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Conserved domains on  [gi|281366099|ref|NP_001163421|]
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uncharacterized protein Dmel_CG5946, isoform E [Drosophila melanogaster]

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

EC:  1.7.1.3|1.6.2.2
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]
 50-259 1.49e-102

nitrate reductase [NADPH]


The actual alignment was detected with superfamily member PLN02252:

Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 317.77  E-value: 1.49e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  50 LVDPNDKYLLPLIEKENLSHDTRRFRFGLPSKQHVLGLPVGQHIHLIATIDNELIIRPYTPISSDEDVGYVDLVVKVYFK 129
Cdd:PLN02252 628 ALNPREKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFELVIKVYFK 707

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 130 DSHPKFPAGGKMTQHLEQLELGDKISFRGPSGRLQYLGNGTFSIKKlrkdPPKHvtAKRVNMIAGGTGITPMLQLAREVL 209
Cdd:PLN02252 708 NVHPKFPNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFLVNG----KPKF--AKKLAMLAGGTGITPMYQVIQAIL 781

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 281366099 210 kRSDKDKTELALLFANQSEKDILLRAELDELAQKHPDQFKIWYTVDKANE 259
Cdd:PLN02252 782 -RDPEDKTEMSLVYANRTEDDILLREELDRWAAEHPDRLKVWYVVSQVKR 830
 
Name Accession Description Interval E-value
PLN02252 PLN02252
nitrate reductase [NADPH]
 50-259 1.49e-102

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 317.77  E-value: 1.49e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  50 LVDPNDKYLLPLIEKENLSHDTRRFRFGLPSKQHVLGLPVGQHIHLIATIDNELIIRPYTPISSDEDVGYVDLVVKVYFK 129
Cdd:PLN02252 628 ALNPREKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFELVIKVYFK 707

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 130 DSHPKFPAGGKMTQHLEQLELGDKISFRGPSGRLQYLGNGTFSIKKlrkdPPKHvtAKRVNMIAGGTGITPMLQLAREVL 209
Cdd:PLN02252 708 NVHPKFPNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFLVNG----KPKF--AKKLAMLAGGTGITPMYQVIQAIL 781

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 281366099 210 kRSDKDKTELALLFANQSEKDILLRAELDELAQKHPDQFKIWYTVDKANE 259
Cdd:PLN02252 782 -RDPEDKTEMSLVYANRTEDDILLREELDRWAAEHPDRLKVWYVVSQVKR 830
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 59-260 4.36e-89

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: 263.66  E-value: 4.36e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  59 LPLIEKENLSHDTRRFRFGLPSKQHVLGLPVGQHIHLIATIDNELIIRPYTPISSDEDVGYVDLVVKVYFkdshpkfpaG 138
Cdd:cd06183    1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYP---------G 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 139 GKMTQHLEQLELGDKISFRGPSGRLQYLGNGTFsikklrkdppkhvtaKRVNMIAGGTGITPMLQLAREVLKRsDKDKTE 218
Cdd:cd06183   72 GKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGKV---------------KHIGMIAGGTGITPMLQLIRAILKD-PEDKTK 135

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 281366099 219 LALLFANQSEKDILLRAELDELAQKHPDQFKIWYTVDKANEG 260
Cdd:cd06183  136 ISLLYANRTEEDILLREELDELAKKHPDRFKVHYVLSRPPEG 177
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
59-165 1.41e-49

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 158.51  E-value: 1.41e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099   59 LPLIEKENLSHDTRRFRFGLPSKQHVLGLPVGQHIHLIATIDNELIIRPYTPISSDEDVGYVDLVVKVYfkdshpkfpAG 138
Cdd:pfam00970   2 LTLVEKELVSHDTRIFRFALPHPDQVLGLPVGQHLFLRLPIDGELVIRSYTPISSDDDKGYLELLVKVY---------PG 72

                          90       100
                  ....*....|....*....|....*..
gi 281366099  139 GKMTQHLEQLELGDKISFRGPSGRLQY 165
Cdd:pfam00970  73 GKMSQYLDELKIGDTIDFKGPLGRFEY 99
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
61-260 2.18e-28

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 107.95  E-value: 2.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  61 LIEKENLSHDTRRFRFGLPSKQHVLG-LPvGQHIHLIATIDNELIIRPYTpISSDEDVGYVDLVVKvyfkdshpKFPaGG 139
Cdd:COG1018    8 VVEVRRETPDVVSFTLEPPDGAPLPRfRP-GQFVTLRLPIDGKPLRRAYS-LSSAPGDGRLEITVK--------RVP-GG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 140 KMTQHL-EQLELGDKISFRGPSGRLQylgngtfsikkLRKDPPKHVTakrvnMIAGGTGITPMLQLAREVLKRSDKDKTE 218
Cdd:COG1018   77 GGSNWLhDHLKVGDTLEVSGPRGDFV-----------LDPEPARPLL-----LIAGGIGITPFLSMLRTLLARGPFRPVT 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 281366099 219 laLLFANQSEKDILLRAELDELAQKHPdQFKIWYTVDKANEG 260
Cdd:COG1018  141 --LVYGARSPADLAFRDELEALAARHP-RLRLHPVLSREPAG 179
 
Name Accession Description Interval E-value
PLN02252 PLN02252
nitrate reductase [NADPH]
 50-259 1.49e-102

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 317.77  E-value: 1.49e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  50 LVDPNDKYLLPLIEKENLSHDTRRFRFGLPSKQHVLGLPVGQHIHLIATIDNELIIRPYTPISSDEDVGYVDLVVKVYFK 129
Cdd:PLN02252 628 ALNPREKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFELVIKVYFK 707

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 130 DSHPKFPAGGKMTQHLEQLELGDKISFRGPSGRLQYLGNGTFSIKKlrkdPPKHvtAKRVNMIAGGTGITPMLQLAREVL 209
Cdd:PLN02252 708 NVHPKFPNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFLVNG----KPKF--AKKLAMLAGGTGITPMYQVIQAIL 781

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 281366099 210 kRSDKDKTELALLFANQSEKDILLRAELDELAQKHPDQFKIWYTVDKANE 259
Cdd:PLN02252 782 -RDPEDKTEMSLVYANRTEDDILLREELDRWAAEHPDRLKVWYVVSQVKR 830
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 59-260 4.36e-89

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: 263.66  E-value: 4.36e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  59 LPLIEKENLSHDTRRFRFGLPSKQHVLGLPVGQHIHLIATIDNELIIRPYTPISSDEDVGYVDLVVKVYFkdshpkfpaG 138
Cdd:cd06183    1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYP---------G 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 139 GKMTQHLEQLELGDKISFRGPSGRLQYLGNGTFsikklrkdppkhvtaKRVNMIAGGTGITPMLQLAREVLKRsDKDKTE 218
Cdd:cd06183   72 GKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGKV---------------KHIGMIAGGTGITPMLQLIRAILKD-PEDKTK 135

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 281366099 219 LALLFANQSEKDILLRAELDELAQKHPDQFKIWYTVDKANEG 260
Cdd:cd06183  136 ISLLYANRTEEDILLREELDELAKKHPDRFKVHYVLSRPPEG 177
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
 51-256 4.22e-84

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 253.60  E-value: 4.22e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  51 VDPNDKYLLPLIEKENLSHDTRRFRFGLPSKQHVLGLPVGQHIHLIATIDN----ELIIRPYTPISSDEDVGYVDLVVKV 126
Cdd:PTZ00319  28 LDPDMFQHFKLIKKTEVTHDTFIFRFALHSPTQRLGLPIGQHIVFRCDCTTpgkpETVQHSYTPISSDDEKGYVDFLIKV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 127 YFKDSHPKFPAGGKMTQHLEQLELGDKISFRGPSGRLQYLGNGTFSIKKLRKD-PPKHVTAkrVNMIAGGTGITPMLQLA 205
Cdd:PTZ00319 108 YFKGVHPSFPNGGRLSQHLYHMKLGDKIEMRGPVGKFEYLGNGTYTVHKGKGGlKTMHVDA--FAMIAGGTGITPMLQII 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 281366099 206 REVLKrSDKDKTELALLFANQSEKDILLRAELDELAQKhpDQFKIWYTVDK 256
Cdd:PTZ00319 186 HAIKK-NKEDRTKVFLVYANQTEDDILLRKELDEAAKD--PRFHVWYTLDR 233
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
59-165 1.41e-49

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 158.51  E-value: 1.41e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099   59 LPLIEKENLSHDTRRFRFGLPSKQHVLGLPVGQHIHLIATIDNELIIRPYTPISSDEDVGYVDLVVKVYfkdshpkfpAG 138
Cdd:pfam00970   2 LTLVEKELVSHDTRIFRFALPHPDQVLGLPVGQHLFLRLPIDGELVIRSYTPISSDDDKGYLELLVKVY---------PG 72

                          90       100
                  ....*....|....*....|....*..
gi 281366099  139 GKMTQHLEQLELGDKISFRGPSGRLQY 165
Cdd:pfam00970  73 GKMSQYLDELKIGDTIDFKGPLGRFEY 99
PTZ00274 PTZ00274
cytochrome b5 reductase; Provisional
 67-261 5.76e-32

cytochrome b5 reductase; Provisional


Pssm-ID: 140300  Cd Length: 325  Bit Score: 119.64  E-value: 5.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  67 LSHDTRRFRFGLPSKQHVLGLPVG--QHIHLIATIDNELIIRPYTPISSDEDVGYVDLVVKVyfkdshpkfPAGGKMTQH 144
Cdd:PTZ00274  63 ITHDTALFRFLLHSEEEFNLKPCStlQACYKYGVQPMDQCQRFYTPVTANHTKGYFDIIVKR---------KKDGLMTNH 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 145 LEQLELGDKISFRGPSGRLQYlgngtfsikklRKDPPKHVtakrvNMIAGGTGITPMLQLAREVLKR----SDKDKTELA 220
Cdd:PTZ00274 134 LFGMHVGDKLLFRSVTFKIQY-----------RPNRWKHV-----GMIAGGTGFTPMLQIIRHSLTEpwdsGEVDRTKLS 197

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 281366099 221 LLFANQSEKDILLRAELDELAQKHPDQFKIWYTVDKANEGE 261
Cdd:PTZ00274 198 FLFCNRTERHILLKGLFDDLARRYSNRFKVYYTIDQAVEPD 238
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 62-263 1.60e-31

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: 116.01  E-value: 1.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  62 IEKENLSHDTRRFRFGLPSkqhVLGLPVGQHIHLIATIDNELIIRPYTPISSDEDVGYVDLVVKVYFkdshpkfpaGGKM 141
Cdd:cd00322    1 VATEDVTDDVRLFRLQLPN---GFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEGELELTVKIVP---------GGPF 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 142 TQHLEQLELGDKISFRGPsgrlqylgNGTFSikkLRKDPPKHVTakrvnMIAGGTGITPMLQLAREVLKrsDKDKTELAL 221
Cdd:cd00322   69 SAWLHDLKPGDEVEVSGP--------GGDFF---LPLEESGPVV-----LIAGGIGITPFRSMLRHLAA--DKPGGEITL 130

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 281366099 222 LFANQSEKDILLRAELDELAQKHPDqFKIWYTVDKANEGELQ 263
Cdd:cd00322  131 LYGARTPADLLFLDELEELAKEGPN-FRLVLALSRESEAKLG 171
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
61-260 2.18e-28

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 107.95  E-value: 2.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  61 LIEKENLSHDTRRFRFGLPSKQHVLG-LPvGQHIHLIATIDNELIIRPYTpISSDEDVGYVDLVVKvyfkdshpKFPaGG 139
Cdd:COG1018    8 VVEVRRETPDVVSFTLEPPDGAPLPRfRP-GQFVTLRLPIDGKPLRRAYS-LSSAPGDGRLEITVK--------RVP-GG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 140 KMTQHL-EQLELGDKISFRGPSGRLQylgngtfsikkLRKDPPKHVTakrvnMIAGGTGITPMLQLAREVLKRSDKDKTE 218
Cdd:COG1018   77 GGSNWLhDHLKVGDTLEVSGPRGDFV-----------LDPEPARPLL-----LIAGGIGITPFLSMLRTLLARGPFRPVT 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 281366099 219 laLLFANQSEKDILLRAELDELAQKHPdQFKIWYTVDKANEG 260
Cdd:COG1018  141 --LVYGARSPADLAFRDELEALAARHP-RLRLHPVLSREPAG 179
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 191-260 9.21e-25

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: 95.02  E-value: 9.21e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  191 MIAGGTGITPMLQLAREVLKRsDKDKTELALLFANQSEKDILLRAELDELAQKHPDQFKIWYTVDKANEG 260
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILED-PKDPTQVVLVFGNRNEDDILYREELDELAEKHPGRLTVVYVVSRPEAG 69
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 57-240 9.95e-23

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: 92.69  E-value: 9.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  57 YLLPLIEKENLSHDTRRFRFglpSKQHVLGLPVGQHIHLiaTIDNE---LIIRPYTPISSDEDvGYVDLVVKVYfkdshp 133
Cdd:cd06196    1 HTVTLLSIEPVTHDVKRLRF---DKPEGYDFTPGQATEV--AIDKPgwrDEKRPFTFTSLPED-DVLEFVIKSY------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 134 kfPAGGKMTQHLEQLELGDKISFRGPSGRLQYLGNGTFsikklrkdppkhvtakrvnmIAGGTGITPMLQLAREvlkRSD 213
Cdd:cd06196   69 --PDHDGVTEQLGRLQPGDTLLIEDPWGAIEYKGPGVF--------------------IAGGAGITPFIAILRD---LAA 123

                        170       180
                 ....*....|....*....|....*...
gi 281366099 214 KDKTE-LALLFANQSEKDILLRAELDEL 240
Cdd:cd06196  124 KGKLEgNTLIFANKTEKDIILKDELEKM 151
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 57-250 1.04e-22

NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation oxidoreductase. PA oxidoreductases of E. coli hydroxylate PA-CoA in the second step of PA degradation. Members of this group typically fuse a ferredoxin reductase-like domain with an iron-sulfur binding cluster domain. Ferredoxins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal portion may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria and participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99810 [Multi-domain]  Cd Length: 241  Bit Score: 92.99  E-value: 1.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  57 YLLPLIEKENLSHDTRRFRFGLPSK-QHVLGLPVGQHIHLIATIDNELIIRPYTpISSDEDVGYVDLVVK-Vyfkdshpk 134
Cdd:cd06214    2 HPLTVAEVVRETADAVSITFDVPEElRDAFRYRPGQFLTLRVPIDGEEVRRSYS-ICSSPGDDELRITVKrV-------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 135 fpAGGKMTQHL-EQLELGDKISFRGPSGRlqylgngtFSikklrkdPPKHVTAKRVNMIAGGTGITPMLQLAREVLKRSD 213
Cdd:cd06214   73 --PGGRFSNWAnDELKAGDTLEVMPPAGR--------FT-------LPPLPGARHYVLFAAGSGITPVLSILKTALAREP 135

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 281366099 214 KDKteLALLFANQSEKDILLRAELDELAQKHPDQFKI 250
Cdd:cd06214  136 ASR--VTLVYGNRTEASVIFREELADLKARYPDRLTV 170
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 62-244 4.48e-22

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 91.46  E-value: 4.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  62 IEKENLSHDTRRFRFGLPsKQHVLGLPvGQHIHLiaTIDNELIIRPYTPISSDEDVGYVDLVVKVYfkdshpkfpagGKM 141
Cdd:COG0543    3 VSVERLAPDVYLLRLEAP-LIALKFKP-GQFVML--RVPGDGLRRPFSIASAPREDGTIELHIRVV-----------GKG 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 142 TQHLEQLELGDKISFRGPsgrlqyLGNGtFSIKKlrkdppkhvTAKRVNMIAGGTGITPMLQLAREVLKRsdkdKTELAL 221
Cdd:COG0543   68 TRALAELKPGDELDVRGP------LGNG-FPLED---------SGRPVLLVAGGTGLAPLRSLAEALLAR----GRRVTL 127

                        170       180
                 ....*....|....*....|...
gi 281366099 222 LFANQSEKDILLRAELDELAQKH 244
Cdd:COG0543  128 YLGARTPEDLYLLDELEALADFR 150
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 59-263 6.21e-22

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: 90.73  E-value: 6.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  59 LPLIEKENLSHDTRRFRFGLPSKQHVLGLPvGQHIHLIATIDNELIIRPYTPISSDEDVGYVDLVVKVYfkdshpkfpAG 138
Cdd:cd06215    1 LRCVKIIQETPDVKTFRFAAPDGSLFAYKP-GQFLTLELEIDGETVYRAYTLSSSPSRPDSLSITVKRV---------PG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 139 GKMTQHL-EQLELGDKISFRGPSGRlqylgngtFSIKklrkDPPkhvtAKRVNMIAGGTGITPMLQLAREVLKRsdKDKT 217
Cdd:cd06215   71 GLVSNWLhDNLKVGDELWASGPAGE--------FTLI----DHP----ADKLLLLSAGSGITPMMSMARWLLDT--RPDA 132

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 281366099 218 ELALLFANQSEKDILLRAELDELAQKHPdQFKIWYTVDKANEGELQ 263
Cdd:cd06215  133 DIVFIHSARSPADIIFADELEELARRHP-NFRLHLILEQPAPGAWG 177
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 46-262 5.10e-19

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: 83.43  E-value: 5.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  46 RLRTLVDPN---DKYLLPLIEKENLSHDTRRFRFgLPSKQHVLGLPvGQHIHLIATIDNELIIRPYTPISSDE-DVGYVD 121
Cdd:cd06216    4 FYLELINPLwsaRELRARVVAVRPETADMVTLTL-RPNRGWPGHRA-GQHVRLGVEIDGVRHWRSYSLSSSPTqEDGTIT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 122 LVVKVyfkdsHPkfpaGGKMTQHL-EQLELGDKISFRGPSGRLQylgngtfsikklrkdpPKHVTAKRVNMIAGGTGITP 200
Cdd:cd06216   82 LTVKA-----QP----DGLVSNWLvNHLAPGDVVELSQPQGDFV----------------LPDPLPPRLLLIAAGSGITP 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281366099 201 MLQLAREVLKRSdkDKTELALLFANQSEKDILLRAELDELAQKHPD-QFKIWYTvDKANEGEL 262
Cdd:cd06216  137 VMSMLRTLLARG--PTADVVLLYYARTREDVIFADELRALAAQHPNlRLHLLYT-REELDGRL 196
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 69-246 1.02e-16

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


Pssm-ID: 99813 [Multi-domain]  Cd Length: 235  Bit Score: 76.92  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  69 HDTRRFRFGLPSKQHVLGLPvGQHIHLIAT-IDNELIIRPYTPISSDEDVGYVDLVVKVYfkdshpkfpAGGKMTQHL-E 146
Cdd:cd06217   14 PTVKTFRLAVPDGVPPPFLA-GQHVDLRLTaIDGYTAQRSYSIASSPTQRGRVELTVKRV---------PGGEVSPYLhD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 147 QLELGDKISFRGPSGRLQYlgngtfsikklrkdPPKHvtAKRVNMIAGGTGITPMLQLAREVLKRSDKdkTELALLFANQ 226
Cdd:cd06217   84 EVKVGDLLEVRGPIGTFTW--------------NPLH--GDPVVLLAGGSGIVPLMSMIRYRRDLGWP--VPFRLLYSAR 145

                        170       180
                 ....*....|....*....|
gi 281366099 227 SEKDILLRAELDELAQKHPD 246
Cdd:cd06217  146 TAEDVIFRDELEQLARRHPN 165
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 110-261 5.63e-15

Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+.


Pssm-ID: 99817 [Multi-domain]  Cd Length: 253  Bit Score: 72.25  E-value: 5.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 110 PIS---SDEDVGYVDLVVKvyfkdshpkfpAGGKMTQHLEQLELGDKISFRGPsgrlqyLGNGtFsikklrkdPPKHVTA 186
Cdd:cd06221   45 PISissDPTRRGPLELTIR-----------RVGRVTEALHELKPGDTVGLRGP------FGNG-F--------PVEEMKG 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281366099 187 KRVNMIAGGTGITPMLQLAREVLKRSDKDKtELALLFANQSEKDILLRAELDELAQKHpdQFKIWYTVDKANEGE 261
Cdd:cd06221   99 KDLLLVAGGLGLAPLRSLINYILDNREDYG-KVTLLYGARTPEDLLFKEELKEWAKRS--DVEVILTVDRAEEGW 170
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 62-254 6.34e-15

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: 71.86  E-value: 6.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  62 IEKENLSHDTRRFRFGLPSKQHVLGlpvGQHIHlIATIDNELIIRPYTPISSDEDVGYVDLVVKVYfkdshpkfpAGGKM 141
Cdd:cd06187    2 VSVERLTHDIAVVRLQLDQPLPFWA---GQYVN-VTVPGRPRTWRAYSPANPPNEDGEIEFHVRAV---------PGGRV 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 142 TQHL-EQLELGDKISFRGPSGrlqylgngTFSIKKLRKDPpkhvtakrVNMIAGGTGITPMLQLAREVLKRSDKDKTelA 220
Cdd:cd06187   69 SNALhDELKVGDRVRLSGPYG--------TFYLRRDHDRP--------VLCIAGGTGLAPLRAIVEDALRRGEPRPV--H 130

                        170       180       190
                 ....*....|....*....|....*....|....
gi 281366099 221 LLFANQSEKDILLRAELDELAQKHPdqfkiWYTV 254
Cdd:cd06187  131 LFFGARTERDLYDLEGLLALAARHP-----WLRV 159
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
107-246 1.86e-14

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 72.23  E-value: 1.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 107 PYTPISSDEDVGYVDLVVKvyfkdshpkfpAGGKMTQHLEQLELGDKISFRGPSGRLqylgngtfsikklrkDPPKHVTA 186
Cdd:COG4097  265 PFSISSAPGGDGRLRFTIK-----------ALGDFTRRLGRLKPGTRVYVEGPYGRF---------------TFDRRDTA 318

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 187 KRVNMIAGGTGITPMLQLAREvLKRSDKDKTELALLFANQSEKDILLRAELDELAQKHPD 246
Cdd:COG4097  319 PRQVWIAGGIGITPFLALLRA-LAARPGDQRPVDLFYCVRDEEDAPFLEELRALAARLAG 377
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 59-245 3.67e-14

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: 69.86  E-value: 3.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  59 LPLIEKENLSHDTRRFRFGLPSKQHVLGLPvGQHIHLIATIDNELIIRPYTpISSDEDVGYVDLVVKvyfkdshpKFPaG 138
Cdd:cd06191    1 LRVAEVRSETPDAVTIVFAVPGPLQYGFRP-GQHVTLKLDFDGEELRRCYS-LCSSPAPDEISITVK--------RVP-G 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 139 GKMTQHL-EQLELGDKISFRGPSGRLQYlgngtfsikklRKDPPKhvtakRVNMIAGGTGITPMLQLAREvlKRSDKDKT 217
Cdd:cd06191   70 GRVSNYLrEHIQPGMTVEVMGPQGHFVY-----------QPQPPG-----RYLLVAAGSGITPLMAMIRA--TLQTAPES 131

                        170       180
                 ....*....|....*....|....*...
gi 281366099 218 ELALLFANQSEKDILLRAELDELAQKHP 245
Cdd:cd06191  132 DFTLIHSARTPADMIFAQELRELADKPQ 159
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 71-260 1.19e-12

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 67.50  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099   71 TRRFRFGLPSKQHVLGLPVGQHIHLIATIDNELIIRPYTPISSDEDVGYVDLVVKvyfKDShpkfpagGKMTQHLEQLEL 150
Cdd:PTZ00306  932 SRVLRFNLPGALQRSGLTLGQFIAIRGDWDGQQLIGYYSPITLPDDLGVISILAR---GDK-------GTLKEWISALRP 1001

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  151 GDKISFRGPSGRLQYLgngTFSIKKL--RKdppkHVTaKRVNMIAGGTGITPMLQLAREVLKRSDKDKTE-LALLFANQS 227
Cdd:PTZ00306 1002 GDSVEMKACGGLRIER---RPADKQFvfRG----HVI-RKLALIAGGTGVAPMLQIIRAALKKPYVDSIEsIRLIYAAED 1073

                         170       180       190
                  ....*....|....*....|....*....|...
gi 281366099  228 EKDILLRAELDELAQKHPDQFKIWYTVDKANEG 260
Cdd:PTZ00306 1074 VSELTYRELLESYRKENPGKFKCHFVLNNPPEG 1106
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 61-249 4.19e-12

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


Pssm-ID: 99807  Cd Length: 238  Bit Score: 63.88  E-value: 4.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  61 LIEKENLSHDTRRFRFGLPSKQHVLGLPvGQHIHLiaTIDNELIIRPYTPISSDEDVGYVDLvvkvyfkdsHPKFPAGGK 140
Cdd:cd06211   11 VVEIEDLTPTIKGVRLKLDEPEEIEFQA-GQYVNL--QAPGYEGTRAFSIASSPSDAGEIEL---------HIRLVPGGI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 141 MTQHL-EQLELGDKISFRGPSGRlqylgngtFSIKKLRKDPpkhvtakrVNMIAGGTGITPMLQLAREVLKRSDKDKTEl 219
Cdd:cd06211   79 ATTYVhKQLKEGDELEISGPYGD--------FFVRDSDQRP--------IIFIAGGSGLSSPRSMILDLLERGDTRKIT- 141

                        170       180       190
                 ....*....|....*....|....*....|
gi 281366099 220 aLLFANQSEKDILLRAELDELAQKHPDqFK 249
Cdd:cd06211  142 -LFFGARTRAELYYLDEFEALEKDHPN-FK 169
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 62-241 2.56e-11

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: 61.79  E-value: 2.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  62 IEKENLSHDTRRFRFGLPSKQHVlGLPvGQHIHLIATIDNELIIRpyTPIS---SDEDVGYVDLVVKVYfkdshpkfpag 138
Cdd:cd06218    2 LSNREIADDIYRLVLEAPEIAAA-AKP-GQFVMLRVPDGSDPLLR--RPISihdVDPEEGTITLLYKVV----------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 139 GKMTQHLEQLELGDKISFRGPsgrlqyLGNGtFSIKklrkDPPKHVTakrvnMIAGGTGITPMLQLAREvLKRSDKDKTe 218
Cdd:cd06218   67 GKGTRLLSELKAGDELDVLGP------LGNG-FDLP----DDDGKVL-----LVGGGIGIAPLLFLAKQ-LAERGIKVT- 128

                        170       180
                 ....*....|....*....|...
gi 281366099 219 laLLFANQSEKDILLRAELDELA 241
Cdd:cd06218  129 --VLLGFRSADDLFLVEEFEALG 149
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 85-250 3.79e-11

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: 61.43  E-value: 3.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  85 LGLPVGqhihliatiDNELIIRPYTpISSDEDVGYVDLVVkVYFKDshpkfpagGKMTQHLEQLELGDKIS-FRGPSGRL 163
Cdd:cd06195   33 LGLPND---------DGKLVRRAYS-IASAPYEENLEFYI-ILVPD--------GPLTPRLFKLKPGDTIYvGKKPTGFL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 164 QylgngtfsikkLRKDPPkhvtAKRVNMIAGGTGITPMLQLAREVLKRSDKDKteLALLFANQSEKDILLRAELDELAQK 243
Cdd:cd06195   94 T-----------LDEVPP----GKRLWLLATGTGIAPFLSMLRDLEIWERFDK--IVLVHGVRYAEELAYQDEIEALAKQ 156


                 ....*..
gi 281366099 244 HPDQFKI 250
Cdd:cd06195  157 YNGKFRY 163
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 65-246 5.69e-11

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: 60.81  E-value: 5.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  65 ENLSHDTRRFRFGLPSKQHVLGLPvGQHIHLiaTIDNELIIRPYTPISSDEDVGYVDLVVKVYfkdshpkfpAGGKMTQH 144
Cdd:cd06212    9 EALTHDIRRLRLRLEEPEPIKFFA-GQYVDI--TVPGTEETRSFSMANTPADPGRLEFIIKKY---------PGGLFSSF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 145 LEQ-LELGDKISFRGPsgrlqYlgnGTFsikKLRKDPPKhvtakRVNMIAGGTGITPMLQLAREVLkrSDKDKTELALLF 223
Cdd:cd06212   77 LDDgLAVGDPVTVTGP-----Y---GTC---TLRESRDR-----PIVLIGGGSGMAPLLSLLRDMA--ASGSDRPVRFFY 138

                        170       180
                 ....*....|....*....|...
gi 281366099 224 ANQSEKDILLRAELDELAQKHPD 246
Cdd:cd06212  139 GARTARDLFYLEEIAALGEKIPD 161
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 90-261 1.65e-09

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: 56.80  E-value: 1.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  90 GQHIHLIATIDNE--LIIRPYTpISSDEDVGYVDLVVKvyfKDshpkfpAGGKMTQHL-EQLELGDKISFRGPSGRlqyl 166
Cdd:cd06184   40 GQYLSVRVKLPGLgyRQIRQYS-LSDAPNGDYYRISVK---RE------PGGLVSNYLhDNVKVGDVLEVSAPAGD---- 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 167 gngtFSIKKLRKDPpkhvtakrVNMIAGGTGITPMLQLAREVLKRsdKDKTELALLFANQSEKDILLRAELDELAQKHPD 246
Cdd:cd06184  106 ----FVLDEASDRP--------LVLISAGVGITPMLSMLEALAAE--GPGRPVTFIHAARNSAVHAFRDELEELAARLPN 171

                        170
                 ....*....|....*.
gi 281366099 247 -QFKIWYTVDKANEGE 261
Cdd:cd06184  172 lKLHVFYSEPEAGDRE 187
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 65-263 9.64e-09

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: 54.14  E-value: 9.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  65 ENLSHDTRRFRFGLPSKQHVLGLPvGQHIHLiaTIDNELIIRPYTPiSSDEDVGYVDLVVKvyfkdshpKFPaGGKMTQH 144
Cdd:cd06209   10 ERLSDSTIGLTLELDEAGALAFLP-GQYVNL--QVPGTDETRSYSF-SSAPGDPRLEFLIR--------LLP-GGAMSSY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 145 LEQL-ELGDKISFRGPSGrlqylgngTFsikKLRkdppkHVTAKRVnMIAGGTGITPML----QLAREVLKRSdkdkteL 219
Cdd:cd06209   77 LRDRaQPGDRLTLTGPLG--------SF---YLR-----EVKRPLL-MLAGGTGLAPFLsmldVLAEDGSAHP------V 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 281366099 220 ALLFANQSEKDILLRAELDELAQKHPDqFKIWYTVDKANEGELQ 263
Cdd:cd06209  134 HLVYGVTRDADLVELDRLEALAERLPG-FSFRTVVADPDSWHPR 176
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 90-241 2.44e-08

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 53.34  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  90 GQHIHLIATIDNELIIRPytpIS-SDEDVGYVDLVVKVYfkdshpkfpagGKMTQHLEQLELGDKISFRGPsgrlqyLGN 168
Cdd:PRK00054  35 GQFVMVWVPGVEPLLERP---ISiSDIDKNEITILYRKV-----------GEGTKKLSKLKEGDELDIRGP------LGN 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281366099 169 GtFSIKKlrkdppkhvTAKRVNMIAGGTGITPMLQLAREVLKRSDKDKTELALlfanQSEKDILLRAELDELA 241
Cdd:PRK00054  95 G-FDLEE---------IGGKVLLVGGGIGVAPLYELAKELKKKGVEVTTVLGA----RTKDEVIFEEEFAKVG 153
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 90-254 5.81e-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: 52.32  E-value: 5.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  90 GQHIHLIATIDNELIIRPYTP----ISS-----DEDVGYVDLVVK--VYFkdsHPKF--PAGGKMTQHLEQLELGDKISF 156
Cdd:cd06208   44 GQSIGIIPPGTDAKNGKPHKLrlysIASsrygdDGDGKTLSLCVKrlVYT---DPETdeTKKGVCSNYLCDLKPGDDVQI 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 157 RGPSGRLQYLgngtfsikklrkdpPKHVTAKRVnMIAGGTGITPMLQLAREVLKRSDKDK--TELALLF---ANQSEkdI 231
Cdd:cd06208  121 TGPVGKTMLL--------------PEDPNATLI-MIATGTGIAPFRSFLRRLFREKHADYkfTGLAWLFfgvPNSDS--L 183

                        170       180
                 ....*....|....*....|...
gi 281366099 232 LLRAELDELAQKHPDQFKIWYTV 254
Cdd:cd06208  184 LYDDELEKYPKQYPDNFRIDYAF 206
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 61-240 1.06e-07

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: 51.10  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  61 LIEKENLSHDTRRFRFGLPSKQHVLglPvGQHihliATIDNELII--RPYTPISSDEDVGYVDLVVKvyfkdshpKFPaG 138
Cdd:cd06190    1 LVDVRELTHDVAEFRFALDGPADFL--P-GQY----ALLALPGVEgaRAYSMANLANASGEWEFIIK--------RKP-G 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 139 GKMTQHL-EQLELGDKISFRGPSGRlqylgngtfsiKKLRKDppkhvTAKRVNMIAGGTGITPMLQLAREVLKRSDKDKT 217
Cdd:cd06190   65 GAASNALfDNLEPGDELELDGPYGL-----------AYLRPD-----EDRDIVCIAGGSGLAPMLSILRGAARSPYLSDR 128

                        170       180
                 ....*....|....*....|...
gi 281366099 218 ELALLFANQSEKDILLRAELDEL 240
Cdd:cd06190  129 PVDLFYGGRTPSDLCALDELSAL 151
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 61-261 1.15e-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: 51.17  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  61 LIEKENLSHDTRRFRFGLPSKQHvLGLPvGQHIHLIATIDNELIIRPYTPISSDEDVGYVDLVVKVyfkdshpkfpaGGK 140
Cdd:cd06192    1 IVKKEQLEPNLVLLTIKAPLAAR-LFRP-GQFVFLRNFESPGLERIPLSLAGVDPEEGTISLLVEI-----------RGP 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 141 MTQHLEQLELGDKISFRGPsgrlqyLGNGTFSIKKlrkdppkhvtAKRVNMIAGGTGITPMLQLAREVLKRSDKDKTela 220
Cdd:cd06192   68 KTKLIAELKPGEKLDVMGP------LGNGFEGPKK----------GGTVLLVAGGIGLAPLLPIAKKLAANGNKVTV--- 128

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 281366099 221 lLFANQSEKDILLRAELDELAQKHPdqfkiwYTVDKANEGE 261
Cdd:cd06192  129 -LAGAKKAKEEFLDEYFELPADVEI------WTTDDGELGL 162
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 101-245 1.39e-07

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: 51.54  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 101 NELIIRPYTPISSDEDVGYVDLVVKVYF-KDSHPKFPAGgKMTQHLEQLELGDKISFRGPsgrlqYlgnGTFSIKKlrkd 179
Cdd:cd06188   82 DEPVSRAYSLANYPAEEGELKLNVRIATpPPGNSDIPPG-IGSSYIFNLKPGDKVTASGP-----F---GEFFIKD---- 148

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281366099 180 ppkhvTAKRVNMIAGGTGITPMLQLAREVLKRsDKDKTELALLFANQSEKDILLRAELDELAQKHP 245
Cdd:cd06188  149 -----TDREMVFIGGGAGMAPLRSHIFHLLKT-LKSKRKISFWYGARSLKELFYQEEFEALEKEFP 208
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 63-252 4.69e-07

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: 49.02  E-value: 4.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  63 EKENLSHDTRRFRFGLPSKQhvlGLPV---GQHIHLiaTIDNELIiRPYTPISSDEDVGYVDLVVKvyfKDSHPKfpaGG 139
Cdd:cd06185    2 RIRDEAPDIRSFELEAPDGA---PLPAfepGAHIDV--HLPNGLV-RQYSLCGDPADRDRYRIAVL---REPASR---GG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 140 KMTQHlEQLELGDKISFRGPSGRLqylgngtfsikKLRKDPPKHVtakrvnMIAGGTGITPMLQLAREvLKRSDKDkteL 219
Cdd:cd06185   70 SRYMH-ELLRVGDELEVSAPRNLF-----------PLDEAARRHL------LIAGGIGITPILSMARA-LAARGAD---F 127

                        170       180       190
                 ....*....|....*....|....*....|...
gi 281366099 220 ALLFANQSEKDIllrAELDELAQKHPDQFKIWY 252
Cdd:cd06185  128 ELHYAGRSREDA---AFLDELAALPGDRVHLHF 157
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 107-243 5.07e-07

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: 49.18  E-value: 5.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 107 PYTPISSDEDVGYVDLVVKvyfkdshpkfpAGGKMTQHL-EQLELGDKISFRGPSGRLqylgngTFSIKklrkdppkhvt 185
Cdd:cd06198   43 PFTISSAPDPDGRLRFTIK-----------ALGDYTRRLaERLKPGTRVTVEGPYGRF------TFDDR----------- 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 281366099 186 AKRVNMIAGGTGITPMLQLAREVLKRSDKDKTElaLLFANQSEKDILLRAELDELAQK 243
Cdd:cd06198   95 RARQIWIAGGIGITPFLALLEALAARGDARPVT--LFYCVRDPEDAVFLDELRALAAA 150
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 139-260 5.50e-07

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.


Pssm-ID: 99816 [Multi-domain]  Cd Length: 233  Bit Score: 49.17  E-value: 5.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 139 GKMTQHLEQLELGDKISFRGPsgrlqyLGNGtFSIKKlrkdppkhvtaKRVNMIAGGTGITPMLQLAREVLKRSDKDkte 218
Cdd:cd06220   59 GEATSALHDLKEGDKLGIRGP------YGNG-FELVG-----------GKVLLIGGGIGIAPLAPLAERLKKAADVT--- 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 281366099 219 laLLFANQSEKDILLRAELDELAqkhpdqfKIWYTVDKANEG 260
Cdd:cd06220  118 --VLLGARTKEELLFLDRLRKSD-------ELIVTTDDGSYG 150
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 61-250 1.70e-06

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: 47.65  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  61 LIEKENLSHDTRRFRFGLPskqHVLGLPVGQHIHLIATidnELIIRPYTPISSDEDVGYVDLVVKVYfkdshpkfpAGGK 140
Cdd:cd06194    1 VVSLQRLSPDVLRVRLEPD---RPLPYLPGQYVNLRRA---GGLARSYSPTSLPDGDNELEFHIRRK---------PNGA 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 141 MTQHL-EQLELGDKISFRGPSGRLQYlgngtfsikklRKDPPkhvtAKRVNMIAGGTGITPMLQLAREVLKRsdKDKTEL 219
Cdd:cd06194   66 FSGWLgEEARPGHALRLQGPFGQAFY-----------RPEYG----EGPLLLVGAGTGLAPLWGIARAALRQ--GHQGEI 128

                        170       180       190
                 ....*....|....*....|....*....|.
gi 281366099 220 ALLFANQSEKDILLRAELDELAQKHPdQFKI 250
Cdd:cd06194  129 RLVHGARDPDDLYLHPALLWLAREHP-NFRY 158
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 137-246 3.63e-06

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: 46.77  E-value: 3.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 137 AGGKMTQH-LEQLELGDKISFRGPsgrlqylgNGTFSikkLRKDPPKHVTakrvnMIAGGTGITPMLQLAREVLKRsdKD 215
Cdd:cd06189   64 PGGSFSDYvFEELKENGLVRIEGP--------LGDFF---LREDSDRPLI-----LIAGGTGFAPIKSILEHLLAQ--GS 125

                         90       100       110
                 ....*....|....*....|....*....|.
gi 281366099 216 KTELALLFANQSEKDILLRAELDELAQKHPD 246
Cdd:cd06189  126 KRPIHLYWGARTEEDLYLDELLEAWAEAHPN 156
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 65-245 3.93e-06

Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent hydroxylation of methane to methanol. This multicomponent enzyme mediates electron transfer via a hydroxylase (MMOH), a coupling protein, and a reductase which is comprised of an N-terminal [2Fe-2S] ferredoxin domain, an FAD binding subdomain, and an NADH binding subdomain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. Dioxygenases add both atom of oxygen to the substrate, while mono-oxygenases add one atom to the substrate and one atom to water.


Pssm-ID: 99806  Cd Length: 236  Bit Score: 46.57  E-value: 3.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  65 ENLSHDTRRFRFGlPSKQHVLGLPV----GQHIHLiaTIDNELIIRPYTPISSDEDVGYVDLVVKVyfkdsHPkfpaGGK 140
Cdd:cd06210   10 DRVSSNVVRLRLQ-PDDAEGAGIAAefvpGQFVEI--EIPGTDTRRSYSLANTPNWDGRLEFLIRL-----LP----GGA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 141 MTQHLEQ-LELGDKISFRGPSGRlqylgngtFSIKKlrkdppkHVTAKRVnMIAGGTGITPMLQLAREVLKRSDKDKTEl 219
Cdd:cd06210   78 FSTYLETrAKVGQRLNLRGPLGA--------FGLRE-------NGLRPRW-FVAGGTGLAPLLSMLRRMAEWGEPQEAR- 140

                        170       180
                 ....*....|....*....|....*.
gi 281366099 220 aLLFANQSEKDILLRAELDELAQKHP 245
Cdd:cd06210  141 -LFFGVNTEAELFYLDELKRLADSLP 165
PLN03116 PLN03116
ferredoxin--NADP+ reductase; Provisional
 151-257 1.31e-05

ferredoxin--NADP+ reductase; Provisional


Pssm-ID: 215586 [Multi-domain]  Cd Length: 307  Bit Score: 45.48  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 151 GDKISFRGPSGRLQYLgngtfsikklrkdpPKHVTAKRVNMIAGGTGITPMlqlaREVLKRSDKDKTE------LALLFA 224
Cdd:PLN03116 135 GDKVQITGPSGKVMLL--------------PEEDPNATHIMVATGTGIAPF----RGFLRRMFMEDVPafkfggLAWLFL 196

                         90       100       110
                 ....*....|....*....|....*....|....
gi 281366099 225 NQSEKDILLRA-ELDELAQKHPDQFKIwytvDKA 257
Cdd:PLN03116 197 GVANSDSLLYDdEFERYLKDYPDNFRY----DYA 226
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 107-214 1.31e-05

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: 44.99  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 107 PYTPISS-DEDVGYVDLVVKVYfkdshpkfpaGGKMTQHLEQLELGD------KISFRGPSGRlqylgngtfsikklrkd 179
Cdd:cd06186   46 PFTIASSpEDEQDTLSLIIRAK----------KGFTTRLLRKALKSPgggvslKVLVEGPYGS----------------- 98

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 281366099 180 PPKHV-TAKRVNMIAGGTGITPMLQLAREVLKRSDK 214
Cdd:cd06186   99 SSEDLlSYDNVLLVAGGSGITFVLPILRDLLRRSSK 134
FNR_like_2 cd06197
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ...
 62-237 1.42e-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: 45.07  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  62 IEKENLSHDTRRFRFGLPSKQHVLGLPVGQHIhliaTID--NELII-----RPYTPISSDEDVgyvdlvVKVYFKDSHPK 134
Cdd:cd06197    1 IKSEVITPTLTRFTFELSPPDVVGKWTPGQYI----TLDfsSELDSgyshmADDDPQSLNDDF------VRTFTVSSAPP 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 135 FPAG-----------GKMTQHLEQ-----LELGDKISFRGPSGrlqylgngTFSIKKLRkdppkhvTAKRVNM--IAGGT 196
Cdd:cd06197   71 HDPAtdefeitvrkkGPVTGFLFQvarrlREQGLEVPVLGVGG--------EFTLSLPG-------EGAERKMvwIAGGV 135

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 281366099 197 GITPMLQLAREVLKrSDKDKTELALLFANQSEKDILLRAEL 237
Cdd:cd06197  136 GITPFLAMLRAILS-SRNTTWDITLLWSLREDDLPLVMDTL 175
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
191-257 4.90e-05

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 42.33  E-value: 4.90e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281366099  191 MIAGGTGITPMLQLAREVLKRSDKDKTELA-LLFANQSEKDI-LLRAELDELAQKHPDQFKI------WYTVDKA 257
Cdd:pfam08030   6 LVAGGIGITPFISILKDLGNKSKKLKTKKIkFYWVVRDLSSLeWFKDVLNELEELKELNIEIhiyltgEYEAEDA 80
PRK06222 PRK06222
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
90-207 6.58e-05

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


Pssm-ID: 235747 [Multi-domain]  Cd Length: 281  Bit Score: 43.25  E-value: 6.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  90 GQHIHLIATIDNELIirPYTPISSDEDVGYVDLVVKVYfkdshpkfpagGKMTQHLEQLELGDKI-SFRGPsgrlqyLGN 168
Cdd:PRK06222  31 GQFVIVRIDEKGERI--PLTIADYDREKGTITIVFQAV-----------GKSTRKLAELKEGDSIlDVVGP------LGK 91

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 281366099 169 GTfSIKKLrkdppkhvtaKRVNMIAGGTGITPMLQLARE 207
Cdd:PRK06222  92 PS-EIEKF----------GTVVCVGGGVGIAPVYPIAKA 119
DHOD_e_trans_like1 cd06219
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 62-255 1.05e-04

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


Pssm-ID: 99815 [Multi-domain]  Cd Length: 248  Bit Score: 42.56  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  62 IEKENLSHDTRRFRFGLPskqHVLGL--PvGQHIHLIATIDNELIirPYTPISSDEDVGYVDLVVKVyfkdshpkfpaGG 139
Cdd:cd06219    4 LEKEELAPNVKLFEIEAP---LIAKKakP-GQFVIVRADEKGERI--PLTIADWDPEKGTITIVVQV-----------VG 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 140 KMTQHLEQLELGDKIS-FRGPSGRlqylgngTFSIKKLrkdppkhvtaKRVNMIAGGTGITPMLQLAREvLKRSdkdKTE 218
Cdd:cd06219   67 KSTRELATLEEGDKIHdVVGPLGK-------PSEIENY----------GTVVFVGGGVGIAPIYPIAKA-LKEA---GNR 125

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 281366099 219 LALLFANQSEKDILLRAELDELAQKHpdqfkIWYTVD 255
Cdd:cd06219  126 VITIIGARTKDLVILEDEFRAVSDEL-----IITTDD 157
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 183-247 4.39e-04

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 40.85  E-value: 4.39e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281366099 183 HVTAKRVNMIAGGTGITPMLQLAREVLKrsDKDKTELALLFANQSEKDILLRAELDELAQKHPDQ 247
Cdd:PRK10684 108 DKAEDKYLLLAAGCGVTPIMSMRRWLLK--NRPQADVQVIFNVRTPQDVIFADEWRQLKQRYPQL 170
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 88-245 8.07e-04

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: 40.01  E-value: 8.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  88 PVGQHIHLIAtiDNELIIRPYTpISS--DEDVGYVDL-VVKVYFKDSHPKFPAGGkMTQHLEQLELGDKISFRGPSGrlq 164
Cdd:cd06182   33 QPGDHLGVIP--PNPLQPRYYS-IASspDVDPGEVHLcVRVVSYEAPAGRIRKGV-CSNFLAGLQLGAKVTVFIRPA--- 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 165 ylgngtfsikkLRKDPPKHVTAKrVNMIAGGTGITPM---LQlAREVLKRSDKDKTELALLF-ANQSEKDILLRAELDEl 240
Cdd:cd06182  106 -----------PSFRLPKDPTTP-IIMVGPGTGIAPFrgfLQ-ERAALRANGKARGPAWLFFgCRNFASDYLYREELQE- 171


                 ....*
gi 281366099 241 AQKHP 245
Cdd:cd06182  172 ALKDG 176
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 139-259 9.31e-04

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 39.79  E-value: 9.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 139 GKMTQHLEQLELGDKISFRGPsgrlqyLGNGtFSIKKLRkdppkhvtAKRVNMIAGGTGITPMLQLAREVLKRSDKdKTE 218
Cdd:PRK08345  76 GRVTTVIHRLKEGDIVGVRGP------YGNG-FPVDEME--------GMDLLLIAGGLGMAPLRSVLLYAMDNRWK-YGN 139

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 281366099 219 LALLFANQSEKDILLRAELDELAqKHPDQFKIWYTVDKANE 259
Cdd:PRK08345 140 ITLIYGAKYYEDLLFYDELIKDL-AEAENVKIIQSVTRDPE 179
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 138-241 1.22e-03

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: 39.22  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 138 GGKMTQHL-EQLELGDKISFRGPSGRLqYLGNGTfsikklrkdppkhvtAKRVnMIAGGTGITPMLQLAREVlkRSDKDK 216
Cdd:cd06213   68 GGAFSGWLfGADRTGERLTVRGPFGDF-WLRPGD---------------APIL-CIAGGSGLAPILAILEQA--RAAGTK 128

                         90       100
                 ....*....|....*....|....*
gi 281366099 217 TELALLFANQSEKDILlraELDELA 241
Cdd:cd06213  129 RDVTLLFGARTQRDLY---ALDEIA 150
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 61-246 1.53e-03

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 39.47  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099  61 LIEKENLSHDTRRFRFGLPSKQHVLGLPvGQHIHLIAtidNELIIRPYTPISSDEDVGYVDLVVKVYfkdshpkfpAGGK 140
Cdd:PRK07609 107 VASLERVAGDVMRLKLRLPATERLQYLA-GQYIEFIL---KDGKRRSYSIANAPHSGGPLELHIRHM---------PGGV 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 141 MTQHL-EQLELGDKISFRGPSGrlqylgngTFSikkLRKDPPKHVTakrvnMIAGGTGITPMLQLAREVlkRSDKDKTEL 219
Cdd:PRK07609 174 FTDHVfGALKERDILRIEGPLG--------TFF---LREDSDKPIV-----LLASGTGFAPIKSIVEHL--RAKGIQRPV 235

                        170       180
                 ....*....|....*....|....*..
gi 281366099 220 ALLFANQSEKDILLRAELDELAQKHPD 246
Cdd:PRK07609 236 TLYWGARRPEDLYLSALAEQWAEELPN 262
PRK05802 PRK05802
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
109-214 2.52e-03

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


Pssm-ID: 235613 [Multi-domain]  Cd Length: 320  Bit Score: 38.42  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 109 TPIS---SDEDVGYVDLVVKVyfkdSHPKfpaggkmTQHLEQLELGDKISFRGPsgrlqyLGNGTFSIKKLrkdppKHVT 185
Cdd:PRK05802 114 VPISimeADTEENIIKVAIEI----RGVK-------TKKIAKLNKGDEILLRGP------YWNGILGLKNI-----KSTK 171

                         90       100
                 ....*....|....*....|....*....
gi 281366099 186 AKRVNMIAGGTGITPMLQLAREVLKRSDK 214
Cdd:PRK05802 172 NGKSLVIARGIGQAPGVPVIKKLYSNGNK 200
bifunctional_CYPOR cd06206
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ...
 106-242 2.74e-03

These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase (CYPOR). NADPH cytochrome p450 reductase 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: 99802 [Multi-domain]  Cd Length: 384  Bit Score: 38.78  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 106 RPYTpISSD--EDVGYVDLVVKVYfkdSHPKFPAGGKM----TQHLEQLELGDKISFR-GPSgrlqylgNGTFsikKLRK 178
Cdd:cd06206  162 RQYS-ISSSplVDPGHATLTVSVL---DAPALSGQGRYrgvaSSYLSSLRPGDSIHVSvRPS-------HSAF---RPPS 227

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281366099 179 DPpkhvtAKRVNMIAGGTGITPMLQLARE-VLKRSDKDKTELALLFA--NQSEKDILLRAELDELAQ 242
Cdd:cd06206  228 DP-----STPLIMIAAGTGLAPFRGFLQErAALLAQGRKLAPALLFFgcRHPDHDDLYRDELEEWEA 289
PRK13289 PRK13289
NO-inducible flavohemoprotein;
137-252 4.06e-03

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 38.24  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366099 137 AGGKMTQHL-EQLELGDKISFRGPSGrlqylgngTFSIKklrkdppkHVTAKRVNMIAGGTGITPMLQLarevLKRSDKD 215
Cdd:PRK13289 227 AGGKVSNYLhDHVNVGDVLELAAPAG--------DFFLD--------VASDTPVVLISGGVGITPMLSM----LETLAAQ 286

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 281366099 216 KTELALLF--ANQSEKDILLRAELDELAQKHPdQFK--IWY 252
Cdd:PRK13289 287 QPKRPVHFihAARNGGVHAFRDEVEALAARHP-NLKahTWY 326
 
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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