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Conserved domains on  [gi|334186381|ref|NP_001190682|]
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root FNR 1 [Arabidopsis thaliana]

Protein Classification

PLN03116 family protein( domain architecture ID 11477438)

PLN03116 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03116 PLN03116
ferredoxin--NADP+ reductase; Provisional
53-350 0e+00

ferredoxin--NADP+ reductase; Provisional


:

Pssm-ID: 215586 [Multi-domain]  Cd Length: 307  Bit Score: 690.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  53 DPKETPLNLFRPKEPYTATIVSVERIVGPQAPGETCHIVIDHDGNVPYWEGQSYGVIPPGENPKKPGAPHNVRLYSIAST 132
Cdd:PLN03116  10 DAKEPPLNLYKPKAPYTATIVSVERIVGPKAPGETCHIVIDHGGNVPYWEGQSYGVIPPGTNPKKPGAPHNVRLYSIAST 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 133 RYGDSFDGKTASLCVRRAIYYDPETGKEDPSKAGVCSNFLCNAKPGDKVKITGPSGKVMLLPEDDPKATHIMIATGTGVA 212
Cdd:PLN03116  90 RYGDDFDGKTASLCVRRAVYYDPETGKEDPAKKGVCSNFLCDAKPGDKVQITGPSGKVMLLPEEDPNATHIMVATGTGIA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 213 PYRGYLRRMFMENVPNFKFDGLAWLFLGVANSDSLLYDEEFAGYRKDYPENFRYDKALSREEKNKKGGKMYVQDKIEEYS 292
Cdd:PLN03116 170 PFRGFLRRMFMEDVPAFKFGGLAWLFLGVANSDSLLYDDEFERYLKDYPDNFRYDYALSREQKNKKGGKMYVQDKIEEYS 249
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334186381 293 DEIFKLLDNGAHIYFCGLKGMMPGIQDTLKRVAEERGESWEQKLTQLRKNKQWHVEVY 350
Cdd:PLN03116 250 DEIFKLLDNGAHIYFCGLKGMMPGIQDTLKRVAEERGESWEEKLSGLKKNKQWHVEVY 307
 
Name Accession Description Interval E-value
PLN03116 PLN03116
ferredoxin--NADP+ reductase; Provisional
53-350 0e+00

ferredoxin--NADP+ reductase; Provisional


Pssm-ID: 215586 [Multi-domain]  Cd Length: 307  Bit Score: 690.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  53 DPKETPLNLFRPKEPYTATIVSVERIVGPQAPGETCHIVIDHDGNVPYWEGQSYGVIPPGENPKKPGAPHNVRLYSIAST 132
Cdd:PLN03116  10 DAKEPPLNLYKPKAPYTATIVSVERIVGPKAPGETCHIVIDHGGNVPYWEGQSYGVIPPGTNPKKPGAPHNVRLYSIAST 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 133 RYGDSFDGKTASLCVRRAIYYDPETGKEDPSKAGVCSNFLCNAKPGDKVKITGPSGKVMLLPEDDPKATHIMIATGTGVA 212
Cdd:PLN03116  90 RYGDDFDGKTASLCVRRAVYYDPETGKEDPAKKGVCSNFLCDAKPGDKVQITGPSGKVMLLPEEDPNATHIMVATGTGIA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 213 PYRGYLRRMFMENVPNFKFDGLAWLFLGVANSDSLLYDEEFAGYRKDYPENFRYDKALSREEKNKKGGKMYVQDKIEEYS 292
Cdd:PLN03116 170 PFRGFLRRMFMEDVPAFKFGGLAWLFLGVANSDSLLYDDEFERYLKDYPDNFRYDYALSREQKNKKGGKMYVQDKIEEYS 249
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334186381 293 DEIFKLLDNGAHIYFCGLKGMMPGIQDTLKRVAEERGESWEQKLTQLRKNKQWHVEVY 350
Cdd:PLN03116 250 DEIFKLLDNGAHIYFCGLKGMMPGIQDTLKRVAEERGESWEEKLSGLKKNKQWHVEVY 307
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
60-350 1.50e-180

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: 501.08  E-value: 1.50e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  60 NLFRPKEPYTATIVSVERIVGPQAPGETCHIVIDHDGNVPYWEGQSYGVIPPGENPKkPGAPHNVRLYSIASTRYGDSFD 139
Cdd:cd06208    1 NLYKPKNPLIGKVVSNTRLTGPDAPGEVCHIVIDHGGKLPYLEGQSIGIIPPGTDAK-NGKPHKLRLYSIASSRYGDDGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 140 GKTASLCVRRAIYYDPETgkeDPSKAGVCSNFLCNAKPGDKVKITGPSGKVMLLPeDDPKATHIMIATGTGVAPYRGYLR 219
Cdd:cd06208   80 GKTLSLCVKRLVYTDPET---DETKKGVCSNYLCDLKPGDDVQITGPVGKTMLLP-EDPNATLIMIATGTGIAPFRSFLR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 220 RMFMENVPNFKFDGLAWLFLGVANSDSLLYDEEFAGYRKDYPENFRYDKALSREEKNKKGGKMYVQDKIEEYSDEIFKLL 299
Cdd:cd06208  156 RLFREKHADYKFTGLAWLFFGVPNSDSLLYDDELEKYPKQYPDNFRIDYAFSREQKNADGGKMYVQDRIAEYAEEIWNLL 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 334186381 300 DNGA-HIYFCGLKGMMPGIQDTLKRVAeERGESWEQKLTQLRKNKQWHVEVY 350
Cdd:cd06208  236 DKDNtHVYICGLKGMEPGVDDALTSVA-EGGLAWEEFWESLKKKGRWHVEVY 286
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
125-350 7.51e-35

Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440138 [Multi-domain]  Cd Length: 561  Bit Score: 133.73  E-value: 7.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 125 RLYSIAStrygdSF--DGKTASLCVRRAIYydPETGKEdpsKAGVCSNFLCNAKPGDKVKI---TGPSGKvmlLPEDdPK 199
Cdd:COG0369  349 RLYSISS-----SPkaHPDEVHLTVGVVRY--EASGRE---RKGVASTYLADLEEGDTVPVfvePNPNFR---LPAD-PD 414
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 200 ATHIMIATGTGVAPYRGYL--RRmfmenvpNFKFDGLAWLFLGVANSDS-LLYDEEFAGYRKDypenfRYDKALSREEkn 276
Cdd:COG0369  415 TPIIMIGPGTGIAPFRAFLqeRE-------ARGASGKNWLFFGDRHFTTdFLYQTELQAWLKDgv-ltRLDLAFSRDQ-- 484
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334186381 277 kkGGKMYVQDKIEEYSDEIFKLLDNGAHIYFCG-LKGMMPGIQDTLKRVAEERG----ESWEQKLTQLRKNKQWHVEVY 350
Cdd:COG0369  485 --AEKIYVQHRLLEQGAELWAWLEEGAHVYVCGdASRMAKDVDAALLDIIAEHGglseEEAEEYLAELRAEKRYQRDVY 561
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
204-319 1.82e-34

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


Pssm-ID: 425503 [Multi-domain]  Cd Length: 109  Bit Score: 122.37  E-value: 1.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  204 MIATGTGVAPYRGYLRRMFMENvpnfKFDGLAWLFLGVANSDSLLYDEEFAGYRKDYPENFRYDKALSREEKNKKGGKMY 283
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDP----KDPTQVVLVFGNRNEDDILYREELDELAEKHPGRLTVVYVVSRPEAGWTGGKGR 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 334186381  284 VQDKIEEYSDEIfklLDNGAHIYFCGLKGMMPGIQD 319
Cdd:pfam00175  77 VQDALLEDHLSL---PDEETHVYVCGPPGMIKAVRK 109
cysJ TIGR01931
sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an ...
125-350 1.11e-31

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: 125.19  E-value: 1.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  125 RLYSIASTRygdSFDGKTASLCVRRAIYydPETGKEdpsKAGVCSNFLCN-AKPGDKVKITGPSGKVMLLPEDdPKATHI 203
Cdd:TIGR01931 384 RLYSISSSQ---SEVGDEVHLTVGVVRY--QAHGRA---RLGGASGFLAErLKEGDTVPVYIEPNDNFRLPED-PDTPII 454
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  204 MIATGTGVAPYRGylrrmFMENVPNFKFDGLAWLFLGVAN-SDSLLYDEEFAGYRKDyPENFRYDKALSREEKNKkggkM 282
Cdd:TIGR01931 455 MIGPGTGVAPFRA-----FMQERAEDGAKGKNWLFFGNPHfTTDFLYQVEWQNYLKK-GVLTKMDLAFSRDQAEK----I 524
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334186381  283 YVQDKIEEYSDEIFKLLDNGAHIYFCG-LKGMMPGIQDTLKRVAEERG----ESWEQKLTQLRKNKQWHVEVY 350
Cdd:TIGR01931 525 YVQHRIREQGAELWQWLQEGAHIYVCGdAKKMAKDVHQALLDIIAKEGhldaEEAEEYLTDLRVEKRYQRDVY 597
 
Name Accession Description Interval E-value
PLN03116 PLN03116
ferredoxin--NADP+ reductase; Provisional
53-350 0e+00

ferredoxin--NADP+ reductase; Provisional


Pssm-ID: 215586 [Multi-domain]  Cd Length: 307  Bit Score: 690.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  53 DPKETPLNLFRPKEPYTATIVSVERIVGPQAPGETCHIVIDHDGNVPYWEGQSYGVIPPGENPKKPGAPHNVRLYSIAST 132
Cdd:PLN03116  10 DAKEPPLNLYKPKAPYTATIVSVERIVGPKAPGETCHIVIDHGGNVPYWEGQSYGVIPPGTNPKKPGAPHNVRLYSIAST 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 133 RYGDSFDGKTASLCVRRAIYYDPETGKEDPSKAGVCSNFLCNAKPGDKVKITGPSGKVMLLPEDDPKATHIMIATGTGVA 212
Cdd:PLN03116  90 RYGDDFDGKTASLCVRRAVYYDPETGKEDPAKKGVCSNFLCDAKPGDKVQITGPSGKVMLLPEEDPNATHIMVATGTGIA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 213 PYRGYLRRMFMENVPNFKFDGLAWLFLGVANSDSLLYDEEFAGYRKDYPENFRYDKALSREEKNKKGGKMYVQDKIEEYS 292
Cdd:PLN03116 170 PFRGFLRRMFMEDVPAFKFGGLAWLFLGVANSDSLLYDDEFERYLKDYPDNFRYDYALSREQKNKKGGKMYVQDKIEEYS 249
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334186381 293 DEIFKLLDNGAHIYFCGLKGMMPGIQDTLKRVAEERGESWEQKLTQLRKNKQWHVEVY 350
Cdd:PLN03116 250 DEIFKLLDNGAHIYFCGLKGMMPGIQDTLKRVAEERGESWEEKLSGLKKNKQWHVEVY 307
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
60-350 1.50e-180

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: 501.08  E-value: 1.50e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  60 NLFRPKEPYTATIVSVERIVGPQAPGETCHIVIDHDGNVPYWEGQSYGVIPPGENPKkPGAPHNVRLYSIASTRYGDSFD 139
Cdd:cd06208    1 NLYKPKNPLIGKVVSNTRLTGPDAPGEVCHIVIDHGGKLPYLEGQSIGIIPPGTDAK-NGKPHKLRLYSIASSRYGDDGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 140 GKTASLCVRRAIYYDPETgkeDPSKAGVCSNFLCNAKPGDKVKITGPSGKVMLLPeDDPKATHIMIATGTGVAPYRGYLR 219
Cdd:cd06208   80 GKTLSLCVKRLVYTDPET---DETKKGVCSNYLCDLKPGDDVQITGPVGKTMLLP-EDPNATLIMIATGTGIAPFRSFLR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 220 RMFMENVPNFKFDGLAWLFLGVANSDSLLYDEEFAGYRKDYPENFRYDKALSREEKNKKGGKMYVQDKIEEYSDEIFKLL 299
Cdd:cd06208  156 RLFREKHADYKFTGLAWLFFGVPNSDSLLYDDELEKYPKQYPDNFRIDYAFSREQKNADGGKMYVQDRIAEYAEEIWNLL 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 334186381 300 DNGA-HIYFCGLKGMMPGIQDTLKRVAeERGESWEQKLTQLRKNKQWHVEVY 350
Cdd:cd06208  236 DKDNtHVYICGLKGMEPGVDDALTSVA-EGGLAWEEFWESLKKKGRWHVEVY 286
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
2-350 4.02e-120

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 351.23  E-value: 4.02e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381   2 ALSTTPSQMSVALPTRIDGSS--RSMIKVQSISFTDKSW-GPPLLRLDSKSRSLDPKETP---------------LNLFR 63
Cdd:PLN03115   7 AAVSLPSSKSSSLPARTSAISpeRIRLKKGPLYYRNNVSsGKRVVSIRAQVTTETTTEAPakvvkvskkneegvvVNKFR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  64 PKEPYTATIVSVERIVGPQAPGETCHIVIDHDGNVPYWEGQSYGVIPPGENpkKPGAPHNVRLYSIASTRYGDSFDGKTA 143
Cdd:PLN03115  87 PKEPYTGRCLLNTKITGDDAPGETWHMVFSTEGEIPYREGQSIGVIPDGID--KNGKPHKLRLYSIASSALGDFGDSKTV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 144 SLCVRRAIYydpeTGKEDPSKAGVCSNFLCNAKPGDKVKITGPSGKVMLLPEDdPKATHIMIATGTGVAPYRGYLRRMFM 223
Cdd:PLN03115 165 SLCVKRLVY----TNDQGEIVKGVCSNFLCDLKPGAEVKITGPVGKEMLMPKD-PNATIIMLATGTGIAPFRSFLWKMFF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 224 ENVPNFKFDGLAWLFLGVANSDSLLYDEEFAGYRKDYPENFRYDKALSREEKNKKGGKMYVQDKIEEYSDEIFKLL--DN 301
Cdd:PLN03115 240 EKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQTNAKGEKMYIQTRMAEYAEELWELLkkDN 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 334186381 302 gAHIYFCGLKGMMPGIQDTLKRVAEERGESWEQKLTQLRKNKQWHVEVY 350
Cdd:PLN03115 320 -TYVYMCGLKGMEKGIDDIMVSLAAKDGIDWFEYKKQLKKAEQWNVEVY 367
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
71-350 2.22e-74

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: 230.69  E-value: 2.22e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  71 TIVSVERIVGPQAPGETCHIVID--HDGNVPYWEGQSYGVIPPGenpkkpgaPHNVRLYSIASTRygdSFDGKTASLCVR 148
Cdd:cd06182    1 AITVNRKLTPPDSPRSTRHLEFDlsGNSVLKYQPGDHLGVIPPN--------PLQPRYYSIASSP---DVDPGEVHLCVR 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 149 RAIYYDPETgkedPSKAGVCSNFLCNAKPGDKVKITGPSGKVMLLPEDdPKATHIMIATGTGVAPYRGYLRRMFMENVPN 228
Cdd:cd06182   70 VVSYEAPAG----RIRKGVCSNFLAGLQLGAKVTVFIRPAPSFRLPKD-PTTPIIMVGPGTGIAPFRGFLQERAALRANG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 229 fKFDGLAWLFLGVANSDS-LLYDEEFAGYRKDyPENFRYDKALSREEKNKKggkMYVQDKIEEYSDEIFKLLDNGAHIYF 307
Cdd:cd06182  145 -KARGPAWLFFGCRNFASdYLYREELQEALKD-GALTRLDVAFSREQAEPK---VYVQDKLKEHAEELRRLLNEGAHIYV 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 334186381 308 CG-LKGMMPGIQDTLKRVAEERG----ESWEQKLTQLRKNKQWHVEVY 350
Cdd:cd06182  220 CGdAKSMAKDVEDALVKIIAKAGgvdeSDAEEYLKELEDEGRYVEDVW 267
SiR cd06199
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
125-350 1.04e-38

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: 140.83  E-value: 1.04e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 125 RLYSIASTRygdSFDGKTASLCVRrAIYYDPETGKedpsKAGVCSNFLCN-AKPGDKVKI---TGPSGKvmlLPEDdPKA 200
Cdd:cd06199  147 RLYSIASSP---KAVPDEVHLTVA-VVRYESHGRE----RKGVASTFLADrLKEGDTVPVfvqPNPHFR---LPED-PDA 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 201 THIMIATGTGVAPYRGYLRRMFMENVPnfkfdGLAWLFLGVANSDS-LLYDEEFAGYRKDYPENfRYDKALSREEKNKkg 279
Cdd:cd06199  215 PIIMVGPGTGIAPFRAFLQEREATGAK-----GKNWLFFGERHFATdFLYQDELQQWLKDGVLT-RLDTAFSRDQAEK-- 286
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334186381 280 gkMYVQDKIEEYSDEIFKLLDNGAHIYFCG-LKGMMPGIQDTLKRVAEERGESWEQK----LTQLRKNKQWHVEVY 350
Cdd:cd06199  287 --VYVQDRMREQGAELWAWLEEGAHFYVCGdAKRMAKDVDAALLDIIATEGGMDEEEaeayLKELKKEKRYQRDVY 360
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
125-350 7.51e-35

Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440138 [Multi-domain]  Cd Length: 561  Bit Score: 133.73  E-value: 7.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 125 RLYSIAStrygdSF--DGKTASLCVRRAIYydPETGKEdpsKAGVCSNFLCNAKPGDKVKI---TGPSGKvmlLPEDdPK 199
Cdd:COG0369  349 RLYSISS-----SPkaHPDEVHLTVGVVRY--EASGRE---RKGVASTYLADLEEGDTVPVfvePNPNFR---LPAD-PD 414
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 200 ATHIMIATGTGVAPYRGYL--RRmfmenvpNFKFDGLAWLFLGVANSDS-LLYDEEFAGYRKDypenfRYDKALSREEkn 276
Cdd:COG0369  415 TPIIMIGPGTGIAPFRAFLqeRE-------ARGASGKNWLFFGDRHFTTdFLYQTELQAWLKDgv-ltRLDLAFSRDQ-- 484
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334186381 277 kkGGKMYVQDKIEEYSDEIFKLLDNGAHIYFCG-LKGMMPGIQDTLKRVAEERG----ESWEQKLTQLRKNKQWHVEVY 350
Cdd:COG0369  485 --AEKIYVQHRLLEQGAELWAWLEEGAHVYVCGdASRMAKDVDAALLDIIAEHGglseEEAEEYLAELRAEKRYQRDVY 561
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
204-319 1.82e-34

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


Pssm-ID: 425503 [Multi-domain]  Cd Length: 109  Bit Score: 122.37  E-value: 1.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  204 MIATGTGVAPYRGYLRRMFMENvpnfKFDGLAWLFLGVANSDSLLYDEEFAGYRKDYPENFRYDKALSREEKNKKGGKMY 283
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDP----KDPTQVVLVFGNRNEDDILYREELDELAEKHPGRLTVVYVVSRPEAGWTGGKGR 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 334186381  284 VQDKIEEYSDEIfklLDNGAHIYFCGLKGMMPGIQD 319
Cdd:pfam00175  77 VQDALLEDHLSL---PDEETHVYVCGPPGMIKAVRK 109
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
78-328 9.14e-34

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: 124.10  E-value: 9.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  78 IVGPQAPGETCHIVIDHDGNVPYWEGQSYGVIPPGENPKKpgaphnVRLYSIASTrygdSFDGKTASLCVRRaiyydpet 157
Cdd:cd00322    1 VATEDVTDDVRLFRLQLPNGFSFKPGQYVDLHLPGDGRGL------RRAYSIASS----PDEEGELELTVKI-------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 158 gkedpSKAGVCSNFLCNAKPGDKVKITGPSGKVMLLPEDDPKAthIMIATGTGVAPYRGYLRRMFmenvpNFKFDGLAWL 237
Cdd:cd00322   63 -----VPGGPFSAWLHDLKPGDEVEVSGPGGDFFLPLEESGPV--VLIAGGIGITPFRSMLRHLA-----ADKPGGEITL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 238 FLGVANSDSLLYDEEFAGYRKDYPeNFRYDKALSREEKNKKGgkmYVQDKIEEYSDEIFKLLDNGAHIYFCGLKGMMPGI 317
Cdd:cd00322  131 LYGARTPADLLFLDELEELAKEGP-NFRLVLALSRESEAKLG---PGGRIDREAEILALLPDDSGALVYICGPPAMAKAV 206
                        250
                 ....*....|...
gi 334186381 318 QDTL--KRVAEER 328
Cdd:cd00322  207 REALvsLGVPEER 219
cysJ TIGR01931
sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an ...
125-350 1.11e-31

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: 125.19  E-value: 1.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  125 RLYSIASTRygdSFDGKTASLCVRRAIYydPETGKEdpsKAGVCSNFLCN-AKPGDKVKITGPSGKVMLLPEDdPKATHI 203
Cdd:TIGR01931 384 RLYSISSSQ---SEVGDEVHLTVGVVRY--QAHGRA---RLGGASGFLAErLKEGDTVPVYIEPNDNFRLPED-PDTPII 454
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  204 MIATGTGVAPYRGylrrmFMENVPNFKFDGLAWLFLGVAN-SDSLLYDEEFAGYRKDyPENFRYDKALSREEKNKkggkM 282
Cdd:TIGR01931 455 MIGPGTGVAPFRA-----FMQERAEDGAKGKNWLFFGNPHfTTDFLYQVEWQNYLKK-GVLTKMDLAFSRDQAEK----I 524
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334186381  283 YVQDKIEEYSDEIFKLLDNGAHIYFCG-LKGMMPGIQDTLKRVAEERG----ESWEQKLTQLRKNKQWHVEVY 350
Cdd:TIGR01931 525 YVQHRIREQGAELWQWLQEGAHIYVCGdAKKMAKDVHQALLDIIAKEGhldaEEAEEYLTDLRVEKRYQRDVY 597
methionine_synthase_red cd06203
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ...
125-350 1.23e-31

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: 122.82  E-value: 1.23e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 125 RLYSIASTRygdSFDGKTASLCVRRAiyydpetgkEDPSKaGVCSNFL-----CNAKPGDKVKITGPSGKVMLLPEDDPK 199
Cdd:cd06203  175 RPYSIASSP---LEGPGKLRFIFSVV---------EFPAK-GLCTSWLeslclSASSHGVKVPFYLRSSSRFRLPPDDLR 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 200 ATHIMIATGTGVAPYRGYL--RRMFMENVPNFKFdGLAWLFLGVANSD-SLLYDEEFAGYRKDYPENfRYDKALSREEkN 276
Cdd:cd06203  242 RPIIMVGPGTGVAPFLGFLqhREKLKESHTETVF-GEAWLFFGCRHRDrDYLFRDELEEFLEEGILT-RLIVAFSRDE-N 318
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 277 KKGGKMYVQDKIEEYSDEIFK-LLDNGAHIYFCG-LKGMMPGIQDTLKR-VAEERGESWEQ---KLTQLRKNKQWHVEVY 350
Cdd:cd06203  319 DGSTPKYVQDKLEERGKKLVDlLLNSNAKIYVCGdAKGMAKDVRDTFVDiLSKELGLDKLEakkLLARLRKEDRYLEDVW 398
CyPoR_like cd06207
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
125-350 1.52e-30

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: 119.30  E-value: 1.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 125 RLYSIASTrygDSFDGKTASLCVRRAIYYDPETGkedpSKAGVCSNFLCNAKPGDKVKI-TGPSgkVMLLPeDDPKATHI 203
Cdd:cd06207  165 RYYSISSS---PLKNPNEVHLLVSLVSWKTPSGR----SRYGLCSSYLAGLKVGQRVTVfIKKS--SFKLP-KDPKKPII 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 204 MIATGTGVAPYRGYLR-RMFMENVPnfKFDGLAWLFLGVANSDS-LLYDEEFAGYRKDYPENfRYDKALSREEKNkkggK 281
Cdd:cd06207  235 MVGPGTGLAPFRAFLQeRAALLAQG--PEIGPVLLYFGCRHEDKdYLYKEELEEYEKSGVLT-TLGTAFSRDQPK----K 307
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334186381 282 MYVQDKIEEYSDEIFKLLDNGAH-IYFCGLKGMMP-----GIQDTLKRVAEERGESWEQKLTQLRKNKQWHVEVY 350
Cdd:cd06207  308 VYVQDLIRENSDLVYQLLEEGAGvIYVCGSTWKMPpdvqeAFEEILKKHGGGDEELAEKKIEELEERGRYVVEAW 382
CYPOR cd06204
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
159-342 9.05e-29

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: 115.05  E-value: 9.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 159 KEDPSKAGVCSNFLCNAKP---GDKVKITGP---------SGKV--------MLLPEDdPKATHIMIATGTGVAPYRGYL 218
Cdd:cd06204  206 PTGRIIKGVATNWLLALKPalnGEKPPTPYYlsgprkkggGSKVpvfvrrsnFRLPTK-PSTPVIMIGPGTGVAPFRGFI 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 219 --RRMFMENVPNFkfdGLAWLFLGVANSDS-LLYDEEFAGYRKDyPENFRYDKALSREEknkkGGKMYVQDKIEEYSDEI 295
Cdd:cd06204  285 qeRAALKESGKKV---GPTLLFFGCRHPDEdFIYKDELEEYAKL-GGLLELVTAFSREQ----PKKVYVQHRLAEHAEQV 356
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 334186381 296 FKLLDNGAHIYFCG-LKGMMPGIQDTLKRVAEERGESWEQKLTQLRKN 342
Cdd:cd06204  357 WELINEGAYIYVCGdAKNMARDVEKTLLEILAEQGGMTETEAEEYVKK 404
bifunctional_CYPOR cd06206
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ...
124-330 3.06e-27

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: 110.43  E-value: 3.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 124 VRLYSIASTrygDSFDGKTASLCVrraIYYDPETGKEDPSKAGVCSNFLCNAKPGDKVKIT-GPSGKVMLLPeDDPKATH 202
Cdd:cd06206  161 PRQYSISSS---PLVDPGHATLTV---SVLDAPALSGQGRYRGVASSYLSSLRPGDSIHVSvRPSHSAFRPP-SDPSTPL 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 203 IMIATGTGVAPYRGYL--RRMFMENVPNFkfdGLAWLFLGVANSDS-LLYDEEFAGYRKDYPENFRYdkALSReekNKKG 279
Cdd:cd06206  234 IMIAAGTGLAPFRGFLqeRAALLAQGRKL---APALLFFGCRHPDHdDLYRDELEEWEAAGVVSVRR--AYSR---PPGG 305
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334186381 280 GKMYVQDKIEEYSDEIFKLLDNGAHIYFCGLKGMMPGIQDTLKRVAEERGE 330
Cdd:cd06206  306 GCRYVQDRLWAEREEVWELWEQGARVYVCGDGRMAPGVREVLKRIYAEKDE 356
PRK06214 PRK06214
sulfite reductase subunit alpha;
65-350 7.57e-27

sulfite reductase subunit alpha;


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 110.93  E-value: 7.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  65 KEPYTATIVSVERIVGPQAPGETCHIVID-HDGNVPYWEGQSYGVIP--------------------------------- 110
Cdd:PRK06214 166 DNPVEATFLSRRRLNKPGSEKETWHVEIDlAGSGLDYEVGDSLGLFPandpalvdaviaalgappefpiggktlrealle 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 111 -------------------------------PGENP--------------KKPGA------------PHNVRLYSIASTR 133
Cdd:PRK06214 246 dvslgpapdglfellsyitggaarkkaralaAGEDPdgdaatldvlaaleKFPGIrpdpeafvealdPLQPRLYSISSSP 325
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 134 YGDSfdGKTaSLCVRRAIYydpETGKEdpSKAGVCSNFLCN-AKPGDKVKITGPSGKVMLLPEDdPKATHIMIATGTGVA 212
Cdd:PRK06214 326 KATP--GRV-SLTVDAVRY---EIGSR--LRLGVASTFLGErLAPGTRVRVYVQKAHGFALPAD-PNTPIIMVGPGTGIA 396
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 213 PYRGYLRRMFMENVPnfkfdGLAWLFLGVANSDS-LLYDEEFAGYRKDYPENfRYDKALSREEknkkGGKMYVQDKIEEY 291
Cdd:PRK06214 397 PFRAFLHERAATKAP-----GRNWLFFGHQRSATdFFYEDELNGLKAAGVLT-RLSLAWSRDG----EEKTYVQDRMREN 466
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334186381 292 SDEIFKLLDNGAHIYFCG-LKGMMPGIQDTLKR-VAEERGESWEQ---KLTQLRKNKQWHVEVY 350
Cdd:PRK06214 467 GAELWKWLEEGAHFYVCGdAKRMAKDVERALVDiVAQFGGRSPDEavaFVAELKKAGRYQADVY 530
Nitric_oxide_synthase cd06202
The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses ...
125-350 1.84e-22

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: 97.40  E-value: 1.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 125 RLYSIAST--RYGDSFDGKTAslcvrrAIYYDPETGKeDPSKAGVCSNFLCNAKPGDKVKITGPSGKVMLLPEDdPKATH 202
Cdd:cd06202  178 RYYSISSSpdMYPGEIHLTVA------VVSYRTRDGQ-GPVHHGVCSTWLNGLTPGDTVPCFVRSAPSFHLPED-PSVPV 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 203 IMIATGTGVAPYRGYLR-RMF---MENVPNFKFdGLAWLFLGVANSDSL-LYDEEFAGYRKDypENF-RYDKALSREEKN 276
Cdd:cd06202  250 IMVGPGTGIAPFRSFWQqRQYdlrMSEDPGKKF-GDMTLFFGCRNSTIDdIYKEETEEAKNK--GVLtEVYTALSREPGK 326
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334186381 277 KkggKMYVQDKIEEYSDEIFKLL-DNGAHIYFCGLKGMMPGIQDTLKRVAEERGESWEQK----LTQLRKNKQWHVEVY 350
Cdd:cd06202  327 P---KTYVQDLLKEQAESVYDALvREGGHIYVCGDVTMAEDVSQTIQRILAEHGNMSAEEaeefILKLRDENRYHEDIF 402
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
166-350 7.93e-22

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


Pssm-ID: 99792 [Multi-domain]  Cd Length: 241  Bit Score: 92.63  E-value: 7.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 166 GVCSNFLCNAKPGDKVKIT-GPSGKvMLLPEDDPKATHIMIATGTGVAPYRGYLRrmfmenvpnfkfDGLAW-------L 237
Cdd:cd06195   68 GPLTPRLFKLKPGDTIYVGkKPTGF-LTLDEVPPGKRLWLLATGTGIAPFLSMLR------------DLEIWerfdkivL 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 238 FLGVANSDSLLYDEEFAGYRKDYPENFRYDKALSReEKNKKGGKMYVQDKIEeySDEIFK-----LLDNGAHIYFCGLKG 312
Cdd:cd06195  135 VHGVRYAEELAYQDEIEALAKQYNGKFRYVPIVSR-EKENGALTGRIPDLIE--SGELEEhaglpLDPETSHVMLCGNPQ 211
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 334186381 313 MmpgIQDTlKRVAEERGesweQKLTQLRKNKQWHVEVY 350
Cdd:cd06195  212 M---IDDT-QELLKEKG----FSKNHRRKPGNITVEKY 241
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
64-324 8.78e-22

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: 93.55  E-value: 8.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  64 PKEPYTATIVSVERIVGPQAPGETCHI-------VIDHDGNVPYWE-GQSYGVIPPGENPkkpgaphnVRLYSIASTryg 135
Cdd:cd06201   40 KRLPRTKALELVERKDYGAAVQAPTAIlrfkpakRKLSGKGLPSFEaGDLLGILPPGSDV--------PRFYSLASS--- 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 136 dSFDGkTASLCVRRaiyydpetgkedpSKAGVCSNFLCNAKPGDKVKITGPSGKVMLLPEDdpKATHIMIATGTGVAPYR 215
Cdd:cd06201  109 -SSDG-FLEICVRK-------------HPGGLCSGYLHGLKPGDTIKAFIRPNPSFRPAKG--AAPVILIGAGTGIAPLA 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 216 GYLRRMFMENvPnfkfdglAWLFLGVANSDS-LLYDEEFAGYRKDYP-ENFRYdkALSREEknkkgGKMYVQDKIEEYSD 293
Cdd:cd06201  172 GFIRANAARR-P-------MHLYWGGRDPASdFLYEDELDQYLADGRlTQLHT--AFSRTP-----DGAYVQDRLRADAE 236
                        250       260       270
                 ....*....|....*....|....*....|.
gi 334186381 294 EIFKLLDNGAHIYFCGLKGMMPGIQDTLKRV 324
Cdd:cd06201  237 RLRRLIEDGAQIMVCGSRAMAQGVAAVLEEI 267
cysJ PRK10953
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
125-350 4.50e-21

NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;


Pssm-ID: 182862 [Multi-domain]  Cd Length: 600  Bit Score: 94.40  E-value: 4.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 125 RLYSIASTRygdSFDGKTASLCVRrAIYYDPEtGKedpSKAGVCSNFLcnakpGDKVKITGPSgKVMLLPED------DP 198
Cdd:PRK10953 387 RLYSIASSQ---AEVENEVHITVG-VVRYDIE-GR---ARAGGASSFL-----ADRLEEEGEV-RVFIEHNDnfrlpaNP 452
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 199 KATHIMIATGTGVAPYRGylrrmFMENVPNFKFDGLAWLFLGVAN-SDSLLYDEEFAGYRKDYPENfRYDKALSREEKNK 277
Cdd:PRK10953 453 ETPVIMIGPGTGIAPFRA-----FMQQRAADGAPGKNWLFFGNPHfTEDFLYQVEWQRYVKEGLLT-RIDLAWSRDQKEK 526
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334186381 278 kggkMYVQDKIEEYSDEIFKLLDNGAHIYFCGLKGMMPGI--QDTLKRVAEERGESWEQK---LTQLRKNKQWHVEVY 350
Cdd:PRK10953 527 ----IYVQDKLREQGAELWRWINDGAHIYVCGDANRMAKDveQALLEVIAEFGGMDTEAAdefLSELRVERRYQRDVY 600
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
68-328 6.98e-21

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 89.85  E-value: 6.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  68 YTATIVSVERivgpQAPGeTCHIVIDHDGNVP---YWEGQSYGVIPPGEnpkkpGAPHnVRLYSIASTRYGDSFdgktaS 144
Cdd:COG1018    4 RPLRVVEVRR----ETPD-VVSFTLEPPDGAPlprFRPGQFVTLRLPID-----GKPL-RRAYSLSSAPGDGRL-----E 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 145 LCVRRaiyyDPEtgkedpskaGVCSNFLC-NAKPGDKVKITGPSGKvmLLPEDDPKATHIMIATGTGVAPYRGYLRRMFM 223
Cdd:COG1018   68 ITVKR----VPG---------GGGSNWLHdHLKVGDTLEVSGPRGD--FVLDPEPARPLLLIAGGIGITPFLSMLRTLLA 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 224 ENvPNFKFdglaWLFLGVANSDSLLYDEEFAGYRKDYPeNFRYDKALSREEKNKKGgkmYV-QDKIEEysdeifkLLDN- 301
Cdd:COG1018  133 RG-PFRPV----TLVYGARSPADLAFRDELEALAARHP-RLRLHPVLSREPAGLQG---RLdAELLAA-------LLPDp 196
                        250       260       270
                 ....*....|....*....|....*....|
gi 334186381 302 -GAHIYFCGLKGMMPGIQDTLKR--VAEER 328
Cdd:COG1018  197 aDAHVYLCGPPPMMEAVRAALAElgVPEER 226
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
56-328 1.05e-19

Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase


Pssm-ID: 442118 [Multi-domain]  Cd Length: 396  Bit Score: 89.15  E-value: 1.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  56 ETPLNLFRPKEpYTATIVSVE-------RIVgpqapgetchIVIDHDGNVPYWEGQ-------------SYGVIPPGENP 115
Cdd:COG2871  121 EVPEEVFGVKK-WEATVVSNEnvttfikELV----------LELPEGEEIDFKAGQyiqievppyevdfKDFDIPEEEKF 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 116 KKPGAPHN--VRLYSIAStrYGDsfDGKTASLCVRRAIYYDPETGkedpskaGVCSNFLCNAKPGDKVKITGPSGKVMLL 193
Cdd:COG2871  190 GLFDKNDEevTRAYSMAN--YPA--EKGIIELNIRIATPPMDVPP-------GIGSSYIFSLKPGDKVTISGPYGEFFLR 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 194 PEDDPKathIMIATGTGVAPYRGYLRRMFMENVPNFKfdglAWLFLGVANSDSLLYDEEFAGYRKDYPeNFRYDKALSR- 272
Cdd:COG2871  259 DSDREM---VFIGGGAGMAPLRSHIFDLLERGKTDRK----ITFWYGARSLRELFYLEEFRELEKEHP-NFKFHPALSEp 330
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334186381 273 -EEKNKKGGKMYVQDKIEEysdeifKLLDN-----GAHIYFCGLKGMMPGIQDTLK--RVAEER 328
Cdd:COG2871  331 lPEDNWDGETGFIHEVLYE------NYLKDhpapeDCEAYLCGPPPMIDAVIKMLDdlGVEEEN 388
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
124-328 5.77e-19

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


Pssm-ID: 99785 [Multi-domain]  Cd Length: 283  Bit Score: 85.43  E-value: 5.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 124 VRLYSIASTRYgdsfDGKTASLCVRRAIyydPETGKEDpSKAGVCSNFLCNAKPGDKVKITGPSGKVMLLPEDdpkATHI 203
Cdd:cd06188   86 SRAYSLANYPA----EEGELKLNVRIAT---PPPGNSD-IPPGIGSSYIFNLKPGDKVTASGPFGEFFIKDTD---REMV 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 204 MIATGTGVAPYRGYLRRMFMENVPNFKFDglawLFLGVANSDSLLYDEEFAGYRKDYPeNFRYDKALSR--EEKNKKGGK 281
Cdd:cd06188  155 FIGGGAGMAPLRSHIFHLLKTLKSKRKIS----FWYGARSLKELFYQEEFEALEKEFP-NFKYHPVLSEpqPEDNWDGYT 229
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 334186381 282 MYVQDKIEEYSDEIFKLLDNgAHIYFCGLKGMMPGIQDTLKRVAEER 328
Cdd:cd06188  230 GFIHQVLLENYLKKHPAPED-IEFYLCGPPPMNSAVIKMLDDLGVPR 275
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
64-328 1.45e-18

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: 83.53  E-value: 1.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  64 PKEPYTATIVSVE----RIVGpqapgetCHIVIDHDGNVPYWEGQSYGV-IPPGENPkkpgaphnvRLYSIASTrygdSF 138
Cdd:cd06211    3 NVKDFEGTVVEIEdltpTIKG-------VRLKLDEPEEIEFQAGQYVNLqAPGYEGT---------RAFSIASS----PS 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 139 DGKTASLCVRRAiyydpetgkedpsKAGVCSNFLCNA-KPGDKVKITGPSGKVMLLPEDDPKAthIMIATGTGVAPYRGY 217
Cdd:cd06211   63 DAGEIELHIRLV-------------PGGIATTYVHKQlKEGDELEISGPYGDFFVRDSDQRPI--IFIAGGSGLSSPRSM 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 218 LRRMFMENvpnfkFDGLAWLFLGVANSDSLLYDEEFAGYRKDYPeNFRYDKALSR--EEKNKKGGKMYVQDKIEEYSDEI 295
Cdd:cd06211  128 ILDLLERG-----DTRKITLFFGARTRAELYYLDEFEALEKDHP-NFKYVPALSRepPESNWKGFTGFVHDAAKKHFKND 201
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 334186381 296 FKlldnGAHIYFCGLKGMMPGIQDTL--KRVAEER 328
Cdd:cd06211  202 FR----GHKAYLCGPPPMIDACIKTLmqGRLFERD 232
SiR_like1 cd06200
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
118-350 3.78e-17

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: 79.63  E-value: 3.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 118 PGAPHNVRLYSIASTRygdsfDGKTASLCVRRAIYYDpetgkedpSKAGVCSNFLC-NAKPGDKVKITGPSGKVMLLPED 196
Cdd:cd06200   42 PRHPLPHREYSIASLP-----ADGALELLVRQVRHAD--------GGLGLGSGWLTrHAPIGASVALRLRENPGFHLPDD 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 197 DpkATHIMIATGTGVAPYRGYLR-RMFMENVPNfkfdglaWLFLGVANSD-SLLYDEEFAGYRKDyPENFRYDKALSREE 274
Cdd:cd06200  109 G--RPLILIGNGTGLAGLRSHLRaRARAGRHRN-------WLLFGERQAAhDFFCREELEAWQAA-GHLARLDLAFSRDQ 178
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334186381 275 KNKKggkmYVQDKIEEYSDEIFKLLDNGAHIYFCG-LKGMMPGIQDTLKRVAeerGESweqKLTQLRKNKQWHVEVY 350
Cdd:cd06200  179 AQKR----YVQDRLRAAADELRAWVAEGAAIYVCGsLQGMAPGVDAVLDEIL---GEE---AVEALLAAGRYRRDVY 245
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
166-334 1.08e-15

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


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 75.30  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 166 GVCSNFLCNAKPGDKVKITGPSGKVMLLPedDPKATHI-MIATGTGVAPYRGYLRRMFmenvPNFKFDGLAWLFLGVANS 244
Cdd:cd06183   72 GKMSQYLHSLKPGDTVEIRGPFGKFEYKP--NGKVKHIgMIAGGTGITPMLQLIRAIL----KDPEDKTKISLLYANRTE 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 245 DSLLYDEEFAGYRKDYPENFRYDKALSREEKNKKGGKMYVQDK-IEEYsdeIFKLLDNGAHIYFCGLKGMmpgIQDTLKR 323
Cdd:cd06183  146 EDILLREELDELAKKHPDRFKVHYVLSRPPEGWKGGVGFITKEmIKEH---LPPPPSEDTLVLVCGPPPM---IEGAVKG 219
                        170
                 ....*....|.
gi 334186381 324 VAEERGESWEQ 334
Cdd:cd06183  220 LLKELGYKKDN 230
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
67-309 1.60e-15

Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. As a Class I bacterial dioxygenases, benzoate dioxygenase like proteins combine an [2Fe-2S] cluster containing N-terminal ferredoxin at the end fused to an FAD/NADP(P) domain. In dioxygenase FAD/NAD(P) binding domain, the reductase transfers 2 electrons from NAD(P)H to the oxygenase which insert into an aromatic substrate, an initial step in microbial aerobic degradation of aromatic rings. Flavin oxidoreductases use flavins as substrates, unlike flavoenzymes which have a flavin prosthetic group.


Pssm-ID: 99805 [Multi-domain]  Cd Length: 228  Bit Score: 74.55  E-value: 1.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  67 PYTATIVSVERIvGPQAPGETchIVIDHDGNVPYWEGQSYGVIPPGENpkkpgaphNVRLYSIASTRygdsfDGKTASLC 146
Cdd:cd06209    1 TFEATVTEVERL-SDSTIGLT--LELDEAGALAFLPGQYVNLQVPGTD--------ETRSYSFSSAP-----GDPRLEFL 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 147 VRRAiyydpetgkedPSkaGVCSNFLCN-AKPGDKVKITGPSGKVMLLPEDDPkatHIMIATGTGVAPYRGYLRRMfmen 225
Cdd:cd06209   65 IRLL-----------PG--GAMSSYLRDrAQPGDRLTLTGPLGSFYLREVKRP---LLMLAGGTGLAPFLSMLDVL---- 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 226 vpnfKFDGLAW---LFLGVANSDSLLYDEEFAGYRKDYPeNFRYDKALSREEKNkKGGKMYVQDKIEEYsdeifKLLDNG 302
Cdd:cd06209  125 ----AEDGSAHpvhLVYGVTRDADLVELDRLEALAERLP-GFSFRTVVADPDSW-HPRKGYVTDHLEAE-----DLNDGD 193

                 ....*..
gi 334186381 303 AHIYFCG 309
Cdd:cd06209  194 VDVYLCG 200
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
71-329 3.56e-14

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 71.05  E-value: 3.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  71 TIVSVERIvgpqAPGeTCHIVIDH-DGNVPYWEGQSYGVIPPGENPKKPgaphnvrlYSIASTrygDSFDGkTASLCVRR 149
Cdd:COG0543    1 KVVSVERL----APD-VYLLRLEApLIALKFKPGQFVMLRVPGDGLRRP--------FSIASA---PREDG-TIELHIRV 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 150 AiyydpetgkedpskaGVCSNFLCNAKPGDKVKITGPSGKVMLLPEDDPKAthIMIATGTGVAPYRGYLRRMFMENVPnf 229
Cdd:COG0543   64 V---------------GKGTRALAELKPGDELDVRGPLGNGFPLEDSGRPV--LLVAGGTGLAPLRSLAEALLARGRR-- 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 230 kfdglAWLFLGVANSDSLLYDEEFAGYRkdypeNFRYDKALSREEKNKKGgkmYVQDKIEEYSDEifkllDNGAHIYFCG 309
Cdd:COG0543  125 -----VTLYLGARTPEDLYLLDELEALA-----DFRVVVTTDDGWYGRKG---FVTDALKELLAE-----DSGDDVYACG 186
                        250       260
                 ....*....|....*....|
gi 334186381 310 LKGMMpgiqDTLKRVAEERG 329
Cdd:COG0543  187 PPPMM----KAVAELLLERG 202
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
90-328 1.21e-12

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate, while mono-oxygenases (aka mixed oxygenases) add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.


Pssm-ID: 99784 [Multi-domain]  Cd Length: 224  Bit Score: 66.46  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  90 IVIDHDGNVPYWEGQSYGVippgenpKKPGAPHNVRLYSIAST--RYGdsfdgkTASLCVRRAiyydpetgkedpsKAGV 167
Cdd:cd06187   14 VRLQLDQPLPFWAGQYVNV-------TVPGRPRTWRAYSPANPpnEDG------EIEFHVRAV-------------PGGR 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 168 CSNFLCN-AKPGDKVKITGPSGKVMLLPEDDpkATHIMIATGTGVAPYRGYLRRMFMENVPNfkfdglaW--LFLGVANS 244
Cdd:cd06187   68 VSNALHDeLKVGDRVRLSGPYGTFYLRRDHD--RPVLCIAGGTGLAPLRAIVEDALRRGEPR-------PvhLFFGARTE 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 245 DSLLYDEEFAGYRKDYPeNFRYDKALSREEKNKKGGKMYVQDKIEEYSDEifkllDNGAHIYFCGLKGMMPGIQDTLKR- 323
Cdd:cd06187  139 RDLYDLEGLLALAARHP-WLRVVPVVSHEEGAWTGRRGLVTDVVGRDGPD-----WADHDIYICGPPAMVDATVDALLAr 212

                 ....*.
gi 334186381 324 -VAEER 328
Cdd:cd06187  213 gAPPER 218
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
68-323 1.05e-11

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate while mono-oxygenases add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.


Pssm-ID: 99809  Cd Length: 227  Bit Score: 63.87  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  68 YTATIVSVERIVGpqapgETCHIVIDHDGNVPYWEGQsYGvippgeNPKKPGAPhNVRLYSIASTRYGDSfdgkTASLCV 147
Cdd:cd06213    1 IRGTIVAQERLTH-----DIVRLTVQLDRPIAYKAGQ-YA------ELTLPGLP-AARSYSFANAPQGDG----QLSFHI 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 148 RRAiyydpetgkedPSkaGVCSNFL-CNAKPGDKVKITGPSGKVMLLPEDDPKathIMIATGTGVAPYRGYLRRMfmenv 226
Cdd:cd06213   64 RKV-----------PG--GAFSGWLfGADRTGERLTVRGPFGDFWLRPGDAPI---LCIAGGSGLAPILAILEQA----- 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 227 pnfKFDGL---AWLFLGVANSDSLLYDEEFAGYRKDYPENFRYDKALSREEKNK--KGGKMYVQDKIEEYsdeifklLDN 301
Cdd:cd06213  123 ---RAAGTkrdVTLLFGARTQRDLYALDEIAAIAARWRGRFRFIPVLSEEPADSswKGARGLVTEHIAEV-------LLA 192
                        250       260
                 ....*....|....*....|..
gi 334186381 302 GAHIYFCGLKGMMPGIQDTLKR 323
Cdd:cd06213  193 ATEAYLCGPPAMIDAAIAVLRA 214
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
176-328 1.96e-09

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 58.75  E-value: 1.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 176 KPGDKVKITGPSGKvMLLPEDDPKATHIMIATGTGVAPYRGYLRrmFMENVPNFKFDglAWLFLGVANSDSLLYDEEFAG 255
Cdd:COG4097  296 KPGTRVYVEGPYGR-FTFDRRDTAPRQVWIAGGIGITPFLALLR--ALAARPGDQRP--VDLFYCVRDEEDAPFLEELRA 370
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334186381 256 YRKDYPeNFRYDKALSREeknkkGGKMYVqDKIEEYSDEifkllDNGAHIYFCGLKGMMPGIQDTLKR--VAEER 328
Cdd:COG4097  371 LAARLA-GLRLHLVVSDE-----DGRLTA-ERLRRLVPD-----LAEADVFFCGPPGMMDALRRDLRAlgVPARR 433
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
125-328 2.68e-09

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


Pssm-ID: 99786 [Multi-domain]  Cd Length: 224  Bit Score: 56.79  E-value: 2.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 125 RLYSIASTRYGDSFdgktASLCVRRaiyydpetgkedpSKAGVCSNFLCNA-KPGDKVKITGPSGKVMLLPEDD-PkatH 202
Cdd:cd06189   42 RPFSIASAPHEDGE----IELHIRA-------------VPGGSFSDYVFEElKENGLVRIEGPLGDFFLREDSDrP---L 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 203 IMIATGTGVAPYRGYLrrmfmENVPNFKFDGLAWLFLGVANSDSLLYDEEFAGYRKDYPeNFRYDKALSREEKNKKGGKM 282
Cdd:cd06189  102 ILIAGGTGFAPIKSIL-----EHLLAQGSKRPIHLYWGARTEEDLYLDELLEAWAEAHP-NFTYVPVLSEPEEGWQGRTG 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 334186381 283 YVQDKI-EEYSDeifkLldNGAHIYFCGLKGMMPGIQDTL--KRVAEER 328
Cdd:cd06189  176 LVHEAVlEDFPD----L--SDFDVYACGSPEMVYAARDDFveKGLPEEN 218
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
122-328 4.52e-09

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


Pssm-ID: 99813 [Multi-domain]  Cd Length: 235  Bit Score: 56.12  E-value: 4.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 122 HNVRLYSIASTRYG-DSFDgktasLCVRRaiyydpetgKEDpskaGVCSNFLCN-AKPGDKVKITGPSGKVMLLP-EDDP 198
Cdd:cd06217   48 TAQRSYSIASSPTQrGRVE-----LTVKR---------VPG----GEVSPYLHDeVKVGDLLEVRGPIGTFTWNPlHGDP 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 199 KathIMIATGTGVAPYRGYLRRMFMENVPnfkfdGLAWLFLGVANSDSLLYDEEFAGYRKDYPeNFRYDKALSREEKNkk 278
Cdd:cd06217  110 V---VLLAGGSGIVPLMSMIRYRRDLGWP-----VPFRLLYSARTAEDVIFRDELEQLARRHP-NLHVTEALTRAAPA-- 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 334186381 279 gGKMYVQDKIEEYSDEIFKLLDNGAHIYFCGLKGMMPGIQDTLKR--VAEER 328
Cdd:cd06217  179 -DWLGPAGRITADLIAELVPPLAGRRVYVCGPPAFVEAATRLLLElgVPRDR 229
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
166-329 1.17e-08

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: 55.04  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 166 GVCSNFLCN-AKPGDKVKITGPSGkVMLLPEDDPkATHIMIATGTGVAPYRGYLRRMfmenvPNFKFDGLAWLFLGVANS 244
Cdd:cd06210   76 GAFSTYLETrAKVGQRLNLRGPLG-AFGLRENGL-RPRWFVAGGTGLAPLLSMLRRM-----AEWGEPQEARLFFGVNTE 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 245 DSLLYDEEFAGYRKDYPeNFRYDKALSREEKNKKGGKMYVQDKIEEYsdeiFKLLDNGAHIYFCGLKGMMPGIQDtlkrV 324
Cdd:cd06210  149 AELFYLDELKRLADSLP-NLTVRICVWRPGGEWEGYRGTVVDALRED----LASSDAKPDIYLCGPPGMVDAAFA----A 219

                 ....*
gi 334186381 325 AEERG 329
Cdd:cd06210  220 AREAG 224
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
66-329 1.55e-08

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


Pssm-ID: 99808 [Multi-domain]  Cd Length: 232  Bit Score: 54.64  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  66 EPYTATIVSVE-RIVGPQApgetchividhdgnVPYWEGQSYGVIPPGENPKkpgaphnvRLYSIASTrygDSFDGKTAS 144
Cdd:cd06212    9 EALTHDIRRLRlRLEEPEP--------------IKFFAGQYVDITVPGTEET--------RSFSMANT---PADPGRLEF 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 145 LCvrraiyydpetgKEDPSkaGVCSNFLCN-AKPGDKVKITGPSGKVMLLPEDDPKAthIMIATGTGVAPYRGYLRRMFM 223
Cdd:cd06212   64 II------------KKYPG--GLFSSFLDDgLAVGDPVTVTGPYGTCTLRESRDRPI--VLIGGGSGMAPLLSLLRDMAA 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 224 ENVpnfkfDGLAWLFLGVANSDSLLYDEEFAGYRKDYPeNFRYDKALSREEKNK--KGGKMYVQDKIEEYSDEIfklldN 301
Cdd:cd06212  128 SGS-----DRPVRFFYGARTARDLFYLEEIAALGEKIP-DFTFIPALSESPDDEgwSGETGLVTEVVQRNEATL-----A 196
                        250       260
                 ....*....|....*....|....*...
gi 334186381 302 GAHIYFCGLKGMMpgiqDTLKRVAEERG 329
Cdd:cd06212  197 GCDVYLCGPPPMI----DAALPVLEMSG 220
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
147-328 2.69e-08

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


Pssm-ID: 99810 [Multi-domain]  Cd Length: 241  Bit Score: 54.09  E-value: 2.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 147 VRRA--IYYDPETG------KEDPSkaGVCSNFLC-NAKPGDKVKITGPSGkVMLLPEDDPKATHIMIATGTGVAPyrgy 217
Cdd:cd06214   50 VRRSysICSSPGDDelritvKRVPG--GRFSNWANdELKAGDTLEVMPPAG-RFTLPPLPGARHYVLFAAGSGITP---- 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 218 lrrMF------MENVPNFKFDglawLFLGVANSDSLLYDEEFAGYRKDYPENFRYDKALSREEKNKKG--GKMyVQDKIE 289
Cdd:cd06214  123 ---VLsilktaLAREPASRVT----LVYGNRTEASVIFREELADLKARYPDRLTVIHVLSREQGDPDLlrGRL-DAAKLN 194
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 334186381 290 EYSDEIFKLlDNGAHIYFCGLKGMMPGIQDTLKR--VAEER 328
Cdd:cd06214  195 ALLKNLLDA-TEFDEAFLCGPEPMMDAVEAALLElgVPAER 234
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
172-329 3.82e-08

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


Pssm-ID: 99814 [Multi-domain]  Cd Length: 246  Bit Score: 53.70  E-value: 3.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 172 LCNAKPGDKVKITGPSGKVMLLPEDDPKAthIMIATGTGVAPYRgYLRRMFMENVPNFkfdglaWLFLGVANSDSLLYDE 251
Cdd:cd06218   73 LSELKAGDELDVLGPLGNGFDLPDDDGKV--LLVGGGIGIAPLL-FLAKQLAERGIKV------TVLLGFRSADDLFLVE 143
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334186381 252 EFAGYRKDYpenfrydkALSREEKNkKGGKMYVQDKIEEYSDEifkllDNGAHIYFCGLKGMMpgiqDTLKRVAEERG 329
Cdd:cd06218  144 EFEALGAEV--------YVATDDGS-AGTKGFVTDLLKELLAE-----ARPDVVYACGPEPML----KAVAELAAERG 203
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
176-323 4.13e-08

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: 53.03  E-value: 4.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 176 KPGDKVKITGPSGKVMLlpeDDPKATHIMIATGTGVAPYRGYLRRMfmenvPNFKFDGLAWLFLGVANSDSLLYDEEFAG 255
Cdd:cd06198   75 KPGTRVTVEGPYGRFTF---DDRRARQIWIAGGIGITPFLALLEAL-----AARGDARPVTLFYCVRDPEDAVFLDELRA 146
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334186381 256 YRKDYPENFrydKALSREEKNKKGGKMYVQDKIEEYSDeifklldngAHIYFCGLKGMMPGIQDTLKR 323
Cdd:cd06198  147 LAAAAGVVL---HVIDSPSDGRLTLEQLVRALVPDLAD---------ADVWFCGPPGMADALEKGLRA 202
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
159-321 3.59e-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: 50.33  E-value: 3.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 159 KEDPSKAGvcSNFLC-NAKPGDKVKITGPSGKVMLLPEDDPKAthIMIATGTGVAPYRGYLRRMfMENVPNFKFDGLawL 237
Cdd:cd06190   60 KRKPGGAA--SNALFdNLEPGDELELDGPYGLAYLRPDEDRDI--VCIAGGSGLAPMLSILRGA-ARSPYLSDRPVD--L 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 238 FLGVANSDSLLYDEEFAGYrKDYPENFRYDKALSREE----KNKKGGKMYVQDKIEEYSDEIFKlldnGAHIYFCGLKGM 313
Cdd:cd06190  133 FYGGRTPSDLCALDELSAL-VALGARLRVTPAVSDAGsgsaAGWDGPTGFVHEVVEATLGDRLA----EFEFYFAGPPPM 207

                 ....*...
gi 334186381 314 MPGIQDTL 321
Cdd:cd06190  208 VDAVQRML 215
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
125-329 4.42e-07

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


Pssm-ID: 99812 [Multi-domain]  Cd Length: 243  Bit Score: 50.30  E-value: 4.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 125 RLYSIASTrygDSFDGKTASLCVRRAiyydpetgkedpsKAGVCSNFLCN-AKPGDKVKITGPSGkVMLLPEDDPKAThI 203
Cdd:cd06216   65 RSYSLSSS---PTQEDGTITLTVKAQ-------------PDGLVSNWLVNhLAPGDVVELSQPQG-DFVLPDPLPPRL-L 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 204 MIATGTGVAPYRGYLR----RMFMENVpnfkfdglawLFLGVANS-DSLLYDEEFAGYRKDYPeNFRYDKALSREEKnkk 278
Cdd:cd06216  127 LIAAGSGITPVMSMLRtllaRGPTADV----------VLLYYARTrEDVIFADELRALAAQHP-NLRLHLLYTREEL--- 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334186381 279 ggkmyvqdkIEEYSDEIFKLLD---NGAHIYFCGLKGMMpgiqDTLKRVAEERG 329
Cdd:cd06216  193 ---------DGRLSAAHLDAVVpdlADRQVYACGPPGFL----DAAEELLEAAG 233
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
144-258 2.79e-06

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: 47.99  E-value: 2.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 144 SLCVRRAiyydpetgkedpskaGVCSNFLCNAKPGDKVKITGPSGKVMLLPEddpKATH--IMIATGTGVAPYRGYLRRm 221
Cdd:cd06221   59 ELTIRRV---------------GRVTEALHELKPGDTVGLRGPFGNGFPVEE---MKGKdlLLVAGGLGLAPLRSLINY- 119
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 334186381 222 FMENVPNFkfdGLAWLFLGVANSDSLLYDEEFAGYRK 258
Cdd:cd06221  120 ILDNREDY---GKVTLLYGARTPEDLLFKEELKEWAK 153
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
89-313 1.30e-04

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


Pssm-ID: 99791 [Multi-domain]  Cd Length: 222  Bit Score: 42.64  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  89 HIVIDHDGNVPYWEGQSYGVIPPGenpkkpGAPhnvRLYSIASTRYGDSFdgktASLCVRRaiyydpetgkedpSKAGVC 168
Cdd:cd06194   13 RVRLEPDRPLPYLPGQYVNLRRAG------GLA---RSYSPTSLPDGDNE----LEFHIRR-------------KPNGAF 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 169 SNFLCN-AKPGDKVKITGPSGKVMLLPE--DDPKathIMIATGTGVAPYRGYLRRMFMENvpnfkFDGLAWLFLGVANSD 245
Cdd:cd06194   67 SGWLGEeARPGHALRLQGPFGQAFYRPEygEGPL---LLVGAGTGLAPLWGIARAALRQG-----HQGEIRLVHGARDPD 138
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334186381 246 SLLYDEEFAGYRKDYPeNFRYDKALSREEknkkggkmyvQDKIEEYSDEIFK---LLDNGAHIYFCGLKGM 313
Cdd:cd06194  139 DLYLHPALLWLAREHP-NFRYIPCVSEGS----------QGDPRVRAGRIAAhlpPLTRDDVVYLCGAPSM 198
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
176-322 1.55e-04

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 42.55  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 176 KPGDKVKITGPSGKVMLLPEDDPKAthIMIATGTGVAP-YrgYLRRMFMENVPNFKFDglawlfLGVANSDSLLYDEEFA 254
Cdd:PRK00054  81 KEGDELDIRGPLGNGFDLEEIGGKV--LLVGGGIGVAPlY--ELAKELKKKGVEVTTV------LGARTKDEVIFEEEFA 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334186381 255 gyrkdypenfRYDKALSREEKNKKGGKMYVQDKIEEysdeifkLLDNGAHIYFCGLKGMMPGIQDTLK 322
Cdd:PRK00054 151 ----------KVGDVYVTTDDGSYGFKGFVTDVLDE-------LDSEYDAIYSCGPEIMMKKVVEILK 201
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
152-288 2.79e-04

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 42.84  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  152 YYDPETGKED--------PSKAGVCSNFLCNAKPGDKVKITGPSGkvmLLPEDDPKATHI-----------MIATGTGVA 212
Cdd:PTZ00306  968 YYSPITLPDDlgvisilaRGDKGTLKEWISALRPGDSVEMKACGG---LRIERRPADKQFvfrghvirklaLIAGGTGVA 1044
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381  213 PY----RGYLRRMFMENVPNFKfdglawLFLGVANSDSLLYDEEFAGYRKDYPENFRYDKALSREEKNKKGGKMYVQDKI 288
Cdd:PTZ00306 1045 PMlqiiRAALKKPYVDSIESIR------LIYAAEDVSELTYRELLESYRKENPGKFKCHFVLNNPPEGWTDGVGFVDRAL 1118
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
166-256 4.48e-04

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: 41.16  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 166 GVCSNFLCNAKPGDKVKITGPSGKVMLLPEDDPKAthIMIATGTGVAPYRGYLRRMFMENVPNFkfdglawLFLGVANSD 245
Cdd:cd06192   66 GPKTKLIAELKPGEKLDVMGPLGNGFEGPKKGGTV--LLVAGGIGLAPLLPIAKKLAANGNKVT-------VLAGAKKAK 136
                         90
                 ....*....|.
gi 334186381 246 SLLYDEEFAGY 256
Cdd:cd06192  137 EEFLDEYFELP 147
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
125-327 6.96e-04

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


Pssm-ID: 99788 [Multi-domain]  Cd Length: 231  Bit Score: 40.59  E-value: 6.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 125 RLYSIASTRYGDsfdgkTASLCVRRAiyydpetgkedpsKAGVCSNFLC-NAKPGDKVKITGPSGKVMLLPEddPKATHI 203
Cdd:cd06191   47 RCYSLCSSPAPD-----EISITVKRV-------------PGGRVSNYLReHIQPGMTVEVMGPQGHFVYQPQ--PPGRYL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 204 MIATGTGVAPYRGYLR-RMFMENVPNFKfdglawLFLGVANSDSLLYDEEFAGYrKDYPENFRYDKALSREeknkkGGKM 282
Cdd:cd06191  107 LVAAGSGITPLMAMIRaTLQTAPESDFT------LIHSARTPADMIFAQELREL-ADKPQRLRLLCIFTRE-----TLDS 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 334186381 283 YVQDKIEEYSDEIFKLLDNG---AHIYFCGLKGMMPGIQDTLKRVAEE 327
Cdd:cd06191  175 DLLHGRIDGEQSLGAALIPDrleREAFICGPAGMMDAVETALKELGMP 222
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
145-273 1.01e-03

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 40.56  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 145 LCVRRAiyydpetgkedpskaGVCSNFLCNAKPGDKVKITGPSGKVmlLPEDDPK-ATHIMIATGTGVAPYRGYLRRMfM 223
Cdd:PRK08345  70 LCIRRA---------------GRVTTVIHRLKEGDIVGVRGPYGNG--FPVDEMEgMDLLLIAGGLGMAPLRSVLLYA-M 131
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334186381 224 ENVPNFkfdGLAWLFLGV-ANSDSLLYDEEFAGYRKDypENFRYDKALSRE 273
Cdd:PRK08345 132 DNRWKY---GNITLIYGAkYYEDLLFYDELIKDLAEA--ENVKIIQSVTRD 177
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
118-213 3.20e-03

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal portion of the FAD/NAD binding domain contains most of the NADP(H) binding residues and the N-terminal sub-domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. In this ferredoxin like sub-group, the FAD/NAD sub-domains is typically fused to a C-terminal iron-sulfur binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins which act as electron carriers in photosynthesis and ferredoxins which participate in redox chains from bacteria to mammals. Ferredoxin reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99811 [Multi-domain]  Cd Length: 231  Bit Score: 38.34  E-value: 3.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186381 118 PGAPHNvRLYSIASTrygdSFDGKTASLCVRRaiyydpetgKEDpskaGVCSNFLC-NAKPGDKVKITGPSGKVMLlpED 196
Cdd:cd06215   41 DGETVY-RAYTLSSS----PSRPDSLSITVKR---------VPG----GLVSNWLHdNLKVGDELWASGPAGEFTL--ID 100
                         90
                 ....*....|....*..
gi 334186381 197 DPKATHIMIATGTGVAP 213
Cdd:cd06215  101 HPADKLLLLSAGSGITP 117
siderophore_interacting cd06193
Siderophore interacting proteins share the domain structure of the ferredoxin reductase like ...
147-206 9.93e-03

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


Pssm-ID: 99790 [Multi-domain]  Cd Length: 235  Bit Score: 37.24  E-value: 9.93e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334186381 147 VRRaiyYDPETGK--------EDpskAGVCSNFLCNAKPGDKVKITGPSGKVMLLPEDDPkatHIMIA 206
Cdd:cd06193   69 VRR---FDPEAGEldidfvlhGD---EGPASRWAASAQPGDTLGIAGPGGSFLPPPDADW---YLLAG 127
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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