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Conserved domains on  [gi|1958642953|ref|XP_038958835|]
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methionine synthase reductase isoform X5 [Rattus norvegicus]

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 ...
 116-537 0e+00

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: 595.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 116 PISKAVELTTNDAIKTTLLLELDISKVEFSHQPGDSFNVICPNSGSEVEDLLQRLQLADKQAHRVILKIKMDTKKKGASL 195
Cdd:cd06203     1 PISSAKKLTEGDDVKTVVDLTLDLSPTGFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVPNTKKKNAKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 196 PQHVPEGSSLQFIFTWCLEIRAVPKKAFLRALSDYTSDATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPSCQP 275
Cdd:cd06203    81 PVHIPKVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDFVRKRGLSLLDLLEAFPSCRP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 276 PLNLLLEHLPKLQPRPYSCASSSLLHPDKLHFVFNIVELPSnttaaslrKGVCTGWLATLVAPflqpntevltadhSDAL 355
Cdd:cd06203   161 PLSLLIEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPA--------KGLCTSWLESLCLS-------------ASSH 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 356 APEILISPRATNSFHLP-DDLSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPDGNFGAMWLFFGCRHKDRDYLFREELRH 434
Cdd:cd06203   220 GVKVPFYLRSSSRFRLPpDDLRRPIIMVGPGTGVAPFLGFLQHREKLKESHTETVFGEAWLFFGCRHRDRDYLFRDELEE 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 435 FLKTGVLTHLKVSFSRDaapeEEEEAPAKYVQDNLQHHSQQVARTLLQENGYIYVCGDAKNMAKDVHDALVEIISKEAGV 514
Cdd:cd06203   300 FLEEGILTRLIVAFSRD----ENDGSTPKYVQDKLEERGKKLVDLLLNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGL 375

                         410       420
                  ....*....|....*....|...
gi 1958642953 515 DKLEAMKTLATLKQEKRYLQDIW 537
Cdd:cd06203   376 DKLEAKKLLARLRKEDRYLEDVW 398
 
Name Accession Description Interval E-value
methionine_synthase_red cd06203
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ...
 116-537 0e+00

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: 595.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 116 PISKAVELTTNDAIKTTLLLELDISKVEFSHQPGDSFNVICPNSGSEVEDLLQRLQLADKQAHRVILKIKMDTKKKGASL 195
Cdd:cd06203     1 PISSAKKLTEGDDVKTVVDLTLDLSPTGFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVPNTKKKNAKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 196 PQHVPEGSSLQFIFTWCLEIRAVPKKAFLRALSDYTSDATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPSCQP 275
Cdd:cd06203    81 PVHIPKVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDFVRKRGLSLLDLLEAFPSCRP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 276 PLNLLLEHLPKLQPRPYSCASSSLLHPDKLHFVFNIVELPSnttaaslrKGVCTGWLATLVAPflqpntevltadhSDAL 355
Cdd:cd06203   161 PLSLLIEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPA--------KGLCTSWLESLCLS-------------ASSH 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 356 APEILISPRATNSFHLP-DDLSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPDGNFGAMWLFFGCRHKDRDYLFREELRH 434
Cdd:cd06203   220 GVKVPFYLRSSSRFRLPpDDLRRPIIMVGPGTGVAPFLGFLQHREKLKESHTETVFGEAWLFFGCRHRDRDYLFRDELEE 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 435 FLKTGVLTHLKVSFSRDaapeEEEEAPAKYVQDNLQHHSQQVARTLLQENGYIYVCGDAKNMAKDVHDALVEIISKEAGV 514
Cdd:cd06203   300 FLEEGILTRLIVAFSRD----ENDGSTPKYVQDKLEERGKKLVDLLLNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGL 375

                         410       420
                  ....*....|....*....|...
gi 1958642953 515 DKLEAMKTLATLKQEKRYLQDIW 537
Cdd:cd06203   376 DKLEAKKLLARLRKEDRYLEDVW 398
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
 92-537 2.28e-103

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: 321.71  E-value: 2.28e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953  92 LQESLGQDENQASVPPSVDP------IFQVPISKAVELTTNDAIKTTLLLELDISKVEFSHQPGDSFNVICPNSGSEVED 165
Cdd:COG0369   170 LAEALGAAAAAAAAAAAAAPaysrknPFPATVLENRELTGRGSAKETRHIEIDLPGSGLSYEPGDALGVWPENDPALVDE 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 166 LLQRLQLadKQAHRVILKikmdtkkkGASLPqhvpegssLQFIFTWCLEIRAVPKKaFLRALSDYTSDAtekrRLQELCS 245
Cdd:COG0369   250 LLARLGL--DGDEPVTLD--------GEPLS--------LREALTEHLELTRLTPP-LLEKYAELTGNA----ELAALLA 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 246 KQGAADYNRFIRDASVclLDLLLTFPSCQPPLNLLLEHLPKLQPRPYSCASSSLLHPDKLHFVFNIVELPSNTTAaslRK 325
Cdd:COG0369   307 DEDKAALREYLAGRQL--LDLLREFPAAELSAEELLELLRPLTPRLYSISSSPKAHPDEVHLTVGVVRYEASGRE---RK 381

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 326 GVCTGWLATL-----VAPFLQPNtevltadhsdalapeilispratNSFHLPDDLSAPIIMVGPGTGVAPFVGFLQHREK 400
Cdd:COG0369   382 GVASTYLADLeegdtVPVFVEPN-----------------------PNFRLPADPDTPIIMIGPGTGIAPFRAFLQEREA 438

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 401 LQEQhpdgnfGAMWLFFGCRHKDRDYLFREELRHFLKTGVLTHLKVSFSRDAAPeeeeeapaK-YVQDNLQHHSQQVARt 479
Cdd:COG0369   439 RGAS------GKNWLFFGDRHFTTDFLYQTELQAWLKDGVLTRLDLAFSRDQAE--------KiYVQHRLLEQGAELWA- 503

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642953 480 LLQENGYIYVCGDAKNMAKDVHDALVEIISKEAGVDKLEAMKTLATLKQEKRYLQDIW 537
Cdd:COG0369   504 WLEEGAHVYVCGDASRMAKDVDAALLDIIAEHGGLSEEEAEEYLAELRAEKRYQRDVY 561
PRK06214 PRK06214
sulfite reductase subunit alpha;
122-537 1.57e-65

sulfite reductase subunit alpha;


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 221.87  E-value: 1.57e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 122 ELTTNDAIKTTLLLELDISKVEFSHQPGDSFNVICPNSGSEVEDLLQRLQlADkqAHRVIlkikmdtkkKGASLPQHVPE 201
Cdd:PRK06214  178 RLNKPGSEKETWHVEIDLAGSGLDYEVGDSLGLFPANDPALVDAVIAALG-AP--PEFPI---------GGKTLREALLE 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 202 GSSLqfiftwcleirAVPKKAFLRALSDYTSDATEK--RRLQELCSKQGAAdynrfirdASVCLLDLLLTFPSCQPPLNL 279
Cdd:PRK06214  246 DVSL-----------GPAPDGLFELLSYITGGAARKkaRALAAGEDPDGDA--------ATLDVLAALEKFPGIRPDPEA 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 280 LLEHLPKLQPRPYSCASSSLLHPDKLHFVFNIVELpsnTTAASLRKGVCTGWLATLVAP------FLQPNtevltadhsd 353
Cdd:PRK06214  307 FVEALDPLQPRLYSISSSPKATPGRVSLTVDAVRY---EIGSRLRLGVASTFLGERLAPgtrvrvYVQKA---------- 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 354 alapeilispratNSFHLPDDLSAPIIMVGPGTGVAPFVGFLQHREKLQEqhPDGNfgamWLFFGCRHKDRDYLFREELR 433
Cdd:PRK06214  374 -------------HGFALPADPNTPIIMVGPGTGIAPFRAFLHERAATKA--PGRN----WLFFGHQRSATDFFYEDELN 434

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 434 HFLKTGVLTHLKVSFSRDAAPEEeeeapakYVQDNLQhhsqQVARTL---LQENGYIYVCGDAKNMAKDVHDALVEIISK 510
Cdd:PRK06214  435 GLKAAGVLTRLSLAWSRDGEEKT-------YVQDRMR----ENGAELwkwLEEGAHFYVCGDAKRMAKDVERALVDIVAQ 503

                         410       420
                  ....*....|....*....|....*..
gi 1958642953 511 EAGVDKLEAMKTLATLKQEKRYLQDIW 537
Cdd:PRK06214  504 FGGRSPDEAVAFVAELKKAGRYQADVY 530
FAD_binding_1 pfam00667
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, ...
 113-331 6.28e-45

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: 157.89  E-value: 6.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 113 FQVPISKAVELTTNDAIKTTLLLELDISKVEFSHQPGDSFNVICPNSGSEVEDLLQRLQLADKQAHRVILKIKMDTKKkg 192
Cdd:pfam00667   8 FTAPVLSNRELTSPSSDRNCIHVELDISGSGLTYQTGDHLGVYPPNNEELVEELLERLGLDPKPDTVVLLKTLDERVK-- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 193 aslpQHVPEGSSLQFIFTWCLEIRAVPKKAFLRALSDYTSDATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPS 272
Cdd:pfam00667  86 ----PPRLPPTTYRQALKYYLDITGPPSKQLLRLLAQFAPEEEEKQRLEFLSSDAGAREYKRWKLNHAPTLLEVLEEFPS 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642953 273 CQPPLNLLLEHLPKLQPRPYSCASSSLLHPDKLHFVFNIVELPsNTTAASLRKGVCTGW 331
Cdd:pfam00667 162 VKLPADFLLTQLPQLQPRYYSISSSSKVHPNEVHLTVVVVEYE-TDGEGRIHYGVCSNW 219
 
Name Accession Description Interval E-value
methionine_synthase_red cd06203
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ...
 116-537 0e+00

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: 595.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 116 PISKAVELTTNDAIKTTLLLELDISKVEFSHQPGDSFNVICPNSGSEVEDLLQRLQLADKQAHRVILKIKMDTKKKGASL 195
Cdd:cd06203     1 PISSAKKLTEGDDVKTVVDLTLDLSPTGFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVPNTKKKNAKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 196 PQHVPEGSSLQFIFTWCLEIRAVPKKAFLRALSDYTSDATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPSCQP 275
Cdd:cd06203    81 PVHIPKVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDFVRKRGLSLLDLLEAFPSCRP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 276 PLNLLLEHLPKLQPRPYSCASSSLLHPDKLHFVFNIVELPSnttaaslrKGVCTGWLATLVAPflqpntevltadhSDAL 355
Cdd:cd06203   161 PLSLLIEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPA--------KGLCTSWLESLCLS-------------ASSH 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 356 APEILISPRATNSFHLP-DDLSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPDGNFGAMWLFFGCRHKDRDYLFREELRH 434
Cdd:cd06203   220 GVKVPFYLRSSSRFRLPpDDLRRPIIMVGPGTGVAPFLGFLQHREKLKESHTETVFGEAWLFFGCRHRDRDYLFRDELEE 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 435 FLKTGVLTHLKVSFSRDaapeEEEEAPAKYVQDNLQHHSQQVARTLLQENGYIYVCGDAKNMAKDVHDALVEIISKEAGV 514
Cdd:cd06203   300 FLEEGILTRLIVAFSRD----ENDGSTPKYVQDKLEERGKKLVDLLLNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGL 375

                         410       420
                  ....*....|....*....|...
gi 1958642953 515 DKLEAMKTLATLKQEKRYLQDIW 537
Cdd:cd06203   376 DKLEAKKLLARLRKEDRYLEDVW 398
CYPOR cd06204
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 111-537 2.63e-113

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: 342.31  E-value: 2.63e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 111 PIFQVPISKAVELTTNdAIKTTLLLELDISKVEFSHQPGDSFNVICPNSGSEVEDLLQRLQLADkqAHRVILKIKMDTKk 190
Cdd:cd06204     4 NPFLAPVAVSRELFTG-SDRSCLHIEFDISGSGIRYQTGDHLAVWPTNPSEEVERLLKVLGLDD--RDTVISLKSLDEP- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 191 kgASLPQHVPEGSSLQFIFTWCLEIRAVPKKAFLRALSDYTSDATEKRRLQELCSkQGAADYNRFIRDASVCLLDLLLTF 270
Cdd:cd06204    80 --ASKKVPFPCPTTYRTALRHYLDITAPVSRQVLAALAQFAPDPEEKERLLKLAS-EGKDEYAKWIVEPHRNLLEVLQDF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 271 PSCQ---PPLNLLLEHLPKLQPRPYSCASSSLLHPDKLHFVFNIVELPSNTtaASLRKGVCTGWLATLvAPFLQPNTEVL 347
Cdd:cd06204   157 PSAKptpPPFDFLIELLPRLQPRYYSISSSSKVHPNRIHITAVVVKYPTPT--GRIIKGVATNWLLAL-KPALNGEKPPT 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 348 TADHSDALAP----EILISPRATNsFHLPDDLSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPDgnFGAMWLFFGCRHKD 423
Cdd:cd06204   234 PYYLSGPRKKgggsKVPVFVRRSN-FRLPTKPSTPVIMIGPGTGVAPFRGFIQERAALKESGKK--VGPTLLFFGCRHPD 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 424 RDYLFREELRHFLKTGVLTHLKVSFSRDAAPEeeeeapaKYVQDNLQHHSQQVARtLLQENGYIYVCGDAKNMAKDVHDA 503
Cdd:cd06204   311 EDFIYKDELEEYAKLGGLLELVTAFSREQPKK-------VYVQHRLAEHAEQVWE-LINEGAYIYVCGDAKNMARDVEKT 382

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1958642953 504 LVEIISKEAGVDKLEAMKTLATLKQEKRYLQDIW 537
Cdd:cd06204   383 LLEILAEQGGMTETEAEEYVKKLKTRGRYQEDVW 416
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
 92-537 2.28e-103

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: 321.71  E-value: 2.28e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953  92 LQESLGQDENQASVPPSVDP------IFQVPISKAVELTTNDAIKTTLLLELDISKVEFSHQPGDSFNVICPNSGSEVED 165
Cdd:COG0369   170 LAEALGAAAAAAAAAAAAAPaysrknPFPATVLENRELTGRGSAKETRHIEIDLPGSGLSYEPGDALGVWPENDPALVDE 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 166 LLQRLQLadKQAHRVILKikmdtkkkGASLPqhvpegssLQFIFTWCLEIRAVPKKaFLRALSDYTSDAtekrRLQELCS 245
Cdd:COG0369   250 LLARLGL--DGDEPVTLD--------GEPLS--------LREALTEHLELTRLTPP-LLEKYAELTGNA----ELAALLA 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 246 KQGAADYNRFIRDASVclLDLLLTFPSCQPPLNLLLEHLPKLQPRPYSCASSSLLHPDKLHFVFNIVELPSNTTAaslRK 325
Cdd:COG0369   307 DEDKAALREYLAGRQL--LDLLREFPAAELSAEELLELLRPLTPRLYSISSSPKAHPDEVHLTVGVVRYEASGRE---RK 381

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 326 GVCTGWLATL-----VAPFLQPNtevltadhsdalapeilispratNSFHLPDDLSAPIIMVGPGTGVAPFVGFLQHREK 400
Cdd:COG0369   382 GVASTYLADLeegdtVPVFVEPN-----------------------PNFRLPADPDTPIIMIGPGTGIAPFRAFLQEREA 438

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 401 LQEQhpdgnfGAMWLFFGCRHKDRDYLFREELRHFLKTGVLTHLKVSFSRDAAPeeeeeapaK-YVQDNLQHHSQQVARt 479
Cdd:COG0369   439 RGAS------GKNWLFFGDRHFTTDFLYQTELQAWLKDGVLTRLDLAFSRDQAE--------KiYVQHRLLEQGAELWA- 503

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642953 480 LLQENGYIYVCGDAKNMAKDVHDALVEIISKEAGVDKLEAMKTLATLKQEKRYLQDIW 537
Cdd:COG0369   504 WLEEGAHVYVCGDASRMAKDVDAALLDIIAEHGGLSEEEAEEYLAELRAEKRYQRDVY 561
CyPoR_like cd06207
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 116-537 1.04e-102

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: 313.83  E-value: 1.04e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 116 PISKAVELTTNDAIKTTLLLELDISKVEFSHQPGDSFNVICPNSGSEVEDLLQRLQLADKQAHRVILKIKMDTKkkgasl 195
Cdd:cd06207     1 KVTENKRLTPADYDRSTRHIEFDLGGSGLSYETGDNLGIYPENSDALVDEFLARLGLDGDDVVRVEPNEQQRGK------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 196 pQHVPEGSSLQFIFTWCLEIRAVPKKAFLRALSDYTSDATEKRRLQELCSKQGAADYNRFIRdasVCLLDLLLTFPSCQP 275
Cdd:cd06207    75 -PPFPEPISVRQLLKKFLDIFGKPTKKFLKLLSQLATDEEEKEDLYKLASREGRTEYKRYEK---YTYLEVLKDFPSVRP 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 276 PLNLLLEHLPKLQPRPYSCASSSLLHPDKLHFVFNIVELpsNTTAASLRKGVCTGWLATLvapflQPNTEVltadhsdal 355
Cdd:cd06207   151 TLEQLLELCPLIKPRYYSISSSPLKNPNEVHLLVSLVSW--KTPSGRSRYGLCSSYLAGL-----KVGQRV--------- 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 356 apEILISPratNSFHLPDDLSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgNFGAMWLFFGCRHKDRDYLFREELRHF 435
Cdd:cd06207   215 --TVFIKK---SSFKLPKDPKKPIIMVGPGTGLAPFRAFLQERAALLAQGP--EIGPVLLYFGCRHEDKDYLYKEELEEY 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 436 LKTGVLTHLKVSFSRDAAPEeeeeapaKYVQDNLQHHSQQVARTLLQENGYIYVCGDAKNMAKDVHDALVEIISKEAGVD 515
Cdd:cd06207   288 EKSGVLTTLGTAFSRDQPKK-------VYVQDLIRENSDLVYQLLEEGAGVIYVCGSTWKMPPDVQEAFEEILKKHGGGD 360

                         410       420
                  ....*....|....*....|..
gi 1958642953 516 KLEAMKTLATLKQEKRYLQDIW 537
Cdd:cd06207   361 EELAEKKIEELEERGRYVVEAW 382
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 264-537 1.51e-97

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: 296.56  E-value: 1.51e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 264 LDLLLTFPSCQPPLNLLLEHLP-KLQPRPYSCASSSLLHPDKLHFVFNIVELPsnTTAASLRKGVCTGWLATLVapflqp 342
Cdd:cd06182    22 FDLSGNSVLKYQPGDHLGVIPPnPLQPRYYSIASSPDVDPGEVHLCVRVVSYE--APAGRIRKGVCSNFLAGLQ------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 343 ntevltadhsdaLAPEILISPRATNSFHLPDDLSAPIIMVGPGTGVAPFVGFLQHREKLQeqHPDGNFGAMWLFFGCRHK 422
Cdd:cd06182    94 ------------LGAKVTVFIRPAPSFRLPKDPTTPIIMVGPGTGIAPFRGFLQERAALR--ANGKARGPAWLFFGCRNF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 423 DRDYLFREELRHFLKTGVLTHLKVSFSRDAAPEEeeeapaKYVQDNLQHHSQQVARtLLQENGYIYVCGDAKNMAKDVHD 502
Cdd:cd06182   160 ASDYLYREELQEALKDGALTRLDVAFSREQAEPK------VYVQDKLKEHAEELRR-LLNEGAHIYVCGDAKSMAKDVED 232

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958642953 503 ALVEIISKEAGVDKLEAMKTLATLKQEKRYLQDIW 537
Cdd:cd06182   233 ALVKIIAKAGGVDESDAEEYLKELEDEGRYVEDVW 267
SiR cd06199
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 123-537 2.88e-95

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: 294.13  E-value: 2.88e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 123 LTTNDAIKTTLLLELDISKVEFSHQPGDSFNVICPNSGSEVEDLLQRLQLAdkqAHRVILKIKMDTKkkgaslpqhvpeg 202
Cdd:cd06199     8 LTGPGSEKETRHIELDLEGSGLSYEPGDALGVYPTNDPALVDELLAALGLS---GDEPVSTVGGGTL------------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 203 sSLQFIFTWCLEIRavpkKAFLRALSDYTSDATEkrrlQELCSKQGAADYNRFIRdasvcLLDLLLTFPscQPPLNL--- 279
Cdd:cd06199    72 -PLREALIKHYEIT----TLLLALLESYAADTGA----LELLALAALEAVLAFAE-----LRDVLDLLP--IPPARLtae 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 280 -LLEHLPKLQPRPYSCASSSLLHPDKLHFVFNIVELPSNTTAaslRKGVCTGWLATLVAP------FLQPNtevltadhs 352
Cdd:cd06199   136 eLLDLLRPLQPRLYSIASSPKAVPDEVHLTVAVVRYESHGRE---RKGVASTFLADRLKEgdtvpvFVQPN--------- 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 353 dalapeilispratNSFHLPDDLSAPIIMVGPGTGVAPFVGFLQHREklQEQHPdgnfGAMWLFFGCRHKDRDYLFREEL 432
Cdd:cd06199   204 --------------PHFRLPEDPDAPIIMVGPGTGIAPFRAFLQERE--ATGAK----GKNWLFFGERHFATDFLYQDEL 263

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 433 RHFLKTGVLTHLKVSFSRDAAPeeeeeapaK-YVQDNLQHHSQQVArTLLQENGYIYVCGDAKNMAKDVHDALVEIISKE 511
Cdd:cd06199   264 QQWLKDGVLTRLDTAFSRDQAE--------KvYVQDRMREQGAELW-AWLEEGAHFYVCGDAKRMAKDVDAALLDIIATE 334

                         410       420
                  ....*....|....*....|....*.
gi 1958642953 512 AGVDKLEAMKTLATLKQEKRYLQDIW 537
Cdd:cd06199   335 GGMDEEEAEAYLKELKKEKRYQRDVY 360
Nitric_oxide_synthase cd06202
The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses ...
 122-536 2.88e-85

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: 269.97  E-value: 2.88e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 122 ELTTNDAIKTTLLLELDISKV-EFSHQPGDSFNVICPNSGSEVEDLLQRLQLADKQAHrvILKIKMDTKKKGASL----- 195
Cdd:cd06202     7 NLQSPKSSRSTILVKLDTNGAqELHYQPGDHVGIFPANRPELVDALLDRLHDAPPPDQ--VIKLEVLEERSTALGiiktw 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 196 -PQHVPEGSSLQFIFTWCLEIRAVPKKAFLRALSDYTSDATEKRRLQELCskQGAADYNRFIRDASVCLLDLLLTFPSCQ 274
Cdd:cd06202    85 tPHERLPPCTLRQALTRYLDITTPPTPQLLQLLATLATDEKDKERLEVLG--KGSSEYEDWKWYKNPNILEVLEEFPSLQ 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 275 PPLNLLLEHLPKLQPRPYSCASSSLLHPDKLHFVFNIVELPSNTTAASLRKGVCTGWLATlvapfLQPNTEVltadhsda 354
Cdd:cd06202   163 VPASLLLTQLPLLQPRYYSISSSPDMYPGEIHLTVAVVSYRTRDGQGPVHHGVCSTWLNG-----LTPGDTV-------- 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 355 lapEILIspRATNSFHLPDDLSAPIIMVGPGTGVAPFVGFLQHR--EKLQEQHPDGNFGAMWLFFGCRHKDRDYLFREEL 432
Cdd:cd06202   230 ---PCFV--RSAPSFHLPEDPSVPVIMVGPGTGIAPFRSFWQQRqyDLRMSEDPGKKFGDMTLFFGCRNSTIDDIYKEET 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 433 RHFLKTGVLTHLKVSFSRDaapeeeEEAPAKYVQDNLQHHSQQVARTLLQENGYIYVCGDAkNMAKDVHDALVEIISKEA 512
Cdd:cd06202   305 EEAKNKGVLTEVYTALSRE------PGKPKTYVQDLLKEQAESVYDALVREGGHIYVCGDV-TMAEDVSQTIQRILAEHG 377

                         410       420
                  ....*....|....*....|....
gi 1958642953 513 GVDKLEAMKTLATLKQEKRYLQDI 536
Cdd:cd06202   378 NMSAEEAEEFILKLRDENRYHEDI 401
bifunctional_CYPOR cd06206
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ...
 143-537 6.20e-67

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: 221.36  E-value: 6.20e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 143 EFSHQPGDSFNVICPNSGSEVEDLLQRLQLA-DKQahrvilkIKMDTKKKGASLPQHVPEGSSLqfIFTWCLEIRAVPKK 221
Cdd:cd06206    27 GMTYRAGDYLAVLPRNPPELVRRALRRFGLAwDTV-------LTISASGSATGLPLGTPISVSE--LLSSYVELSQPATR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 222 AFLRALSDYTSDAtEKRRLQELCSKQGaadYNRFIRDASVCLLDLLLTFPSCQPPLNLLLEHLPKLQPRPYSCASSSLLH 301
Cdd:cd06206    98 RQLAALAEATRCP-DTKALLERLAGEA---YAAEVLAKRVSVLDLLERFPSIALPLATFLAMLPPMRPRQYSISSSPLVD 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 302 PDKLHFVFNIVELPSnTTAASLRKGVCTGWLATLvapflqpntevLTADHsdalapeILISPRATNS-FHLPDDLSAPII 380
Cdd:cd06206   174 PGHATLTVSVLDAPA-LSGQGRYRGVASSYLSSL-----------RPGDS-------IHVSVRPSHSaFRPPSDPSTPLI 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 381 MVGPGTGVAPFVGFLQHREKLQEQhpDGNFGAMWLFFGCRHKDRDYLFREELRHFLKTGVLThLKVSFSRDaapeeeEEA 460
Cdd:cd06206   235 MIAAGTGLAPFRGFLQERAALLAQ--GRKLAPALLFFGCRHPDHDDLYRDELEEWEAAGVVS-VRRAYSRP------PGG 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 461 PAKYVQDNLQHHSQQVARtLLQENGYIYVCGDAKnMAKDVHDALVEIISKE----AGVDKLEAMKTLATLKQEKRYLQDI 536
Cdd:cd06206   306 GCRYVQDRLWAEREEVWE-LWEQGARVYVCGDGR-MAPGVREVLKRIYAEKdergGGSDDEEAEEWLEELRNKGRYATDV 383


                  .
gi 1958642953 537 W 537
Cdd:cd06206   384 F 384
PRK06214 PRK06214
sulfite reductase subunit alpha;
122-537 1.57e-65

sulfite reductase subunit alpha;


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 221.87  E-value: 1.57e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 122 ELTTNDAIKTTLLLELDISKVEFSHQPGDSFNVICPNSGSEVEDLLQRLQlADkqAHRVIlkikmdtkkKGASLPQHVPE 201
Cdd:PRK06214  178 RLNKPGSEKETWHVEIDLAGSGLDYEVGDSLGLFPANDPALVDAVIAALG-AP--PEFPI---------GGKTLREALLE 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 202 GSSLqfiftwcleirAVPKKAFLRALSDYTSDATEK--RRLQELCSKQGAAdynrfirdASVCLLDLLLTFPSCQPPLNL 279
Cdd:PRK06214  246 DVSL-----------GPAPDGLFELLSYITGGAARKkaRALAAGEDPDGDA--------ATLDVLAALEKFPGIRPDPEA 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 280 LLEHLPKLQPRPYSCASSSLLHPDKLHFVFNIVELpsnTTAASLRKGVCTGWLATLVAP------FLQPNtevltadhsd 353
Cdd:PRK06214  307 FVEALDPLQPRLYSISSSPKATPGRVSLTVDAVRY---EIGSRLRLGVASTFLGERLAPgtrvrvYVQKA---------- 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 354 alapeilispratNSFHLPDDLSAPIIMVGPGTGVAPFVGFLQHREKLQEqhPDGNfgamWLFFGCRHKDRDYLFREELR 433
Cdd:PRK06214  374 -------------HGFALPADPNTPIIMVGPGTGIAPFRAFLHERAATKA--PGRN----WLFFGHQRSATDFFYEDELN 434

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 434 HFLKTGVLTHLKVSFSRDAAPEEeeeapakYVQDNLQhhsqQVARTL---LQENGYIYVCGDAKNMAKDVHDALVEIISK 510
Cdd:PRK06214  435 GLKAAGVLTRLSLAWSRDGEEKT-------YVQDRMR----ENGAELwkwLEEGAHFYVCGDAKRMAKDVERALVDIVAQ 503

                         410       420
                  ....*....|....*....|....*..
gi 1958642953 511 EAGVDKLEAMKTLATLKQEKRYLQDIW 537
Cdd:PRK06214  504 FGGRSPDEAVAFVAELKKAGRYQADVY 530
cysJ PRK10953
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
102-537 1.66e-48

NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;


Pssm-ID: 182862 [Multi-domain]  Cd Length: 600  Bit Score: 177.22  E-value: 1.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 102 QASVPPSVDPIFQVPISKAVELT----TNDAI------KTTLLLELDISKVEFSHQPGDSFNVICPNSGSEVEDLLQRLQ 171
Cdd:PRK10953  217 QSVATGAVNEIHTSPYSKEAPLTaslsVNQKItgrnseKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVKELVELLW 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 172 L-ADKQahrvilkIKMDTKKkgaslpqhVPEGSSLQfiftWCLEI-----RAVPKKAFLRALSDYTSDATEKRRLQELCS 245
Cdd:PRK10953  297 LkGDEP-------VTVDGKT--------LPLAEALQ----WHFELtvntaNIVENYATLTRSETLLPLVGDKAALQHYAA 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 246 KQGAADYNRFIrdasvclldllltfPScQPPLNLLLEHLPKLQPRPYSCASSSLLHPDKLHFVFNIVELPSNTTAaslRK 325
Cdd:PRK10953  358 TTPIVDMVRFA--------------PA-QLDAEQLIGLLRPLTPRLYSIASSQAEVENEVHITVGVVRYDIEGRA---RA 419

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 326 GVCTGWLATLvapfLQPNTEV-LTADHSDalapeilispratnSFHLPDDLSAPIIMVGPGTGVAPFVGFLQHREKlqeq 404
Cdd:PRK10953  420 GGASSFLADR----LEEEGEVrVFIEHND--------------NFRLPANPETPVIMIGPGTGIAPFRAFMQQRAA---- 477

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 405 hpDGNFGAMWLFFGCRHKDRDYLFREELRHFLKTGVLTHLKVSFSRDAAPEEeeeapakYVQDNLQHHSQQVARtLLQEN 484
Cdd:PRK10953  478 --DGAPGKNWLFFGNPHFTEDFLYQVEWQRYVKEGLLTRIDLAWSRDQKEKI-------YVQDKLREQGAELWR-WINDG 547

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958642953 485 GYIYVCGDAKNMAKDVHDALVEIISKEAGVDKLEAMKTLATLKQEKRYLQDIW 537
Cdd:PRK10953  548 AHIYVCGDANRMAKDVEQALLEVIAEFGGMDTEAADEFLSELRVERRYQRDVY 600
FAD_binding_1 pfam00667
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, ...
 113-331 6.28e-45

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: 157.89  E-value: 6.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 113 FQVPISKAVELTTNDAIKTTLLLELDISKVEFSHQPGDSFNVICPNSGSEVEDLLQRLQLADKQAHRVILKIKMDTKKkg 192
Cdd:pfam00667   8 FTAPVLSNRELTSPSSDRNCIHVELDISGSGLTYQTGDHLGVYPPNNEELVEELLERLGLDPKPDTVVLLKTLDERVK-- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 193 aslpQHVPEGSSLQFIFTWCLEIRAVPKKAFLRALSDYTSDATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPS 272
Cdd:pfam00667  86 ----PPRLPPTTYRQALKYYLDITGPPSKQLLRLLAQFAPEEEEKQRLEFLSSDAGAREYKRWKLNHAPTLLEVLEEFPS 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642953 273 CQPPLNLLLEHLPKLQPRPYSCASSSLLHPDKLHFVFNIVELPsNTTAASLRKGVCTGW 331
Cdd:pfam00667 162 VKLPADFLLTQLPQLQPRYYSISSSSKVHPNEVHLTVVVVEYE-TDGEGRIHYGVCSNW 219
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 289-537 1.42e-31

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: 123.59  E-value: 1.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 289 PRPYSCASSSllhPDklhfvfNIVELpsnttaaSLRK---GVCTGWLATL-----VAPFLQPNTevltadhsdalapeil 360
Cdd:cd06201   100 PRFYSLASSS---SD------GFLEI-------CVRKhpgGLCSGYLHGLkpgdtIKAFIRPNP---------------- 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 361 ispratnSFHLPDDlSAPIIMVGPGTGVAPFVGFLQHREKlqeQHPdgnfgaMWLFFGCRHKDRDYLFREELRHFLKTGV 440
Cdd:cd06201   148 -------SFRPAKG-AAPVILIGAGTGIAPLAGFIRANAA---RRP------MHLYWGGRDPASDFLYEDELDQYLADGR 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 441 LTHLKVSFSRdaapeeeeEAPAKYVQDNLQHHSQQVARtLLQENGYIYVCGdAKNMAKDVHDALVEIIskeagvdkLEAM 520
Cdd:cd06201   211 LTQLHTAFSR--------TPDGAYVQDRLRADAERLRR-LIEDGAQIMVCG-SRAMAQGVAAVLEEIL--------APQP 272

                         250
                  ....*....|....*..
gi 1958642953 521 KTLATLKQEKRYLQDIW 537
Cdd:cd06201   273 LSLDELKLQGRYAEDVY 289
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 277-507 2.17e-30

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: 118.32  E-value: 2.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 277 LNLLLEHLPKLQPRPYSCASSSLLhPDKLHFVFNIVElpsnttaaslrKGVCTGWLATLvapflQPNTEVltadhsDALA 356
Cdd:cd00322    29 VDLHLPGDGRGLRRAYSIASSPDE-EGELELTVKIVP-----------GGPFSAWLHDL-----KPGDEV------EVSG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 357 PeilispraTNSFHLPDDLSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgnfgaMWLFFGCRHKDrDYLFREELRHFL 436
Cdd:cd00322    86 P--------GGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGE------ITLLYGARTPA-DLLFLDELEELA 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642953 437 KTGVLTHLKVSFSRDaapeeeeEAPAKYVQDNLQHHSQQVARTLLQENGYIYVCGDAkNMAKDVHDALVEI 507
Cdd:cd00322   151 KEGPNFRLVLALSRE-------SEAKLGPGGRIDREAEILALLPDDSGALVYICGPP-AMAKAVREALVSL 213
SiR_like1 cd06200
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 280-537 1.14e-29

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: 116.99  E-value: 1.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 280 LLEHLPK--LQPRPYSCASssllhpdklhfvfniveLPSN---------TTAASLRKGVCTGWLaTLVAPflqpntevlt 348
Cdd:cd06200    37 IAEIGPRhpLPHREYSIAS-----------------LPADgalellvrqVRHADGGLGLGSGWL-TRHAP---------- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 349 adhsdaLAPEILISPRATNSFHLPDDlSAPIIMVGPGTGVAPFVGFLQHREKlQEQHPDgnfgamWLFFGCRHKDRDYLF 428
Cdd:cd06200    89 ------IGASVALRLRENPGFHLPDD-GRPLILIGNGTGLAGLRSHLRARAR-AGRHRN------WLLFGERQAAHDFFC 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 429 REELRHFLKTGVLTHLKVSFSRDaapeeeeEAPAKYVQDNLQHHSQQVaRTLLQENGYIYVCGDAKNMAKDVHDALVEII 508
Cdd:cd06200   155 REELEAWQAAGHLARLDLAFSRD-------QAQKRYVQDRLRAAADEL-RAWVAEGAAIYVCGSLQGMAPGVDAVLDEIL 226

                         250       260
                  ....*....|....*....|....*....
gi 1958642953 509 skeaGVDKLEAmktlatLKQEKRYLQDIW 537
Cdd:cd06200   227 ----GEEAVEA------LLAAGRYRRDVY 245
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 289-532 8.93e-24

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: 101.24  E-value: 8.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 289 PRPYSCASSSL---LHPDKLHFVFNIVELpSNTTAASLRKGVCTGWLATLVapflqPNTEV-LTADHSDAlapeilispr 364
Cdd:cd06208    64 LRLYSIASSRYgddGDGKTLSLCVKRLVY-TDPETDETKKGVCSNYLCDLK-----PGDDVqITGPVGKT---------- 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 365 atnsFHLPDDLSAPIIMVGPGTGVAPFVGFLQHRekLQEQHPDGNF-GAMWLFFGCRHKDrDYLFREELRHFLKT-GVLT 442
Cdd:cd06208   128 ----MLLPEDPNATLIMIATGTGIAPFRSFLRRL--FREKHADYKFtGLAWLFFGVPNSD-SLLYDDELEKYPKQyPDNF 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 443 HLKVSFSRDAAPEEEEEApakYVQDNLQHHSQQVARTLLQENGYIYVCGdAKNMAKDVHDALveiiSKEAGVDKLEAMKt 522
Cdd:cd06208   201 RIDYAFSREQKNADGGKM---YVQDRIAEYAEEIWNLLDKDNTHVYICG-LKGMEPGVDDAL----TSVAEGGLAWEEF- 271

                         250
                  ....*....|
gi 1958642953 523 LATLKQEKRY 532
Cdd:cd06208   272 WESLKKKGRW 281
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
 290-528 3.08e-16

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 80.43  E-value: 3.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 290 RPYSCASSSLLH-PDKLHFVFNIVELPSNTTAASLRKGVCTGWLATLvapflQPNTEVLTadhSDALAPEILispratns 368
Cdd:PLN03115  146 RLYSIASSALGDfGDSKTVSLCVKRLVYTNDQGEIVKGVCSNFLCDL-----KPGAEVKI---TGPVGKEML-------- 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 369 fhLPDDLSAPIIMVGPGTGVAPFVGFLQhrEKLQEQHPDGNF-GAMWLFFGCRHKDrDYLFREELRHfLKTGVLTHLKVS 447
Cdd:PLN03115  210 --MPKDPNATIIMLATGTGIAPFRSFLW--KMFFEKHDDYKFnGLAWLFLGVPTSS-SLLYKEEFEK-MKEKAPENFRLD 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 448 F--SRDAAPEEEEEApakYVQDNLQHHSQQVARTLLQENGYIYVCGdAKNMAKDVHDALVEIISKEaGVDKLEAMKTLAT 525
Cdd:PLN03115  284 FavSREQTNAKGEKM---YIQTRMAEYAEELWELLKKDNTYVYMCG-LKGMEKGIDDIMVSLAAKD-GIDWFEYKKQLKK 358


                  ...
gi 1958642953 526 LKQ 528
Cdd:PLN03115  359 AEQ 361
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 381-502 1.45e-13

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: 66.90  E-value: 1.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 381 MVGPGTGVAPFVGFLQHRekLQEQHPDGNfgaMWLFFGCRHkDRDYLFREELRHFLKT--GVLTHLKVSfSRDaapEEEE 458
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAI--LEDPKDPTQ---VVLVFGNRN-EDDILYREELDELAEKhpGRLTVVYVV-SRP---EAGW 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958642953 459 EAPAKYVQDNL--QHHSqqvartLLQENGYIYVCGdAKNMAKDVHD 502
Cdd:pfam00175  71 TGGKGRVQDALleDHLS------LPDEETHVYVCG-PPGMIKAVRK 109
PLN03116 PLN03116
ferredoxin--NADP+ reductase; Provisional
 371-532 4.62e-13

ferredoxin--NADP+ reductase; Provisional


Pssm-ID: 215586 [Multi-domain]  Cd Length: 307  Bit Score: 70.13  E-value: 4.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 371 LP-DDLSAPIIMVGPGTGVAPFVGFLqhREKLQEQHPDGNF-GAMWLFFGCRHKDRdYLFREELrhflkTGVLTHLKVSF 448
Cdd:PLN03116  150 LPeEDPNATHIMVATGTGIAPFRGFL--RRMFMEDVPAFKFgGLAWLFLGVANSDS-LLYDDEF-----ERYLKDYPDNF 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 449 SRDAAPEEEEEAPAK---YVQDNLQHHSQQVArTLLQENGYIYVCGdAKNMAKDVHDALvEIISKEAGVDKLEamkTLAT 525
Cdd:PLN03116  222 RYDYALSREQKNKKGgkmYVQDKIEEYSDEIF-KLLDNGAHIYFCG-LKGMMPGIQDTL-KRVAEERGESWEE---KLSG 295


                  ....*..
gi 1958642953 526 LKQEKRY 532
Cdd:PLN03116  296 LKKNKQW 302
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
353-516 1.59e-10

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 61.34  E-value: 1.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 353 DALAP--EILISPrATNSFHLPDDLSAPIIMVGPGTGVAPFVGFLQHrekLQEQHPDGNFgamWLFFGCRHKDrDYLFRE 430
Cdd:COG1018    84 DHLKVgdTLEVSG-PRGDFVLDPEPARPLLLIAGGIGITPFLSMLRT---LLARGPFRPV---TLVYGARSPA-DLAFRD 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 431 ELRHFLKTGVLTHLKVSFSRDAapeeeeeapakyvQDNLQHHSQQVARTLLQ--ENGYIYVCGDAkNMAKDVHDALveii 508
Cdd:COG1018   156 ELEALAARHPRLRLHPVLSREP-------------AGLQGRLDAELLAALLPdpADAHVYLCGPP-PMMEAVRAAL---- 217


                  ....*...
gi 1958642953 509 sKEAGVDK 516
Cdd:COG1018   218 -AELGVPE 224
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 290-506 4.00e-07

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: 51.41  E-value: 4.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 290 RPYSCASssllHPDKLHFVFNIVELPSnttaaslrkGVCTGWLATLvapflQPNtevltadhsDalapEILISPRATNSF 369
Cdd:cd06195    45 RAYSIAS----APYEENLEFYIILVPD---------GPLTPRLFKL-----KPG---------D----TIYVGKKPTGFL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 370 HLpDDLSAP--IIMVGPGTGVAPFVGFLQHREKLQEqhpdgnFGAMWLFFGCRHKDrDYLFREELRHFLKtgvLTHLKVS 447
Cdd:cd06195    94 TL-DEVPPGkrLWLLATGTGIAPFLSMLRDLEIWER------FDKIVLVHGVRYAE-ELAYQDEIEALAK---QYNGKFR 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642953 448 F----SRDAAPEEEEEAPAKYVQD-NLQHHsqqVARTLLQENGYIYVCGDaKNMAKDVHDALVE 506
Cdd:cd06195   163 YvpivSREKENGALTGRIPDLIESgELEEH---AGLPLDPETSHVMLCGN-PQMIDDTQELLKE 222
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 289-433 2.63e-05

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: 45.72  E-value: 2.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 289 PRPYSCASssllHPDKLHF-VFNIvelpsnttaASLRKGVCTGWLATLVapflQPNTEVLtadhsdalapeilISPRATN 367
Cdd:cd06194    39 ARSYSPTS----LPDGDNElEFHI---------RRKPNGAFSGWLGEEA----RPGHALR-------------LQGPFGQ 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642953 368 SFHLPDDLSAPIIMVGPGTGVAPFVGFLqhREKLQEQHPdgnfGAMWLFFGCRHKDRDYLfREELR 433
Cdd:cd06194    89 AFYRPEYGEGPLLLVGAGTGLAPLWGIA--RAALRQGHQ----GEIRLVHGARDPDDLYL-HPALL 147
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 367-506 4.96e-05

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 44.85  E-value: 4.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 367 NSFHLPDDlSAPIIMVGPGTGVAPFVGFLQHrekLQEQHPDgnfgaMWLFFGCRHKDrDYLFREELRHflktgvLTHLKV 446
Cdd:COG0543    88 NGFPLEDS-GRPVLLVAGGTGLAPLRSLAEA---LLARGRR-----VTLYLGARTPE-DLYLLDELEA------LADFRV 151

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642953 447 SFSRDaapeeeeeapakyvqDNLQHHS---QQVARTLLQENGY--IYVCGdAKNMAKDVHDALVE 506
Cdd:COG0543   152 VVTTD---------------DGWYGRKgfvTDALKELLAEDSGddVYACG-PPPMMKAVAELLLE 200
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 350-516 9.11e-05

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: 43.78  E-value: 9.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 350 DHSDALAPEILISPRAT-----NSFHLPDDlSAPIIMVGPGTGVAPFVGFLQHREKLQEQHP-DgnfgamwLFFGCRhKD 423
Cdd:cd06198    65 DYTRRLAERLKPGTRVTvegpyGRFTFDDR-RARQIWIAGGIGITPFLALLEALAARGDARPvT-------LFYCVR-DP 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 424 RDYLFREELRHfLKTGVLTHLKVSFSRDAAPEEEEEAPAKYVQDNLQHHsqqvartllqengyIYVCGDAKnMAKDVHDA 503
Cdd:cd06198   136 EDAVFLDELRA-LAAAAGVVLHVIDSPSDGRLTLEQLVRALVPDLADAD--------------VWFCGPPG-MADALEKG 199

                         170
                  ....*....|...
gi 1958642953 504 LveiisKEAGVDK 516
Cdd:cd06198   200 L-----RALGVPA 207
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 290-423 9.88e-05

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


Pssm-ID: 99805 [Multi-domain]  Cd Length: 228  Bit Score: 43.74  E-value: 9.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 290 RPYSCASSsllhPDKLHFVFNIVELPSnttaaslrkGVCTGWLATLVAPflqpntevltadhSDALApeiLISPRAtnSF 369
Cdd:cd06209    48 RSYSFSSA----PGDPRLEFLIRLLPG---------GAMSSYLRDRAQP-------------GDRLT---LTGPLG--SF 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958642953 370 HLpDDLSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgnfgaMWLFFGCRHKD 423
Cdd:cd06209    97 YL-REVKRPLLMLAGGTGLAPFLSMLDVLAEDGSAHP------VHLVYGVTRDA 143
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 385-507 2.01e-04

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


Pssm-ID: 99793 [Multi-domain]  Cd Length: 218  Bit Score: 43.00  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 385 GTGVAPFVGFLqhREKLQEQHPDGNFgamwLFFGCRhKDRDYLFREELRHFLKTG---VLTHLKVSfsrdaapeeeeeap 461
Cdd:cd06196   108 GAGITPFIAIL--RDLAAKGKLEGNT----LIFANK-TEKDIILKDELEKMLGLKfinVVTDEKDP-------------- 166

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958642953 462 akyvqdnlQHHSQQVARTLLQE-----NGYIYVCGDAKnMAKDVHDALVEI 507
Cdd:cd06196   167 --------GYAHGRIDKAFLKQhvtdfNQHFYVCGPPP-MEEAINGALKEL 208
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 290-433 4.42e-04

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: 41.87  E-value: 4.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 290 RPYSCASSsllhPDKLHFVfnivELpsntTAASLRKGVCTGWLATLVAPflqpntevltADHSDALAPeilispraTNSF 369
Cdd:cd06217    51 RSYSIASS----PTQRGRV----EL----TVKRVPGGEVSPYLHDEVKV----------GDLLEVRGP--------IGTF 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642953 370 HLPDDLSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgnfgaMWLFFGCRHKDrDYLFREELR 433
Cdd:cd06217   101 TWNPLHGDPVVLLAGGSGIVPLMSMIRYRRDLGWPVP------FRLLYSARTAE-DVIFRDELE 157
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 379-506 1.88e-03

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 40.56  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642953 379 IIMVGPGTGVAPFVGFLQH----REKlqeqhpdgnFGAMWLFFGCRHKdRDYLFREELRHFLKTGVLTHLKVSFSRDAAP 454
Cdd:PRK08345  111 LLLIAGGLGMAPLRSVLLYamdnRWK---------YGNITLIYGAKYY-EDLLFYDELIKDLAEAENVKIIQSVTRDPEW 180

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958642953 455 EEEEEAPAKYVQDNLQHHSQQVAR--TLLQENGYIYVCGDAKnMAKDVHDALVE 506
Cdd:PRK08345  181 PGCHGLPQGFIERVCKGVVTDLFReaNTDPKNTYAAICGPPV-MYKFVFKELIN 233
 
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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