NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|4930119]
View 

Protein Classification

PLN03115 family protein (domain architecture ID 11477437)

PLN03115 family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
1-307 0e+00

ferredoxin--NADP(+) reductase; Provisional


:

Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 655.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119     1 QVTT----EAPAKVVKHSKKQDENIVVNKFKPKEPYVGRCLLNTKITGDDAPGETWHMVFSTEGEVPYREGQSIGIVPDG 76
Cdd:PLN03115  56 QVTTetttEAPAKVVKVSKKNEEGVVVNKFRPKEPYTGRCLLNTKITGDDAPGETWHMVFSTEGEIPYREGQSIGVIPDG 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119    77 IDKNGKPHKLRLYSIASSAIGDFGDSKTVSLCVKRLVYTNDAGEVVKGVCSNFLCDLKPGSEVKITGPVGKEMLMPKDPN 156
Cdd:PLN03115 136 IDKNGKPHKLRLYSIASSALGDFGDSKTVSLCVKRLVYTNDQGEIVKGVCSNFLCDLKPGAEVKITGPVGKEMLMPKDPN 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   157 ATVIMLGTGTGIAPFRSFLWKMFFEKHEDYQFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQVNDKG 236
Cdd:PLN03115 216 ATIIMLATGTGIAPFRSFLWKMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQTNAKG 295
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4930119   237 EKMYIQTRMAQYAEELWELLKKDNTFVYMCGLKGMEKGIDDIMVSLAAKDGIDWIEYKRTLKKAEQWNVEV 307
Cdd:PLN03115 296 EKMYIQTRMAEYAEELWELLKKDNTYVYMCGLKGMEKGIDDIMVSLAAKDGIDWFEYKKQLKKAEQWNVEV 366
 
Name Accession Description Interval E-value
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
1-307 0e+00

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 655.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119     1 QVTT----EAPAKVVKHSKKQDENIVVNKFKPKEPYVGRCLLNTKITGDDAPGETWHMVFSTEGEVPYREGQSIGIVPDG 76
Cdd:PLN03115  56 QVTTetttEAPAKVVKVSKKNEEGVVVNKFRPKEPYTGRCLLNTKITGDDAPGETWHMVFSTEGEIPYREGQSIGVIPDG 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119    77 IDKNGKPHKLRLYSIASSAIGDFGDSKTVSLCVKRLVYTNDAGEVVKGVCSNFLCDLKPGSEVKITGPVGKEMLMPKDPN 156
Cdd:PLN03115 136 IDKNGKPHKLRLYSIASSALGDFGDSKTVSLCVKRLVYTNDQGEIVKGVCSNFLCDLKPGAEVKITGPVGKEMLMPKDPN 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   157 ATVIMLGTGTGIAPFRSFLWKMFFEKHEDYQFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQVNDKG 236
Cdd:PLN03115 216 ATIIMLATGTGIAPFRSFLWKMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQTNAKG 295
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4930119   237 EKMYIQTRMAQYAEELWELLKKDNTFVYMCGLKGMEKGIDDIMVSLAAKDGIDWIEYKRTLKKAEQWNVEV 307
Cdd:PLN03115 296 EKMYIQTRMAEYAEELWELLKKDNTYVYMCGLKGMEKGIDDIMVSLAAKDGIDWFEYKKQLKKAEQWNVEV 366
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
24-307 1.12e-173

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: 481.82  E-value: 1.12e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   24 NKFKPKEPYVGRCLLNTKITGDDAPGETWHMVFSTEGEVPYREGQSIGIVPDGID-KNGKPHKLRLYSIASSAIGDFGDS 102
Cdd:cd06208   1 NLYKPKNPLIGKVVSNTRLTGPDAPGEVCHIVIDHGGKLPYLEGQSIGIIPPGTDaKNGKPHKLRLYSIASSRYGDDGDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  103 KTVSLCVKRLVYTNDAG-EVVKGVCSNFLCDLKPGSEVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLWKMFFE 181
Cdd:cd06208  81 KTLSLCVKRLVYTDPETdETKKGVCSNYLCDLKPGDDVQITGPVGKTMLLPEDPNATLIMIATGTGIAPFRSFLRRLFRE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  182 KHEDYQFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQVNDKGEKMYIQTRMAQYAEELWELLKKDNT 261
Cdd:cd06208 161 KHADYKFTGLAWLFFGVPNSDSLLYDDELEKYPKQYPDNFRIDYAFSREQKNADGGKMYVQDRIAEYAEEIWNLLDKDNT 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 4930119  262 FVYMCGLKGMEKGIDDIMVSLaAKDGIDWIEYKRTLKKAEQWNVEV 307
Cdd:cd06208 241 HVYICGLKGMEPGVDDALTSV-AEGGLAWEEFWESLKKKGRWHVEV 285
benzo_boxA TIGR03224
benzoyl-CoA oxygenase/reductase, BoxA protein; Members of this protein family are BoxA, the A ...
23-306 3.28e-61

benzoyl-CoA oxygenase/reductase, BoxA protein; Members of this protein family are BoxA, the A component of the BoxAB benzoyl-CoA oxygenase/reductase. This oxygen-requiring enzyme acts in an aerobic pathway of benzoate catabolism via coenzyme A ligation. BoxA is a homodimeric iron-sulphur-flavoprotein and acts as an NADPH-dependent reductase for BoxB. [Energy metabolism, Other]


Pssm-ID: 132268 [Multi-domain]  Cd Length: 411  Bit Score: 199.72  E-value: 3.28e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119     23 VNKFKPKEPYVGRCLLNTKITGDDAPGETWHMVFSTeGEVPYR--EGQSIGIVPDGIDKNGKPHKLRLYSIASSAIGDFG 100
Cdd:TIGR03224 134 VNLYGVKAPITATVVGNYRLTDEDASSDIHHIVLDF-GSHPFPvlEGQSIGILPPGTDASGKPHYARMYSVASPRNGERP 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119    101 DSKTVSLCVKRlVYTNDAGEVVKGVCSNFLCDLKPGSEVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLWKMff 180
Cdd:TIGR03224 213 GYNNLALTVKR-VTTDHQGNAVRGVASNYLCDLKKGDKVQVIGPFGSTFLMPNHPESSIMMICTGTGSAPMRAMTERR-- 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119    181 EKHEDYQFNGLAWLFLGVPTSSSLLYKEEFEKMkekaPENF-RLDFAVSReqvnDKGE-KMYIQTRMAQYAEELWELLKK 258
Cdd:TIGR03224 290 RRRRDHGEGGKLMLFFGARTKEELPYFGPLQKL----PKDFiDINFAFSR----TPEQpKRYVQDAIRERAADVAALLKD 361
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 4930119    259 DNTFVYMCGLKGMEKGIDDIMVSLAAKDGIDWIEYKRTLKKAEQWNVE 306
Cdd:TIGR03224 362 PNTYIYICGLKGMEEGVLDAFRDVCATNGLSWETLEPRLRAEGRLHLE 409
CysJ COG0369
Sulfite reductase, alpha subunit (flavoprotein) [Inorganic ion transport and metabolism];
65-307 7.67e-59

Sulfite reductase, alpha subunit (flavoprotein) [Inorganic ion transport and metabolism];


Pssm-ID: 223446 [Multi-domain]  Cd Length: 587  Bit Score: 198.03  E-value: 7.67e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   65 REGQSIGIVPDGIDKNGKPHKLRLYSIASSAIGDFgdsKTVSLCVKRLVYTNDAGEVvKGVCSNFLCDLKP-GSEVKITG 143
Cdd:COG0369 352 RDFPPAKLPAEELIDLLPPLKPRLYSIASSPGVSP---DEVHLTVGVVRYQAEGRER-YGVCSGYLADLLEeGDTIPVFV 427
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  144 PVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLWKMFFEKHEdyqfnGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRL 223
Cdd:COG0369 428 QPNKNFRLPEDPETPIIMIGPGTGIAPFRAFVQERAANGAE-----GKNWLFFGCRHFTEDFLYQEEWEEYLKDGVLTRL 502
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  224 DFAVSREQvndkGEKMYIQTRMAQYAEELWELLkKDNTFVYMCG-LKGMEKGIDDIMVSLAAKDG----IDWIEYKRTLK 298
Cdd:COG0369 503 DLAFSRDQ----EEKIYVQDRLREQADELWEWL-EEGAHIYVCGdAKGMAKDVEEALLDILAKEGglsrEEAEEYLKELK 577

                ....*....
gi 4930119  299 KAEQWNVEV 307
Cdd:COG0369 578 KEGRYQRDV 586
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
161-276 2.91e-31

Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.


Pssm-ID: 333901  Cd Length: 108  Bit Score: 112.72  E-value: 2.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119    161 MLGTGTGIAPFRSFLWKMFfekhEDYQFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQVNDKGEKMY 240
Cdd:pfam00175   1 MIAGGTGITPVRSVLRAVL----EDPDDPTQVWLVFGNRNEDDILYREELDELAAKYPGRLRVVYVVSRPEAGWTGGKGY 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 4930119    241 IQTRMAQYAEElwelLKKDNTFVYMCGLKGMEKGID 276
Cdd:pfam00175  77 VQDAVLEDHLS----LPDEETHVYVCGPPGMIKAVR 108
 
Name Accession Description Interval E-value
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
1-307 0e+00

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 655.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119     1 QVTT----EAPAKVVKHSKKQDENIVVNKFKPKEPYVGRCLLNTKITGDDAPGETWHMVFSTEGEVPYREGQSIGIVPDG 76
Cdd:PLN03115  56 QVTTetttEAPAKVVKVSKKNEEGVVVNKFRPKEPYTGRCLLNTKITGDDAPGETWHMVFSTEGEIPYREGQSIGVIPDG 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119    77 IDKNGKPHKLRLYSIASSAIGDFGDSKTVSLCVKRLVYTNDAGEVVKGVCSNFLCDLKPGSEVKITGPVGKEMLMPKDPN 156
Cdd:PLN03115 136 IDKNGKPHKLRLYSIASSALGDFGDSKTVSLCVKRLVYTNDQGEIVKGVCSNFLCDLKPGAEVKITGPVGKEMLMPKDPN 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   157 ATVIMLGTGTGIAPFRSFLWKMFFEKHEDYQFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQVNDKG 236
Cdd:PLN03115 216 ATIIMLATGTGIAPFRSFLWKMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQTNAKG 295
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4930119   237 EKMYIQTRMAQYAEELWELLKKDNTFVYMCGLKGMEKGIDDIMVSLAAKDGIDWIEYKRTLKKAEQWNVEV 307
Cdd:PLN03115 296 EKMYIQTRMAEYAEELWELLKKDNTYVYMCGLKGMEKGIDDIMVSLAAKDGIDWFEYKKQLKKAEQWNVEV 366
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
24-307 1.12e-173

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: 481.82  E-value: 1.12e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   24 NKFKPKEPYVGRCLLNTKITGDDAPGETWHMVFSTEGEVPYREGQSIGIVPDGID-KNGKPHKLRLYSIASSAIGDFGDS 102
Cdd:cd06208   1 NLYKPKNPLIGKVVSNTRLTGPDAPGEVCHIVIDHGGKLPYLEGQSIGIIPPGTDaKNGKPHKLRLYSIASSRYGDDGDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  103 KTVSLCVKRLVYTNDAG-EVVKGVCSNFLCDLKPGSEVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLWKMFFE 181
Cdd:cd06208  81 KTLSLCVKRLVYTDPETdETKKGVCSNYLCDLKPGDDVQITGPVGKTMLLPEDPNATLIMIATGTGIAPFRSFLRRLFRE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  182 KHEDYQFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQVNDKGEKMYIQTRMAQYAEELWELLKKDNT 261
Cdd:cd06208 161 KHADYKFTGLAWLFFGVPNSDSLLYDDELEKYPKQYPDNFRIDYAFSREQKNADGGKMYVQDRIAEYAEEIWNLLDKDNT 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 4930119  262 FVYMCGLKGMEKGIDDIMVSLaAKDGIDWIEYKRTLKKAEQWNVEV 307
Cdd:cd06208 241 HVYICGLKGMEPGVDDALTSV-AEGGLAWEEFWESLKKKGRWHVEV 285
PLN03116 PLN03116
ferredoxin--NADP+ reductase; Provisional
23-307 3.74e-131

ferredoxin--NADP+ reductase; Provisional


Pssm-ID: 215586 [Multi-domain]  Cd Length: 307  Bit Score: 374.82  E-value: 3.74e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119    23 VNKFKPKEPYVGRCLLNTKITGDDAPGETWHMVFSTEGEVPYREGQSIGIVPDGID--KNGKPHKLRLYSIASSAIGDFG 100
Cdd:PLN03116  16 LNLYKPKAPYTATIVSVERIVGPKAPGETCHIVIDHGGNVPYWEGQSYGVIPPGTNpkKPGAPHNVRLYSIASTRYGDDF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   101 DSKTVSLCVKRLVY----TNDAGEVVKGVCSNFLCDLKPGSEVKITGPVGKEMLMP-KDPNATVIMLGTGTGIAPFRSFL 175
Cdd:PLN03116  96 DGKTASLCVRRAVYydpeTGKEDPAKKGVCSNFLCDAKPGDKVQITGPSGKVMLLPeEDPNATHIMVATGTGIAPFRGFL 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   176 WKMFFEKHEDYQFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQVNDKGEKMYIQTRMAQYAEELWEL 255
Cdd:PLN03116 176 RRMFMEDVPAFKFGGLAWLFLGVANSDSLLYDDEFERYLKDYPDNFRYDYALSREQKNKKGGKMYVQDKIEEYSDEIFKL 255
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4930119   256 LkKDNTFVYMCGLKGMEKGIDDIMVSLAAKDGIDWIEYKRTLKKAEQWNVEV 307
Cdd:PLN03116 256 L-DNGAHIYFCGLKGMMPGIQDTLKRVAEERGESWEEKLSGLKKNKQWHVEV 306
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
35-307 2.63e-94

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: 279.99  E-value: 2.63e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   35 RCLLNTKITGDDAPGETWHMVFST--EGEVPYREGQSIGIVPDGidkngkPHKLRLYSIASSAIGDfgdSKTVSLCVKRL 112
Cdd:cd06182   1 AITVNRKLTPPDSPRSTRHLEFDLsgNSVLKYQPGDHLGVIPPN------PLQPRYYSIASSPDVD---PGEVHLCVRVV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  113 VYTNDAGEVVKGVCSNFLCDLKPGSEVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLWKMFFEKHeDYQFNGLA 192
Cdd:cd06182  72 SYEAPAGRIRKGVCSNFLAGLQLGAKVTVFIRPAPSFRLPKDPTTPIIMVGPGTGIAPFRGFLQERAALRA-NGKARGPA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  193 WLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQvndKGEKMYIQTRMAQYAEELWELLKKDNtFVYMCG-LKGM 271
Cdd:cd06182 151 WLFFGCRNFASDYLYREELQEALKDGALTRLDVAFSREQ---AEPKVYVQDKLKEHAEELRRLLNEGA-HIYVCGdAKSM 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 4930119  272 EKGIDDIMVSLAAK----DGIDWIEYKRTLKKAEQWNVEV 307
Cdd:cd06182 227 AKDVEDALVKIIAKaggvDESDAEEYLKELEDEGRYVEDV 266
benzo_boxA TIGR03224
benzoyl-CoA oxygenase/reductase, BoxA protein; Members of this protein family are BoxA, the A ...
23-306 3.28e-61

benzoyl-CoA oxygenase/reductase, BoxA protein; Members of this protein family are BoxA, the A component of the BoxAB benzoyl-CoA oxygenase/reductase. This oxygen-requiring enzyme acts in an aerobic pathway of benzoate catabolism via coenzyme A ligation. BoxA is a homodimeric iron-sulphur-flavoprotein and acts as an NADPH-dependent reductase for BoxB. [Energy metabolism, Other]


Pssm-ID: 132268 [Multi-domain]  Cd Length: 411  Bit Score: 199.72  E-value: 3.28e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119     23 VNKFKPKEPYVGRCLLNTKITGDDAPGETWHMVFSTeGEVPYR--EGQSIGIVPDGIDKNGKPHKLRLYSIASSAIGDFG 100
Cdd:TIGR03224 134 VNLYGVKAPITATVVGNYRLTDEDASSDIHHIVLDF-GSHPFPvlEGQSIGILPPGTDASGKPHYARMYSVASPRNGERP 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119    101 DSKTVSLCVKRlVYTNDAGEVVKGVCSNFLCDLKPGSEVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLWKMff 180
Cdd:TIGR03224 213 GYNNLALTVKR-VTTDHQGNAVRGVASNYLCDLKKGDKVQVIGPFGSTFLMPNHPESSIMMICTGTGSAPMRAMTERR-- 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119    181 EKHEDYQFNGLAWLFLGVPTSSSLLYKEEFEKMkekaPENF-RLDFAVSReqvnDKGE-KMYIQTRMAQYAEELWELLKK 258
Cdd:TIGR03224 290 RRRRDHGEGGKLMLFFGARTKEELPYFGPLQKL----PKDFiDINFAFSR----TPEQpKRYVQDAIRERAADVAALLKD 361
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 4930119    259 DNTFVYMCGLKGMEKGIDDIMVSLAAKDGIDWIEYKRTLKKAEQWNVE 306
Cdd:TIGR03224 362 PNTYIYICGLKGMEEGVLDAFRDVCATNGLSWETLEPRLRAEGRLHLE 409
CysJ COG0369
Sulfite reductase, alpha subunit (flavoprotein) [Inorganic ion transport and metabolism];
65-307 7.67e-59

Sulfite reductase, alpha subunit (flavoprotein) [Inorganic ion transport and metabolism];


Pssm-ID: 223446 [Multi-domain]  Cd Length: 587  Bit Score: 198.03  E-value: 7.67e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   65 REGQSIGIVPDGIDKNGKPHKLRLYSIASSAIGDFgdsKTVSLCVKRLVYTNDAGEVvKGVCSNFLCDLKP-GSEVKITG 143
Cdd:COG0369 352 RDFPPAKLPAEELIDLLPPLKPRLYSIASSPGVSP---DEVHLTVGVVRYQAEGRER-YGVCSGYLADLLEeGDTIPVFV 427
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  144 PVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLWKMFFEKHEdyqfnGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRL 223
Cdd:COG0369 428 QPNKNFRLPEDPETPIIMIGPGTGIAPFRAFVQERAANGAE-----GKNWLFFGCRHFTEDFLYQEEWEEYLKDGVLTRL 502
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  224 DFAVSREQvndkGEKMYIQTRMAQYAEELWELLkKDNTFVYMCG-LKGMEKGIDDIMVSLAAKDG----IDWIEYKRTLK 298
Cdd:COG0369 503 DLAFSRDQ----EEKIYVQDRLREQADELWEWL-EEGAHIYVCGdAKGMAKDVEEALLDILAKEGglsrEEAEEYLKELK 577

                ....*....
gi 4930119  299 KAEQWNVEV 307
Cdd:COG0369 578 KEGRYQRDV 586
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
50-292 1.22e-38

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: 135.65  E-value: 1.22e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   50 ETWHMVFSTEGEVPYREGQSIGIVPDGIDKngkpHKLRLYSIASSAigdfGDSKTVSLCVKRlvytndageVVKGVCSNF 129
Cdd:cd00322   9 DVRLFRLQLPNGFSFKPGQYVDLHLPGDGR----GLRRAYSIASSP----DEEGELELTVKI---------VPGGPFSAW 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  130 LCDLKPGSEVKITGPVGKEMLmPKDPNATVIMLGTGTGIAPFRSFLWKMFFEKHedyqfNGLAWLFLGVPTSSSLLYKEE 209
Cdd:cd00322  72 LHDLKPGDEVEVSGPGGDFFL-PLEESGPVVLIAGGIGITPFRSMLRHLAADKP-----GGEITLLYGARTPADLLFLDE 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  210 FEKMKEKAPeNFRLDFAVSREQVNDKGEkmyiQTRMAQYAEELWELLKKDNTFVYMCGLKGMEKGIDDIMVSLAAKDGID 289
Cdd:cd00322 146 LEELAKEGP-NFRLVLALSRESEAKLGP----GGRIDREAEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPEERI 220

                ...
gi 4930119  290 WIE 292
Cdd:cd00322 221 HTE 223
SiR cd06199
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
87-287 7.40e-34

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.


Pssm-ID: 99796 [Multi-domain]  Cd Length: 360  Bit Score: 126.57  E-value: 7.40e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   87 RLYSIASS--AIGDfgdskTVSLCVKRLVYTNdAGEVVKGVCSNFLCD-LKPGSEVKITGPVGKEMLMPKDPNATVIMLG 163
Cdd:cd06199 147 RLYSIASSpkAVPD-----EVHLTVAVVRYES-HGRERKGVASTFLADrLKEGDTVPVFVQPNPHFRLPEDPDAPIIMVG 220
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  164 TGTGIAPFRSFL------------WkMFF-EKHED----YQFNGLAWLFLGVPTsssllykeefekmkekapenfRLDFA 226
Cdd:cd06199 221 PGTGIAPFRAFLqereatgakgknW-LFFgERHFAtdflYQDELQQWLKDGVLT---------------------RLDTA 278
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4930119  227 VSREQVndkgEKMYIQTRMAQYAEELWELLKKDNTFvYMCG-LKGMEKGIDDIMVSLAAKDG 287
Cdd:cd06199 279 FSRDQA----EKVYVQDRMREQGAELWAWLEEGAHF-YVCGdAKRMAKDVDAALLDIIATEG 335
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
161-276 2.91e-31

Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.


Pssm-ID: 333901  Cd Length: 108  Bit Score: 112.72  E-value: 2.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119    161 MLGTGTGIAPFRSFLWKMFfekhEDYQFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQVNDKGEKMY 240
Cdd:pfam00175   1 MIAGGTGITPVRSVLRAVL----EDPDDPTQVWLVFGNRNEDDILYREELDELAAKYPGRLRVVYVVSRPEAGWTGGKGY 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 4930119    241 IQTRMAQYAEElwelLKKDNTFVYMCGLKGMEKGID 276
Cdd:pfam00175  77 VQDAVLEDHLS----LPDEETHVYVCGPPGMIKAVR 108
CyPoR_like cd06207
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
87-307 8.23e-31

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: 99803 [Multi-domain]  Cd Length: 382  Bit Score: 118.92  E-value: 8.23e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   87 RLYSIASSAIGDfgdSKTVSLCVKRLVYTNDAGEVVKGVCSNFLCDLKPGSEVKITGPVGKeMLMPKDPNATVIMLGTGT 166
Cdd:cd06207 165 RYYSISSSPLKN---PNEVHLLVSLVSWKTPSGRSRYGLCSSYLAGLKVGQRVTVFIKKSS-FKLPKDPKKPIIMVGPGT 240
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  167 GIAPFRSFL-WKMFFEKHEdyQFNGLAWLFLGVPT-SSSLLYKEEFEKMKEKAPENfRLDFAVSREQvndkGEKMYIQTR 244
Cdd:cd06207 241 GLAPFRAFLqERAALLAQG--PEIGPVLLYFGCRHeDKDYLYKEELEEYEKSGVLT-TLGTAFSRDQ----PKKVYVQDL 313
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4930119  245 MAQYAEELWELLKKDNTFVYMCG-----LKGMEKGIDDIMVSLAAKDGIDWIEYKRTLKKAEQWNVEV 307
Cdd:cd06207 314 IRENSDLVYQLLEEGAGVIYVCGstwkmPPDVQEAFEEILKKHGGGDEELAEKKIEELEERGRYVVEA 381
PRK06214 PRK06214
sulfite reductase; Provisional
83-307 7.27e-30

sulfite reductase; Provisional


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 118.25  E-value: 7.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119    83 PHKLRLYSIASSAIGDFGdskTVSLCVKRLVYTNdAGEVVKGVCSNFLCD-LKPGSEVKITGPVGKEMLMPKDPNATVIM 161
Cdd:PRK06214 313 PLQPRLYSISSSPKATPG---RVSLTVDAVRYEI-GSRLRLGVASTFLGErLAPGTRVRVYVQKAHGFALPADPNTPIIM 388
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   162 LGTGTGIAPFRSFLWkmffEKHEdYQFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSReqvnDKGEKMYI 241
Cdd:PRK06214 389 VGPGTGIAPFRAFLH----ERAA-TKAPGRNWLFFGHQRSATDFFYEDELNGLKAAGVLTRLSLAWSR----DGEEKTYV 459
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4930119   242 QTRMAQYAEELWELLKKDNTFvYMCG-LKGMEKGIDDIMVSLAAKDGI----DWIEYKRTLKKAEQWNVEV 307
Cdd:PRK06214 460 QDRMRENGAELWKWLEEGAHF-YVCGdAKRMAKDVERALVDIVAQFGGrspdEAVAFVAELKKAGRYQADV 529
cysJ TIGR01931
sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an ...
82-287 3.12e-27

sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an NADPH-dependent sulfite reductase flavoprotein subunit. Most members of this family are found in Cys biosynthesis gene clusters. The closest homologs below the trusted cutoff are designated as subunits nitrate reductase.


Pssm-ID: 273882 [Multi-domain]  Cd Length: 597  Bit Score: 110.94  E-value: 3.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119     82 KPHKLRLYSIASS--AIGDfgdskTVSLCVKRLVYTNDaGEVVKGVCSNFLCD-LKPGSEVKITGPVGKEMLMPKDPNAT 158
Cdd:TIGR01931 379 RPLTPRLYSISSSqsEVGD-----EVHLTVGVVRYQAH-GRARLGGASGFLAErLKEGDTVPVYIEPNDNFRLPEDPDTP 452
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119    159 VIMLGTGTGIAPFRSFLwkmffEKHEDYQFNGLAWLFLGVPT-SSSLLYKEEFekmkekapENF-------RLDFAVSRe 230
Cdd:TIGR01931 453 IIMIGPGTGVAPFRAFM-----QERAEDGAKGKNWLFFGNPHfTTDFLYQVEW--------QNYlkkgvltKMDLAFSR- 518
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 4930119    231 qvnDKGEKMYIQTRMAQYAEELWELLkKDNTFVYMCG-LKGMEKGIDDIMVSLAAKDG 287
Cdd:TIGR01931 519 ---DQAEKIYVQHRIREQGAELWQWL-QEGAHIYVCGdAKKMAKDVHQALLDIIAKEG 572
CYPOR cd06204
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
87-303 1.93e-24

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: 99801 [Multi-domain]  Cd Length: 416  Bit Score: 101.95  E-value: 1.93e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   87 RLYSIASSaigdfgdSKT----VSLCVKRLVYTNDAGEVVKGVCSNFLCDLKPgSEVKITGPVGKEML------------ 150
Cdd:cd06204 179 RYYSISSS-------SKVhpnrIHITAVVVKYPTPTGRIIKGVATNWLLALKP-ALNGEKPPTPYYLSgprkkgggskvp 250
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  151 ---------MPKDPNATVIMLGTGTGIAPFRSFL-----WKmffEKHEDYqfnGLAWLFLGVPTSSS-LLYKEEFEKMKE 215
Cdd:cd06204 251 vfvrrsnfrLPTKPSTPVIMIGPGTGVAPFRGFIqeraaLK---ESGKKV---GPTLLFFGCRHPDEdFIYKDELEEYAK 324
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  216 KApENFRLDFAVSREQvndkGEKMYIQTRMAQYAEELWELLKKDnTFVYMCG-LKGMEKGIDDIMVSLAAKDGidwieyK 294
Cdd:cd06204 325 LG-GLLELVTAFSREQ----PKKVYVQHRLAEHAEQVWELINEG-AYIYVCGdAKNMARDVEKTLLEILAEQG------G 392

                ....*....
gi 4930119  295 RTLKKAEQW 303
Cdd:cd06204 393 MTETEAEEY 401
bifunctional_CYPOR cd06206
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ...
83-303 1.88e-22

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: 95.79  E-value: 1.88e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   83 PHKLRLYSIASSAigdFGDSKTVSLCVKRLVYTNDAGEV-VKGVCSNFLCDLKPGSEVKIT-GPVGKEMLMPKDPNATVI 160
Cdd:cd06206 158 PMRPRQYSISSSP---LVDPGHATLTVSVLDAPALSGQGrYRGVASSYLSSLRPGDSIHVSvRPSHSAFRPPSDPSTPLI 234
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  161 MLGTGTGIAPFRSFLWKMfFEKHEDYQFNGLAWLFLGV--PTSSSlLYKeefekmkekapENFR---------LDFAVSR 229
Cdd:cd06206 235 MIAAGTGLAPFRGFLQER-AALLAQGRKLAPALLFFGCrhPDHDD-LYR-----------DELEeweaagvvsVRRAYSR 301
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4930119  230 eqVNDKGEKmYIQTRMAQYAEELWELLKKDNTfVYMCGLKGMEKGIDDIMVSLAAKdgIDWIEYKRTLKKAEQW 303
Cdd:cd06206 302 --PPGGGCR-YVQDRLWAEREEVWELWEQGAR-VYVCGDGRMAPGVREVLKRIYAE--KDERGGGSDDEEAEEW 369
methionine_synthase_red cd06203
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ...
87-307 2.30e-21

Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for the regeneration of methionine from homocysteine, as well as the coversion of methyltetrahydrofolate to tetrahydrofolate. In MSR, electrons are transferred from NADPH to FAD to FMN to cob(II)alamin. MSR resembles proteins of the cytochrome p450 family including nitric oxide synthase, the alpha subunit of sulfite reductase, but contains an extended hinge region. 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. CYPORs resemble ferredoxin reductase (FNR) but have a connecting subdomain inserted within the flavin binding region, which helps orient the FMN binding doamin with the FNR module. 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: 99800 [Multi-domain]  Cd Length: 398  Bit Score: 92.77  E-value: 2.30e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   87 RLYSIASSAIGDFGdskTVSLCVKRLvytndaGEVVKGVCSNFLCDLKpGSEVKITGPVGKEM-------LMPKDPNATV 159
Cdd:cd06203 175 RPYSIASSPLEGPG---KLRFIFSVV------EFPAKGLCTSWLESLC-LSASSHGVKVPFYLrsssrfrLPPDDLRRPI 244
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  160 IMLGTGTGIAPFRSFL--WKMFFEKHEDYQFnGLAWLFLGVPTSS-SLLYKEEFEKMKEKAPENfRLDFAVSREQvNDKG 236
Cdd:cd06203 245 IMVGPGTGVAPFLGFLqhREKLKESHTETVF-GEAWLFFGCRHRDrDYLFRDELEEFLEEGILT-RLIVAFSRDE-NDGS 321
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4930119  237 EKMYIQTRMAQYAEELWELLKKDNTFVYMCG-LKGMEKGIDDIMVSLAAK----DGIDWIEYKRTLKKAEQWNVEV 307
Cdd:cd06203 322 TPKYVQDKLEERGKKLVDLLLNSNAKIYVCGdAKGMAKDVRDTFVDILSKelglDKLEAKKLLARLRKEDRYLEDV 397
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
53-279 1.70e-18

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  Cd Length: 241  Bit Score: 82.61  E-value: 1.70e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   53 HMVFSTEGEV--PYREGQ--SIGIVPDgidkNGKPhKLRLYSIASSAigdfgDSKTVSlcvkrlVYtndAGEVVKGVCSN 128
Cdd:cd06195  12 LFSFRVTRDIpfRFQAGQftKLGLPND----DGKL-VRRAYSIASAP-----YEENLE------FY---IILVPDGPLTP 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  129 FLCDLKPGSEVKIT-GPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLWkmffEKHEDYQFNGLAwLFLGVPTSSSLLYK 207
Cdd:cd06195  73 RLFKLKPGDTIYVGkKPTGFLTLDEVPPGKRLWLLATGTGIAPFLSMLR----DLEIWERFDKIV-LVHGVRYAEELAYQ 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4930119  208 EEFEKMKEKAPENFRLDFAVSREQVNdKGEKMYIQTRMAQ-YAEELWEL-LKKDNTFVYMCGLKGMekgIDDIM 279
Cdd:cd06195 148 DEIEALAKQYNGKFRYVPIVSREKEN-GALTGRIPDLIESgELEEHAGLpLDPETSHVMLCGNPQM---IDDTQ 217
cysJ PRK10953
sulfite reductase subunit alpha; Provisional
87-287 9.89e-18

sulfite reductase subunit alpha; Provisional


Pssm-ID: 182862 [Multi-domain]  Cd Length: 600  Bit Score: 83.23  E-value: 9.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119    87 RLYSIASSAiGDFGDSKTVSLCVKRlvYTNDaGEVVKGVCSNFLCD-LKPGSEVKITGPVGKEMLMPKDPNATVIMLGTG 165
Cdd:PRK10953 387 RLYSIASSQ-AEVENEVHITVGVVR--YDIE-GRARAGGASSFLADrLEEEGEVRVFIEHNDNFRLPANPETPVIMIGPG 462
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   166 TGIAPFRSFLwkmffEKHEDYQFNGLAWLFLGVPT-SSSLLYKEEFEKMKEKAPENfRLDFAVSREQvndkGEKMYIQTR 244
Cdd:PRK10953 463 TGIAPFRAFM-----QQRAADGAPGKNWLFFGNPHfTEDFLYQVEWQRYVKEGLLT-RIDLAWSRDQ----KEKIYVQDK 532
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 4930119   245 MAQYAEELWELLkKDNTFVYMCG-LKGMEKGIDDIMVSLAAKDG 287
Cdd:PRK10953 533 LREQGAELWRWI-NDGAHIYVCGdANRMAKDVEQALLEVIAEFG 575
Nitric_oxide_synthase cd06202
The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses ...
87-267 1.10e-15

The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses with a heme-containing N-terminal oxidase domain. The reductase portion is similar in structure to NADPH dependent cytochrome-450 reductase (CYPOR), having an inserted connecting sub-domain within the FAD binding portion of FNR. NOS differs from CYPOR in a requirement for the cofactor tetrahydrobiopterin and unlike most CYPOR is dimeric. Nitric oxide synthase produces nitric oxide in the conversion of L-arginine to L-citruline. NOS has been implicated in a variety of processes including cytotoxicity, anti-inflamation, neurotransmission, and vascular smooth muscle relaxation.


Pssm-ID: 99799 [Multi-domain]  Cd Length: 406  Bit Score: 76.60  E-value: 1.10e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   87 RLYSIASSAigDFgDSKTVSLCVKRLVY-TND-AGEVVKGVCSNFLCDLKPGSEVKITGPVGKEMLMPKDPNATVIMLGT 164
Cdd:cd06202 178 RYYSISSSP--DM-YPGEIHLTVAVVSYrTRDgQGPVHHGVCSTWLNGLTPGDTVPCFVRSAPSFHLPEDPSVPVIMVGP 254
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  165 GTGIAPFRSFlWK-----MFFEKHEDYQFnGLAWLFLGVPTSSSL-LYKEEFEKMKEKapENF-RLDFAVSREQvnDKgE 237
Cdd:cd06202 255 GTGIAPFRSF-WQqrqydLRMSEDPGKKF-GDMTLFFGCRNSTIDdIYKEETEEAKNK--GVLtEVYTALSREP--GK-P 327
                       170       180       190
                ....*....|....*....|....*....|
gi 4930119  238 KMYIQTRMAQYAEELWELLKKDNTFVYMCG 267
Cdd:cd06202 328 KTYVQDLLKEQAESVYDALVREGGHIYVCG 357
Fpr COG1018
Ferredoxin-NADP reductase [Energy production and conversion];
62-282 1.17e-14

Ferredoxin-NADP reductase [Energy production and conversion];


Pssm-ID: 223949 [Multi-domain]  Cd Length: 266  Bit Score: 72.32  E-value: 1.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   62 VPYREGQSIGIvpdGIDKNGKPHkLRLYSIASSAigdfGDSKTVSLCVKRlvytNDAGEVvkgvcSNFLCD-LKPGSEVK 140
Cdd:COG1018  33 LDFEPGQYITV---GLPNGGEPL-LRAYSLSSAP----DEDSLYRISVKR----EDGGGG-----SNWLHDhLKVGDTLE 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  141 ITGPVGkEMLMPKDPNATVIMLGTGTGIAPFRSFLwkmffEKHEDYQFNGLAWLFlGVPTSSSLLYkEEFEKMKEKAPEN 220
Cdd:COG1018  96 VSAPAG-DFVLDDLPERKLLLLAGGIGITPFLSML-----RTLLDRGPADVVLVH-AARTPADLAF-RDELELAAELPNA 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4930119  221 FRLDFAVSREQvndkgekmyIQTRMAQYAEELWelLKKDNTFVYMCGLKGMEKGIDDIMVSL 282
Cdd:COG1018 168 LLLGLYTERGK---------LQGRIDVSRLLSA--APDGGREVYLCGPGPFMQAVRLALEAL 218
SiR_like1 cd06200
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
33-289 5.27e-14

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: 99797  Cd Length: 245  Bit Score: 70.00  E-value: 5.27e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   33 VGRCLLNTKITGddapGETWHMVFSTEGE-VPYREGQSIGIVPdgidKNGKPHklRLYSIASsaIGDFGDsktVSLCVkR 111
Cdd:cd06200   4 QARVLLNPGSQG----APLWRLRLTPPDAgAQWQAGDIAEIGP----RHPLPH--REYSIAS--LPADGA---LELLV-R 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  112 LVYTNDAGevvKGVCSNFLCDLKP-GSEVKITgPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFL-----------WKMF 179
Cdd:cd06200  68 QVRHADGG---LGLGSGWLTRHAPiGASVALR-LRENPGFHLPDDGRPLILIGNGTGLAGLRSHLrararagrhrnWLLF 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  180 FEKHEDYQF----NGLAWLFLGVPTsssllykeefekmkekapenfRLDFAVSReqvnDKGEKMYIQTRMAQYAEELWEL 255
Cdd:cd06200 144 GERQAAHDFfcreELEAWQAAGHLA---------------------RLDLAFSR----DQAQKRYVQDRLRAAADELRAW 198
                       250       260       270
                ....*....|....*....|....*....|....*
gi 4930119  256 LKKdNTFVYMCG-LKGMEKGIDDIMVSLAAKDGID 289
Cdd:cd06200 199 VAE-GAAIYVCGsLQGMAPGVDAVLDEILGEEAVE 232
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
63-280 9.15e-14

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: 70.05  E-value: 9.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   63 PYREGQSIGIVPDGIDKngkPhklRLYSIASSAIGDFgdsktVSLCVKRLVytndagevvKGVCSNFLCDLKPGSEVKIT 142
Cdd:cd06201  83 SFEAGDLLGILPPGSDV---P---RFYSLASSSSDGF-----LEICVRKHP---------GGLCSGYLHGLKPGDTIKAF 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  143 GPVGKEMLMPKDpNATVIMLGTGTGIAPFRSFLwKMFFEKHEDYQFNGlawlflGVPTSSSLLYKEEFEKMKEKAP-ENF 221
Cdd:cd06201 143 IRPNPSFRPAKG-AAPVILIGAGTGIAPLAGFI-RANAARRPMHLYWG------GRDPASDFLYEDELDQYLADGRlTQL 214
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4930119  222 RLDFavSREQvndkgEKMYIQTRMAQYAEELWELLkKDNTFVYMCGLKGMEKG----IDDIMV 280
Cdd:cd06201 215 HTAF--SRTP-----DGAYVQDRLRADAERLRRLI-EDGAQIMVCGSRAMAQGvaavLEEILA 269
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
87-271 1.10e-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: 66.19  E-value: 1.10e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   87 RLYSIASSAigdfGDSKTVSLCVKRlvytndageVVKGVCSNFLCD-LKPGSEVKITGPVGkEMLMPKDPNATVIMLGTG 165
Cdd:cd06211  53 RAFSIASSP----SDAGEIELHIRL---------VPGGIATTYVHKqLKEGDELEISGPYG-DFFVRDSDQRPIIFIAGG 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  166 TGIAPFRSFLWKMfFEKHEDYQfnglAWLFLGVPTSSSLLYKEEFEKMKEKAPeNFRLDFAVSREQVND--KGEKMYIQT 243
Cdd:cd06211 119 SGLSSPRSMILDL-LERGDTRK----ITLFFGARTRAELYYLDEFEALEKDHP-NFKYVPALSREPPESnwKGFTGFVHD 192
                       170       180
                ....*....|....*....|....*...
gi 4930119  244 RMAQYAEElwellKKDNTFVYMCGLKGM 271
Cdd:cd06211 193 AAKKHFKN-----DFRGHKAYLCGPPPM 215
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
114-274 2.68e-12

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  Cd Length: 234  Bit Score: 64.90  E-value: 2.68e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  114 YT-----NDAGE---VVK----GVCSNFLCDLKPGSEVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLwKMFFE 181
Cdd:cd06183  50 YTpispdDDKGYfdlLIKiypgGKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGKVKHIGMIAGGTGITPMLQLI-RAILK 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  182 KHEDyqfNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQVNDKGEKMYIQtrmAQYAEELWELLKKDNT 261
Cdd:cd06183 129 DPED---KTKISLLYANRTEEDILLREELDELAKKHPDRFKVHYVLSRPPEGWKGGVGFIT---KEMIKEHLPPPPSEDT 202
                       170
                ....*....|...
gi 4930119  262 FVYMCGLKGMEKG 274
Cdd:cd06183 203 LVLVCGPPPMIEG 215
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
87-267 4.53e-11

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  Cd Length: 283  Bit Score: 61.94  E-value: 4.53e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   87 RLYSIASSAigdfGDSKTVSLCVKRLVYTNDAGEVVKGVCSNFLCDLKPGSEVKITGPVGkEMLMpKDPNATVIMLGTGT 166
Cdd:cd06188  87 RAYSLANYP----AEEGELKLNVRIATPPPGNSDIPPGIGSSYIFNLKPGDKVTASGPFG-EFFI-KDTDREMVFIGGGA 160
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  167 GIAPFRSFLWKMFFEKHEDYQfnglAWLFLGVPTSSSLLYKEEFEKMKEKAPeNFRLDFAVSREQVND--KGEKMYIQTR 244
Cdd:cd06188 161 GMAPLRSHIFHLLKTLKSKRK----ISFWYGARSLKELFYQEEFEALEKEFP-NFKYHPVLSEPQPEDnwDGYTGFIHQV 235
                       170       180
                ....*....|....*....|....*...
gi 4930119  245 MAQYaeelweLLKK-----DNTFvYMCG 267
Cdd:cd06188 236 LLEN------YLKKhpapeDIEF-YLCG 256
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
51-282 6.60e-10

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  Cd Length: 235  Bit Score: 58.05  E-value: 6.60e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   51 TWHMVFSTEGEVPYREGQSIGIVPDGIDknGKpHKLRLYSIASSAIGDFGdsktVSLCVKRLvytnDAGEVvkgvcSNFL 130
Cdd:cd06217  18 TFRLAVPDGVPPPFLAGQHVDLRLTAID--GY-TAQRSYSIASSPTQRGR----VELTVKRV----PGGEV-----SPYL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  131 CD-LKPGSEVKITGPVGKEMLMPKDPNaTVIMLGTGTGIAPFRSFLwkmffEKHEDYQFNGLAWLFLGVPTSSSLLYKEE 209
Cdd:cd06217  82 HDeVKVGDLLEVRGPIGTFTWNPLHGD-PVVLLAGGSGIVPLMSMI-----RYRRDLGWPVPFRLLYSARTAEDVIFRDE 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4930119  210 FEKMKEKAPeNFRLDFAVSREQVND-KGEKMYIQTRMAQyaeELWELLkkDNTFVYMCGLKGMEKGIDDIMVSL 282
Cdd:cd06217 156 LEQLARRHP-NLHVTEALTRAAPADwLGPAGRITADLIA---ELVPPL--AGRRVYVCGPPAFVEAATRLLLEL 223
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
64-175 6.65e-10

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  Cd Length: 243  Bit Score: 58.00  E-value: 6.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   64 YREGQSIGIvpdGIDKNGKPHKlRLYSIASSAIGDFGdskTVSLCVKRlvytndageVVKGVCSNFLCD-LKPGSEVKIT 142
Cdd:cd06216  46 HRAGQHVRL---GVEIDGVRHW-RSYSLSSSPTQEDG---TITLTVKA---------QPDGLVSNWLVNhLAPGDVVELS 109
                        90       100       110
                ....*....|....*....|....*....|...
gi 4930119  143 GPVGkEMLMPKDPNATVIMLGTGTGIAPFRSFL 175
Cdd:cd06216 110 QPQG-DFVLPDPLPPRLLLIAAGSGITPVMSML 141
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
63-170 9.10e-10

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  Cd Length: 231  Bit Score: 57.60  E-value: 9.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   63 PYREGQSIGIvpdGIDKNGKPHkLRLYSIASSAigdfGDSKTVSLCVKRlvytndageVVKGVCSNFLCD-LKPGSEVKI 141
Cdd:cd06215  27 AYKPGQFLTL---ELEIDGETV-YRAYTLSSSP----SRPDSLSITVKR---------VPGGLVSNWLHDnLKVGDELWA 89
                        90       100
                ....*....|....*....|....*....
gi 4930119  142 TGPVGkEMLMPKDPNATVIMLGTGTGIAP 170
Cdd:cd06215  90 SGPAG-EFTLIDHPADKLLLLSAGSGITP 117
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
64-282 6.66e-09

Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with a C-terminal iron-sulfur binding cluster domain. FNR was intially identified as a chloroplast reductase activity catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methnae assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99788  Cd Length: 231  Bit Score: 55.23  E-value: 6.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   64 YREGQSIGIvpdGIDKNGKPHKlRLYSIASSAIGDfgdskTVSLCVKRLvytnDAGEVvkgvcSNFLCD-LKPGSEVKIT 142
Cdd:cd06191  28 FRPGQHVTL---KLDFDGEELR-RCYSLCSSPAPD-----EISITVKRV----PGGRV-----SNYLREhIQPGMTVEVM 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  143 GPVGKEMLMPKDPnATVIMLGTGTGIAPFRSFLwKMFFEKHEDYQFNglawLFLGVPTSSSLLYkEEFEKMKEKAPENFR 222
Cdd:cd06191  90 GPQGHFVYQPQPP-GRYLLVAAGSGITPLMAMI-RATLQTAPESDFT----LIHSARTPADMIF-AQELRELADKPQRLR 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  223 LDFAVSREqVNDKGEKMYIQTRMAQYAEELWELLKKDNTFVymCGLKGMEKGIDDIMVSL 282
Cdd:cd06191 163 LLCIFTRE-TLDSDLLHGRIDGEQSLGAALIPDRLEREAFI--CGPAGMMDAVETALKEL 219
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
119-267 3.13e-08

Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion];


Pssm-ID: 225426 [Multi-domain]  Cd Length: 410  Bit Score: 54.04  E-value: 3.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  119 GEVVKGVCSNFLCDLKPGSEVKITGPVGkEMLMpKDPNATVIMLGTGTGIAPFRSFLWKMFFEKHEDYQFNglawLFLGV 198
Cdd:COG2871 240 PDAPPGQMSSYIWSLKPGDKVTISGPFG-EFFA-KDTDAEMVFIGGGAGMAPMRSHIFDQLKRLHSKRKIS----FWYGA 313
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4930119  199 PTSSSLLYKEEFEKMKEKAPeNFRLDFAVSREQVNDKGEKMYIQTRMAQYAEELWELLKKDNTFVYMCG 267
Cdd:COG2871 314 RSLREMFYQEDFDQLQAENP-NFHWHLALSDPLPEDNWDGYTGFIHNVLYENYLKDHEAPEDCEYYMCG 381
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
58-271 8.47e-08

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


Pssm-ID: 99791  Cd Length: 222  Bit Score: 51.89  E-value: 8.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   58 TEGEVPYREGQSIGIV-PDGIdkngkphkLRLYSIASsaigDFGDSKTVSLCVKRlvYTNdagevvkGVCSNFLCDL-KP 135
Cdd:cd06194  18 PDRPLPYLPGQYVNLRrAGGL--------ARSYSPTS----LPDGDNELEFHIRR--KPN-------GAFSGWLGEEaRP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  136 GSEVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPfrsfLWKM----FFEKHEdyqfnGLAWLFLGVPTSSSlLYKEEFE 211
Cdd:cd06194  77 GHALRLQGPFGQAFYRPEYGEGPLLLVGAGTGLAP----LWGIaraaLRQGHQ-----GEIRLVHGARDPDD-LYLHPAL 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  212 KMKEKAPENFRLDFAVSREQVNDKGekmyiqTRMAQYAEELWELLKkdNTFVYMCGLKGM 271
Cdd:cd06194 147 LWLAREHPNFRYIPCVSEGSQGDPR------VRAGRIAAHLPPLTR--DDVVYLCGAPSM 198
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
90-282 1.58e-07

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


Pssm-ID: 99817 [Multi-domain]  Cd Length: 253  Bit Score: 51.07  E-value: 1.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   90 SIASSAigdfGDSKTVSLCVKRLvytndagevvkGVCSNFLCDLKPGSEVKITGPVGKEMLMPKDPNATVIMLGTGTGIA 169
Cdd:cd06221  47 SISSDP----TRRGPLELTIRRV-----------GRVTEALHELKPGDTVGLRGPFGNGFPVEEMKGKDLLLVAGGLGLA 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  170 PFRSFLWKmFFEKHEDYqfnGLAWLFLGVPTSSSLLYKEEFEKMKEKapENFRLDFAVSREQVNDKGEKMYIQTRMAQya 249
Cdd:cd06221 112 PLRSLINY-ILDNREDY---GKVTLLYGARTPEDLLFKEELKEWAKR--SDVEVILTVDRAEEGWTGNVGLVTDLLPE-- 183
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 4930119  250 eelwELLKKDNTFVYMCGLKGM---------EKGI--DDIMVSL 282
Cdd:cd06221 184 ----LTLDPDNTVAIVCGPPIMmrfvakellKLGVpeEQIWVSL 223
nqrF TIGR01941
NADH:ubiquinone oxidoreductase, Na(+)-translocating, F subunit; This model represents the NqrF ...
124-183 3.45e-07

NADH:ubiquinone oxidoreductase, Na(+)-translocating, F subunit; This model represents the NqrF subunit of the six-protein, Na(+)-pumping NADH-quinone reductase of a number of marine and pathogenic Gram-negative bacteria. This oxidoreductase complex functions primarily as a sodium ion pump. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130996 [Multi-domain]  Cd Length: 405  Bit Score: 50.95  E-value: 3.45e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119    124 GVCSNFLCDLKPGSEVKITGPVGkEMLMpKDPNATVIMLGTGTGIAPFRSFLWKMFFEKH 183
Cdd:TIGR01941 240 GIMSSYIFSLKPGDKVTISGPFG-EFFA-KDTDAEMVFIGGGAGMAPMRSHIFDQLKRLK 297
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
49-267 3.58e-07

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  Cd Length: 224  Bit Score: 49.85  E-value: 3.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   49 GETWHMVFSTEGEVPYREGQSIGIVPDGIDKngkphklRLYSIASSAigdfGDSKTVSLCVKRlvytndageVVKGVCSN 128
Cdd:cd06189  11 DDVYRVRLKPPAPLDFLAGQYLDLLLDDGDK-------RPFSIASAP----HEDGEIELHIRA---------VPGGSFSD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  129 FLCD-LKPGSEVKITGPVGKEMLMPkDPNATVIMLGTGTGIAPFRSFLwkmffEKHEDYQFNGLAWLFLGVPTSSSlLYK 207
Cdd:cd06189  71 YVFEeLKENGLVRIEGPLGDFFLRE-DSDRPLILIAGGTGFAPIKSIL-----EHLLAQGSKRPIHLYWGARTEED-LYL 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  208 EEFEKMKEKAPENFRLDFAVSREQVNDKGEKMYIQTRMAQYAEELwellkkDNTFVYMCG 267
Cdd:cd06189 144 DELLEAWAEAHPNFTYVPVLSEPEEGWQGRTGLVHEAVLEDFPDL------SDFDVYACG 197
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
56-279 8.11e-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: 48.79  E-value: 8.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   56 FSTEGEVPYREGQSIGIVPDGIDKNgkphklRLYSIASSAigdfGDSKTVSLCVKRlvytndageVVKGVCSNFLCD-LK 134
Cdd:cd06190  16 FALDGPADFLPGQYALLALPGVEGA------RAYSMANLA----NASGEWEFIIKR---------KPGGAASNALFDnLE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  135 PGSEVKITGPVGKEMLMPKDPNaTVIMLGTGTGIAPFRSFL-----WKMFFEKHEDyqfnglawLFLGVPTSSSlLYKEE 209
Cdd:cd06190  77 PGDELELDGPYGLAYLRPDEDR-DIVCIAGGSGLAPMLSILrgaarSPYLSDRPVD--------LFYGGRTPSD-LCALD 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4930119  210 FEKMKEKAPENFRLDFAVSREQVNDK----GEKMYIQTRMAQYAEELWellkkDNTFVYMCGLKGMekgIDDIM 279
Cdd:cd06190 147 ELSALVALGARLRVTPAVSDAGSGSAagwdGPTGFVHEVVEATLGDRL-----AEFEFYFAGPPPM---VDAVQ 212
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
121-271 8.99e-07

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


Pssm-ID: 223617 [Multi-domain]  Cd Length: 252  Bit Score: 48.94  E-value: 8.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  121 VVKGVCSNFLCDLKPGSEVKITGPVGKEMLMPKDPNaTVIMLGTGTGIAPFRSFLWKMFFEKHEDYQFnglawLFLGVPT 200
Cdd:COG0543  73 YEVGKVTKYIFGLKEGDKIRVRGPLGNGFLREKIGK-PVLLIAGGTGIAPLYAIAKELKEKGDANKVT-----LLYGART 146
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4930119  201 SSSLLYKeefekmkekaPENFRLDFAVSREQVND--KGEKMYIQTrmaqyaEELWELLKKDNTFVYMCGLKGM 271
Cdd:COG0543 147 AKDLLLL----------DELEELAEKEVHPVTDDgwKGRKGFVTT------DVLKELLDLEVDDVYICGPPAM 203
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
48-175 1.00e-06

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


Pssm-ID: 99795 [Multi-domain]  Cd Length: 216  Bit Score: 48.41  E-value: 1.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   48 PGETWHMVFSTEG-EVPYREGQSIGIVPDGIDKNGkPHKlrlYSIASSAigdfGDSKTVSLCVKRL-VYTNDAGEvvkgv 125
Cdd:cd06198   6 VRPTTTLTLEPRGpALGHRAGQFAFLRFDASGWEE-PHP---FTISSAP----DPDGRLRFTIKALgDYTRRLAE----- 72
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4930119  126 csnflcDLKPGSEVKITGPVGKemLMPKDPNATVIMLGTGTGIAPFRSFL 175
Cdd:cd06198  73 ------RLKPGTRVTVEGPYGR--FTFDDRRARQIWIAGGIGITPFLALL 114
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
59-271 1.56e-06

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  Cd Length: 224  Bit Score: 47.97  E-value: 1.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   59 EGEVPYREGQSIGI-VPdgidknGKPHKLRLYSIASSAigdfGDSKTVSLCVKRlvytndageVVKGVCSNFLCD-LKPG 136
Cdd:cd06187  19 DQPLPFWAGQYVNVtVP------GRPRTWRAYSPANPP----NEDGEIEFHVRA---------VPGGRVSNALHDeLKVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  137 SEVKITGPVGkEMLMPKDPNATVIMLGTGTGIAPFRSFLwkmffEKHEDYQFNGLAWLFLGVPTSSSLLYKEEFEKMKEK 216
Cdd:cd06187  80 DRVRLSGPYG-TFYLRRDHDRPVLCIAGGTGLAPLRAIV-----EDALRRGEPRPVHLFFGARTERDLYDLEGLLALAAR 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4930119  217 APeNFRLDFAVSREQVNDKGEKMYIQTRMAQYAEEL--WEllkkdntfVYMCGLKGM 271
Cdd:cd06187 154 HP-WLRVVPVVSHEEGAWTGRRGLVTDVVGRDGPDWadHD--------IYICGPPAM 201
PRK05464 PRK05464
Na(+)-translocating NADH-quinone reductase subunit F; Provisional
124-183 1.78e-06

Na(+)-translocating NADH-quinone reductase subunit F; Provisional


Pssm-ID: 235481 [Multi-domain]  Cd Length: 409  Bit Score: 48.71  E-value: 1.78e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   124 GVCSNFLCDLKPGSEVKITGPVGKemLMPKDPNATVIMLGTGTGIAPFRSFLWKMFFEKH 183
Cdd:PRK05464 244 GIMSSYIFSLKPGDKVTISGPFGE--FFAKDTDAEMVFIGGGAGMAPMRSHIFDQLKRLK 301
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
124-271 1.86e-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: 47.72  E-value: 1.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  124 GVCSNFL-CDLKPGSEVKITGPVGKEMLMPKDPnATVIMLGTGTGIAPFRSFLWKMffekhEDYQFNGLAWLFLGVPTSS 202
Cdd:cd06210  76 GAFSTYLeTRAKVGQRLNLRGPLGAFGLRENGL-RPRWFVAGGTGLAPLLSMLRRM-----AEWGEPQEARLFFGVNTEA 149
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4930119  203 SLLYKEEFEKMKEKAPeNFRLDFAVSREQVNDKGEKmyiQTRMAQYAEELWELLKKDNtfVYMCGLKGM 271
Cdd:cd06210 150 ELFYLDELKRLADSLP-NLTVRICVWRPGGEWEGYR---GTVVDALREDLASSDAKPD--IYLCGPPGM 212
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
64-289 6.17e-06

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  Cd Length: 241  Bit Score: 46.38  E-value: 6.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   64 YREGQSIGIVPDgidKNGKPHkLRLYSIASSAigdfgDSKTVSLCVKRlvytndageVVKGVCSNFLCD-LKPGSEVKIT 142
Cdd:cd06214  33 YRPGQFLTLRVP---IDGEEV-RRSYSICSSP-----GDDELRITVKR---------VPGGRFSNWANDeLKAGDTLEVM 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  143 GPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLwKMFFEKHEDYQFNglawLFLGVPTSSSLLYKEEFEKMKEKAPENFR 222
Cdd:cd06214  95 PPAGRFTLPPLPGARHYVLFAAGSGITPVLSIL-KTALAREPASRVT----LVYGNRTEASVIFREELADLKARYPDRLT 169
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4930119  223 LDFAVSREQVNDKGEKMYIQTRMAQYAEELWeLLKKDNTFVYMCGLKGMekgIDDIMVSLAAKdGID 289
Cdd:cd06214 170 VIHVLSREQGDPDLLRGRLDAAKLNALLKNL-LDATEFDEAFLCGPEPM---MDAVEAALLEL-GVP 231
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
130-296 6.79e-06

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: 46.38  E-value: 6.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  130 LCDLKPGSEVKITGPVGKEmLMPKDPNATVIMLGTGTGIAPFRsFLWKMFFEKHEDyqfnglAWLFLGVPTSSSLLYKee 209
Cdd:cd06218  73 LSELKAGDELDVLGPLGNG-FDLPDDDGKVLLVGGGIGIAPLL-FLAKQLAERGIK------VTVLLGFRSADDLFLV-- 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  210 fekmkekapENFRLDFAVSREQVND--KGEKMYIQTRMAQYAEELwellkkDNTFVYMCGLKGMEKGIDDIM-------- 279
Cdd:cd06218 143 ---------EEFEALGAEVYVATDDgsAGTKGFVTDLLKELLAEA------RPDVVYACGPEPMLKAVAELAaergvpcq 207
                       170       180       190
                ....*....|....*....|....*....|.
gi 4930119  280 VSL--------------AAKDGIDWIEYKRT 296
Cdd:cd06218 208 VSLeermacgigaclgcVVKTKDDEGGYKRV 238
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
107-176 3.53e-05

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 44.41  E-value: 3.53e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   107 LCVKRlvytndAGEVvkgvcSNFLCDLKPGSEVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLW 176
Cdd:PRK08345  70 LCIRR------AGRV-----TTVIHRLKEGDIVGVRGPYGNGFPVDEMEGMDLLLIAGGLGMAPLRSVLL 128
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
124-267 4.11e-05

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  Cd Length: 228  Bit Score: 43.74  E-value: 4.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  124 GVCSNFLCDL-KPGSEVKITGPVGKEMLmpKDPNATVIMLGTGTGIAPFRSFLWKMffekhedyQFNGLAW---LFLGVP 199
Cdd:cd06209  71 GAMSSYLRDRaQPGDRLTLTGPLGSFYL--REVKRPLLMLAGGTGLAPFLSMLDVL--------AEDGSAHpvhLVYGVT 140
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4930119  200 TSSSLLYKEEFEKMKEKAPeNFRLDFAVSREQVNDkGEKMYIQTRMAQyaeelwELLKKDNTFVYMCG 267
Cdd:cd06209 141 RDADLVELDRLEALAERLP-GFSFRTVVADPDSWH-PRKGYVTDHLEA------EDLNDGDVDVYLCG 200
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
63-267 3.17e-04

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


Pssm-ID: 99781  Cd Length: 247  Bit Score: 41.39  E-value: 3.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   63 PYREGQSIGI-VPdgIDKNGKPHkLRLYSIaSSAIGdfGDSKTVSlcVKRLvytnDAGEVvkgvcSNFLCD-LKPGSEVK 140
Cdd:cd06184  36 PFLPGQYLSVrVK--LPGLGYRQ-IRQYSL-SDAPN--GDYYRIS--VKRE----PGGLV-----SNYLHDnVKVGDVLE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119  141 ITGPVGkEMLMPKDPNATVIMLGTGTGIAPFRSFLwkmffekhedyqfNGLA--------WLFLGVPTSSSLLYKEEFEK 212
Cdd:cd06184  99 VSAPAG-DFVLDEASDRPLVLISAGVGITPMLSML-------------EALAaegpgrpvTFIHAARNSAVHAFRDELEE 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4930119  213 MKEKAPeNFRLDFAVSREQVNDKGEKMYIQTRMAqyAEELWELLKKDNTFVYMCG 267
Cdd:cd06184 165 LAARLP-NLKLHVFYSEPEAGDREEDYDHAGRID--LALLRELLLPADADFYLCG 216
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
61-178 7.11e-04

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  Cd Length: 232  Bit Score: 40.01  E-value: 7.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   61 EVPYREGQSIGI-VPDGIDKngkphklRLYSIASSAigdfGDSKTVSLCVKrlVYTNdagevvkGVCSNFLCD-LKPGSE 138
Cdd:cd06212  27 PIKFFAGQYVDItVPGTEET-------RSFSMANTP----ADPGRLEFIIK--KYPG-------GLFSSFLDDgLAVGDP 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 4930119  139 VKITGPVGKEMLMPKDPNAtVIMLGTGTGIAPFRSFLWKM 178
Cdd:cd06212  87 VTVTGPYGTCTLRESRDRP-IVLIGGGSGMAPLLSLLRDM 125
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
63-173 1.38e-03

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 39.69  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119    63 PYREGQ----SIgivpdgidkNGKPHKLRLYSIASSAigdfGDSKTVSLCVKRLvytndagevVKGVCSNFLC-DLKPGS 137
Cdd:PRK10684  36 PYRAGQyalvSI---------RNSAETLRAYTLSSTP----GVSEFITLTVRRI---------DDGVGSQWLTrDVKRGD 93
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 4930119   138 EVKITGPVGkEMLMPKDPNATVIMLGTGTGIAPFRS 173
Cdd:PRK10684  94 YLWLSDAMG-EFTCDDKAEDKYLLLAAGCGVTPIMS 128
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
83-170 2.87e-03

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: 38.46  E-value: 2.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930119   83 PHKLRLYSIASSAIGDFGDSKTVSLCVKrlvytndagevVKGVCSNFLCDLKPGSEVKITGPVGKEMLMPKDpNATVIML 162
Cdd:cd06192  36 FESPGLERIPLSLAGVDPEEGTISLLVE-----------IRGPKTKLIAELKPGEKLDVMGPLGNGFEGPKK-GGTVLLV 103

                ....*...
gi 4930119  163 GTGTGIAP 170
Cdd:cd06192 104 AGGIGLAP 111
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH