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Conserved domains on  [gi|27369650|ref|NP_766068|]
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methionine synthase reductase [Mus musculus]

Protein Classification

sulfite reductase flavoprotein subunit alpha; NADPH--cytochrome P450 reductase( domain architecture ID 10446937)

sulfite reductase [NADPH] flavoprotein subunit alpha multimerizes with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide| NADPH--cytochrome P450 reductase, also called NADPH--hemoprotein reductase, is required for electron transfer from NADP to cytochrome P450 in microsomes

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 ...
 275-695 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: 596.23  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 275 PISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHRVILKIKTDTKKKGAAL 354
Cdd:cd06203   1 PISSAKKLTEGDDVKTVVDLTLDLSPTGFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVPNTKKKNAKV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 355 PAHVPEGRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPSCQP 434
Cdd:cd06203  81 PVHIPKVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDFVRKRGLSLLDLLEAFPSCRP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 435 PLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPPsttaaslrKGVCTGWLATLVApflqpntdvsnvdSGDAL 514
Cdd:cd06203 161 PLSLLIEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPA--------KGLCTSWLESLCL-------------SASSH 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 515 APEIRISPRATNAFHLPED-PSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPDGKFGAMWLFFGCRHKDRDYLFREELRH 593
Cdd:cd06203 220 GVKVPFYLRSSSRFRLPPDdLRRPIIMVGPGTGVAPFLGFLQHREKLKESHTETVFGEAWLFFGCRHRDRDYLFRDELEE 299

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 594 FLKTGVLTHLKVSFSRDAapdGEEAPAKYVQDNLQRHSQQVARTLLQENGYVYVCGDAKNMAKDVNDTLIGIISNEAGVD 673
Cdd:cd06203 300 FLEEGILTRLIVAFSRDE---NDGSTPKYVQDKLEERGKKLVDLLLNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGLD 376

                       410       420
                ....*....|....*....|..
gi 27369650 674 KLEAMKTLATLKQEKRYLQDIW 695
Cdd:cd06203 377 KLEAKKLLARLRKEDRYLEDVW 398
Flavodoxin_1 pfam00258
Flavodoxin;
6-142 1.73e-33

Flavodoxin;


:

Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 125.17  E-value: 1.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650     6 LLYATQRGQAKAIAEEISEQAVSHGFSADLHCISE-SEKYDLKTETGPLVMVVSTTGTGDPPDTARKFVKEIHNKTLPTD 84
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDDvDETLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGTLED 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27369650    85 -YFAHLQYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDTGHADDC---VGLELVVEPW 142
Cdd:pfam00258  81 gDLSGLKYAVFGLGDSGYEGFCGAAKKLDEKLSELGASRVGPLGEGDEDpqeDGLEEAFEAW 142
 
Name Accession Description Interval E-value
methionine_synthase_red cd06203
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ...
 275-695 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: 596.23  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 275 PISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHRVILKIKTDTKKKGAAL 354
Cdd:cd06203   1 PISSAKKLTEGDDVKTVVDLTLDLSPTGFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVPNTKKKNAKV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 355 PAHVPEGRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPSCQP 434
Cdd:cd06203  81 PVHIPKVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDFVRKRGLSLLDLLEAFPSCRP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 435 PLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPPsttaaslrKGVCTGWLATLVApflqpntdvsnvdSGDAL 514
Cdd:cd06203 161 PLSLLIEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPA--------KGLCTSWLESLCL-------------SASSH 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 515 APEIRISPRATNAFHLPED-PSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPDGKFGAMWLFFGCRHKDRDYLFREELRH 593
Cdd:cd06203 220 GVKVPFYLRSSSRFRLPPDdLRRPIIMVGPGTGVAPFLGFLQHREKLKESHTETVFGEAWLFFGCRHRDRDYLFRDELEE 299

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 594 FLKTGVLTHLKVSFSRDAapdGEEAPAKYVQDNLQRHSQQVARTLLQENGYVYVCGDAKNMAKDVNDTLIGIISNEAGVD 673
Cdd:cd06203 300 FLEEGILTRLIVAFSRDE---NDGSTPKYVQDKLEERGKKLVDLLLNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGLD 376

                       410       420
                ....*....|....*....|..
gi 27369650 674 KLEAMKTLATLKQEKRYLQDIW 695
Cdd:cd06203 377 KLEAKKLLARLRKEDRYLEDVW 398
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
 2-695 1.67e-147

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: 440.74  E-value: 1.67e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650   2 RRFLLLYATQRGQAKAIAEEISEQAVSHGFSADLHCISESEKYDLKTEtGPLVMVVSTTGTGDPPDTARKFVKEIHNKTL 81
Cdd:COG0369  27 TPLTILYGSQTGNAEGLAEQLAERAKAAGLAVTLASLDDYKPKDLAKE-GLLLIVTSTYGEGEPPDNARAFYEFLHSKKA 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  82 PTdyFAHLQYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDTGHADdcVGLELVVEPWIDGLWAALTKHFKslggqe 161
Cdd:COG0369 106 PK--LDGLRYAVLGLGDSSYETFCQTGKDFDARLEELGATRLLPRVDCD--VDYEEAAEAWLAAVLAALAEALG------ 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 162 nmsdtlsrASDAPLSTAmkpellhiqsqvellrledmgerdselreqnetnrgqqgriedfdsslvhsvpplsqsslsiP 241
Cdd:COG0369 176 --------AAAAAAAAA--------------------------------------------------------------A 185

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 242 AVPPEYlevhlqeslgqeenqasvpSGDPSFQVPISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDRE 321
Cdd:COG0369 186 AAAPAY-------------------SRKNPFPATVLENRELTGRGSAKETRHIEIDLPGSGLSYEPGDALGVWPENDPAL 246

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 322 VEELLQRLQLadKRAHRVILKIKTdtkkkgaalpahvpegRSLQFILTWCLEIRAVPKKaFLRALAEHTSSAtekrRLQE 401
Cdd:COG0369 247 VDELLARLGL--DGDEPVTLDGEP----------------LSLREALTEHLELTRLTPP-LLEKYAELTGNA----ELAA 303

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 402 LCSKQGAADYNRFIRDASVclLDLLLTFPSCQPPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPPSTTAas 481
Cdd:COG0369 304 LLADEDKAALREYLAGRQL--LDLLREFPAAELSAEELLELLRPLTPRLYSISSSPKAHPDEVHLTVGVVRYEASGRE-- 379

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 482 lRKGVCTGWLATLvapflqpntdvsnvDSGDalapEIRISPRATNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQ 561
Cdd:COG0369 380 -RKGVASTYLADL--------------EEGD----TVPVFVEPNPNFRLPADPDTPIIMIGPGTGIAPFRAFLQEREARG 440

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 562 EQhpdgkfGAMWLFFGCRHKDRDYLFREELRHFLKTGVLTHLKVSFSRDAAPdgeeapaK-YVQDNLQRHSQQVARtLLQ 640
Cdd:COG0369 441 AS------GKNWLFFGDRHFTTDFLYQTELQAWLKDGVLTRLDLAFSRDQAE-------KiYVQHRLLEQGAELWA-WLE 506

                       650       660       670       680       690
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27369650 641 ENGYVYVCGDAKNMAKDVNDTLIGIISNEAGVDKLEAMKTLATLKQEKRYLQDIW 695
Cdd:COG0369 507 EGAHVYVCGDASRMAKDVDAALLDIIAEHGGLSEEEAEEYLAELRAEKRYQRDVY 561
PRK06214 PRK06214
sulfite reductase subunit alpha;
281-695 5.07e-66

sulfite reductase subunit alpha;


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 226.88  E-value: 5.07e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  281 RLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQladKRAHRVIlkiktdtkkkgaalpahvpE 360
Cdd:PRK06214 178 RLNKPGSEKETWHVEIDLAGSGLDYEVGDSLGLFPANDPALVDAVIAALG---APPEFPI-------------------G 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  361 GRSLQFILTWCLEIRAVPKKAFLRaLAEHTSSATEK--RRLQELCSKQGAAdynrfirdASVCLLDLLLTFPSCQPPLSL 438
Cdd:PRK06214 236 GKTLREALLEDVSLGPAPDGLFEL-LSYITGGAARKkaRALAAGEDPDGDA--------ATLDVLAALEKFPGIRPDPEA 306

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  439 LLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFppsTTAASLRKGVCTGWLATLVAP------FLQPNtdvsnvdsgd 512
Cdd:PRK06214 307 FVEALDPLQPRLYSISSSPKATPGRVSLTVDAVRY---EIGSRLRLGVASTFLGERLAPgtrvrvYVQKA---------- 373

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  513 alapeirispratNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQhpdgkfGAMWLFFGCRHKDRDYLFREELR 592
Cdd:PRK06214 374 -------------HGFALPADPNTPIIMVGPGTGIAPFRAFLHERAATKAP------GRNWLFFGHQRSATDFFYEDELN 434

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  593 HFLKTGVLTHLKVSFSRDaapdGEEApaKYVQDNLQrhsqQVARTL---LQENGYVYVCGDAKNMAKDVNDTLIGIISNE 669
Cdd:PRK06214 435 GLKAAGVLTRLSLAWSRD----GEEK--TYVQDRMR----ENGAELwkwLEEGAHFYVCGDAKRMAKDVERALVDIVAQF 504

                        410       420
                 ....*....|....*....|....*.
gi 27369650  670 AGVDKLEAMKTLATLKQEKRYLQDIW 695
Cdd:PRK06214 505 GGRSPDEAVAFVAELKKAGRYQADVY 530
FAD_binding_1 pfam00667
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, ...
 272-490 1.60e-48

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: 169.83  E-value: 1.60e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650   272 FQVPISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHRVILKIKTDTKKkg 351
Cdd:pfam00667   8 FTAPVLSNRELTSPSSDRNCIHVELDISGSGLTYQTGDHLGVYPPNNEELVEELLERLGLDPKPDTVVLLKTLDERVK-- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650   352 aalpAHVPEGRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPS 431
Cdd:pfam00667  86 ----PPRLPPTTYRQALKYYLDITGPPSKQLLRLLAQFAPEEEEKQRLEFLSSDAGAREYKRWKLNHAPTLLEVLEEFPS 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 27369650   432 CQPPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFpPSTTAASLRKGVCTGW 490
Cdd:pfam00667 162 VKLPADFLLTQLPQLQPRYYSISSSSKVHPNEVHLTVVVVEY-ETDGEGRIHYGVCSNW 219
Flavodoxin_1 pfam00258
Flavodoxin;
6-142 1.73e-33

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 125.17  E-value: 1.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650     6 LLYATQRGQAKAIAEEISEQAVSHGFSADLHCISE-SEKYDLKTETGPLVMVVSTTGTGDPPDTARKFVKEIHNKTLPTD 84
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDDvDETLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGTLED 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27369650    85 -YFAHLQYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDTGHADDC---VGLELVVEPW 142
Cdd:pfam00258  81 gDLSGLKYAVFGLGDSGYEGFCGAAKKLDEKLSELGASRVGPLGEGDEDpqeDGLEEAFEAW 142
PRK08105 PRK08105
flavodoxin; Provisional
 1-150 2.28e-18

flavodoxin; Provisional


Pssm-ID: 181230 [Multi-domain]  Cd Length: 149  Bit Score: 82.24  E-value: 2.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650    1 MRRFLLLYATQRGQAKAIAEEISEQAVSHGFSADL---HCISESEKYDLKTetgpLVMVVSTTGTGDPPDTARKFVKEIh 77
Cdd:PRK08105   1 MAKVGIFVGTVYGNALLVAEEAEAILTAQGHEVTLfedPELSDWQPYQDEL----VLVVTSTTGQGDLPDSIVPLFQAL- 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27369650   78 NKTLPtdYFAHLQYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDTGHADDCVGLELVVE--PWIDGlWAAL 150
Cdd:PRK08105  76 KDTAG--YQPNLRYGVIALGDSSYDNFCGAGKQFDALLQEQGAKRVGERLEIDACETPEPEVEanPWVEQ-WGTL 147
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
 5-146 7.19e-11

Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440480 [Multi-domain]  Cd Length: 135  Bit Score: 60.30  E-value: 7.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650   5 LLLYATQRGQAKAIAEEISEQAVSHGfsADLHCISES-----EKYDLktetgpLVMVVSTTGtGDPPDTARKFVKEIhnk 79
Cdd:COG0716   2 LIVYGSTTGNTEKVAEAIAEALGAAG--VDLFEIEDAdlddlEDYDL------LILGTPTWA-GELPDDWEDFLEEL--- 69

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27369650  80 tlpTDYFAHLQYGLLGLGDSEytYFCNGGKVIDKRLQELGAQR----FYDTGHADDCVGLELVVEPWIDGL 146
Cdd:COG0716  70 ---KEDLSGKKVALFGTGDSS--GYGDALGELKELLEEKGAKVvggyDFEGSKAPDAEDTEERAEEWLKQL 135
 
Name Accession Description Interval E-value
methionine_synthase_red cd06203
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ...
 275-695 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: 596.23  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 275 PISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHRVILKIKTDTKKKGAAL 354
Cdd:cd06203   1 PISSAKKLTEGDDVKTVVDLTLDLSPTGFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVPNTKKKNAKV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 355 PAHVPEGRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPSCQP 434
Cdd:cd06203  81 PVHIPKVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDFVRKRGLSLLDLLEAFPSCRP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 435 PLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPPsttaaslrKGVCTGWLATLVApflqpntdvsnvdSGDAL 514
Cdd:cd06203 161 PLSLLIEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPA--------KGLCTSWLESLCL-------------SASSH 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 515 APEIRISPRATNAFHLPED-PSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPDGKFGAMWLFFGCRHKDRDYLFREELRH 593
Cdd:cd06203 220 GVKVPFYLRSSSRFRLPPDdLRRPIIMVGPGTGVAPFLGFLQHREKLKESHTETVFGEAWLFFGCRHRDRDYLFRDELEE 299

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 594 FLKTGVLTHLKVSFSRDAapdGEEAPAKYVQDNLQRHSQQVARTLLQENGYVYVCGDAKNMAKDVNDTLIGIISNEAGVD 673
Cdd:cd06203 300 FLEEGILTRLIVAFSRDE---NDGSTPKYVQDKLEERGKKLVDLLLNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGLD 376

                       410       420
                ....*....|....*....|..
gi 27369650 674 KLEAMKTLATLKQEKRYLQDIW 695
Cdd:cd06203 377 KLEAKKLLARLRKEDRYLEDVW 398
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
 2-695 1.67e-147

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: 440.74  E-value: 1.67e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650   2 RRFLLLYATQRGQAKAIAEEISEQAVSHGFSADLHCISESEKYDLKTEtGPLVMVVSTTGTGDPPDTARKFVKEIHNKTL 81
Cdd:COG0369  27 TPLTILYGSQTGNAEGLAEQLAERAKAAGLAVTLASLDDYKPKDLAKE-GLLLIVTSTYGEGEPPDNARAFYEFLHSKKA 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  82 PTdyFAHLQYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDTGHADdcVGLELVVEPWIDGLWAALTKHFKslggqe 161
Cdd:COG0369 106 PK--LDGLRYAVLGLGDSSYETFCQTGKDFDARLEELGATRLLPRVDCD--VDYEEAAEAWLAAVLAALAEALG------ 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 162 nmsdtlsrASDAPLSTAmkpellhiqsqvellrledmgerdselreqnetnrgqqgriedfdsslvhsvpplsqsslsiP 241
Cdd:COG0369 176 --------AAAAAAAAA--------------------------------------------------------------A 185

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 242 AVPPEYlevhlqeslgqeenqasvpSGDPSFQVPISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDRE 321
Cdd:COG0369 186 AAAPAY-------------------SRKNPFPATVLENRELTGRGSAKETRHIEIDLPGSGLSYEPGDALGVWPENDPAL 246

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 322 VEELLQRLQLadKRAHRVILKIKTdtkkkgaalpahvpegRSLQFILTWCLEIRAVPKKaFLRALAEHTSSAtekrRLQE 401
Cdd:COG0369 247 VDELLARLGL--DGDEPVTLDGEP----------------LSLREALTEHLELTRLTPP-LLEKYAELTGNA----ELAA 303

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 402 LCSKQGAADYNRFIRDASVclLDLLLTFPSCQPPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPPSTTAas 481
Cdd:COG0369 304 LLADEDKAALREYLAGRQL--LDLLREFPAAELSAEELLELLRPLTPRLYSISSSPKAHPDEVHLTVGVVRYEASGRE-- 379

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 482 lRKGVCTGWLATLvapflqpntdvsnvDSGDalapEIRISPRATNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQ 561
Cdd:COG0369 380 -RKGVASTYLADL--------------EEGD----TVPVFVEPNPNFRLPADPDTPIIMIGPGTGIAPFRAFLQEREARG 440

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 562 EQhpdgkfGAMWLFFGCRHKDRDYLFREELRHFLKTGVLTHLKVSFSRDAAPdgeeapaK-YVQDNLQRHSQQVARtLLQ 640
Cdd:COG0369 441 AS------GKNWLFFGDRHFTTDFLYQTELQAWLKDGVLTRLDLAFSRDQAE-------KiYVQHRLLEQGAELWA-WLE 506

                       650       660       670       680       690
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27369650 641 ENGYVYVCGDAKNMAKDVNDTLIGIISNEAGVDKLEAMKTLATLKQEKRYLQDIW 695
Cdd:COG0369 507 EGAHVYVCGDASRMAKDVDAALLDIIAEHGGLSEEEAEEYLAELRAEKRYQRDVY 561
CYPOR cd06204
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 272-695 1.41e-112

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: 345.78  E-value: 1.41e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 272 FQVPISKAIRLTTNdAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADkraHRVILKIKTDTKKKG 351
Cdd:cd06204   6 FLAPVAVSRELFTG-SDRSCLHIEFDISGSGIRYQTGDHLAVWPTNPSEEVERLLKVLGLDD---RDTVISLKSLDEPAS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 352 AALPahVPEGRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSkQGAADYNRFIRDASVCLLDLLLTFPS 431
Cdd:cd06204  82 KKVP--FPCPTTYRTALRHYLDITAPVSRQVLAALAQFAPDPEEKERLLKLAS-EGKDEYAKWIVEPHRNLLEVLQDFPS 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 432 CQ---PPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPpsTTAASLRKGVCTGWLATLVAPFLQPNTDVSNV 508
Cdd:cd06204 159 AKptpPPFDFLIELLPRLQPRYYSISSSSKVHPNRIHITAVVVKYP--TPTGRIIKGVATNWLLALKPALNGEKPPTPYY 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 509 DSGDALAPEIRISP---RATNaFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgKFGAMWLFFGCRHKDRDY 585
Cdd:cd06204 237 LSGPRKKGGGSKVPvfvRRSN-FRLPTKPSTPVIMIGPGTGVAPFRGFIQERAALKESGK--KVGPTLLFFGCRHPDEDF 313

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 586 LFREELRHFLKTGVLTHLKVSFSRdaapdgEEAPAKYVQDNLQRHSQQVARtLLQENGYVYVCGDAKNMAKDVNDTLIGI 665
Cdd:cd06204 314 IYKDELEEYAKLGGLLELVTAFSR------EQPKKVYVQHRLAEHAEQVWE-LINEGAYIYVCGDAKNMARDVEKTLLEI 386

                       410       420       430
                ....*....|....*....|....*....|
gi 27369650 666 ISNEAGVDKLEAMKTLATLKQEKRYLQDIW 695
Cdd:cd06204 387 LAEQGGMTETEAEEYVKKLKTRGRYQEDVW 416
CyPoR_like cd06207
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 281-695 6.42e-100

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: 311.51  E-value: 6.42e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 281 RLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHRVILKIKTDTKKkgaalpaHVPE 360
Cdd:cd06207   7 RLTPADYDRSTRHIEFDLGGSGLSYETGDNLGIYPENSDALVDEFLARLGLDGDDVVRVEPNEQQRGKP-------PFPE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 361 GRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSKQGAADYNRFIRdasVCLLDLLLTFPSCQPPLSLLL 440
Cdd:cd06207  80 PISVRQLLKKFLDIFGKPTKKFLKLLSQLATDEEEKEDLYKLASREGRTEYKRYEK---YTYLEVLKDFPSVRPTLEQLL 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 441 EHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFppSTTAASLRKGVCTGWLAtlvapflqpntdvsNVDSGDALAPEIRI 520
Cdd:cd06207 157 ELCPLIKPRYYSISSSPLKNPNEVHLLVSLVSW--KTPSGRSRYGLCSSYLA--------------GLKVGQRVTVFIKK 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 521 SpratnAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgKFGAMWLFFGCRHKDRDYLFREELRHFLKTGVL 600
Cdd:cd06207 221 S-----SFKLPKDPKKPIIMVGPGTGLAPFRAFLQERAALLAQGP--EIGPVLLYFGCRHEDKDYLYKEELEEYEKSGVL 293

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 601 THLKVSFSRDaapdgeEAPAKYVQDNLQRHSQQVARTLLQENGYVYVCGDAKNMAKDVNDTLIGIISNEAGVDKLEAMKT 680
Cdd:cd06207 294 TTLGTAFSRD------QPKKVYVQDLIRENSDLVYQLLEEGAGVIYVCGSTWKMPPDVQEAFEEILKKHGGGDEELAEKK 367

                       410
                ....*....|....*
gi 27369650 681 LATLKQEKRYLQDIW 695
Cdd:cd06207 368 IEELEERGRYVVEAW 382
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 423-695 1.20e-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: 301.56  E-value: 1.20e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 423 LDLLLTFPSCQPPLSLLLEHLP-KLQPRPYSCASSSLRHPDKLHFVFNIVEFPpsTTAASLRKGVCTGWLATLVapflqp 501
Cdd:cd06182  22 FDLSGNSVLKYQPGDHLGVIPPnPLQPRYYSIASSPDVDPGEVHLCVRVVSYE--APAGRIRKGVCSNFLAGLQ------ 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 502 ntdvsnvdsgdaLAPEIRISPRATNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQeqHPDGKFGAMWLFFGCRHK 581
Cdd:cd06182  94 ------------LGAKVTVFIRPAPSFRLPKDPTTPIIMVGPGTGIAPFRGFLQERAALR--ANGKARGPAWLFFGCRNF 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 582 DRDYLFREELRHFLKTGVLTHLKVSFSRDAApdgeeAPAKYVQDNLQRHSQQVARtLLQENGYVYVCGDAKNMAKDVNDT 661
Cdd:cd06182 160 ASDYLYREELQEALKDGALTRLDVAFSREQA-----EPKVYVQDKLKEHAEELRR-LLNEGAHIYVCGDAKSMAKDVEDA 233

                       250       260       270
                ....*....|....*....|....*....|....
gi 27369650 662 LIGIISNEAGVDKLEAMKTLATLKQEKRYLQDIW 695
Cdd:cd06182 234 LVKIIAKAGGVDESDAEEYLKELEDEGRYVEDVW 267
SiR cd06199
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 276-695 4.84e-92

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: 290.28  E-value: 4.84e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 276 ISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLAdkrahrvilkiktdtkkkGAALP 355
Cdd:cd06199   2 VLENRLLTGPGSEKETRHIELDLEGSGLSYEPGDALGVYPTNDPALVDELLAALGLS------------------GDEPV 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 356 AHVPEG-RSLQFILTWCLEIRAVpkkafLRALAEHTSSATEKRRLQELCSKQGAADYNRfirdasvcLLDLLLTFPSCQP 434
Cdd:cd06199  64 STVGGGtLPLREALIKHYEITTL-----LLALLESYAADTGALELLALAALEAVLAFAE--------LRDVLDLLPIPPA 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 435 PLSL--LLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFppsTTAASLRKGVCTGWLATLVAP------FLQPNtdvs 506
Cdd:cd06199 131 RLTAeeLLDLLRPLQPRLYSIASSPKAVPDEVHLTVAVVRY---ESHGRERKGVASTFLADRLKEgdtvpvFVQPN---- 203

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 507 nvdsgdalapeirispratNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLqeqhpdGKFGAMWLFFGCRHKDRDYL 586
Cdd:cd06199 204 -------------------PHFRLPEDPDAPIIMVGPGTGIAPFRAFLQEREAT------GAKGKNWLFFGERHFATDFL 258

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 587 FREELRHFLKTGVLTHLKVSFSRDaapdGEEapaK-YVQDNLQRHSQQVArTLLQENGYVYVCGDAKNMAKDVNDTLIGI 665
Cdd:cd06199 259 YQDELQQWLKDGVLTRLDTAFSRD----QAE---KvYVQDRMREQGAELW-AWLEEGAHFYVCGDAKRMAKDVDAALLDI 330

                       410       420       430
                ....*....|....*....|....*....|
gi 27369650 666 ISNEAGVDKLEAMKTLATLKQEKRYLQDIW 695
Cdd:cd06199 331 IATEGGMDEEEAEAYLKELKKEKRYQRDVY 360
Nitric_oxide_synthase cd06202
The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses ...
 281-694 1.16e-89

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: 285.76  E-value: 1.16e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 281 RLTTNDAVKSTLLLELDISKI-EFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHrvILKIKTDTKKKGAALPAHV- 358
Cdd:cd06202   7 NLQSPKSSRSTILVKLDTNGAqELHYQPGDHVGIFPANRPELVDALLDRLHDAPPPDQ--VIKLEVLEERSTALGIIKTw 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 359 -PEGR----SLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCskQGAADYNRFIRDASVCLLDLLLTFPSCQ 433
Cdd:cd06202  85 tPHERlppcTLRQALTRYLDITTPPTPQLLQLLATLATDEKDKERLEVLG--KGSSEYEDWKWYKNPNILEVLEEFPSLQ 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 434 PPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPPSTTAASLRKGVCTGWLATLvapflqpntdvsnvDSGDA 513
Cdd:cd06202 163 VPASLLLTQLPLLQPRYYSISSSPDMYPGEIHLTVAVVSYRTRDGQGPVHHGVCSTWLNGL--------------TPGDT 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 514 LAPEIRISPratnAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHR--EKLQEQHPDGKFGAMWLFFGCRHKDRDYLFREEL 591
Cdd:cd06202 229 VPCFVRSAP----SFHLPEDPSVPVIMVGPGTGIAPFRSFWQQRqyDLRMSEDPGKKFGDMTLFFGCRNSTIDDIYKEET 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 592 RHFLKTGVLTHLKVSFSRDaaPDgeeAPAKYVQDNLQRHSQQVARTLLQENGYVYVCGDAkNMAKDVNDTLIGIISNEAG 671
Cdd:cd06202 305 EEAKNKGVLTEVYTALSRE--PG---KPKTYVQDLLKEQAESVYDALVREGGHIYVCGDV-TMAEDVSQTIQRILAEHGN 378

                       410       420
                ....*....|....*....|...
gi 27369650 672 VDKLEAMKTLATLKQEKRYLQDI 694
Cdd:cd06202 379 MSAEEAEEFILKLRDENRYHEDI 401
bifunctional_CYPOR cd06206
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ...
 278-695 2.81e-70

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: 234.08  E-value: 2.81e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 278 KAIRLTTNDAV-KSTLLLELDISKiEFSHQPGDSFNVTCPNSDREVEELLQRLQLAdkrahrvilkIKTDTKKKGAALPA 356
Cdd:cd06206   3 VENRELTAPGVgPSKRHLELRLPD-GMTYRAGDYLAVLPRNPPELVRRALRRFGLA----------WDTVLTISASGSAT 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 357 HVPEGRSLQF--ILTWCLEIRAVPKKAFLRALAEHTSsATEKRRLQELCSKQGaadYNRFIRDASVCLLDLLLTFPSCQP 434
Cdd:cd06206  72 GLPLGTPISVseLLSSYVELSQPATRRQLAALAEATR-CPDTKALLERLAGEA---YAAEVLAKRVSVLDLLERFPSIAL 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 435 PLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPpSTTAASLRKGVCTGWLATLvapflQPntdvsnvdsGDal 514
Cdd:cd06206 148 PLATFLAMLPPMRPRQYSISSSPLVDPGHATLTVSVLDAP-ALSGQGRYRGVASSYLSSL-----RP---------GD-- 210

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 515 apEIRISPRATN-AFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQhpDGKFGAMWLFFGCRHKDRDYLFREELRH 593
Cdd:cd06206 211 --SIHVSVRPSHsAFRPPSDPSTPLIMIAAGTGLAPFRGFLQERAALLAQ--GRKLAPALLFFGCRHPDHDDLYRDELEE 286

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 594 FLKTGVLThLKVSFSRDAapdgeEAPAKYVQDNLQRHSQQVARtLLQENGYVYVCGDAKnMAKDVNDTLIGIISNE---- 669
Cdd:cd06206 287 WEAAGVVS-VRRAYSRPP-----GGGCRYVQDRLWAEREEVWE-LWEQGARVYVCGDGR-MAPGVREVLKRIYAEKderg 358

                       410       420
                ....*....|....*....|....*.
gi 27369650 670 AGVDKLEAMKTLATLKQEKRYLQDIW 695
Cdd:cd06206 359 GGSDDEEAEEWLEELRNKGRYATDVF 384
PRK06214 PRK06214
sulfite reductase subunit alpha;
281-695 5.07e-66

sulfite reductase subunit alpha;


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 226.88  E-value: 5.07e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  281 RLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQladKRAHRVIlkiktdtkkkgaalpahvpE 360
Cdd:PRK06214 178 RLNKPGSEKETWHVEIDLAGSGLDYEVGDSLGLFPANDPALVDAVIAALG---APPEFPI-------------------G 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  361 GRSLQFILTWCLEIRAVPKKAFLRaLAEHTSSATEK--RRLQELCSKQGAAdynrfirdASVCLLDLLLTFPSCQPPLSL 438
Cdd:PRK06214 236 GKTLREALLEDVSLGPAPDGLFEL-LSYITGGAARKkaRALAAGEDPDGDA--------ATLDVLAALEKFPGIRPDPEA 306

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  439 LLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFppsTTAASLRKGVCTGWLATLVAP------FLQPNtdvsnvdsgd 512
Cdd:PRK06214 307 FVEALDPLQPRLYSISSSPKATPGRVSLTVDAVRY---EIGSRLRLGVASTFLGERLAPgtrvrvYVQKA---------- 373

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  513 alapeirispratNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQhpdgkfGAMWLFFGCRHKDRDYLFREELR 592
Cdd:PRK06214 374 -------------HGFALPADPNTPIIMVGPGTGIAPFRAFLHERAATKAP------GRNWLFFGHQRSATDFFYEDELN 434

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  593 HFLKTGVLTHLKVSFSRDaapdGEEApaKYVQDNLQrhsqQVARTL---LQENGYVYVCGDAKNMAKDVNDTLIGIISNE 669
Cdd:PRK06214 435 GLKAAGVLTRLSLAWSRD----GEEK--TYVQDRMR----ENGAELwkwLEEGAHFYVCGDAKRMAKDVERALVDIVAQF 504

                        410       420
                 ....*....|....*....|....*.
gi 27369650  670 AGVDKLEAMKTLATLKQEKRYLQDIW 695
Cdd:PRK06214 505 GGRSPDEAVAFVAELKKAGRYQADVY 530
cysJ PRK10953
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
6-695 9.49e-64

NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;


Pssm-ID: 182862 [Multi-domain]  Cd Length: 600  Bit Score: 222.67  E-value: 9.49e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650    6 LLYATQRGQAKAIAEEISEQAVSHGFSADLhciSESEKYDLK--TETGPLVMVVSTTGTGDPPDTARKFVKEIHNKTLPT 83
Cdd:PRK10953  66 LISASQTGNARRVAEQLRDDLLAAKLNVNL---VNAGDYKFKqiAQEKLLIVVTSTQGEGEPPEEAVALHKFLFSKKAPK 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650   84 dyFAHLQYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDTGHADdcVGLELVVEPWidglWAALTKHFKSlggqenm 163
Cdd:PRK10953 143 --LENTAFAVFGLGDTSYEFFCQAGKDFDSKLAELGAERLLDRVDAD--VEYQAAASEW----RARVVDALKS------- 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  164 sdtlsrasDAPLSTAmkpellhiQSQVellrledmgerdselreqnetnrGQQGRIEDFDSSLVHSVPPLSqSSLSIpav 243
Cdd:PRK10953 208 --------RAPAVAA--------PSQS-----------------------VATGAVNEIHTSPYSKEAPLT-ASLSV--- 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  244 ppeylevhlqeslgqeeNQasvpsgdpsfqvpiskaiRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVE 323
Cdd:PRK10953 245 -----------------NQ------------------KITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVK 289

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  324 ELLQRLQLadKRAHRVILKIKTdtkkkgaalpahVPEGRSLQfiltWCLEI-----RAVPKKAFLRALAEHTSSATEKRR 398
Cdd:PRK10953 290 ELVELLWL--KGDEPVTVDGKT------------LPLAEALQ----WHFELtvntaNIVENYATLTRSETLLPLVGDKAA 351

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  399 LQELCSKQGAADYNRFIrdasvclldllltfPScQPPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPPSTT 478
Cdd:PRK10953 352 LQHYAATTPIVDMVRFA--------------PA-QLDAEQLIGLLRPLTPRLYSIASSQAEVENEVHITVGVVRYDIEGR 416

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  479 AaslRKGVCTGWLATLVApflqpntdvsnvDSGdalapEIRISPRATNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHRE 558
Cdd:PRK10953 417 A---RAGGASSFLADRLE------------EEG-----EVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRA 476

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  559 KlqeqhpDGKFGAMWLFFGCRHKDRDYLFREELRHFLKTGVLTHLKVSFSRDaapdgeEAPAKYVQDNLQRHSQQVARtL 638
Cdd:PRK10953 477 A------DGAPGKNWLFFGNPHFTEDFLYQVEWQRYVKEGLLTRIDLAWSRD------QKEKIYVQDKLREQGAELWR-W 543

                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 27369650  639 LQENGYVYVCGDAKNMAKDVNDTLIGIISNEAGVDKLEAMKTLATLKQEKRYLQDIW 695
Cdd:PRK10953 544 INDGAHIYVCGDANRMAKDVEQALLEVIAEFGGMDTEAADEFLSELRVERRYQRDVY 600
FAD_binding_1 pfam00667
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, ...
 272-490 1.60e-48

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: 169.83  E-value: 1.60e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650   272 FQVPISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHRVILKIKTDTKKkg 351
Cdd:pfam00667   8 FTAPVLSNRELTSPSSDRNCIHVELDISGSGLTYQTGDHLGVYPPNNEELVEELLERLGLDPKPDTVVLLKTLDERVK-- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650   352 aalpAHVPEGRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPS 431
Cdd:pfam00667  86 ----PPRLPPTTYRQALKYYLDITGPPSKQLLRLLAQFAPEEEEKQRLEFLSSDAGAREYKRWKLNHAPTLLEVLEEFPS 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 27369650   432 CQPPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFpPSTTAASLRKGVCTGW 490
Cdd:pfam00667 162 VKLPADFLLTQLPQLQPRYYSISSSSKVHPNEVHLTVVVVEY-ETDGEGRIHYGVCSNW 219
Flavodoxin_1 pfam00258
Flavodoxin;
6-142 1.73e-33

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 125.17  E-value: 1.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650     6 LLYATQRGQAKAIAEEISEQAVSHGFSADLHCISE-SEKYDLKTETGPLVMVVSTTGTGDPPDTARKFVKEIHNKTLPTD 84
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDDvDETLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGTLED 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27369650    85 -YFAHLQYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDTGHADDC---VGLELVVEPW 142
Cdd:pfam00258  81 gDLSGLKYAVFGLGDSGYEGFCGAAKKLDEKLSELGASRVGPLGEGDEDpqeDGLEEAFEAW 142
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 448-695 3.44e-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: 3.44e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 448 PRPYSCASSSLRhpdklhfvfNIVEFppsttaaSLRK---GVCTGWLATLvapflqpntdvsnvDSGDALAPEIRISPRa 524
Cdd:cd06201 100 PRFYSLASSSSD---------GFLEI-------CVRKhpgGLCSGYLHGL--------------KPGDTIKAFIRPNPS- 148

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 525 tnaFHLPEDpSAPIIMVGPGTGVAPFVGFLQHREKlqeQHPdgkfgaMWLFFGCRHKDRDYLFREELRHFLKTGVLTHLK 604
Cdd:cd06201 149 ---FRPAKG-AAPVILIGAGTGIAPLAGFIRANAA---RRP------MHLYWGGRDPASDFLYEDELDQYLADGRLTQLH 215

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 605 VSFSRdaAPDGeeapaKYVQDNLQRHSQQVARtLLQENGYVYVCGdAKNMAKDVNDTLIGIIsneagvdkLEAMKTLATL 684
Cdd:cd06201 216 TAFSR--TPDG-----AYVQDRLRADAERLRR-LIEDGAQIMVCG-SRAMAQGVAAVLEEIL--------APQPLSLDEL 278

                       250
                ....*....|.
gi 27369650 685 KQEKRYLQDIW 695
Cdd:cd06201 279 KLQGRYAEDVY 289
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 436-662 1.31e-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: 119.86  E-value: 1.31e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 436 LSLLLEHLPKLQPRPYSCASSSlRHPDKLHFVFNIVEfppsttaaslrKGVCTGWLATLvapflqpntdvsnvDSGDala 515
Cdd:cd00322  29 VDLHLPGDGRGLRRAYSIASSP-DEEGELELTVKIVP-----------GGPFSAWLHDL--------------KPGD--- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 516 pEIRISPRATNaFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgkfgaMWLFFGCRHKDrDYLFREELRHFL 595
Cdd:cd00322  80 -EVEVSGPGGD-FFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGE------ITLLYGARTPA-DLLFLDELEELA 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27369650 596 KTGVLTHLKVSFSRDAAPDgeeapaKYVQDNLQRHSQQVARTLLQENGYVYVCGDAkNMAKDVNDTL 662
Cdd:cd00322 151 KEGPNFRLVLALSRESEAK------LGPGGRIDREAEILALLPDDSGALVYICGPP-AMAKAVREAL 210
SiR_like1 cd06200
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 439-695 1.11e-27

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: 111.99  E-value: 1.11e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 439 LLEHLPK--LQPRPYSCAS-----------SSLRHPDKLHfvfnivefppsttaaslrkGVCTGWLaTLVAPflqpntdv 505
Cdd:cd06200  37 IAEIGPRhpLPHREYSIASlpadgalellvRQVRHADGGL-------------------GLGSGWL-TRHAP-------- 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 506 snvdsgdaLAPEIRISPRATNAFHLPEDpSAPIIMVGPGTGVAPFVGFLQHREKlQEQHPDgkfgamWLFFGCRHKDRDY 585
Cdd:cd06200  89 --------IGASVALRLRENPGFHLPDD-GRPLILIGNGTGLAGLRSHLRARAR-AGRHRN------WLLFGERQAAHDF 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 586 LFREELRHFLKTGVLTHLKVSFSRDAapdgeeAPAKYVQDNLQRHSQQVaRTLLQENGYVYVCGDAKNMAKDVNDTLIGI 665
Cdd:cd06200 153 FCREELEAWQAAGHLARLDLAFSRDQ------AQKRYVQDRLRAAADEL-RAWVAEGAAIYVCGSLQGMAPGVDAVLDEI 225

                       250       260       270
                ....*....|....*....|....*....|
gi 27369650 666 IsneaGVDKLEAmktlatLKQEKRYLQDIW 695
Cdd:cd06200 226 L----GEEAVEA------LLAAGRYRRDVY 245
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 448-690 1.51e-27

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: 112.80  E-value: 1.51e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 448 PRPYSCASSSL---RHPDKLHFVFNIVEFPPSTTAaSLRKGVCTGWLATLVApflqpntdvsnvdsGDalapEIRISPRA 524
Cdd:cd06208  64 LRLYSIASSRYgddGDGKTLSLCVKRLVYTDPETD-ETKKGVCSNYLCDLKP--------------GD----DVQITGPV 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 525 TNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHRekLQEQHPDGKF-GAMWLFFGCRHKDrDYLFREELRHFLKT-GVLTH 602
Cdd:cd06208 125 GKTMLLPEDPNATLIMIATGTGIAPFRSFLRRL--FREKHADYKFtGLAWLFFGVPNSD-SLLYDDELEKYPKQyPDNFR 201

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 603 LKVSFSRDaaPDGEEAPAKYVQDNLQRHSQQVARTLLQENGYVYVCGdAKNMAKDVNDTLigiiSNEAGVDKLEAMKtLA 682
Cdd:cd06208 202 IDYAFSRE--QKNADGGKMYVQDRIAEYAEEIWNLLDKDNTHVYICG-LKGMEPGVDDAL----TSVAEGGLAWEEF-WE 273


                ....*...
gi 27369650 683 TLKQEKRY 690
Cdd:cd06208 274 SLKKKGRW 281
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
 484-686 5.30e-20

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 92.37  E-value: 5.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  484 KGVCTGWLATLvapflQPNTDVSnvdsgdalapeirISPRATNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQhrEKLQEQ 563
Cdd:PLN03115 182 KGVCSNFLCDL-----KPGAEVK-------------ITGPVGKEMLMPKDPNATIIMLATGTGIAPFRSFLW--KMFFEK 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  564 HPDGKF-GAMWLFFGCRHKDrDYLFREELRHfLKTGVLTHLKVSFSRDAAPDGEEAPAKYVQDNLQRHSQQVARTLLQEN 642
Cdd:PLN03115 242 HDDYKFnGLAWLFLGVPTSS-SLLYKEEFEK-MKEKAPENFRLDFAVSREQTNAKGEKMYIQTRMAEYAEELWELLKKDN 319

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 27369650  643 GYVYVCGdAKNMAKDVNDTLIGIISNEaGVDKLEAMKTLATLKQ 686
Cdd:PLN03115 320 TYVYMCG-LKGMEKGIDDIMVSLAAKD-GIDWFEYKKQLKKAEQ 361
PRK08105 PRK08105
flavodoxin; Provisional
 1-150 2.28e-18

flavodoxin; Provisional


Pssm-ID: 181230 [Multi-domain]  Cd Length: 149  Bit Score: 82.24  E-value: 2.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650    1 MRRFLLLYATQRGQAKAIAEEISEQAVSHGFSADL---HCISESEKYDLKTetgpLVMVVSTTGTGDPPDTARKFVKEIh 77
Cdd:PRK08105   1 MAKVGIFVGTVYGNALLVAEEAEAILTAQGHEVTLfedPELSDWQPYQDEL----VLVVTSTTGQGDLPDSIVPLFQAL- 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27369650   78 NKTLPtdYFAHLQYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDTGHADDCVGLELVVE--PWIDGlWAAL 150
Cdd:PRK08105  76 KDTAG--YQPNLRYGVIALGDSSYDNFCGAGKQFDALLQEQGAKRVGERLEIDACETPEPEVEanPWVEQ-WGTL 147
PLN03116 PLN03116
ferredoxin--NADP+ reductase; Provisional
 448-690 2.65e-18

ferredoxin--NADP+ reductase; Provisional


Pssm-ID: 215586 [Multi-domain]  Cd Length: 307  Bit Score: 86.31  E-value: 2.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  448 PRPYSCASSslRHPDKLH------FVFNIVEFPPSTTAA-SLRKGVCTGWLAtlvapflqpntdvsNVDSGDalapEIRI 520
Cdd:PLN03116  81 VRLYSIAST--RYGDDFDgktaslCVRRAVYYDPETGKEdPAKKGVCSNFLC--------------DAKPGD----KVQI 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  521 SPRATNAFHLPE-DPSAPIIMVGPGTGVAPFVGFLqhREKLQEQHPDGKF-GAMWLFFGCRHKDRdYLFREELrhflkTG 598
Cdd:PLN03116 141 TGPSGKVMLLPEeDPNATHIMVATGTGIAPFRGFL--RRMFMEDVPAFKFgGLAWLFLGVANSDS-LLYDDEF-----ER 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  599 VLTHLKVSFSRDAAPDGEEAPAK----YVQDNLQRHSQQVArTLLQENGYVYVCGdAKNMAKDVNDTLIGiISNEAGVDK 674
Cdd:PLN03116 213 YLKDYPDNFRYDYALSREQKNKKggkmYVQDKIEEYSDEIF-KLLDNGAHIYFCG-LKGMMPGIQDTLKR-VAEERGESW 289

                        250
                 ....*....|....*.
gi 27369650  675 LEamkTLATLKQEKRY 690
Cdd:PLN03116 290 EE---KLSGLKKNKQW 302
PRK09004 PRK09004
FMN-binding protein MioC; Provisional
 13-126 2.36e-16

FMN-binding protein MioC; Provisional


Pssm-ID: 181608 [Multi-domain]  Cd Length: 146  Bit Score: 76.41  E-value: 2.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650   13 GQAKAIAEEISEQAVSHGFSADLHCISESEkyDLKTEtGPLVMVVSTTGTGDPPDTARKFVKEIHNKTLPtdyFAHLQYG 92
Cdd:PRK09004  13 GGAEYVADHLAEKLEEAGFSTETLHGPLLD--DLSAS-GLWLIVTSTHGAGDLPDNLQPFFEELQEQKPD---LSQVRFA 86

                         90       100       110
                 ....*....|....*....|....*....|....
gi 27369650   93 LLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDT 126
Cdd:PRK09004  87 AIGIGSSEYDTFCGAIDKLEQLLKAKGAKQIGET 120
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 540-658 7.67e-16

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: 73.83  E-value: 7.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650   540 MVGPGTGVAPFVGFLQHRekLQEQHPDGKfgaMWLFFGCRHkDRDYLFREELRHFLKT--GVLTHLKVSFSRDAAPDGEE 617
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAI--LEDPKDPTQ---VVLVFGNRN-EDDILYREELDELAEKhpGRLTVVYVVSRPEAGWTGGK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 27369650   618 apaKYVQDNLQRHSQQvartLLQENGYVYVCGdAKNMAKDV 658
Cdd:pfam00175  75 ---GRVQDALLEDHLS----LPDEETHVYVCG-PPGMIKAV 107
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
436-674 2.89e-12

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 66.74  E-value: 2.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 436 LSLLLEHLPKLQPRPYSCASSslrhPDKLHFVFnivefppsttaASLR--KGVCTGWLATLVAPflqpntdvsnvdsGDa 513
Cdd:COG1018  40 VTLRLPIDGKPLRRAYSLSSA----PGDGRLEI-----------TVKRvpGGGGSNWLHDHLKV-------------GD- 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 514 lapEIRISPrATNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHrekLQEQHPDGKFgamWLFFGCRHKDrDYLFREELRH 593
Cdd:COG1018  91 ---TLEVSG-PRGDFVLDPEPARPLLLIAGGIGITPFLSMLRT---LLARGPFRPV---TLVYGARSPA-DLAFRDELEA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 594 FLKTGVLTHLKVSFSRDAAPDG----EEAPAKYVQDNLQRHsqqvartllqengyVYVCGDAkNMAKDVNDTLIgiisnE 669
Cdd:COG1018 160 LAARHPRLRLHPVLSREPAGLQgrldAELLAALLPDPADAH--------------VYLCGPP-PMMEAVRAALA-----E 219


                ....*
gi 27369650 670 AGVDK 674
Cdd:COG1018 220 LGVPE 224
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
 5-146 7.19e-11

Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440480 [Multi-domain]  Cd Length: 135  Bit Score: 60.30  E-value: 7.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650   5 LLLYATQRGQAKAIAEEISEQAVSHGfsADLHCISES-----EKYDLktetgpLVMVVSTTGtGDPPDTARKFVKEIhnk 79
Cdd:COG0716   2 LIVYGSTTGNTEKVAEAIAEALGAAG--VDLFEIEDAdlddlEDYDL------LILGTPTWA-GELPDDWEDFLEEL--- 69

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27369650  80 tlpTDYFAHLQYGLLGLGDSEytYFCNGGKVIDKRLQELGAQR----FYDTGHADDCVGLELVVEPWIDGL 146
Cdd:COG0716  70 ---KEDLSGKKVALFGTGDSS--GYGDALGELKELLEEKGAKVvggyDFEGSKAPDAEDTEERAEEWLKQL 135
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 436-662 2.79e-09

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: 58.35  E-value: 2.79e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 436 LSLLLEHLPKLQpRPYSCASsslrHPDKLHFVFNIVEFPpsttaaslrKGVCTGWLATLvapflQPntdvsnvdsGDala 515
Cdd:cd06195  33 LGLPNDDGKLVR-RAYSIAS----APYEENLEFYIILVP---------DGPLTPRLFKL-----KP---------GD--- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 516 pEIRISPRATNAFHLPEDPSAP-IIMVGPGTGVAPFVGFLQHREKLQeqhpdgKFGAMWLFFGCRHKDrDYLFREELRHF 594
Cdd:cd06195  82 -TIYVGKKPTGFLTLDEVPPGKrLWLLATGTGIAPFLSMLRDLEIWE------RFDKIVLVHGVRYAE-ELAYQDEIEAL 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27369650 595 LKtgvLTHLKVSF----SRDAAPDGEEA--PAKYVQDNLQRHsqqVARTLLQENGYVYVCGDaKNMAKDVNDTL 662
Cdd:cd06195 154 AK---QYNGKFRYvpivSREKENGALTGriPDLIESGELEEH---AGLPLDPETSHVMLCGN-PQMIDDTQELL 220
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 448-651 6.61e-09

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: 56.89  E-value: 6.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 448 PRPYSCASsslrHPDKLHF-VFNIVEFPPsttaaslrkGVCTGWLATLVAPflqpntdvsnvdsGDALapeiRISPRATN 526
Cdd:cd06194  39 ARSYSPTS----LPDGDNElEFHIRRKPN---------GAFSGWLGEEARP-------------GHAL----RLQGPFGQ 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 527 AFHLPEDPSAPIIMVGPGTGVAPFVGFLqhREKLQEQHPdgkfGAMWLFFGCRHKDRDYLfREELRHF-LKTGVLTHLKV 605
Cdd:cd06194  89 AFYRPEYGEGPLLLVGAGTGLAPLWGIA--RAALRQGHQ----GEIRLVHGARDPDDLYL-HPALLWLaREHPNFRYIPC 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 27369650 606 SfSRDAAPDGEEAPAKYVQDNLQRHSQQVartllqengyVYVCGDA 651
Cdd:cd06194 162 V-SEGSQGDPRVRAGRIAAHLPPLTRDDV----------VYLCGAP 196
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 526-674 2.23e-06

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 49.48  E-value: 2.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 526 NAFHLPEDPSaPIIMVGPGTGVAPFVGFLQHrekLQEQHPDgkfgaMWLFFGCRHKDrDYLFREELRHflktgvLTHLKV 605
Cdd:COG0543  88 NGFPLEDSGR-PVLLVAGGTGLAPLRSLAEA---LLARGRR-----VTLYLGARTPE-DLYLLDELEA------LADFRV 151

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27369650 606 SFSRDAAPDGEEApakYVQDNLQRHSQqvartlLQENGYVYVCGdAKNMAKDVNDTLIgiisnEAGVDK 674
Cdd:COG0543 152 VVTTDDGWYGRKG---FVTDALKELLA------EDSGDDVYACG-PPPMMKAVAELLL-----ERGVPP 205
PRK05723 PRK05723
flavodoxin; Provisional
 53-151 3.09e-06

flavodoxin; Provisional


Pssm-ID: 168208  Cd Length: 151  Bit Score: 47.48  E-value: 3.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650   53 LVMVVSTTGTGDPPDTARKFVKEIHNkTLPTDYFAhLQYGLLGLGDSEY-TYFCNGGKVIDKRLQELGAQRFYDTGHAD- 130
Cdd:PRK05723  51 LLAVTSTTGMGELPDNLMPLYSAIRD-QLPAAWRG-LPGAVIALGDSSYgDTFCGGGEQMRELFAELGVREVQPMLRLDa 128

                         90       100
                 ....*....|....*....|..
gi 27369650  131 -DCVGLELVVEPWIDGLWAALT 151
Cdd:PRK05723 129 sETVTPETDAEPWLAEFAAALK 150
PRK09267 PRK09267
flavodoxin FldA; Validated
 1-120 4.98e-06

flavodoxin FldA; Validated


Pssm-ID: 236439 [Multi-domain]  Cd Length: 169  Bit Score: 47.13  E-value: 4.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650    1 MRRFLLLYATQRGQAKAIAEEISEQAVSHgfSADLHCISES-----EKYDLktetgpLVMVVSTTGTGDPPDTARKFVKE 75
Cdd:PRK09267   1 MAKIGIFFGSDTGNTEDIAKMIQKKLGKD--VADVVDIAKAskedfEAYDL------LILGIPTWGYGELQCDWDDFLPE 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 27369650   76 ihnktLPTDYFAHLQYGLLGLGDSE-YT-YFCNGGKVIDKRLQELGA 120
Cdd:PRK09267  73 -----LEEIDFSGKKVALFGLGDQEdYAeYFCDAMGTLYDIVEPRGA 114
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 449-649 6.87e-06

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: 47.97  E-value: 6.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 449 RPYSCASSSlrHPDKLHFVFNIVEfppsttaaslrKGVCTGWLATLVAPflqpntdvsnvdsGDALAPEiriSPRAtnAF 528
Cdd:cd06209  48 RSYSFSSAP--GDPRLEFLIRLLP-----------GGAMSSYLRDRAQP-------------GDRLTLT---GPLG--SF 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 529 HLpEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgkfgaMWLFFGCRHK------DRDYLFREELRHFlktgvlth 602
Cdd:cd06209  97 YL-REVKRPLLMLAGGTGLAPFLSMLDVLAEDGSAHP------VHLVYGVTRDadlvelDRLEALAERLPGF-------- 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 27369650 603 lkvSFSRDAAPDGEEAPAK-YVQDNLQrhsqqvARTLLQENGYVYVCG 649
Cdd:cd06209 162 ---SFRTVVADPDSWHPRKgYVTDHLE------AEDLNDGDVDVYLCG 200
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 526-649 7.89e-06

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


Pssm-ID: 99817 [Multi-domain]  Cd Length: 253  Bit Score: 47.99  E-value: 7.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 526 NAFHLPEDPSAPIIMVGPGTGVAPFVG----FLQHREklqeqhpdgKFGAMWLFFGCRHKDrDYLFREELRHFLKtgvLT 601
Cdd:cd06221  89 NGFPVEEMKGKDLLLVAGGLGLAPLRSlinyILDNRE---------DYGKVTLLYGARTPE-DLLFKEELKEWAK---RS 155

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 27369650 602 HLKVSFSRDAAPDGEEAPAKYVQDNLQRHSQQVARTllqengYVYVCG 649
Cdd:cd06221 156 DVEVILTVDRAEEGWTGNVGLVTDLLPELTLDPDNT------VAIVCG 197
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 500-674 9.25e-06

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


Pssm-ID: 99781  Cd Length: 247  Bit Score: 47.55  E-value: 9.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 500 QPNTDVSN-----VDSGDalapEIRISPRATNaFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgkfgaMWL 574
Cdd:cd06184  78 EPGGLVSNylhdnVKVGD----VLEVSAPAGD-FVLDEASDRPLVLISAGVGITPMLSMLEALAAEGPGRP------VTF 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 575 FFGCRHKDrDYLFREELRHFLKTGVLTHLKVSFSRDAAPDGEEAPAKYVQDNLQRhsqqVARTLLQENGYVYVCGDAKNM 654
Cdd:cd06184 147 IHAARNSA-VHAFRDELEELAARLPNLKLHVFYSEPEAGDREEDYDHAGRIDLAL----LRELLLPADADFYLCGPVPFM 221

                       170       180
                ....*....|....*....|
gi 27369650 655 aKDVNDTLIgiisnEAGVDK 674
Cdd:cd06184 222 -QAVREGLK-----ALGVPA 235
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 511-649 2.53e-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: 46.10  E-value: 2.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 511 GD---ALAPEIRISPRAT-----NAFHLPeDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHP-DgkfgamwLFFGCRhK 581
Cdd:cd06198  64 GDytrRLAERLKPGTRVTvegpyGRFTFD-DRRARQIWIAGGIGITPFLALLEALAARGDARPvT-------LFYCVR-D 134

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27369650 582 DRDYLFREELRHfLKTGVLTHLKVSFSRDAAPDGEEAPAKYVQDNLQRHSqqvartllqengyVYVCG 649
Cdd:cd06198 135 PEDAVFLDELRA-LAAAAGVVLHVIDSPSDGRLTLEQLVRALVPDLADAD-------------VWFCG 188
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 526-663 3.67e-05

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 46.34  E-value: 3.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  526 NAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHreklqEQHPDGKFGAMWLFFGCRHKdRDYLFREELRHFLKTGVLTHLKV 605
Cdd:PRK08345  99 NGFPVDEMEGMDLLLIAGGLGMAPLRSVLLY-----AMDNRWKYGNITLIYGAKYY-EDLLFYDELIKDLAEAENVKIIQ 172

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27369650  606 SFSRDA-APDGEEAPAKYVqdnlQRHSQQVARTLLQE------NGYVYVCGDAKnMAKDVNDTLI 663
Cdd:PRK08345 173 SVTRDPeWPGCHGLPQGFI----ERVCKGVVTDLFREantdpkNTYAAICGPPV-MYKFVFKELI 232
Flavodoxin_5 pfam12724
Flavodoxin domain; This is a family of flavodoxins. Flavodoxins are electron transfer proteins ...
 5-103 4.43e-05

Flavodoxin domain; This is a family of flavodoxins. Flavodoxins are electron transfer proteins that carry a molecule of non-covalently bound FMN.


Pssm-ID: 463681 [Multi-domain]  Cd Length: 144  Bit Score: 43.79  E-value: 4.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650     5 LLLYATQRGQAKAIAEEISEQAVSHGFSADLHCISESEK---YDlktetgpLVMVVSTTGTGDPPDTARKFVKEiHNKTL 81
Cdd:pfam12724   1 LILYSSRDGQTKKIAERIAEELREEGELVDVEDVEAGEDlssYD-------AVVIGASIYYGKHLPELRQFVTK-HRDEL 72

                          90       100
                  ....*....|....*....|..
gi 27369650    82 PTDYFAHLQYGLLGLGDSEYTY 103
Cdd:pfam12724  73 SSKPVAFFSVNLTARKPEKNPY 94
PRK06703 PRK06703
flavodoxin; Provisional
 1-126 4.73e-05

flavodoxin; Provisional


Pssm-ID: 235854 [Multi-domain]  Cd Length: 151  Bit Score: 43.98  E-value: 4.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650    1 MRRFLLLYATQRGQAKAIAEEISEQAVSHGFSADLHCISESEKYDLKTETGplVMVVSTT-GTGDPPDTARKFVKEIHNK 79
Cdd:PRK06703   1 MAKILIAYASMSGNTEDIADLIKVSLDAFDHEVVLQEMDGMDAEELLAYDG--IILGSYTwGDGDLPYEAEDFHEDLENI 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 27369650   80 TLptdyfAHLQYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDT 126
Cdd:PRK06703  79 DL-----SGKKVAVFGSGDTAYPLFCEAVTIFEERLVERGAELVQEG 120
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 449-673 8.87e-05

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: 44.56  E-value: 8.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 449 RPYSCASSslrhPDKLHFVfnivefppSTTAASLRKGVCTGWLATLVAPflqpntdvsnvdsGDALapEIRiSPRATnaF 528
Cdd:cd06217  51 RSYSIASS----PTQRGRV--------ELTVKRVPGGEVSPYLHDEVKV-------------GDLL--EVR-GPIGT--F 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 529 HLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgkfgaMWLFFGCRHKDrDYLFREELRHF-LKTGVLtHLKVSF 607
Cdd:cd06217 101 TWNPLHGDPVVLLAGGSGIVPLMSMIRYRRDLGWPVP------FRLLYSARTAE-DVIFRDELEQLaRRHPNL-HVTEAL 172

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27369650 608 SRDAAPDGEEAPAKYVQDNLQRHSQQVARTLlqengyVYVCGDAkNMAKDVNDTLIgiisnEAGVD 673
Cdd:cd06217 173 TRAAPADWLGPAGRITADLIAELVPPLAGRR------VYVCGPP-AFVEAATRLLL-----ELGVP 226
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 538-649 1.09e-03

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


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 41.01  E-value: 1.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 538 IIMVGPGTGVAPFVGFLQHRekLQEQHPDGKfgaMWLFFGCRHKDrDYLFREELRHFLKTGVlTHLKVSFSRDAAPDGEE 617
Cdd:cd06183 107 IGMIAGGTGITPMLQLIRAI--LKDPEDKTK---ISLLYANRTEE-DILLREELDELAKKHP-DRFKVHYVLSRPPEGWK 179

                        90       100       110
                ....*....|....*....|....*....|...
gi 27369650 618 APAKYV-QDNLQRHSQQVARtllqENGYVYVCG 649
Cdd:cd06183 180 GGVGFItKEMIKEHLPPPPS----EDTLVLVCG 208
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 528-649 1.95e-03

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 41.01  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650  528 FHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgkfgaMWLFFGCRHKDRDYL------FREELRHFLKTGVLT 601
Cdd:PRK07609 197 FFLREDSDKPIVLLASGTGFAPIKSIVEHLRAKGIQRP------VTLYWGARRPEDLYLsalaeqWAEELPNFRYVPVVS 270

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 27369650  602 hlkvsfsrDAAPDgeeapakyvqDNLQRHSQQVARTLLQE----NGY-VYVCG 649
Cdd:PRK07609 271 --------DALDD----------DAWTGRTGFVHQAVLEDfpdlSGHqVYACG 305
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 532-672 2.10e-03

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: 40.30  E-value: 2.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 532 EDPSAPIIMVGPGT------GVAPFVGFLQHREKlqeqhpDGKFGAMWLFFGCRhKDRDYLFREELRHFLKTG---VLTH 602
Cdd:cd06196  90 EDPWGAIEYKGPGVfiaggaGITPFIAILRDLAA------KGKLEGNTLIFANK-TEKDIILKDELEKMLGLKfinVVTD 162

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 603 LKVSFSRDAAPDGEeapakYVQDNLQRHSQQvartllqengyVYVCGDAKnMAKDVNDTLIGIISNEAGV 672
Cdd:cd06196 163 EKDPGYAHGRIDKA-----FLKQHVTDFNQH-----------FYVCGPPP-MEEAINGALKELGVPEDSI 215
HemG COG4635
Protoporphyrinogen IX oxidase, menaquinone-dependent (flavodoxin domain) [Coenzyme transport ...
 3-46 2.86e-03

Protoporphyrinogen IX oxidase, menaquinone-dependent (flavodoxin domain) [Coenzyme transport and metabolism];


Pssm-ID: 443673  Cd Length: 179  Bit Score: 39.11  E-value: 2.86e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 27369650   3 RFLLLYATQRGQAKAIAEEISEQAVSHGFSADLHCISESEKYDL 46
Cdd:COG4635   2 KVLILYASRDGQTRKIAERIAEVLREAGHDVDLVDLEDAPDLDL 45
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 528-663 3.85e-03

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: 39.45  E-value: 3.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 528 FHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgkfgaMWLFFGCRHKDRDYL------FREELRHFLKTGVLT 601
Cdd:cd06189  91 FFLREDSDRPLILIAGGTGFAPIKSILEHLLAQGSKRP------IHLYWGARTEEDLYLdelleaWAEAHPNFTYVPVLS 164

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27369650 602 HLkvsfsrDAAPDGEEApakYVQdnlqrhsQQVARTLLQENGY-VYVCGDAkNMAKDVNDTLI 663
Cdd:cd06189 165 EP------EEGWQGRTG---LVH-------EAVLEDFPDLSDFdVYACGSP-EMVYAARDDFV 210
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 528-663 8.84e-03

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


Pssm-ID: 99784 [Multi-domain]  Cd Length: 224  Bit Score: 38.34  E-value: 8.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369650 528 FHLPEDPSAPIIMVGPGTGVAPFV----GFLQHREKlQEQHpdgkfgamwLFFGCRHK----DRDYLFREELRH--FLKT 597
Cdd:cd06187  91 FYLRRDHDRPVLCIAGGTGLAPLRaiveDALRRGEP-RPVH---------LFFGARTErdlyDLEGLLALAARHpwLRVV 160

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27369650 598 GVLTHlkvsfsrdaAPDGEEAPAKYVQDnlqrhsqQVARTLLQENGY-VYVCGDAKnMAKDVNDTLI 663
Cdd:cd06187 161 PVVSH---------EEGAWTGRRGLVTD-------VVGRDGPDWADHdIYICGPPA-MVDATVDALL 210
 
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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