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Conserved domains on  [gi|442619426|ref|NP_001262637|]
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uncharacterized protein Dmel_CG14882, isoform B [Drosophila melanogaster]

Protein Classification

ferredoxin reductase domain-containing protein; ferredoxin reductase( domain architecture ID 10153102)

ferredoxin reductase (FNR) domain-containing protein may bind FAD and/or NAD(P)| ferredoxin-NADP+ (oxido)reductase (FNR) is a FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
methionine_synthase_red cd06203
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ...
 66-453 1.69e-179

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: 507.24  E-value: 1.69e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426  66 VLVSADKATET---KRVVELTLEST---FDYQPGDTIGILPANKLEQVESLLHRLELLDQADTTCHLKLVFNCANKNAKL 139
Cdd:cd06203    1 PISSAKKLTEGddvKTVVDLTLDLSptgFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVPNTKKKNAKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 140 PAHIPATTTPREILTHCLSLNFVPQKQLLSALAGFTSDDKERCFLSCLSSKQATEYYQSLILEQGLLFIDILEVCVNCRP 219
Cdd:cd06203   81 PVHIPKVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDFVRKRGLSLLDLLEAFPSCRP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 220 PLAFLAEHLPRLLPRPYSIANSPLEAsNRELRVIYSLLSLK-PGVTTSMLEaAAQQSSPEHSKKVVIYPRMSNLFRYTER 298
Cdd:cd06203  161 PLSLLIEHLPRLQPRPYSIASSPLEG-PGKLRFIFSVVEFPaKGLCTSWLE-SLCLSASSHGVKVPFYLRSSSRFRLPPD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 299 DVGRNQILIAVGTGLAPFLGFLAHKEELIKQQPQQPSGQSWLYIGAKTP-EAVLKREKLMEWQESSLLERLRMCYSRGES 377
Cdd:cd06203  239 DLRRPIIMVGPGTGVAPFLGFLQHREKLKESHTETVFGEAWLFFGCRHRdRDYLFRDELEEFLEEGILTRLIVAFSRDEN 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 378 ----PSYVQHMLEEDCEDLVEFLMKSETVLYICADGAKISQSIAGVLSRCLQKAMHLTEEEASQLLKKLRKQDKYREDVW 453
Cdd:cd06203  319 dgstPKYVQDKLEERGKKLVDLLLNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGLDKLEAKKLLARLRKEDRYLEDVW 398
 
Name Accession Description Interval E-value
methionine_synthase_red cd06203
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ...
 66-453 1.69e-179

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: 507.24  E-value: 1.69e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426  66 VLVSADKATET---KRVVELTLEST---FDYQPGDTIGILPANKLEQVESLLHRLELLDQADTTCHLKLVFNCANKNAKL 139
Cdd:cd06203    1 PISSAKKLTEGddvKTVVDLTLDLSptgFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVPNTKKKNAKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 140 PAHIPATTTPREILTHCLSLNFVPQKQLLSALAGFTSDDKERCFLSCLSSKQATEYYQSLILEQGLLFIDILEVCVNCRP 219
Cdd:cd06203   81 PVHIPKVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDFVRKRGLSLLDLLEAFPSCRP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 220 PLAFLAEHLPRLLPRPYSIANSPLEAsNRELRVIYSLLSLK-PGVTTSMLEaAAQQSSPEHSKKVVIYPRMSNLFRYTER 298
Cdd:cd06203  161 PLSLLIEHLPRLQPRPYSIASSPLEG-PGKLRFIFSVVEFPaKGLCTSWLE-SLCLSASSHGVKVPFYLRSSSRFRLPPD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 299 DVGRNQILIAVGTGLAPFLGFLAHKEELIKQQPQQPSGQSWLYIGAKTP-EAVLKREKLMEWQESSLLERLRMCYSRGES 377
Cdd:cd06203  239 DLRRPIIMVGPGTGVAPFLGFLQHREKLKESHTETVFGEAWLFFGCRHRdRDYLFRDELEEFLEEGILTRLIVAFSRDEN 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 378 ----PSYVQHMLEEDCEDLVEFLMKSETVLYICADGAKISQSIAGVLSRCLQKAMHLTEEEASQLLKKLRKQDKYREDVW 453
Cdd:cd06203  319 dgstPKYVQDKLEERGKKLVDLLLNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGLDKLEAKKLLARLRKEDRYLEDVW 398
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
 55-453 6.43e-36

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: 139.51  E-value: 6.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426  55 QPSSVEIKESKVLVSADKATETkRVVELTLE-STFDYQPGDTIGILPANKLEQVESLLHRLELldQADTTCHLKlvfnca 133
Cdd:COG0369  195 NPFPATVLENRELTGRGSAKET-RHIEIDLPgSGLSYEPGDALGVWPENDPALVDELLARLGL--DGDEPVTLD------ 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 134 NKNAKLpahipatttpREILTHCLSLNfVPQKQLLSALAGFTSDDKercfLSCLSSKQATEYYQSLILEQGLlfIDILEV 213
Cdd:COG0369  266 GEPLSL----------REALTEHLELT-RLTPPLLEKYAELTGNAE----LAALLADEDKAALREYLAGRQL--LDLLRE 328

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 214 CVNCRPPLAFLAEHLPRLLPRPYSIANSPL---------------EASNRELRviysllslkpGVTTSMLeAAAQQSSpe 278
Cdd:COG0369  329 FPAAELSAEELLELLRPLTPRLYSISSSPKahpdevhltvgvvryEASGRERK----------GVASTYL-ADLEEGD-- 395

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 279 hskKVVIYPRMSNLFR---YTERDVgrnqILIAVGTGLAPFLGFLAHKEELikqqpqQPSGQSWLYIGAKTPEA-VLKRE 354
Cdd:COG0369  396 ---TVPVFVEPNPNFRlpaDPDTPI----IMIGPGTGIAPFRAFLQEREAR------GASGKNWLFFGDRHFTTdFLYQT 462

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 355 KLMEWQESSLLERLRMCYSR-GESPSYVQHMLEEDCEDLVEFLmKSETVLYICADGAKISQSIAGVLSRCLQKAMHLTEE 433
Cdd:COG0369  463 ELQAWLKDGVLTRLDLAFSRdQAEKIYVQHRLLEQGAELWAWL-EEGAHVYVCGDASRMAKDVDAALLDIIAEHGGLSEE 541

                        410       420
                 ....*....|....*....|
gi 442619426 434 EASQLLKKLRKQDKYREDVW 453
Cdd:COG0369  542 EAEEYLAELRAEKRYQRDVY 561
FAD_binding_1 pfam00667
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, ...
 55-248 7.48e-28

FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, Nitric oxide synthase and methionine synthase reductase.


Pssm-ID: 395540 [Multi-domain]  Cd Length: 219  Bit Score: 110.12  E-value: 7.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426   55 QPSSVEIKESKVLVSADKateTKRVVELTL---ESTFDYQPGDTIGILPANKLEQVESLLHRLELLDQADTTCHLKlvfn 131
Cdd:pfam00667   6 KPFTAPVLSNRELTSPSS---DRNCIHVELdisGSGLTYQTGDHLGVYPPNNEELVEELLERLGLDPKPDTVVLLK---- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426  132 caNKNAKLPAHIPATTTPREILTHCLSLNFVPQKQLLSALAGFTSDDKERCFLSCLSSKQATEYYQSLILEQGLLFIDIL 211
Cdd:pfam00667  79 --TLDERVKPPRLPPTTYRQALKYYLDITGPPSKQLLRLLAQFAPEEEEKQRLEFLSSDAGAREYKRWKLNHAPTLLEVL 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 442619426  212 EVCVNCRPPLAFLAEHLPRLLPRPYSIANSPLEASNR 248
Cdd:pfam00667 157 EEFPSVKLPADFLLTQLPQLQPRYYSISSSSKVHPNE 193
PRK06214 PRK06214
sulfite reductase subunit alpha;
56-453 1.14e-26

sulfite reductase subunit alpha;


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 112.47  E-value: 1.14e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426  56 PSSVEIKESKVLVSADKATETkRVVELTLE-STFDYQPGDTIGILPANKLEQVESLLHRLelldQAdttchlklvfncan 134
Cdd:PRK06214 168 PVEATFLSRRRLNKPGSEKET-WHVEIDLAgSGLDYEVGDSLGLFPANDPALVDAVIAAL----GA-------------- 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 135 knaklPAHIPATTTP-REILTHCLSLNFVPQK--QLLSALAGftSDDKERcflsclsskqateyyqSLILEQG------- 204
Cdd:PRK06214 229 -----PPEFPIGGKTlREALLEDVSLGPAPDGlfELLSYITG--GAARKK----------------ARALAAGedpdgda 285

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 205 --LLFIDILEVCVNCRP-PLAFLaEHLPRLLPRPYSIANSPlEASNREL-----RVIYSLLS-LKPGVTTSMLeaaAQQS 275
Cdd:PRK06214 286 atLDVLAALEKFPGIRPdPEAFV-EALDPLQPRLYSISSSP-KATPGRVsltvdAVRYEIGSrLRLGVASTFL---GERL 360

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 276 SPEHSKKVVIYPrmSNLFRYTErDVGRNQILIAVGTGLAPFLGFLAHKEELikqqpqQPSGQSWLYIGAKTPEA-VLKRE 354
Cdd:PRK06214 361 APGTRVRVYVQK--AHGFALPA-DPNTPIIMVGPGTGIAPFRAFLHERAAT------KAPGRNWLFFGHQRSATdFFYED 431

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 355 KLMEWQESSLLERLRMCYSR-GESPSYVQHMLEEDCEDLVEFLMKSeTVLYICADGAKISQSIAGVLSRCLQKAMHLTEE 433
Cdd:PRK06214 432 ELNGLKAAGVLTRLSLAWSRdGEEKTYVQDRMRENGAELWKWLEEG-AHFYVCGDAKRMAKDVERALVDIVAQFGGRSPD 510

                        410       420
                 ....*....|....*....|
gi 442619426 434 EASQLLKKLRKQDKYREDVW 453
Cdd:PRK06214 511 EAVAFVAELKKAGRYQADVY 530
 
Name Accession Description Interval E-value
methionine_synthase_red cd06203
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ...
 66-453 1.69e-179

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: 507.24  E-value: 1.69e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426  66 VLVSADKATET---KRVVELTLEST---FDYQPGDTIGILPANKLEQVESLLHRLELLDQADTTCHLKLVFNCANKNAKL 139
Cdd:cd06203    1 PISSAKKLTEGddvKTVVDLTLDLSptgFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVPNTKKKNAKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 140 PAHIPATTTPREILTHCLSLNFVPQKQLLSALAGFTSDDKERCFLSCLSSKQATEYYQSLILEQGLLFIDILEVCVNCRP 219
Cdd:cd06203   81 PVHIPKVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDFVRKRGLSLLDLLEAFPSCRP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 220 PLAFLAEHLPRLLPRPYSIANSPLEAsNRELRVIYSLLSLK-PGVTTSMLEaAAQQSSPEHSKKVVIYPRMSNLFRYTER 298
Cdd:cd06203  161 PLSLLIEHLPRLQPRPYSIASSPLEG-PGKLRFIFSVVEFPaKGLCTSWLE-SLCLSASSHGVKVPFYLRSSSRFRLPPD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 299 DVGRNQILIAVGTGLAPFLGFLAHKEELIKQQPQQPSGQSWLYIGAKTP-EAVLKREKLMEWQESSLLERLRMCYSRGES 377
Cdd:cd06203  239 DLRRPIIMVGPGTGVAPFLGFLQHREKLKESHTETVFGEAWLFFGCRHRdRDYLFRDELEEFLEEGILTRLIVAFSRDEN 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 378 ----PSYVQHMLEEDCEDLVEFLMKSETVLYICADGAKISQSIAGVLSRCLQKAMHLTEEEASQLLKKLRKQDKYREDVW 453
Cdd:cd06203  319 dgstPKYVQDKLEERGKKLVDLLLNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGLDKLEAKKLLARLRKEDRYLEDVW 398
CYPOR cd06204
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 55-453 1.00e-53

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: 185.15  E-value: 1.00e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426  55 QPSSVEIKESKVL-VSADKATetkRVVELTLEST-FDYQPGDTIGILPANKLEQVESLLHRLELlDQADTTCHLKLVFNC 132
Cdd:cd06204    4 NPFLAPVAVSRELfTGSDRSC---LHIEFDISGSgIRYQTGDHLAVWPTNPSEEVERLLKVLGL-DDRDTVISLKSLDEP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 133 ANKnaKLPahIPATTTPREILTHCLSLNFVPQKQLLSALAGFTSDDKERCFLSCLSSkQATEYYQSLILEqglLFIDILE 212
Cdd:cd06204   80 ASK--KVP--FPCPTTYRTALRHYLDITAPVSRQVLAALAQFAPDPEEKERLLKLAS-EGKDEYAKWIVE---PHRNLLE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 213 V------CVNCRPPLAFLAEHLPRLLPRPYSIANSPLEASNR-------------ELRVIYsllslkpGVTTSMLEAAAQ 273
Cdd:cd06204  152 VlqdfpsAKPTPPPFDFLIELLPRLQPRYYSISSSSKVHPNRihitavvvkyptpTGRIIK-------GVATNWLLALKP 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 274 QSSPEHSK---------------KVVIYPRMSNlFRY---TERDVgrnqILIAVGTGLAPFLGFL----AHKEELIKQQP 331
Cdd:cd06204  225 ALNGEKPPtpyylsgprkkgggsKVPVFVRRSN-FRLptkPSTPV----IMIGPGTGVAPFRGFIqeraALKESGKKVGP 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 332 QqpsgqsWLYIGAKTP-EAVLKREKLMEWQESSLLERLRMCYSR-GESPSYVQHMLEEDCEDLVEfLMKSETVLYICADG 409
Cdd:cd06204  300 T------LLFFGCRHPdEDFIYKDELEEYAKLGGLLELVTAFSReQPKKVYVQHRLAEHAEQVWE-LINEGAYIYVCGDA 372

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 442619426 410 AKISQSIAGVLSRCLQKAMHLTEEEASQLLKKLRKQDKYREDVW 453
Cdd:cd06204  373 KNMARDVEKTLLEILAEQGGMTETEAEEYVKKLKTRGRYQEDVW 416
CyPoR_like cd06207
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 60-453 2.96e-44

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: 158.98  E-value: 2.96e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426  60 EIKESKVLVSADKATETkRVVELTLEST-FDYQPGDTIGILPANKLEQVESLLHRLEL-LDQadttchLKLVFNCANKNA 137
Cdd:cd06207    1 KVTENKRLTPADYDRST-RHIEFDLGGSgLSYETGDNLGIYPENSDALVDEFLARLGLdGDD------VVRVEPNEQQRG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 138 KLPahIPATTTPREILTHCLSLNFVPQKQLLSALAGFTSDDKERCFLSCLSSK-QATEYYQSlileQGLLFIDILEVCVN 216
Cdd:cd06207   74 KPP--FPEPISVRQLLKKFLDIFGKPTKKFLKLLSQLATDEEEKEDLYKLASReGRTEYKRY----EKYTYLEVLKDFPS 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 217 CRPPLAFLAEHLPRLLPRPYSIANSPLEASNR-ELRViySLLSLKP-------GVTTSMLEAAA---------QQSS--- 276
Cdd:cd06207  148 VRPTLEQLLELCPLIKPRYYSISSSPLKNPNEvHLLV--SLVSWKTpsgrsryGLCSSYLAGLKvgqrvtvfiKKSSfkl 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 277 PEHSKKVVIyprmsnlfryterdvgrnqiLIAVGTGLAPFLGFLAHKEELIKQQPQQPSGQswLYIGAKTPEA-VLKREK 355
Cdd:cd06207  226 PKDPKKPII--------------------MVGPGTGLAPFRAFLQERAALLAQGPEIGPVL--LYFGCRHEDKdYLYKEE 283

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 356 LMEWQESSLLERLRMCYSR-GESPSYVQHMLEEDCEDLVEFLMKSETVLYICADGAKISQSIAGVLSRCLQKAMHLTEEE 434
Cdd:cd06207  284 LEEYEKSGVLTTLGTAFSRdQPKKVYVQDLIRENSDLVYQLLEEGAGVIYVCGSTWKMPPDVQEAFEEILKKHGGGDEEL 363

                        410
                 ....*....|....*....
gi 442619426 435 ASQLLKKLRKQDKYREDVW 453
Cdd:cd06207  364 AEKKIEELEERGRYVVEAW 382
bifunctional_CYPOR cd06206
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ...
 61-453 3.06e-44

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: 158.96  E-value: 3.06e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426  61 IKESKVLVSADKATEtKRVVELTLESTFDYQPGDTIGILPANKLEQVESLLHRLELLDQADTTCHlklvfncankNAKLP 140
Cdd:cd06206    2 VVENRELTAPGVGPS-KRHLELRLPDGMTYRAGDYLAVLPRNPPELVRRALRRFGLAWDTVLTIS----------ASGSA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 141 AHIPaTTTP---REILTHCLSLNFVPQKQLLSALAGFTSDDKERCFLSCLSSkqatEYYQSLILEQGLLFIDILEVCVNC 217
Cdd:cd06206   71 TGLP-LGTPisvSELLSSYVELSQPATRRQLAALAEATRCPDTKALLERLAG----EAYAAEVLAKRVSVLDLLERFPSI 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 218 RPPLAFLAEHLPRLLPRPYSIANSPLEASNReLRVIYSLLSlKP---------GVTTSMLeaaaqqSSPEHSKKVVIYPR 288
Cdd:cd06206  146 ALPLATFLAMLPPMRPRQYSISSSPLVDPGH-ATLTVSVLD-APalsgqgryrGVASSYL------SSLRPGDSIHVSVR 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 289 MSNL-FRYTErDVGRNQILIAVGTGLAPFLGFLAHKEELIKQQPQQPSGQswLYIGAKTPEA-VLKREKLMEWQESSLLE 366
Cdd:cd06206  218 PSHSaFRPPS-DPSTPLIMIAAGTGLAPFRGFLQERAALLAQGRKLAPAL--LFFGCRHPDHdDLYRDELEEWEAAGVVS 294

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 367 rLRMCYSR--GESPSYVQHMLEEDCEDLVEfLMKSETVLYICADGaKISQSIAGVLSRCLQKAMHL----TEEEASQLLK 440
Cdd:cd06206  295 -VRRAYSRppGGGCRYVQDRLWAEREEVWE-LWEQGARVYVCGDG-RMAPGVREVLKRIYAEKDERgggsDDEEAEEWLE 371

                        410
                 ....*....|...
gi 442619426 441 KLRKQDKYREDVW 453
Cdd:cd06206  372 ELRNKGRYATDVF 384
Nitric_oxide_synthase cd06202
The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses ...
 88-452 1.49e-39

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: 147.09  E-value: 1.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426  88 FDYQPGDTIGILPANKLEQVESLLHRLELLDQADTT-----CHLKLVFNCANKNAKLPAHIPATTTpREILTHCLSLNFV 162
Cdd:cd06202   30 LHYQPGDHVGIFPANRPELVDALLDRLHDAPPPDQViklevLEERSTALGIIKTWTPHERLPPCTL-RQALTRYLDITTP 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 163 PQKQLLSALAGFTSDDKERCFLSCLsSKQATEY------YQSLILEqgllfidILEVCVNCRPPLAFLAEHLPRLLPRPY 236
Cdd:cd06202  109 PTPQLLQLLATLATDEKDKERLEVL-GKGSSEYedwkwyKNPNILE-------VLEEFPSLQVPASLLLTQLPLLQPRYY 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 237 SIANSPlEASNRELRVIYSLLSLKP---------GVTTSMLEAAAQQSSpehskkVVIYPRMSNLFRYTErDVGRNQILI 307
Cdd:cd06202  181 SISSSP-DMYPGEIHLTVAVVSYRTrdgqgpvhhGVCSTWLNGLTPGDT------VPCFVRSAPSFHLPE-DPSVPVIMV 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 308 AVGTGLAPFLGFLAHKEELIKQQPQQPSG--QSWLYIGAKTPEAV-LKREKLMEWQESSLLERLRMCYSR--GESPSYVQ 382
Cdd:cd06202  253 GPGTGIAPFRSFWQQRQYDLRMSEDPGKKfgDMTLFFGCRNSTIDdIYKEETEEAKNKGVLTEVYTALSRepGKPKTYVQ 332

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442619426 383 HMLEEDCEDLVEFLMKSETVLYICAD---GAKISQSIagvlSRCLQKAMHLTEEEASQLLKKLRKQDKYREDV 452
Cdd:cd06202  333 DLLKEQAESVYDALVREGGHIYVCGDvtmAEDVSQTI----QRILAEHGNMSAEEAEEFILKLRDENRYHEDI 401
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
 55-453 6.43e-36

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: 139.51  E-value: 6.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426  55 QPSSVEIKESKVLVSADKATETkRVVELTLE-STFDYQPGDTIGILPANKLEQVESLLHRLELldQADTTCHLKlvfnca 133
Cdd:COG0369  195 NPFPATVLENRELTGRGSAKET-RHIEIDLPgSGLSYEPGDALGVWPENDPALVDELLARLGL--DGDEPVTLD------ 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 134 NKNAKLpahipatttpREILTHCLSLNfVPQKQLLSALAGFTSDDKercfLSCLSSKQATEYYQSLILEQGLlfIDILEV 213
Cdd:COG0369  266 GEPLSL----------REALTEHLELT-RLTPPLLEKYAELTGNAE----LAALLADEDKAALREYLAGRQL--LDLLRE 328

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 214 CVNCRPPLAFLAEHLPRLLPRPYSIANSPL---------------EASNRELRviysllslkpGVTTSMLeAAAQQSSpe 278
Cdd:COG0369  329 FPAAELSAEELLELLRPLTPRLYSISSSPKahpdevhltvgvvryEASGRERK----------GVASTYL-ADLEEGD-- 395

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 279 hskKVVIYPRMSNLFR---YTERDVgrnqILIAVGTGLAPFLGFLAHKEELikqqpqQPSGQSWLYIGAKTPEA-VLKRE 354
Cdd:COG0369  396 ---TVPVFVEPNPNFRlpaDPDTPI----IMIGPGTGIAPFRAFLQEREAR------GASGKNWLFFGDRHFTTdFLYQT 462

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 355 KLMEWQESSLLERLRMCYSR-GESPSYVQHMLEEDCEDLVEFLmKSETVLYICADGAKISQSIAGVLSRCLQKAMHLTEE 433
Cdd:COG0369  463 ELQAWLKDGVLTRLDLAFSRdQAEKIYVQHRLLEQGAELWAWL-EEGAHVYVCGDASRMAKDVDAALLDIIAEHGGLSEE 541

                        410       420
                 ....*....|....*....|
gi 442619426 434 EASQLLKKLRKQDKYREDVW 453
Cdd:COG0369  542 EAEEYLAELRAEKRYQRDVY 561
SiR cd06199
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 60-453 3.29e-35

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: 133.89  E-value: 3.29e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426  60 EIKESKVLVSADKATETkRVVELTLE-STFDYQPGDTIGILPANKLEQVESLLHRLELldQADTTCHLKLvfncanknak 138
Cdd:cd06199    1 TVLENRLLTGPGSEKET-RHIELDLEgSGLSYEPGDALGVYPTNDPALVDELLAALGL--SGDEPVSTVG---------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 139 lpahiPATTTPREILTHCLSLNFVpqkqLLSALAGFTSDDKERCFLSCLSSKQATEYYQsliLEQGLLFIDILEVcvncR 218
Cdd:cd06199   68 -----GGTLPLREALIKHYEITTL----LLALLESYAADTGALELLALAALEAVLAFAE---LRDVLDLLPIPPA----R 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 219 PPLAFLAEHLPRLLPRPYSIANSPLEASNR-EL---RVIYSLLSLK-PGVTTSMLEAAAQQSSPehskkVVIYPRMSNLF 293
Cdd:cd06199  132 LTAEELLDLLRPLQPRLYSIASSPKAVPDEvHLtvaVVRYESHGRErKGVASTFLADRLKEGDT-----VPVFVQPNPHF 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 294 RY---TERDVgrnqILIAVGTGLAPFLGFLAHKEELikqqpqQPSGQSWLYIGAKTPEA-VLKREKLMEWQESSLLERLR 369
Cdd:cd06199  207 RLpedPDAPI----IMVGPGTGIAPFRAFLQEREAT------GAKGKNWLFFGERHFATdFLYQDELQQWLKDGVLTRLD 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 370 MCYSR-GESPSYVQHMLEEDCEDLVEFLMKSETVlYICADGAKISQSIAGVLSRCLQKAMHLTEEEASQLLKKLRKQDKY 448
Cdd:cd06199  277 TAFSRdQAEKVYVQDRMREQGAELWAWLEEGAHF-YVCGDAKRMAKDVDAALLDIIATEGGMDEEEAEAYLKELKKEKRY 355


                 ....*
gi 442619426 449 REDVW 453
Cdd:cd06199  356 QRDVY 360
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 185-453 3.57e-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. 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: 117.82  E-value: 3.57e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 185 SCLSSKQAT--EYYQSLILeqglLFIDILEVCVNCRPPLAFLAEHLPRLL-PRPYSIANSPLEASNR-EL---RVIYSLL 257
Cdd:cd06182    1 AITVNRKLTppDSPRSTRH----LEFDLSGNSVLKYQPGDHLGVIPPNPLqPRYYSIASSPDVDPGEvHLcvrVVSYEAP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 258 SLKP--GVTTSMLEAAAQQSspehskKVVIYPRMSNLFRYTeRDVGRNQILIAVGTGLAPFLGFLAHKEELIKQQPQQPS 335
Cdd:cd06182   77 AGRIrkGVCSNFLAGLQLGA------KVTVFIRPAPSFRLP-KDPTTPIIMVGPGTGIAPFRGFLQERAALRANGKARGP 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 336 GqsWLYIGAKTP-EAVLKREKLMEWQESSLLERLRMCYSR--GESPSYVQHMLEEDCEDLVEfLMKSETVLYICADGAKI 412
Cdd:cd06182  150 A--WLFFGCRNFaSDYLYREELQEALKDGALTRLDVAFSReqAEPKVYVQDKLKEHAEELRR-LLNEGAHIYVCGDAKSM 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 442619426 413 SQSIAGVLSRCLQKAMHLTEEEASQLLKKLRKQDKYREDVW 453
Cdd:cd06182  227 AKDVEDALVKIIAKAGGVDESDAEEYLKELEDEGRYVEDVW 267
FAD_binding_1 pfam00667
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, ...
 55-248 7.48e-28

FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, Nitric oxide synthase and methionine synthase reductase.


Pssm-ID: 395540 [Multi-domain]  Cd Length: 219  Bit Score: 110.12  E-value: 7.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426   55 QPSSVEIKESKVLVSADKateTKRVVELTL---ESTFDYQPGDTIGILPANKLEQVESLLHRLELLDQADTTCHLKlvfn 131
Cdd:pfam00667   6 KPFTAPVLSNRELTSPSS---DRNCIHVELdisGSGLTYQTGDHLGVYPPNNEELVEELLERLGLDPKPDTVVLLK---- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426  132 caNKNAKLPAHIPATTTPREILTHCLSLNFVPQKQLLSALAGFTSDDKERCFLSCLSSKQATEYYQSLILEQGLLFIDIL 211
Cdd:pfam00667  79 --TLDERVKPPRLPPTTYRQALKYYLDITGPPSKQLLRLLAQFAPEEEEKQRLEFLSSDAGAREYKRWKLNHAPTLLEVL 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 442619426  212 EVCVNCRPPLAFLAEHLPRLLPRPYSIANSPLEASNR 248
Cdd:pfam00667 157 EEFPSVKLPADFLLTQLPQLQPRYYSISSSSKVHPNE 193
PRK06214 PRK06214
sulfite reductase subunit alpha;
56-453 1.14e-26

sulfite reductase subunit alpha;


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 112.47  E-value: 1.14e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426  56 PSSVEIKESKVLVSADKATETkRVVELTLE-STFDYQPGDTIGILPANKLEQVESLLHRLelldQAdttchlklvfncan 134
Cdd:PRK06214 168 PVEATFLSRRRLNKPGSEKET-WHVEIDLAgSGLDYEVGDSLGLFPANDPALVDAVIAAL----GA-------------- 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 135 knaklPAHIPATTTP-REILTHCLSLNFVPQK--QLLSALAGftSDDKERcflsclsskqateyyqSLILEQG------- 204
Cdd:PRK06214 229 -----PPEFPIGGKTlREALLEDVSLGPAPDGlfELLSYITG--GAARKK----------------ARALAAGedpdgda 285

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 205 --LLFIDILEVCVNCRP-PLAFLaEHLPRLLPRPYSIANSPlEASNREL-----RVIYSLLS-LKPGVTTSMLeaaAQQS 275
Cdd:PRK06214 286 atLDVLAALEKFPGIRPdPEAFV-EALDPLQPRLYSISSSP-KATPGRVsltvdAVRYEIGSrLRLGVASTFL---GERL 360

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 276 SPEHSKKVVIYPrmSNLFRYTErDVGRNQILIAVGTGLAPFLGFLAHKEELikqqpqQPSGQSWLYIGAKTPEA-VLKRE 354
Cdd:PRK06214 361 APGTRVRVYVQK--AHGFALPA-DPNTPIIMVGPGTGIAPFRAFLHERAAT------KAPGRNWLFFGHQRSATdFFYED 431

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 355 KLMEWQESSLLERLRMCYSR-GESPSYVQHMLEEDCEDLVEFLMKSeTVLYICADGAKISQSIAGVLSRCLQKAMHLTEE 433
Cdd:PRK06214 432 ELNGLKAAGVLTRLSLAWSRdGEEKTYVQDRMRENGAELWKWLEEG-AHFYVCGDAKRMAKDVERALVDIVAQFGGRSPD 510

                        410       420
                 ....*....|....*....|
gi 442619426 434 EASQLLKKLRKQDKYREDVW 453
Cdd:PRK06214 511 EAVAFVAELKKAGRYQADVY 530
SiR_like1 cd06200
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 224-453 3.44e-14

Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues, and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule, which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99797  Cd Length: 245  Bit Score: 71.93  E-value: 3.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 224 LAEHLPR--LLPRPYSIANSP----LEASNRELRVIYSLLSLKPGVTTsmlEAAAQQSSPEHskkvviypRMSNLFRYTE 297
Cdd:cd06200   37 IAEIGPRhpLPHREYSIASLPadgaLELLVRQVRHADGGLGLGSGWLT---RHAPIGASVAL--------RLRENPGFHL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 298 RDVGRNQILIAVGTGLAPFLGFLahkeeliKQQPQQPSGQSWLYIGAKTPEA-VLKREKLMEWQESSLLERLRMCYSR-G 375
Cdd:cd06200  106 PDDGRPLILIGNGTGLAGLRSHL-------RARARAGRHRNWLLFGERQAAHdFFCREELEAWQAAGHLARLDLAFSRdQ 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 376 ESPSYVQHMLEEDCEDLVEFLMKSeTVLYIC--ADGakISQSIAGVLSRCLQKAMhlteeeasqlLKKLRKQDKYREDVW 453
Cdd:cd06200  179 AQKRYVQDRLRAAADELRAWVAEG-AAIYVCgsLQG--MAPGVDAVLDEILGEEA----------VEALLAAGRYRRDVY 245
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 305-453 1.51e-13

Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99798 [Multi-domain]  Cd Length: 289  Bit Score: 70.82  E-value: 1.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 305 ILIAVGTGLAPFLGFLAHKEelikqqpqqPSGQSWLYIGAKTPEA-VLKREKLMEWQESSLLERLRMCYSRGESPSYVQH 383
Cdd:cd06201  159 ILIGAGTGIAPLAGFIRANA---------ARRPMHLYWGGRDPASdFLYEDELDQYLADGRLTQLHTAFSRTPDGAYVQD 229

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 384 MLEEDCEDLVEFLMKSETVLyICAdGAKISQSIAGVLSRCLqKAMHLTeeeasqlLKKLRKQDKYREDVW 453
Cdd:cd06201  230 RLRADAERLRRLIEDGAQIM-VCG-SRAMAQGVAAVLEEIL-APQPLS-------LDELKLQGRYAEDVY 289
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 206-410 2.18e-13

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: 69.40  E-value: 2.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 206 LFIDILEVCVNCRPPLAFLA--------EHLPRLLPRPYSIANSPLEASNRELRVIYSLlslkPGVTTSMLEAAAQQSsp 277
Cdd:cd00322    6 VTDDVRLFRLQLPNGFSFKPgqyvdlhlPGDGRGLRRAYSIASSPDEEGELELTVKIVP----GGPFSAWLHDLKPGD-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 278 ehskKVVIYPRMSNLFRYteRDVGRNQILIAVGTGLAPFLGFLAHKEELIkqqpqqPSGQSWLYIGAKTPEAVLKREKLM 357
Cdd:cd00322   80 ----EVEVSGPGGDFFLP--LEESGPVVLIAGGIGITPFRSMLRHLAADK------PGGEITLLYGARTPADLLFLDELE 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442619426 358 EWQESSLLERLRMCYSRGESPS-YVQHMLEEDCEDLVEFLMKSETVLYICADGA 410
Cdd:cd00322  148 ELAKEGPNFRLVLALSRESEAKlGPGGRIDREAEILALLPDDSGALVYICGPPA 201
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 303-448 1.99e-09

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: 58.49  E-value: 1.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 303 NQILIAVGTGLAPFLGFLAH--KEeliKQQPQQPSGQSWLYIGAKTPEAVLKREKL--MEWQESSLLeRLRMCYSRGESP 378
Cdd:cd06208  137 TLIMIATGTGIAPFRSFLRRlfRE---KHADYKFTGLAWLFFGVPNSDSLLYDDELekYPKQYPDNF-RIDYAFSREQKN 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 379 S-----YVQHMLEEDCEDLVEFLMKSETVLYICadGAK-----ISQSIAGVLSRCLQKAMHlteeeasqlLKKLRKQDKY 448
Cdd:cd06208  213 AdggkmYVQDRIAEYAEEIWNLLDKDNTHVYIC--GLKgmepgVDDALTSVAEGGLAWEEF---------WESLKKKGRW 281
cysJ PRK10953
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
78-453 1.33e-08

NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;


Pssm-ID: 182862 [Multi-domain]  Cd Length: 600  Bit Score: 57.04  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426  78 RVVELTL-ESTFDYQPGDTIGILPANKLEQVESLLHRLELLDQADTTCHLKlvfncanknaKLPahipatttpreiLTHC 156
Cdd:PRK10953 258 RHIEIDLgDSGLRYQPGDALGVWYQNDPALVKELVELLWLKGDEPVTVDGK----------TLP------------LAEA 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 157 LSLNF---VPQKQLLSALAGFTSDDKercFLSCLSSKQATEYYQslileQGLLFIDILEvcvncRPPLAFLAEHLPRLL- 232
Cdd:PRK10953 316 LQWHFeltVNTANIVENYATLTRSET---LLPLVGDKAALQHYA-----ATTPIVDMVR-----FAPAQLDAEQLIGLLr 382

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 233 ---PRPYSIANSPLEASNrELRVIYSLLSL------KPGVTTSMLEAAAQQSSPehskkVVIYPRMSNLFRYTErDVGRN 303
Cdd:PRK10953 383 pltPRLYSIASSQAEVEN-EVHITVGVVRYdiegraRAGGASSFLADRLEEEGE-----VRVFIEHNDNFRLPA-NPETP 455

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 304 QILIAVGTGLAPFLGFLAHKEelikqqPQQPSGQSWLYIGakTP---EAVLKReklMEWQ---ESSLLERLRMCYSRGES 377
Cdd:PRK10953 456 VIMIGPGTGIAPFRAFMQQRA------ADGAPGKNWLFFG--NPhftEDFLYQ---VEWQryvKEGLLTRIDLAWSRDQK 524

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 378 PS-YVQHMLEEDCEDLVEFLmKSETVLYICADG---AK-ISQSIAGVLSrcLQKAMHltEEEASQLLKKLRKQDKYREDV 452
Cdd:PRK10953 525 EKiYVQDKLREQGAELWRWI-NDGAHIYVCGDAnrmAKdVEQALLEVIA--EFGGMD--TEAADEFLSELRVERRYQRDV 599


                 .
gi 442619426 453 W 453
Cdd:PRK10953 600 Y 600
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
 298-406 1.03e-06

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 50.77  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 298 RDVGRNQILIAVGTGLAPFLGFLaHKEELIKQQPQQPSGQSWLYIGAKTPEAVLKREKLMEWQESSLLE-RLRMCYSRGE 376
Cdd:PLN03115 212 KDPNATIIMLATGTGIAPFRSFL-WKMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENfRLDFAVSREQ 290

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 442619426 377 SPS-----YVQHMLEEDCEDLVEFLMKSETVLYIC 406
Cdd:PLN03115 291 TNAkgekmYIQTRMAEYAEELWELLKKDNTYVYMC 325
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 209-356 4.75e-06

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


Pssm-ID: 99791 [Multi-domain]  Cd Length: 222  Bit Score: 47.65  E-value: 4.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 209 DILEVCVNCRPPLAFLAEHLPRL-----LPRPYSIANSPLEASNRELRViysllSLKPGvtTSMLEAAAQQSSPEHSkkV 283
Cdd:cd06194   10 DVLRVRLEPDRPLPYLPGQYVNLrraggLARSYSPTSLPDGDNELEFHI-----RRKPN--GAFSGWLGEEARPGHA--L 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442619426 284 VIYPRMSNLFRYTERDVGRnQILIAVGTGLAPFLGFLA------HKEELikqqpqqpsgqsWLYIGAKTPEAVLKREKL 356
Cdd:cd06194   81 RLQGPFGQAFYRPEYGEGP-LLLVGAGTGLAPLWGIARaalrqgHQGEI------------RLVHGARDPDDLYLHPAL 146
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 306-406 5.13e-06

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: 45.33  E-value: 5.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426  306 LIAVGTGLAPFLGFLAHKEELIKqqpqqPSGQSWLYIGAKTPEAVLKREKLMEWQEsSLLERLRMCY--SRGE-----SP 378
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDPK-----DPTQVVLVFGNRNEDDILYREELDELAE-KHPGRLTVVYvvSRPEagwtgGK 74

                          90       100
                  ....*....|....*....|....*...
gi 442619426  379 SYVQHMLEEDCEDlvefLMKSETVLYIC 406
Cdd:pfam00175  75 GRVQDALLEDHLS----LPDEETHVYVC 98
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 230-406 1.33e-05

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 46.39  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 230 RLLPRPYSIANSPLEasNRELRVIYSLLslkpGVTTSMLeaaaqqsspeHSKKV-----VIYPrMSNLFRYteRDVGRNQ 304
Cdd:COG0543   39 DGLRRPFSIASAPRE--DGTIELHIRVV----GKGTRAL----------AELKPgdeldVRGP-LGNGFPL--EDSGRPV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 305 ILIAVGTGLAPFLGFLahkEELIKQQPQQPsgqswLYIGAKTPEAVLKREKLMEWQESSLLerlrmCYSRGESPS---YV 381
Cdd:COG0543  100 LLVAGGTGLAPLRSLA---EALLARGRRVT-----LYLGARTPEDLYLLDELEALADFRVV-----VTTDDGWYGrkgFV 166

                        170       180
                 ....*....|....*....|....*
gi 442619426 382 QHMLEEDCEDlveflmKSETVLYIC 406
Cdd:COG0543  167 TDALKELLAE------DSGDDVYAC 185
PLN03116 PLN03116
ferredoxin--NADP+ reductase; Provisional
 297-453 2.56e-04

ferredoxin--NADP+ reductase; Provisional


Pssm-ID: 215586 [Multi-domain]  Cd Length: 307  Bit Score: 42.78  E-value: 2.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 297 ERDVGRNQILIAVGTGLAPFLGFLaHKEELIKQQPQQPSGQSWLYIGAKTPEAVLKREklmEWQE--SSLLERLRMCY-- 372
Cdd:PLN03116 152 EEDPNATHIMVATGTGIAPFRGFL-RRMFMEDVPAFKFGGLAWLFLGVANSDSLLYDD---EFERylKDYPDNFRYDYal 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 373 SRGESPS-----YVQHMLEEDCEDLVEfLMKSETVLYICadGAK-----ISQSIAGVlsrCLQKAmhlteEEASQLLKKL 442
Cdd:PLN03116 228 SREQKNKkggkmYVQDKIEEYSDEIFK-LLDNGAHIYFC--GLKgmmpgIQDTLKRV---AEERG-----ESWEEKLSGL 296

                        170
                 ....*....|.
gi 442619426 443 RKQDKYREDVW 453
Cdd:PLN03116 297 KKNKQWHVEVY 307
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
230-406 3.49e-04

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 42.08  E-value: 3.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 230 RLLPRPYSIANSPleaSNRELRvIYSLL------------SLKPGvttSMLEAAAqqsspehskkvviyPRmsNLFRYTE 297
Cdd:COG1018   49 KPLRRAYSLSSAP---GDGRLE-ITVKRvpggggsnwlhdHLKVG---DTLEVSG--------------PR--GDFVLDP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 298 RDvGRNQILIAVGTGLAPFLGFLAHKEELikqqpQQPSGQSWLYiGAKTPEAVLKREKLMEWQESslLERLRM--CYSRg 375
Cdd:COG1018  106 EP-ARPLLLIAGGIGITPFLSMLRTLLAR-----GPFRPVTLVY-GARSPADLAFRDELEALAAR--HPRLRLhpVLSR- 175

                        170       180       190
                 ....*....|....*....|....*....|.
gi 442619426 376 ESPSYVQHMLEEDCEDLVEFLmkSETVLYIC 406
Cdd:COG1018  176 EPAGLQGRLDAELLAALLPDP--ADAHVYLC 204
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 301-366 5.02e-04

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: 41.82  E-value: 5.02e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 301 GRNQILIAVGTGLAP----FLGFLAHKEELIKQQpqqpsgqswLYIGAKTPEAVLKREKLMEWQESSLLE 366
Cdd:cd06221   98 GKDLLLVAGGLGLAPlrslINYILDNREDYGKVT---------LLYGARTPEDLLFKEELKEWAKRSDVE 158
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 213-322 5.56e-04

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


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 41.14  E-value: 5.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 213 VCVNCRPPLAFLAEHlprllprPYSIANSPLEASNrELRVIysllsLKP--GVTTSMLEAAAQQSSPEHSKKVVI---YP 287
Cdd:cd06186   31 VYLNFPSLLSFWQSH-------PFTIASSPEDEQD-TLSLI-----IRAkkGFTTRLLRKALKSPGGGVSLKVLVegpYG 97

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 442619426 288 RMSNLFRYTERDVgrnqiLIAVGTGLAPFLGFLAH 322
Cdd:cd06186   98 SSSEDLLSYDNVL-----LVAGGSGITFVLPILRD 127
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 209-406 7.62e-04

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: 41.00  E-value: 7.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 209 DILEVCVNCRPPLAFLAE-----HLPRLLPRPYSIANSPLEASNRELRVIYSllslkPGVTTSM--LEAAAQQSspehsk 281
Cdd:cd06189   12 DVYRVRLKPPAPLDFLAGqyldlLLDDGDKRPFSIASAPHEDGEIELHIRAV-----PGGSFSDyvFEELKENG------ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 282 KVVIYPRMSNLFrYTERDVgRNQILIAVGTGLAPFLGFLahkEELIKQQPQQPSGqswLYIGAKTPEAVLKREKLMEWQE 361
Cdd:cd06189   81 LVRIEGPLGDFF-LREDSD-RPLILIAGGTGFAPIKSIL---EHLLAQGSKRPIH---LYWGARTEEDLYLDELLEAWAE 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442619426 362 S-------SLLERLR--MCYSRGespsYVQHMLEEDCEDLveflmkSETVLYIC 406
Cdd:cd06189  153 AhpnftyvPVLSEPEegWQGRTG----LVHEAVLEDFPDL------SDFDVYAC 196
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 211-406 8.32e-04

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: 40.65  E-value: 8.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 211 LEVCVNCRPPLAFLAEHLPRL-LP-----RPYSIANSPleaSNRELRVIYSLLslkP-GVTTSMLEAAAQQ------SSP 277
Cdd:cd06209   19 LTLELDEAGALAFLPGQYVNLqVPgtdetRSYSFSSAP---GDPRLEFLIRLL---PgGAMSSYLRDRAQPgdrltlTGP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619426 278 EHSKKVviyprmsnlfryteRDVGRNQILIAVGTGLAPFLGFLAHKEElikqqpQQPSGQSWLYIGAKTPEAVLKREKLM 357
Cdd:cd06209   93 LGSFYL--------------REVKRPLLMLAGGTGLAPFLSMLDVLAE------DGSAHPVHLVYGVTRDADLVELDRLE 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442619426 358 EWQESSLLERLRMCYSRGESPS----YV-QHMLEEDCEDlveflmkSETVLYIC 406
Cdd:cd06209  153 ALAERLPGFSFRTVVADPDSWHprkgYVtDHLEAEDLND-------GDVDVYLC 199
 
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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