKTLADHLGMIAGGTGITPMLQLIRHITKDPSDRtR 178
Cdd:cd06215   71 GLVSNWLhDNLKVGDELWASGPAGE-FT---------------LIDHPADKLLLLSAGSGITPMMSMARWLLDTRPDA-D 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 179 MSLIFANQTEEDILVRKELEEIARTHPdQFNLWYTLDRPPIG-WKYSSGFVTADMIkEHLPPPAKSTLILVCGPPPLIQt 257
Cdd:cd06215  134 IVFIHSARSPADIIFADELEELARRHP-NFRLHLILEQPAPGaWGGYRGRLNAELL-ALLVPDLKERTVFVCGPAGFMK- 210
                        250
                 ....*....|....*...
gi 723586615 258 AAHPNLEKLGYTQDMIFT 275
Cdd:cd06215  211 AVKSLLAELGFPMSRFHQ 228
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
32-275 1.95e-29

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 117.19  E-value: 1.95e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615   32 TRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKiyfknvhpqyPEGGKMTQYLENMKI 111
Cdd:PTZ00306  932 SRVLRFNLPGALQRSGLTLGQFIAIRGDWDGQQLIGYYSPITLPDDLGVISILAR----------GDKGTLKEWISALRP 1001
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  112 GETIFFRGPRGRLFYHGPGnlgirpDQTSEPKKTLADHLGMIAGGTGITPMLQLIRHITKDPSDRTRMS--LIFANQTEE 189
Cdd:PTZ00306 1002 GDSVEMKACGGLRIERRPA------DKQFVFRGHVIRKLALIAGGTGVAPMLQIIRAALKKPYVDSIESirLIYAAEDVS 1075
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  190 DILVRKELEEIARTHPDQFNLWYTLDRPPIGWKYSSGFVTADMIKEHLPPPAKSTLILVCGpPPLIQTAAHPNLEKLGYT 269
Cdd:PTZ00306 1076 ELTYRELLESYRKENPGKFKCHFVLNNPPEGWTDGVGFVDRALLQSALQPPSKDLLVAICG-PPVMQRAVKADLLALGYN 1154

                  ....*.
gi 723586615  270 QDMIFT 275
Cdd:PTZ00306 1155 MELVRT 1160
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
18-267 1.02e-28

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: 109.56  E-value: 1.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  18 YPLPLIEKEKISHNTRRFRFGLPSP-DHVLGLPVGNYVQLLAKIDNELVVRAY---TPVSSDDdrgfvdliIKIYFKNVh 93
Cdd:cd06214    2 HPLTVAEVVRETADAVSITFDVPEElRDAFRYRPGQFLTLRVPIDGEEVRRSYsicSSPGDDE--------LRITVKRV- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  94 pqypEGGKMTQYL-ENMKIGETIFFRGPRGRLFYhgpgnlgirpdqtsePKKTLADHLGMIAGGTGITPMLQLIRHITKD 172
Cdd:cd06214   73 ----PGGRFSNWAnDELKAGDTLEVMPPAGRFTL---------------PPLPGARHYVLFAAGSGITPVLSILKTALAR 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 173 PSDRtRMSLIFANQTEEDILVRKELEEIARTHPDQFNLWYTLDRPPIGWKYSSGFVTADMIKE---HLPPPAKSTLILVC 249
Cdd:cd06214  134 EPAS-RVTLVYGNRTEASVIFREELADLKARYPDRLTVIHVLSREQGDPDLLRGRLDAAKLNAllkNLLDATEFDEAFLC 212
                        250
                 ....*....|....*...
gi 723586615 250 GPPPLIQTAAHpNLEKLG 267
Cdd:cd06214  213 GPEPMMDAVEA-ALLELG 229
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
51-258 2.29e-25

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal 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: 100.76  E-value: 2.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  51 GNYVQLLAKIDNELVVRAYTPVSSDDDR-GFVDLIIKIyfknvHPqypeGGKMTQYL-ENMKIGETIFFRGPRGRlFYhg 128
Cdd:cd06216   49 GQHVRLGVEIDGVRHWRSYSLSSSPTQEdGTITLTVKA-----QP----DGLVSNWLvNHLAPGDVVELSQPQGD-FV-- 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 129 pgnlgiRPDQTSEPkktladhLGMIAGGTGITPMLQLIRHITKDPsDRTRMSLIFANQTEEDILVRKELEEIARTHPD-Q 207
Cdd:cd06216  117 ------LPDPLPPR-------LLLIAAGSGITPVMSMLRTLLARG-PTADVVLLYYARTREDVIFADELRALAAQHPNlR 182
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 723586615 208 FNLWYTLDRPpigwkysSGFVTADMIKEHlPPPAKSTLILVCGPPPLIQTA 258
Cdd:cd06216  183 LHLLYTREEL-------DGRLSAAHLDAV-VPDLADRQVYACGPPGFLDAA 225
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
22-275 8.55e-24

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: 96.24  E-value: 8.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  22 LIEKEKISHNTRRFRFGLPSPDHVLGLPvGNYVQLlaKIDNELVVRAYTPVSSDDDRGFVDLIIKiyfknvhpqYPEGGK 101
Cdd:cd06211   11 VVEIEDLTPTIKGVRLKLDEPEEIEFQA-GQYVNL--QAPGYEGTRAFSIASSPSDAGEIELHIR---------LVPGGI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 102 MTQYL-ENMKIGETIFFRGPRGRLFYHgpgnlgirpDQTSEPkktladhLGMIAGGTGITPMLQLIRHITKDPSDRTrMS 180
Cdd:cd06211   79 ATTYVhKQLKEGDELEISGPYGDFFVR---------DSDQRP-------IIFIAGGSGLSSPRSMILDLLERGDTRK-IT 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 181 LIFANQTEEDILVRKELEEIARTHPDqFNLWYTLDRPP--IGWKYSSGFVTaDMIKEHLPPPAKSTLILVCGPPPLIQtA 258
Cdd:cd06211  142 LFFGARTRAELYYLDEFEALEKDHPN-FKYVPALSREPpeSNWKGFTGFVH-DAAKKHFKNDFRGHKAYLCGPPPMID-A 218
                        250
                 ....*....|....*..
gi 723586615 259 AHPNLEKLGYTQDMIFT 275
Cdd:cd06211  219 CIKTLMQGRLFERDIYY 235
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
69-267 3.13e-23

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 98.04  E-value: 3.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  69 YTPVSSDDDRGFVDLIIKiyfknvhpqypEGGKMTQYLENMKIGETIFFRGPRGRLFYHGpgnlgiRPDqtsepkktlAD 148
Cdd:COG4097  266 FSISSAPGGDGRLRFTIK-----------ALGDFTRRLGRLKPGTRVYVEGPYGRFTFDR------RDT---------AP 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 149 HLGMIAGGTGITPMLQLIRHITKDPSDRTRMSLIFANQTEEDILVRKELEEIARTHPDqFNLWYTLDRPpigwkysSGFV 228
Cdd:COG4097  320 RQVWIAGGIGITPFLALLRALAARPGDQRPVDLFYCVRDEEDAPFLEELRALAARLAG-LRLHLVVSDE-------DGRL 391
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 723586615 229 TADMIKEHLPPPAKSTlILVCGPPPLIQTAAHpNLEKLG 267
Cdd:COG4097  392 TAERLRRLVPDLAEAD-VFFCGPPGMMDALRR-DLRALG 428
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
22-256 3.68e-23

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: 94.63  E-value: 3.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  22 LIEKEKISHNTRRFRFGLPSPDHVLglPvGNYVQLlaKIDNELVVRAYTPVSSDDDRGFVDLIIKiyfknvhpQYPeGGK 101
Cdd:cd06190    1 LVDVRELTHDVAEFRFALDGPADFL--P-GQYALL--ALPGVEGARAYSMANLANASGEWEFIIK--------RKP-GGA 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 102 MTQYL-ENMKIGETIFFRGPRGRLFyhgpgnlgIRPDqtsEPKKTLadhlgMIAGGTGITPMLQLIRHITKDPSDRTR-M 179
Cdd:cd06190   67 ASNALfDNLEPGDELELDGPYGLAY--------LRPD---EDRDIV-----CIAGGSGLAPMLSILRGAARSPYLSDRpV 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 180 SLIFANQTEEDILVrkeLEEIARTHPDQFNLWYTLD------RPPIGWKYSSGFVTaDMIKEHLPPPAKSTLILVCGPPP 253
Cdd:cd06190  131 DLFYGGRTPSDLCA---LDELSALVALGARLRVTPAvsdagsGSAAGWDGPTGFVH-EVVEATLGDRLAEFEFYFAGPPP 206

                 ...
gi 723586615 254 LIQ 256
Cdd:cd06190  207 MVD 209
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
26-258 4.92e-23

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: 94.33  E-value: 4.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  26 EKISHNTRRFRFGlPSPDHVLGLPV----GNYVQLlaKIDNELVVRAYTPVSSDDDRGFVDLIIKiyfknVHPqypeGGK 101
Cdd:cd06210   10 DRVSSNVVRLRLQ-PDDAEGAGIAAefvpGQFVEI--EIPGTDTRRSYSLANTPNWDGRLEFLIR-----LLP----GGA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 102 MTQYLEN-MKIGETIFFRGPRGR--LFYHGPgnlgiRPdqtsepkktladhLGMIAGGTGITPMLQLIRHITK--DPSDR 176
Cdd:cd06210   78 FSTYLETrAKVGQRLNLRGPLGAfgLRENGL-----RP-------------RWFVAGGTGLAPLLSMLRRMAEwgEPQEA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 177 TrmsLIFANQTEEDILVRKELEEIARTHPdQFNLWYTLDRPPIGWKYSSGFVtADMIKEHLPPPAKSTLILVCGPPPLIQ 256
Cdd:cd06210  140 R---LFFGVNTEAELFYLDELKRLADSLP-NLTVRICVWRPGGEWEGYRGTV-VDALREDLASSDAKPDIYLCGPPGMVD 214

                 ..
gi 723586615 257 TA 258
Cdd:cd06210  215 AA 216
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
26-274 1.32e-22

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: 93.04  E-value: 1.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  26 EKISHNTRRFRFGLPSPDHVLGLPvGNYVQLlaKIDNELVVRAYTPVSSDDDRGFVDLIikiyfKNVhpqypEGGKMTQY 105
Cdd:cd06209   10 ERLSDSTIGLTLELDEAGALAFLP-GQYVNL--QVPGTDETRSYSFSSAPGDPRLEFLI-----RLL-----PGGAMSSY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 106 LENM-KIGETIFFRGPRGRlFYHGPGNlgiRPdqtsepkktladHLgMIAGGTGITPMLQLIRHITKDPSDRtRMSLIFA 184
Cdd:cd06209   77 LRDRaQPGDRLTLTGPLGS-FYLREVK---RP------------LL-MLAGGTGLAPFLSMLDVLAEDGSAH-PVHLVYG 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 185 NQTEEDILVRKELEEIARTHPDqFNLWYTLDRPPiGWKYSSGFVTADMIKEHLPPPAksTLILVCGPPPLIQtAAHPNLE 264
Cdd:cd06209  139 VTRDADLVELDRLEALAERLPG-FSFRTVVADPD-SWHPRKGYVTDHLEAEDLNDGD--VDVYLCGPPPMVD-AVRSWLD 213
                        250
                 ....*....|
gi 723586615 265 KLGYTQDMIF 274
Cdd:cd06209  214 EQGIEPANFY 223
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
23-275 4.46e-22

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: 91.50  E-value: 4.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  23 IEKEKISHNTRRFRFGLPSPDHVLGlpvGNYVQLLAkIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypEGGKM 102
Cdd:cd06187    2 VSVERLTHDIAVVRLQLDQPLPFWA---GQYVNVTV-PGRPRTWRAYSPANPPNEDGEIEFHVRAV---------PGGRV 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 103 TQYLEN-MKIGETIFFRGPRGRLFYHGPGNlgiRPdqtsepkktladhLGMIAGGTGITPMLQLIRHITKDPSDRtRMSL 181
Cdd:cd06187   69 SNALHDeLKVGDRVRLSGPYGTFYLRRDHD---RP-------------VLCIAGGTGLAPLRAIVEDALRRGEPR-PVHL 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 182 IFANQTEEDILVRKELEEIARTHPdqfNLWYT--LDRPPIGWKYSSGFVTaDMIKEHLPPPAKSTlILVCGPPPLIQtAA 259
Cdd:cd06187  132 FFGARTERDLYDLEGLLALAARHP---WLRVVpvVSHEEGAWTGRRGLVT-DVVGRDGPDWADHD-IYICGPPAMVD-AT 205
                        250
                 ....*....|....*.
gi 723586615 260 HPNLEKLGYTQDMIFT 275
Cdd:cd06187  206 VDALLARGAPPERIHF 221
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
26-274 1.41e-21

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


Pssm-ID: 99808 [Multi-domain]  Cd Length: 232  Bit Score: 90.08  E-value: 1.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  26 EKISHNTRRFRFGLPSPDHVLGLPvGNYVQLLakIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypEGGKMTQY 105
Cdd:cd06212    9 EALTHDIRRLRLRLEEPEPIKFFA-GQYVDIT--VPGTEETRSFSMANTPADPGRLEFIIKKY---------PGGLFSSF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 106 LEN-MKIGETIFFRGPRGRLFyhgpgnlgIRPDQTSEpkktladhLGMIAGGTGITPMLQLIRHITKDPSDRtRMSLIFA 184
Cdd:cd06212   77 LDDgLAVGDPVTVTGPYGTCT--------LRESRDRP--------IVLIGGGSGMAPLLSLLRDMAASGSDR-PVRFFYG 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 185 NQTEEDILVRKELEEIARTHPDqFNLWYTLDRPP--IGWKYSSGFVTaDMIKEHLPPPAkSTLILVCGPPPLIQtAAHPN 262
Cdd:cd06212  140 ARTARDLFYLEEIAALGEKIPD-FTFIPALSESPddEGWSGETGLVT-EVVQRNEATLA-GCDVYLCGPPPMID-AALPV 215
                        250
                 ....*....|..
gi 723586615 263 LEKLGYTQDMIF 274
Cdd:cd06212  216 LEMSGVPPDQIF 227
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
18-275 1.99e-21

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


Pssm-ID: 99793 [Multi-domain]  Cd Length: 218  Bit Score: 89.61  E-value: 1.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  18 YPLPLIEKEKISHNTRRFRFGLPspdHVLGLPVGNYVQL-LAKIDNELVVRAYTPVSSDDDRgFVDLIIKIYfknvhpqy 96
Cdd:cd06196    1 HTVTLLSIEPVTHDVKRLRFDKP---EGYDFTPGQATEVaIDKPGWRDEKRPFTFTSLPEDD-VLEFVIKSY-------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  97 PEGGKMTQYLENMKIGETIFFRGPRGRLFYHGPGNLgirpdqtsepkktladhlgmIAGGTGITPMLQLIRHITKDP--S 174
Cdd:cd06196   69 PDHDGVTEQLGRLQPGDTLLIEDPWGAIEYKGPGVF--------------------IAGGAGITPFIAILRDLAAKGklE 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 175 DRTrmsLIFANQTEEDILVRKELEEIARthpDQFNLWYTLDRPPigwKYSSGFVTADMIKEHLPPPAKStlILVCGPPPL 254
Cdd:cd06196  129 GNT---LIFANKTEKDIILKDELEKMLG---LKFINVVTDEKDP---GYAHGRIDKAFLKQHVTDFNQH--FYVCGPPPM 197
                        250       260
                 ....*....|....*....|.
gi 723586615 255 IQtAAHPNLEKLGYTQDMIFT 275
Cdd:cd06196  198 EE-AINGALKELGVPEDSIVF 217
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
22-275 1.79e-20

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: 89.92  E-value: 1.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  22 LIEKEKISHNTRRFRFGLPSPDHVLGLPvGNYVQL---------------------LAKIDNELVVRAYTPVSSDDDRGF 80
Cdd:COG2871  136 VVSNENVTTFIKELVLELPEGEEIDFKA-GQYIQIevppyevdfkdfdipeeekfgLFDKNDEEVTRAYSMANYPAEKGI 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  81 VDLIIKIyfKNVHPQYPeGGKMTQYLENMKIGETIFFRGPRGRLFYhgpgnlgirpdqtsepKKTLADHLgMIAGGTGIT 160
Cdd:COG2871  215 IELNIRI--ATPPMDVP-PGIGSSYIFSLKPGDKVTISGPYGEFFL----------------RDSDREMV-FIGGGAGMA 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 161 PMLQLIRH-ITKDPSDRtRMSLIFANQTEEDILVRKELEEIARTHPDqFNLWYTLDRPPIG--WKYSSGFVTADMIKEHL 237
Cdd:COG2871  275 PLRSHIFDlLERGKTDR-KITFWYGARSLRELFYLEEFRELEKEHPN-FKFHPALSEPLPEdnWDGETGFIHEVLYENYL 352
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 723586615 238 --PPPAKSTLILVCGPPPLIQtAAHPNLEKLGYTQDMIFT 275
Cdd:COG2871  353 kdHPAPEDCEAYLCGPPPMID-AVIKMLDDLGVEEENIYF 391
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
20-275 2.69e-19

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: 84.12  E-value: 2.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  20 LPLIEKEKISHNTRRFRFGLPSPDHVLGLPvGNYVQLLAKIDNELVVRAYTPVSSD-DDRgfvdliIKIYFKNVhpqypE 98
Cdd:cd06191    1 LRVAEVRSETPDAVTIVFAVPGPLQYGFRP-GQHVTLKLDFDGEELRRCYSLCSSPaPDE------ISITVKRV-----P 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  99 GGKMTQYL-ENMKIGETIFFRGPRGRLFYhgpgnlgirpdQTSEPKKTLAdhlgmIAGGTGITPMLQLIRhITKDPSDRT 177
Cdd:cd06191   69 GGRVSNYLrEHIQPGMTVEVMGPQGHFVY-----------QPQPPGRYLL-----VAAGSGITPLMAMIR-ATLQTAPES 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 178 RMSLIFANQTEEDILVRKELEEIARTHPD-QFNLWYTLDRPPIGWKYSSGFVTADMIKEHLPPPAKSTlILVCGPPPLIQ 256
Cdd:cd06191  132 DFTLIHSARTPADMIFAQELRELADKPQRlRLLCIFTRETLDSDLLHGRIDGEQSLGAALIPDRLERE-AFICGPAGMMD 210
                        250
                 ....*....|....*....
gi 723586615 257 tAAHPNLEKLGYTQDMIFT 275
Cdd:cd06191  211 -AVETALKELGMPPERIHT 228
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
98-274 1.03e-16

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


Pssm-ID: 99781  Cd Length: 247  Bit Score: 77.21  E-value: 1.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  98 EGGKMTQYL-ENMKIGETIFFRGPRGRLFYhgpgnlgirPDQTSEPkktladhLGMIAGGTGITPMLQLIRHITKDPSDR 176
Cdd:cd06184   79 PGGLVSNYLhDNVKVGDVLEVSAPAGDFVL---------DEASDRP-------LVLISAGVGITPMLSMLEALAAEGPGR 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 177 tRMSLIFANQTEEDILVRKELEEIARTHPD-QFNLWYT--LDRPPIGWKYSSGFVTADMIKEHLPPPakSTLILVCGPPP 253
Cdd:cd06184  143 -PVTFIHAARNSAVHAFRDELEELAARLPNlKLHVFYSepEAGDREEDYDHAGRIDLALLRELLLPA--DADFYLCGPVP 219
                        170       180
                 ....*....|....*....|.
gi 723586615 254 LIQtAAHPNLEKLGYTQDMIF 274
Cdd:cd06184  220 FMQ-AVREGLKALGVPAERIH 239
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
26-258 6.26e-15

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


Pssm-ID: 99786 [Multi-domain]  Cd Length: 224  Bit Score: 71.81  E-value: 6.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  26 EKISHNTRRFRFGLPSPDHVLGlpvGNYVQLLAKiDNELvvRAYTPVSSDDDRGFVDLIIKIYfknvhpqypEGGKMTQY 105
Cdd:cd06189    7 EPLNDDVYRVRLKPPAPLDFLA---GQYLDLLLD-DGDK--RPFSIASAPHEDGEIELHIRAV---------PGGSFSDY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 106 -LENMKIGETIFFRGPRGRLFYHgpgnlgirpDQTSEPkktladhLGMIAGGTGITPMLQLIRHITKDPSDRTrMSLIFA 184
Cdd:cd06189   72 vFEELKENGLVRIEGPLGDFFLR---------EDSDRP-------LILIAGGTGFAPIKSILEHLLAQGSKRP-IHLYWG 134
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 723586615 185 NQTEEDILVRKELEEIARTHPdqfNLWYT--LDRPPIGWKYSSGFVtADMIKEHLPPPAKSTlILVCGPPPLIQTA 258
Cdd:cd06189  135 ARTEEDLYLDELLEAWAEAHP---NFTYVpvLSEPEEGWQGRTGLV-HEAVLEDFPDLSDFD-VYACGSPEMVYAA 205
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
46-271 6.48e-14

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


Pssm-ID: 99792 [Multi-domain]  Cd Length: 241  Bit Score: 69.52  E-value: 6.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  46 LGLPVGnyvqllakiDNELVVRAYTPVSSDDDRGFVDLIIKIyfknvhpqypEGGKMTQYLENMKIGETIF-FRGPRGRL 124
Cdd:cd06195   33 LGLPND---------DGKLVRRAYSIASAPYEENLEFYIILV----------PDGPLTPRLFKLKPGDTIYvGKKPTGFL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 125 FyhgpgnlgIRPDQTSEpkktladHLGMIAGGTGITPmlqlIRHITKDPSDRTR---MSLIFANQTEEDILVRKELEEIA 201
Cdd:cd06195   94 T--------LDEVPPGK-------RLWLLATGTGIAP----FLSMLRDLEIWERfdkIVLVHGVRYAEELAYQDEIEALA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 723586615 202 RTHPDQFNLWYTLDRPPIGWKYS---SGFVTADMIKEH--LPPPAKSTLILVCGPPPLIQTAAHpNLEKLGYTQD 271
Cdd:cd06195  155 KQYNGKFRYVPIVSREKENGALTgriPDLIESGELEEHagLPLDPETSHVMLCGNPQMIDDTQE-LLKEKGFSKN 228
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
62-274 9.60e-14

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


Pssm-ID: 99785 [Multi-domain]  Cd Length: 283  Bit Score: 69.64  E-value: 9.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  62 NELVVRAYTPVSSDDDRGFVDLIIKIyfKNVHPQYPEG--GKMTQYLENMKIGETIFFRGPRGrlFYHgpgnlgirpdqT 139
Cdd:cd06188   82 DEPVSRAYSLANYPAEEGELKLNVRI--ATPPPGNSDIppGIGSSYIFNLKPGDKVTASGPFG--EFF-----------I 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 140 SEPKKTLAdhlgMIAGGTGITPMLQLIRHITKDPSDRTRMSLIFANQTEEDILVRKELEEIARTHPdqfNLWY--TLDRP 217
Cdd:cd06188  147 KDTDREMV----FIGGGAGMAPLRSHIFHLLKTLKSKRKISFWYGARSLKELFYQEEFEALEKEFP---NFKYhpVLSEP 219
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 723586615 218 -PI-GWKYSSGFV----TADMIKEHLPPPAksTLILVCGPPPLIQtAAHPNLEKLGYTQDMIF 274
Cdd:cd06188  220 qPEdNWDGYTGFIhqvlLENYLKKHPAPED--IEFYLCGPPPMNS-AVIKMLDDLGVPRENIA 279
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
99-274 2.48e-13

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: 67.72  E-value: 2.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  99 GGKMTQYL-ENMKIGETIFFRGPRGRLFYHGPGNlgirpdqtsepkktladHLGMIAGGTGITPMLQLIRHITKDPSDRT 177
Cdd:cd06213   68 GGAFSGWLfGADRTGERLTVRGPFGDFWLRPGDA-----------------PILCIAGGSGLAPILAILEQARAAGTKRD 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 178 rMSLIFANQTEEDILVRKELEEIARTHPDQFNLWYTLDRPPIG--WKYSSGFVTaDMIKEHLPPPAKSTLilvCGPPPLI 255
Cdd:cd06213  131 -VTLLFGARTQRDLYALDEIAAIAARWRGRFRFIPVLSEEPADssWKGARGLVT-EHIAEVLLAATEAYL---CGPPAMI 205
                        170
                 ....*....|....*....
gi 723586615 256 QtAAHPNLEKLGYTQDMIF 274
Cdd:cd06213  206 D-AAIAVLRALGIAREHIH 223
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
23-254 5.25e-13

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: 66.80  E-value: 5.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  23 IEKEKISHNTRRFRFGLPSPDHVlGLPvGNYVQLLAKIDNELVVRayTPVS---SDDDRGFVDLIIKIYfknvhpqypeg 99
Cdd:cd06218    2 LSNREIADDIYRLVLEAPEIAAA-AKP-GQFVMLRVPDGSDPLLR--RPISihdVDPEEGTITLLYKVV----------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 100 GKMTQYLENMKIGETIFFRGPRGRLFyhgpgnlgirpDQTSEPKKTLadhlgMIAGGTGITPMLQLIRHITKDPSdrtRM 179
Cdd:cd06218   67 GKGTRLLSELKAGDELDVLGPLGNGF-----------DLPDDDGKVL-----LVGGGIGIAPLLFLAKQLAERGI---KV 127
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 723586615 180 SLIFANQTEEDILVRKELEEIARTHpdqfnLWYTLDrPPIGWKyssGFVTaDMIKEHLpPPAKSTLILVCGPPPL 254
Cdd:cd06218  128 TVLLGFRSADDLFLVEEFEALGAEV-----YVATDD-GSAGTK---GFVT-DLLKELL-AEARPDVVYACGPEPM 191
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
100-254 1.11e-12

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: 65.73  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 100 GKMTQYLENMKIGETIFFRGPRGRLFyhgpgnlgirpdqTSEPKKTLAdhlgmIAGGTGITPMLQLIRHITKdpsdRTRM 179
Cdd:cd06220   59 GEATSALHDLKEGDKLGIRGPYGNGF-------------ELVGGKVLL-----IGGGIGIAPLAPLAERLKK----AADV 116
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 723586615 180 SLIFANQTEEDILVRKELEEIARthpdqfnLWYTLDRPPIGWKyssGFVTaDMIKEHLppPAKSTLILVCGPPPL 254
Cdd:cd06220  117 TVLLGARTKEELLFLDRLRKSDE-------LIVTTDDGSYGFK---GFVT-DLLKELD--LEEYDAIYVCGPEIM 178
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
69-257 8.57e-12

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


Pssm-ID: 99795 [Multi-domain]  Cd Length: 216  Bit Score: 63.04  E-value: 8.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  69 YTPVSSDDDRGFVDLIIKiyfknvhpqypEGGKMTQYL-ENMKIGETIFFRGPRGRlFYHGPGnlgiRPDQTsepkktla 147
Cdd:cd06198   44 FTISSAPDPDGRLRFTIK-----------ALGDYTRRLaERLKPGTRVTVEGPYGR-FTFDDR----RARQI-------- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 148 dhlgMIAGGTGITPMLQLIRHITKDPSDRtRMSLIFANQTEEDILVRKELEEIARTHPDQFNLwytLDRPPIGWkyssgf 227
Cdd:cd06198  100 ----WIAGGIGITPFLALLEALAARGDAR-PVTLFYCVRDPEDAVFLDELRALAAAAGVVLHV---IDSPSDGR------ 165
                        170       180       190
                 ....*....|....*....|....*....|
gi 723586615 228 VTADMIKEHLPPPAKSTLILVCGPPPLIQT 257
Cdd:cd06198  166 LTLEQLVRALVPDLADADVWFCGPPGMADA 195
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
71-253 1.33e-11

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 62.97  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  71 PVS-SDDDRGFVDLIIKIYfknvhpqypegGKMTQYLENMKIGETIFFRGPRGRLFyhgpgnlgirpDQTSEPKKTLAdh 149
Cdd:PRK00054  52 PISiSDIDKNEITILYRKV-----------GEGTKKLSKLKEGDELDIRGPLGNGF-----------DLEEIGGKVLL-- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 150 lgmIAGGTGITPMLQLIRHITKDPSDRTrmsLIFANQTEEDILVRKELEEIARTHPdqfnlwyTLDRPPIGWKyssGFVT 229
Cdd:PRK00054 108 ---VGGGIGVAPLYELAKELKKKGVEVT---TVLGARTKDEVIFEEEFAKVGDVYV-------TTDDGSYGFK---GFVT 171
                        170       180
                 ....*....|....*....|....
gi 723586615 230 aDMIKEHLpppAKSTLILVCGPPP 253
Cdd:PRK00054 172 -DVLDELD---SEYDAIYSCGPEI 191
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
22-255 2.45e-11

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: 61.90  E-value: 2.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  22 LIEKEKISHNTRRFRFglpSPDHVLGLPVGNYVQLlakIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypEGGK 101
Cdd:cd06194    1 VVSLQRLSPDVLRVRL---EPDRPLPYLPGQYVNL---RRAGGLARSYSPTSLPDGDNELEFHIRRK---------PNGA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 102 MTQYL-ENMKIGETIFFRGPRGRLFYhgpgnlgiRPDQtsepkktLADHLGMIAGGTGITPMLQLIRH-ITKDPSdRTrM 179
Cdd:cd06194   66 FSGWLgEEARPGHALRLQGPFGQAFY--------RPEY-------GEGPLLLVGAGTGLAPLWGIARAaLRQGHQ-GE-I 128
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 723586615 180 SLIFANQTEEDILVRKELEEIARTHPdQFNLWYTLDRPPIGwkysSGFVTADMIKEHLPPPAKSTLILVCGPPPLI 255
Cdd:cd06194  129 RLVHGARDPDDLYLHPALLWLAREHP-NFRYIPCVSEGSQG----DPRVRAGRIAAHLPPLTRDDVVYLCGAPSMV 199
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
21-274 2.11e-10

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 59.82  E-value: 2.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  21 PLIEKEKIShntrRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVrayTPVSSDDDRGFVDLIIKiyfknvhpqypEGG 100
Cdd:PRK08345  15 DLTEREKLF----LLRFEDPELAESFTFKPGQFVQVTIPGVGEVPI---SICSSPTRKGFFELCIR-----------RAG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 101 KMTQYLENMKIGETIFFRGPRGRLFyhgpgnlgirPDQTSEPKKTLadhlgMIAGGTGITPMLQLIRHITKDPSDRTRMS 180
Cdd:PRK08345  77 RVTTVIHRLKEGDIVGVRGPYGNGF----------PVDEMEGMDLL-----LIAGGLGMAPLRSVLLYAMDNRWKYGNIT 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 181 LIFANQTEEDILVRKELEEIARtHPDQFNLWYTLDRPP-----------IGWKYSSGFVTADMIKEHLPPpaKSTLILVC 249
Cdd:PRK08345 142 LIYGAKYYEDLLFYDELIKDLA-EAENVKIIQSVTRDPewpgchglpqgFIERVCKGVVTDLFREANTDP--KNTYAAIC 218
                        250       260
                 ....*....|....*....|....*
gi 723586615 250 GPPPLIQtAAHPNLEKLGYTQDMIF 274
Cdd:PRK08345 219 GPPVMYK-FVFKELINRGYRPERIY 242
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
17-258 4.38e-09

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 56.42  E-value: 4.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  17 KYPLPLIEKEKISHNTRRFRFGLPSPDHVLGLPvGNYVQLLAKiDNElvVRAYTPVSSDDDRGFVDLiikiyfknvHPQY 96
Cdd:PRK07609 102 KLPCRVASLERVAGDVMRLKLRLPATERLQYLA-GQYIEFILK-DGK--RRSYSIANAPHSGGPLEL---------HIRH 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  97 PEGGKMTQYL-ENMKIGETIFFRGPRGRLFYHgpgnlgirpdqtSEPKKTLAdhlgMIAGGTGITPMLQLIRHITKDPSD 175
Cdd:PRK07609 169 MPGGVFTDHVfGALKERDILRIEGPLGTFFLR------------EDSDKPIV----LLASGTGFAPIKSIVEHLRAKGIQ 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 176 RTrMSLIFANQTEEDILVRKELEEIARTHPdqfNLWYTL----DRPPIGWKYSSGFVTADMIKEHlpPPAKSTLILVCGP 251
Cdd:PRK07609 233 RP-VTLYWGARRPEDLYLSALAEQWAEELP---NFRYVPvvsdALDDDAWTGRTGFVHQAVLEDF--PDLSGHQVYACGS 306

                 ....*..
gi 723586615 252 PPLIQTA 258
Cdd:PRK07609 307 PVMVYAA 313
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
58-216 1.09e-08

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


Pssm-ID: 99804 [Multi-domain]  Cd Length: 286  Bit Score: 55.02  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  58 AKIDNELVVRAYTPVSSDD-DRGF---VDLIIKIyfknvHPQY-PEGGKM-----TQYLENMKIGETIFFRGPRGRLFyh 127
Cdd:cd06208   56 AKNGKPHKLRLYSIASSRYgDDGDgktLSLCVKR-----LVYTdPETDETkkgvcSNYLCDLKPGDDVQITGPVGKTM-- 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 128 gpgnlgIRPDQTSepkktlADHLgMIAGGTGITPMLQLIRHI----TKDPSDRTRMSLIFANQTEEDILVRKELEEIART 203
Cdd:cd06208  129 ------LLPEDPN------ATLI-MIATGTGIAPFRSFLRRLfrekHADYKFTGLAWLFFGVPNSDSLLYDDELEKYPKQ 195
                        170
                 ....*....|...
gi 723586615 204 HPDQFNLWYTLDR 216
Cdd:cd06208  196 YPDNFRIDYAFSR 208
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
57-275 1.04e-07

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 52.02  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  57 LAKIDN-ELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypEGGKMTQYLEN-MKIGETIFFRGPRGrlfyhgpgnlgi 134
Cdd:PRK10684  44 LVSIRNsAETLRAYTLSSTPGVSEFITLTVRRI---------DDGVGSQWLTRdVKRGDYLWLSDAMG------------ 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 135 rpDQTSEPKktLADHLGMIAGGTGITPMLQLIRHITKD-PSdrTRMSLIFANQTEEDILVRKELEEIARTHPDQ-FNLWY 212
Cdd:PRK10684 103 --EFTCDDK--AEDKYLLLAAGCGVTPIMSMRRWLLKNrPQ--ADVQVIFNVRTPQDVIFADEWRQLKQRYPQLnLTLVA 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 723586615 213 TLDRPPigwKYSSGFVTADMIKEHLPPPAKSTlILVCGPPPLIQTAAHPNLEkLGYTQDMIFT 275
Cdd:PRK10684 177 ENNATE---GFIAGRLTRELLQQAVPDLASRT-VMTCGPAPYMDWVEQEVKA-LGVTADRFFK 234
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
22-254 3.63e-07

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


Pssm-ID: 99789 [Multi-domain]  Cd Length: 243  Bit Score: 50.02  E-value: 3.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  22 LIEKEKISHNTRRFRFGLPSPDHvLGLPvGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKIyfknvhpqypeGGK 101
Cdd:cd06192    1 IVKKEQLEPNLVLLTIKAPLAAR-LFRP-GQFVFLRNFESPGLERIPLSLAGVDPEEGTISLLVEI-----------RGP 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 102 MTQYLENMKIGETIFFRGPRGRLFYHGPGNlgirpdqtsepKKTLadhlgMIAGGTGITPMLQLIRhitKDPSDRTRMSL 181
Cdd:cd06192   68 KTKLIAELKPGEKLDVMGPLGNGFEGPKKG-----------GTVL-----LVAGGIGLAPLLPIAK---KLAANGNKVTV 128
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 723586615 182 IFANQTEEDILVRKELEEIARTHPdqfnlwYTLDRPPIGWKYSSGFVTADMIKEhlpppaKSTLILVCGPPPL 254
Cdd:cd06192  129 LAGAKKAKEEFLDEYFELPADVEI------WTTDDGELGLEGKVTDSDKPIPLE------DVDRIIVAGSDIM 189
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
99-256 5.31e-07

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 50.13  E-value: 5.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  99 GGKMTQYL-ENMKIGETIFFRGPRGRlFYhgpgnlgIRpdQTSEPkktladhLGMIAGGTGITPMLQLIRHITKDPSDRT 177
Cdd:PRK11872 177 DGVMSNYLrERCQVGDEILFEAPLGA-FY-------LR--EVERP-------LVFVAGGTGLSAFLGMLDELAEQGCSPP 239
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 723586615 178 rMSLIFANQTEEDILVRKELEEIARTHPDqFNLWYTLDRPPIGWKYSSGFVTADMIKEHLppPAKSTLILVCGPPPLIQ 256
Cdd:PRK11872 240 -VHLYYGVRHAADLCELQRLAAYAERLPN-FRYHPVVSKASADWQGKRGYIHEHFDKAQL--RDQAFDMYLCGPPPMVE 314
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
15-205 9.14e-07

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: 49.25  E-value: 9.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  15 EAKYPLPLIE----KEKISHNTRRFRFGLP-SPDHVLGLP---VGNYVQLLAKidNELVVRAYTPVSSDDDrGFVDLIIK 86
Cdd:cd06201   43 PRTKALELVErkdyGAAVQAPTAILRFKPAkRKLSGKGLPsfeAGDLLGILPP--GSDVPRFYSLASSSSD-GFLEICVR 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  87 iyfknVHPqypeGGKMTQYLENMKIGETI--FFRGprgrlfyhgpgNLGIRPDQTSEPkktladhLGMIAGGTGITPMLQ 164
Cdd:cd06201  120 -----KHP----GGLCSGYLHGLKPGDTIkaFIRP-----------NPSFRPAKGAAP-------VILIGAGTGIAPLAG 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 723586615 165 LIRHITKdpsdRTRMSLIFANQTEE-DILVRKELEEIARTHP 205
Cdd:cd06201  173 FIRANAA----RRPMHLYWGGRDPAsDFLYEDELDQYLADGR 210
FNR_like_2 cd06197
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ...
23-198 2.08e-05

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


Pssm-ID: 99794  Cd Length: 220  Bit Score: 44.69  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  23 IEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQL------------LAKID----NELVVRAYTpVSSDDDRGFVDLIIK 86
Cdd:cd06197    1 IKSEVITPTLTRFTFELSPPDVVGKWTPGQYITLdfsseldsgyshMADDDpqslNDDFVRTFT-VSSAPPHDPATDEFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  87 IYFKNVhpqypegGKMTQYLENMkiGETIFFRGPRGRLFYHGpGNLGIRPDQTSEPKKTLadhlgMIAGGTGITPMLQLI 166
Cdd:cd06197   80 ITVRKK-------GPVTGFLFQV--ARRLREQGLEVPVLGVG-GEFTLSLPGEGAERKMV-----WIAGGVGITPFLAML 144
                        170       180       190
                 ....*....|....*....|....*....|..
gi 723586615 167 RHITKDPSDRTRMSLIFANQTEEDILVRKELE 198
Cdd:cd06197  145 RAILSSRNTTWDITLLWSLREDDLPLVMDTLV 176
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
148-191 1.04e-04

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 43.30  E-value: 1.04e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 723586615 148 DHLGMIAGGTGITPMLQLIRHITKDPSDR----TRMSLIFANQTEEDI 191
Cdd:PLN02844 424 DSLLLVAGGIGITPFLSILKEIASQSSSRyrfpKRVQLIYVVKKSQDI 471
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
69-204 1.18e-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: 42.29  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  69 YTPVSS-DDDRGFVDLIIKiyfknvhpqyPEGGKMT---QYLENMKIGE---TIFFRGPrgrlfYHGPGNLGIRpdqtse 141
Cdd:cd06186   47 FTIASSpEDEQDTLSLIIR----------AKKGFTTrllRKALKSPGGGvslKVLVEGP-----YGSSSEDLLS------ 105
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 723586615 142 pkktlADHLGMIAGGTGITPMLQLIRHITKDPSDRT---RMSLIFANQTEEDIL-------VRKELEEIARTH 204
Cdd:cd06186  106 -----YDNVLLVAGGSGITFVLPILRDLLRRSSKTSrtrRVKLVWVVRDREDLEwfldelrAAQELEVDGEIE 173
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
148-260 2.05e-04

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 40.79  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  148 DHLGMIAGGTGITPMLQLIRHITKDPS-DRTRM-SLIFANQTEEDI-LVRKELEEIARTHPDQFNL------WYTLD--- 215
Cdd:pfam08030   2 ENVLLVAGGIGITPFISILKDLGNKSKkLKTKKiKFYWVVRDLSSLeWFKDVLNELEELKELNIEIhiyltgEYEAEdas 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 723586615  216 RPPIGWKYSSGF-------VTADMIKEH--------------LPPPAKSTLILVCGPPPLIQTAAH 260
Cdd:pfam08030  82 DQSDSSIRSENFdslmnevIGVDFVEFHfgrpnwkevlkdiaKQHPNGSIGVFSCGPPSLVDELRN 147
PRK05802 PRK05802
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
70-168 2.82e-04

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


Pssm-ID: 235613 [Multi-domain]  Cd Length: 320  Bit Score: 41.50  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  70 TPVS---SDDDRGFVDLIIKIYfknvhpqypegGKMTQYLENMKIGETIFFRGPrgrlFYHGPgnLGIRPDQTSEPKKTL 146
Cdd:PRK05802 114 VPISimeADTEENIIKVAIEIR-----------GVKTKKIAKLNKGDEILLRGP----YWNGI--LGLKNIKSTKNGKSL 176
                         90       100
                 ....*....|....*....|..
gi 723586615 147 adhlgMIAGGTGITPMLQLIRH 168
Cdd:PRK05802 177 -----VIARGIGQAPGVPVIKK 193
siderophore_interacting cd06193
Siderophore interacting proteins share the domain structure of the ferredoxin reductase like ...
34-127 1.91e-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: 38.78  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  34 RFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKiyfknVHpqyPEGGKMTQYLENMKIGE 113
Cdd:cd06193   32 HVKLLFPDPGQAPPVLPVLGRRRWPPEEPRPVMRTYTVRRFDPEAGELDIDFV-----LH---GDEGPASRWAASAQPGD 103
                         90
                 ....*....|....
gi 723586615 114 TIFFRGPRGRLFYH 127
Cdd:cd06193  104 TLGIAGPGGSFLPP 117
PLN03116 PLN03116
ferredoxin--NADP+ reductase; Provisional
105-216 2.96e-03

ferredoxin--NADP+ reductase; Provisional


Pssm-ID: 215586 [Multi-domain]  Cd Length: 307  Bit Score: 38.54  E-value: 2.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 105 YLENMKIGETIFFRGPRGRLFyhgpgnlgIRPDqtSEPKktlADHLgMIAGGTGITPMLQLIRH--ITKDPSDRTRMS-- 180
Cdd:PLN03116 128 FLCDAKPGDKVQITGPSGKVM--------LLPE--EDPN---ATHI-MVATGTGIAPFRGFLRRmfMEDVPAFKFGGLaw 193
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 723586615 181 LIFANQTEEDILVRKELEEIARTHPDQFNLWYTLDR 216
Cdd:PLN03116 194 LFLGVANSDSLLYDDEFERYLKDYPDNFRYDYALSR 229
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
107-258 3.94e-03

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


Pssm-ID: 99782 [Multi-domain]  Cd Length: 211  Bit Score: 37.46  E-value: 3.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 107 ENMKIGETIFFRGPRGrlfyhgpgNLGIRPDqtsepkktlADHLGMIAGGTGITPMLQLIRHITKdpsDRTRMSLIFANQ 186
Cdd:cd06185   75 ELLRVGDELEVSAPRN--------LFPLDEA---------ARRHLLIAGGIGITPILSMARALAA---RGADFELHYAGR 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615 187 TEEDILVRKELEEIA----RTHPD----QFNLWYTLDRPPIGwkyssgfvtadmikehlpppaksTLILVCGPPPLIQTA 258
Cdd:cd06185  135 SREDAAFLDELAALPgdrvHLHFDdeggRLDLAALLAAPPAG-----------------------THVYVCGPEGMMDAV 191
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
61-203 5.67e-03

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. CYPOR has a C-terminal ferredoxin reducatase (FNR)- like FAD and NAD binding module, an FMN-binding domain, and an additional conecting domain (inserted within the FAD binding region) that orients the FNR and FMN binding domains. 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: 99779 [Multi-domain]  Cd Length: 267  Bit Score: 37.32  E-value: 5.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586615  61 DNELVVRAYTPVSS-DDDRGFVDLIIKIY-FKNvhpqyPEG----GKMTQYLENMKIGE--TIFFRGprgrlfyhgpgNL 132
Cdd:cd06182   43 PNPLQPRYYSIASSpDVDPGEVHLCVRVVsYEA-----PAGrirkGVCSNFLAGLQLGAkvTVFIRP-----------AP 106
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 723586615 133 GIRPdqtsePKKTLADhLGMIAGGTGITPMLQLIRH---ITKDPSDRTRMSLIF-ANQTEEDILVRKELEEIART 203
Cdd:cd06182  107 SFRL-----PKDPTTP-IIMVGPGTGIAPFRGFLQEraaLRANGKARGPAWLFFgCRNFASDYLYREELQEALKD 175
 
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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