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Conserved domains on  [gi|568983212|ref|XP_006517245|]
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methionine synthase reductase isoform X1 [Mus musculus]

Protein Classification

Flavodoxin_1 and methionine_synthase_red domain-containing protein( domain architecture ID 10446937)

Flavodoxin_1 and methionine_synthase_red domain-containing protein

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 568983212 275 PISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHRVILKIKTDTKKKGAAL 354
Cdd:cd06203    1 PISSAKKLTEGDDVKTVVDLTLDLSPTGFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVPNTKKKNAKV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 355 PAHVPEGRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPSCQP 434
Cdd:cd06203   81 PVHIPKVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDFVRKRGLSLLDLLEAFPSCRP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 435 PLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPPsttaaslrKGVCTGWLATLVApflqpntdvsnvdSGDAL 514
Cdd:cd06203  161 PLSLLIEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPA--------KGLCTSWLESLCL-------------SASSH 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 515 APEIRISPRATNAFHLPED-PSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPDGKFGAMWLFFGCRHKDRDYLFREELRH 593
Cdd:cd06203  220 GVKVPFYLRSSSRFRLPPDdLRRPIIMVGPGTGVAPFLGFLQHREKLKESHTETVFGEAWLFFGCRHRDRDYLFRDELEE 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 594 FLKTGVLTHLKVSFSRDAapdGEEAPAKYVQDNLQRHSQQVARTLLQENGYVYVCGDAKNMAKDVNDTLIGIISNEAGVD 673
Cdd:cd06203  300 FLEEGILTRLIVAFSRDE---NDGSTPKYVQDKLEERGKKLVDLLLNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGLD 376
                        410       420
                 ....*....|....*....|..
gi 568983212 674 KLEAMKTLATLKQEKRYLQDIW 695
Cdd:cd06203  377 KLEAKKLLARLRKEDRYLEDVW 398
Flavodoxin_1 pfam00258
Flavodoxin;
6-142 1.66e-33

Flavodoxin;


:

Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 125.17  E-value: 1.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212    6 LLYATQRGQAKAIAEEISEQAVSHGFSADLHCISE-SEKYDLKTETGPLVMVVSTTGTGDPPDTARKFVKEIHNKTLPTD 84
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDDvDETLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGTLED 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568983212   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 568983212 275 PISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHRVILKIKTDTKKKGAAL 354
Cdd:cd06203    1 PISSAKKLTEGDDVKTVVDLTLDLSPTGFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVPNTKKKNAKV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 355 PAHVPEGRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPSCQP 434
Cdd:cd06203   81 PVHIPKVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDFVRKRGLSLLDLLEAFPSCRP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 435 PLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPPsttaaslrKGVCTGWLATLVApflqpntdvsnvdSGDAL 514
Cdd:cd06203  161 PLSLLIEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPA--------KGLCTSWLESLCL-------------SASSH 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 515 APEIRISPRATNAFHLPED-PSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPDGKFGAMWLFFGCRHKDRDYLFREELRH 593
Cdd:cd06203  220 GVKVPFYLRSSSRFRLPPDdLRRPIIMVGPGTGVAPFLGFLQHREKLKESHTETVFGEAWLFFGCRHRDRDYLFRDELEE 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 594 FLKTGVLTHLKVSFSRDAapdGEEAPAKYVQDNLQRHSQQVARTLLQENGYVYVCGDAKNMAKDVNDTLIGIISNEAGVD 673
Cdd:cd06203  300 FLEEGILTRLIVAFSRDE---NDGSTPKYVQDKLEERGKKLVDLLLNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGLD 376
                        410       420
                 ....*....|....*....|..
gi 568983212 674 KLEAMKTLATLKQEKRYLQDIW 695
Cdd:cd06203  377 KLEAKKLLARLRKEDRYLEDVW 398
CysJ COG0369
Sulfite reductase, alpha subunit (flavoprotein) [Inorganic ion transport and metabolism];
5-695 7.26e-124

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


Pssm-ID: 223446 [Multi-domain]  Cd Length: 587  Bit Score: 381.00  E-value: 7.26e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212   5 LLLYATQRGQAKAIAEEISEQAVSHGFSADLHCISESEKYDLKTETGpLVMVVSTTGTGDPPDTARKFVKEIHNKTLPTd 84
Cdd:COG0369   51 TVLYGSQTGNAEGLAEELAKELEAAGLQVLVASLDDYKPKDIAEERL-LLFVVSTQGEGEPPDNAVAFHEFLKGKKAPK- 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212  85 yFAHLQYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDTGHADDcVGLELVVEPWIDGLWAALtkhFKSLGGQENms 164
Cdd:COG0369  129 -LDGLRYAVLGLGDSSYEFFCQAGKDFDRRLQELGATRLFPRVEADV-QDFEAAAAPWRDDVLELL---KSKFPGQEA-- 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 165 dtlsrasdaplstamkpellhiqsqvellrledmgerdselreqnetnrgqqgriedfdsslvHSVPPLSQSSLSIPAVP 244
Cdd:COG0369  202 ---------------------------------------------------------------APAQVATSPQSESPYSK 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 245 PEYLEVHLQEslgqeeNQasvpsgdpsfqvpiskaiRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEE 324
Cdd:COG0369  219 PAPSVAILLE------NR------------------KLTGRDSDKDVRHIELDLPDSGLRYEPGDALGVWPENDPELVDE 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 325 LLQRLQLadkrahrvilkiktdtkkKGAALPAHVPEGRSLQFILTWCLEIrAVPKKAFLRALAEHTSSATEKRRLQELCs 404
Cdd:COG0369  275 FLELLGL------------------DPEEPVTVDGETLPLVEALKSHFEF-TSAPKSLLENLAHFAGQEELRRLLEQLD- 334
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 405 kqgAADYNRFIRdaSVCLLDLLLTFPSCQPPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPpstTAASLRK 484
Cdd:COG0369  335 ---IADLQDYAK--RRTLIDVLRDFPPAKLPAEELIDLLPPLKPRLYSIASSPGVSPDEVHLTVGVVRYQ---AEGRERY 406
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 485 GVCTGWLATLVAPflqpntdvsnvdsGDalapEIRISPRATNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQh 564
Cdd:COG0369  407 GVCSGYLADLLEE-------------GD----TIPVFVQPNKNFRLPEDPETPIIMIGPGTGIAPFRAFVQERAANGAE- 468
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 565 pdgkfGAMWLFFGCRHKDRDYLFREELRHFLKTGVLTHLKVSFSRDaapdgeEAPAKYVQDNLQRHSQQVaRTLLQENGY 644
Cdd:COG0369  469 -----GKNWLFFGCRHFTEDFLYQEEWEEYLKDGVLTRLDLAFSRD------QEEKIYVQDRLREQADEL-WEWLEEGAH 536
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568983212 645 VYVCGDAKNMAKDVNDTLIGIISNEAGVDKLEAMKTLATLKQEKRYLQDIW 695
Cdd:COG0369  537 IYVCGDAKGMAKDVEEALLDILAKEGGLSREEAEEYLKELKKEGRYQRDVY 587
PRK06214 PRK06214
sulfite reductase subunit alpha;
281-695 4.86e-66

sulfite reductase subunit alpha;


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 226.88  E-value: 4.86e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 281 RLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQladKRAHRVIlkiktdtkkkgaalpahvpE 360
Cdd:PRK06214 178 RLNKPGSEKETWHVEIDLAGSGLDYEVGDSLGLFPANDPALVDAVIAALG---APPEFPI-------------------G 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 361 GRSLQFILTWCLEIRAVPKKAFLRaLAEHTSSATEK--RRLQELCSKQGAAdynrfirdASVCLLDLLLTFPSCQPPLSL 438
Cdd:PRK06214 236 GKTLREALLEDVSLGPAPDGLFEL-LSYITGGAARKkaRALAAGEDPDGDA--------ATLDVLAALEKFPGIRPDPEA 306
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 439 LLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFppsTTAASLRKGVCTGWLATLVAP------FLQPNtdvsnvdsgd 512
Cdd:PRK06214 307 FVEALDPLQPRLYSISSSPKATPGRVSLTVDAVRY---EIGSRLRLGVASTFLGERLAPgtrvrvYVQKA---------- 373
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 513 alapeirispratNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQhpdgkfGAMWLFFGCRHKDRDYLFREELR 592
Cdd:PRK06214 374 -------------HGFALPADPNTPIIMVGPGTGIAPFRAFLHERAATKAP------GRNWLFFGHQRSATDFFYEDELN 434
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 593 HFLKTGVLTHLKVSFSRDaapdGEEApaKYVQDNLQrhsqQVARTL---LQENGYVYVCGDAKNMAKDVNDTLIGIISNE 669
Cdd:PRK06214 435 GLKAAGVLTRLSLAWSRD----GEEK--TYVQDRMR----ENGAELwkwLEEGAHFYVCGDAKRMAKDVERALVDIVAQF 504
                        410       420
                 ....*....|....*....|....*.
gi 568983212 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 1.54e-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  Cd Length: 219  Bit Score: 169.83  E-value: 1.54e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212  272 FQVPISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHRVILKIKTDTKKkg 351
Cdd:pfam00667   8 FTAPVLSNRELTSPSSDRNCIHVELDISGSGLTYQTGDHLGVYPPNNEELVEELLERLGLDPKPDTVVLLKTLDERVK-- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212  352 aalpAHVPEGRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPS 431
Cdd:pfam00667  86 ----PPRLPPTTYRQALKYYLDITGPPSKQLLRLLAQFAPEEEEKQRLEFLSSDAGAREYKRWKLNHAPTLLEVLEEFPS 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568983212  432 CQPPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFpPSTTAASLRKGVCTGW 490
Cdd:pfam00667 162 VKLPADFLLTQLPQLQPRYYSISSSSKVHPNEVHLTVVVVEY-ETDGEGRIHYGVCSNW 219
Flavodoxin_1 pfam00258
Flavodoxin;
6-142 1.66e-33

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 125.17  E-value: 1.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212    6 LLYATQRGQAKAIAEEISEQAVSHGFSADLHCISE-SEKYDLKTETGPLVMVVSTTGTGDPPDTARKFVKEIHNKTLPTD 84
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDDvDETLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGTLED 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568983212   85 -YFAHLQYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDTGHADDC---VGLELVVEPW 142
Cdd:pfam00258  81 gDLSGLKYAVFGLGDSGYEGFCGAAKKLDEKLSELGASRVGPLGEGDEDpqeDGLEEAFEAW 142
PRK08105 PRK08105
flavodoxin; Provisional
1-150 2.19e-18

flavodoxin; Provisional


Pssm-ID: 181230 [Multi-domain]  Cd Length: 149  Bit Score: 82.24  E-value: 2.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212   1 MRRFLLLYATQRGQAKAIAEEISEQAVSHGFSADL---HCISESEKYDLKTetgpLVMVVSTTGTGDPPDTARKFVKEIh 77
Cdd:PRK08105   1 MAKVGIFVGTVYGNALLVAEEAEAILTAQGHEVTLfedPELSDWQPYQDEL----VLVVTSTTGQGDLPDSIVPLFQAL- 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568983212  78 NKTLPtdYFAHLQYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDTGHADDCVGLELVVE--PWIDGlWAAL 150
Cdd:PRK08105  76 KDTAG--YQPNLRYGVIALGDSSYDNFCGAGKQFDALLQEQGAKRVGERLEIDACETPEPEVEanPWVEQ-WGTL 147
FldA COG0716
Flavodoxin [Energy production and conversion];
1-150 1.68e-13

Flavodoxin [Energy production and conversion];


Pssm-ID: 223788 [Multi-domain]  Cd Length: 151  Bit Score: 68.56  E-value: 1.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212   1 MRRFLLLYATQRGQAKAIAEEISEQAVSHGFSADLHcISESEKYDLKTETGPLVMVVSTTGTGDPPDTARKFVKEIHNKT 80
Cdd:COG0716    1 MMKILIVYGSRTGNTEKVAEIIAEELGADGFEVDID-IRPGIKDDLLESYDELLLGTPTWGAGELPDDWYDFIEELEPID 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568983212  81 LPTdyfahLQYGLLGLGDSEY-TYFCNGGKVIDKRLQELGAQ--------RFYDTGHADDcvGLELVVEPWIDGLWAAL 150
Cdd:COG0716   80 FKG-----KLVAVFGLGDQSYyGYFCEAGGNFEDILEEKGAKavgiletlGYIFDASPNE--EDEKRIKEWVKQILNEL 151
 
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 568983212 275 PISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHRVILKIKTDTKKKGAAL 354
Cdd:cd06203    1 PISSAKKLTEGDDVKTVVDLTLDLSPTGFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVPNTKKKNAKV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 355 PAHVPEGRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPSCQP 434
Cdd:cd06203   81 PVHIPKVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDFVRKRGLSLLDLLEAFPSCRP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 435 PLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPPsttaaslrKGVCTGWLATLVApflqpntdvsnvdSGDAL 514
Cdd:cd06203  161 PLSLLIEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPA--------KGLCTSWLESLCL-------------SASSH 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 515 APEIRISPRATNAFHLPED-PSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPDGKFGAMWLFFGCRHKDRDYLFREELRH 593
Cdd:cd06203  220 GVKVPFYLRSSSRFRLPPDdLRRPIIMVGPGTGVAPFLGFLQHREKLKESHTETVFGEAWLFFGCRHRDRDYLFRDELEE 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 594 FLKTGVLTHLKVSFSRDAapdGEEAPAKYVQDNLQRHSQQVARTLLQENGYVYVCGDAKNMAKDVNDTLIGIISNEAGVD 673
Cdd:cd06203  300 FLEEGILTRLIVAFSRDE---NDGSTPKYVQDKLEERGKKLVDLLLNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGLD 376
                        410       420
                 ....*....|....*....|..
gi 568983212 674 KLEAMKTLATLKQEKRYLQDIW 695
Cdd:cd06203  377 KLEAKKLLARLRKEDRYLEDVW 398
CysJ COG0369
Sulfite reductase, alpha subunit (flavoprotein) [Inorganic ion transport and metabolism];
5-695 7.26e-124

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


Pssm-ID: 223446 [Multi-domain]  Cd Length: 587  Bit Score: 381.00  E-value: 7.26e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212   5 LLLYATQRGQAKAIAEEISEQAVSHGFSADLHCISESEKYDLKTETGpLVMVVSTTGTGDPPDTARKFVKEIHNKTLPTd 84
Cdd:COG0369   51 TVLYGSQTGNAEGLAEELAKELEAAGLQVLVASLDDYKPKDIAEERL-LLFVVSTQGEGEPPDNAVAFHEFLKGKKAPK- 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212  85 yFAHLQYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDTGHADDcVGLELVVEPWIDGLWAALtkhFKSLGGQENms 164
Cdd:COG0369  129 -LDGLRYAVLGLGDSSYEFFCQAGKDFDRRLQELGATRLFPRVEADV-QDFEAAAAPWRDDVLELL---KSKFPGQEA-- 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 165 dtlsrasdaplstamkpellhiqsqvellrledmgerdselreqnetnrgqqgriedfdsslvHSVPPLSQSSLSIPAVP 244
Cdd:COG0369  202 ---------------------------------------------------------------APAQVATSPQSESPYSK 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 245 PEYLEVHLQEslgqeeNQasvpsgdpsfqvpiskaiRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEE 324
Cdd:COG0369  219 PAPSVAILLE------NR------------------KLTGRDSDKDVRHIELDLPDSGLRYEPGDALGVWPENDPELVDE 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 325 LLQRLQLadkrahrvilkiktdtkkKGAALPAHVPEGRSLQFILTWCLEIrAVPKKAFLRALAEHTSSATEKRRLQELCs 404
Cdd:COG0369  275 FLELLGL------------------DPEEPVTVDGETLPLVEALKSHFEF-TSAPKSLLENLAHFAGQEELRRLLEQLD- 334
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 405 kqgAADYNRFIRdaSVCLLDLLLTFPSCQPPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPpstTAASLRK 484
Cdd:COG0369  335 ---IADLQDYAK--RRTLIDVLRDFPPAKLPAEELIDLLPPLKPRLYSIASSPGVSPDEVHLTVGVVRYQ---AEGRERY 406
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 485 GVCTGWLATLVAPflqpntdvsnvdsGDalapEIRISPRATNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQh 564
Cdd:COG0369  407 GVCSGYLADLLEE-------------GD----TIPVFVQPNKNFRLPEDPETPIIMIGPGTGIAPFRAFVQERAANGAE- 468
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 565 pdgkfGAMWLFFGCRHKDRDYLFREELRHFLKTGVLTHLKVSFSRDaapdgeEAPAKYVQDNLQRHSQQVaRTLLQENGY 644
Cdd:COG0369  469 -----GKNWLFFGCRHFTEDFLYQEEWEEYLKDGVLTRLDLAFSRD------QEEKIYVQDRLREQADEL-WEWLEEGAH 536
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568983212 645 VYVCGDAKNMAKDVNDTLIGIISNEAGVDKLEAMKTLATLKQEKRYLQDIW 695
Cdd:COG0369  537 IYVCGDAKGMAKDVEEALLDILAKEGGLSREEAEEYLKELKKEGRYQRDVY 587
CYPOR cd06204
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
272-695 1.35e-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: 1.35e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 272 FQVPISKAIRLTTNdAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADkraHRVILKIKTDTKKKG 351
Cdd:cd06204    6 FLAPVAVSRELFTG-SDRSCLHIEFDISGSGIRYQTGDHLAVWPTNPSEEVERLLKVLGLDD---RDTVISLKSLDEPAS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 352 AALPahVPEGRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSkQGAADYNRFIRDASVCLLDLLLTFPS 431
Cdd:cd06204   82 KKVP--FPCPTTYRTALRHYLDITAPVSRQVLAALAQFAPDPEEKERLLKLAS-EGKDEYAKWIVEPHRNLLEVLQDFPS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 432 CQ---PPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPpsTTAASLRKGVCTGWLATLVAPFLQPNTDVSNV 508
Cdd:cd06204  159 AKptpPPFDFLIELLPRLQPRYYSISSSSKVHPNRIHITAVVVKYP--TPTGRIIKGVATNWLLALKPALNGEKPPTPYY 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 509 DSGDALAPEIRISP---RATNaFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgKFGAMWLFFGCRHKDRDY 585
Cdd:cd06204  237 LSGPRKKGGGSKVPvfvRRSN-FRLPTKPSTPVIMIGPGTGVAPFRGFIQERAALKESGK--KVGPTLLFFGCRHPDEDF 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 586 LFREELRHFLKTGVLTHLKVSFSRdaapdgEEAPAKYVQDNLQRHSQQVARtLLQENGYVYVCGDAKNMAKDVNDTLIGI 665
Cdd:cd06204  314 IYKDELEEYAKLGGLLELVTAFSR------EQPKKVYVQHRLAEHAEQVWE-LINEGAYIYVCGDAKNMARDVEKTLLEI 386
                        410       420       430
                 ....*....|....*....|....*....|
gi 568983212 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 6.15e-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: 6.15e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 281 RLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHRVILKIKTDTKKkgaalpaHVPE 360
Cdd:cd06207    7 RLTPADYDRSTRHIEFDLGGSGLSYETGDNLGIYPENSDALVDEFLARLGLDGDDVVRVEPNEQQRGKP-------PFPE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 361 GRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSKQGAADYNRFIRdasVCLLDLLLTFPSCQPPLSLLL 440
Cdd:cd06207   80 PISVRQLLKKFLDIFGKPTKKFLKLLSQLATDEEEKEDLYKLASREGRTEYKRYEK---YTYLEVLKDFPSVRPTLEQLL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 441 EHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFppSTTAASLRKGVCTGWLAtlvapflqpntdvsNVDSGDALAPEIRI 520
Cdd:cd06207  157 ELCPLIKPRYYSISSSPLKNPNEVHLLVSLVSW--KTPSGRSRYGLCSSYLA--------------GLKVGQRVTVFIKK 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 521 SpratnAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgKFGAMWLFFGCRHKDRDYLFREELRHFLKTGVL 600
Cdd:cd06207  221 S-----SFKLPKDPKKPIIMVGPGTGLAPFRAFLQERAALLAQGP--EIGPVLLYFGCRHEDKDYLYKEELEEYEKSGVL 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 601 THLKVSFSRDaapdgeEAPAKYVQDNLQRHSQQVARTLLQENGYVYVCGDAKNMAKDVNDTLIGIISNEAGVDKLEAMKT 680
Cdd:cd06207  294 TTLGTAFSRD------QPKKVYVQDLIRENSDLVYQLLEEGAGVIYVCGSTWKMPPDVQEAFEEILKKHGGGDEELAEKK 367
                        410
                 ....*....|....*
gi 568983212 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 1.15e-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: 1.15e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 423 LDLLLTFPSCQPPLSLLLEHLP-KLQPRPYSCASSSLRHPDKLHFVFNIVEFPpsTTAASLRKGVCTGWLATLVapflqp 501
Cdd:cd06182   22 FDLSGNSVLKYQPGDHLGVIPPnPLQPRYYSIASSPDVDPGEVHLCVRVVSYE--APAGRIRKGVCSNFLAGLQ------ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 502 ntdvsnvdsgdaLAPEIRISPRATNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQeqHPDGKFGAMWLFFGCRHK 581
Cdd:cd06182   94 ------------LGAKVTVFIRPAPSFRLPKDPTTPIIMVGPGTGIAPFRGFLQERAALR--ANGKARGPAWLFFGCRNF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 582 DRDYLFREELRHFLKTGVLTHLKVSFSRDAApdgeeAPAKYVQDNLQRHSQQVARtLLQENGYVYVCGDAKNMAKDVNDT 661
Cdd:cd06182  160 ASDYLYREELQEALKDGALTRLDVAFSREQA-----EPKVYVQDKLKEHAEELRR-LLNEGAHIYVCGDAKSMAKDVEDA 233
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568983212 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 4.64e-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: 4.64e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 276 ISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLAdkrahrvilkiktdtkkkGAALP 355
Cdd:cd06199    2 VLENRLLTGPGSEKETRHIELDLEGSGLSYEPGDALGVYPTNDPALVDELLAALGLS------------------GDEPV 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 356 AHVPEG-RSLQFILTWCLEIRAVpkkafLRALAEHTSSATEKRRLQELCSKQGAADYNRfirdasvcLLDLLLTFPSCQP 434
Cdd:cd06199   64 STVGGGtLPLREALIKHYEITTL-----LLALLESYAADTGALELLALAALEAVLAFAE--------LRDVLDLLPIPPA 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 435 PLSL--LLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFppsTTAASLRKGVCTGWLATLVAP------FLQPNtdvs 506
Cdd:cd06199  131 RLTAeeLLDLLRPLQPRLYSIASSPKAVPDEVHLTVAVVRY---ESHGRERKGVASTFLADRLKEgdtvpvFVQPN---- 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 507 nvdsgdalapeirispratNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLqeqhpdGKFGAMWLFFGCRHKDRDYL 586
Cdd:cd06199  204 -------------------PHFRLPEDPDAPIIMVGPGTGIAPFRAFLQEREAT------GAKGKNWLFFGERHFATDFL 258
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 587 FREELRHFLKTGVLTHLKVSFSRDaapdGEEapaK-YVQDNLQRHSQQVArTLLQENGYVYVCGDAKNMAKDVNDTLIGI 665
Cdd:cd06199  259 YQDELQQWLKDGVLTRLDTAFSRD----QAE---KvYVQDRMREQGAELW-AWLEEGAHFYVCGDAKRMAKDVDAALLDI 330
                        410       420       430
                 ....*....|....*....|....*....|
gi 568983212 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 1.11e-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: 1.11e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 281 RLTTNDAVKSTLLLELDISKI-EFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHrvILKIKTDTKKKGAALPAHV- 358
Cdd:cd06202    7 NLQSPKSSRSTILVKLDTNGAqELHYQPGDHVGIFPANRPELVDALLDRLHDAPPPDQ--VIKLEVLEERSTALGIIKTw 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 359 -PEGR----SLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCskQGAADYNRFIRDASVCLLDLLLTFPSCQ 433
Cdd:cd06202   85 tPHERlppcTLRQALTRYLDITTPPTPQLLQLLATLATDEKDKERLEVLG--KGSSEYEDWKWYKNPNILEVLEEFPSLQ 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 434 PPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPPSTTAASLRKGVCTGWLATLvapflqpntdvsnvDSGDA 513
Cdd:cd06202  163 VPASLLLTQLPLLQPRYYSISSSPDMYPGEIHLTVAVVSYRTRDGQGPVHHGVCSTWLNGL--------------TPGDT 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 514 LAPEIRISPratnAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHR--EKLQEQHPDGKFGAMWLFFGCRHKDRDYLFREEL 591
Cdd:cd06202  229 VPCFVRSAP----SFHLPEDPSVPVIMVGPGTGIAPFRSFWQQRqyDLRMSEDPGKKFGDMTLFFGCRNSTIDDIYKEET 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 592 RHFLKTGVLTHLKVSFSRDaaPDgeeAPAKYVQDNLQRHSQQVARTLLQENGYVYVCGDAkNMAKDVNDTLIGIISNEAG 671
Cdd:cd06202  305 EEAKNKGVLTEVYTALSRE--PG---KPKTYVQDLLKEQAESVYDALVREGGHIYVCGDV-TMAEDVSQTIQRILAEHGN 378
                        410       420
                 ....*....|....*....|...
gi 568983212 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 2.69e-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: 2.69e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 278 KAIRLTTNDAV-KSTLLLELDISKiEFSHQPGDSFNVTCPNSDREVEELLQRLQLAdkrahrvilkIKTDTKKKGAALPA 356
Cdd:cd06206    3 VENRELTAPGVgPSKRHLELRLPD-GMTYRAGDYLAVLPRNPPELVRRALRRFGLA----------WDTVLTISASGSAT 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 357 HVPEGRSLQF--ILTWCLEIRAVPKKAFLRALAEHTSsATEKRRLQELCSKQGaadYNRFIRDASVCLLDLLLTFPSCQP 434
Cdd:cd06206   72 GLPLGTPISVseLLSSYVELSQPATRRQLAALAEATR-CPDTKALLERLAGEA---YAAEVLAKRVSVLDLLERFPSIAL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 435 PLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPpSTTAASLRKGVCTGWLATLvapflQPntdvsnvdsGDal 514
Cdd:cd06206  148 PLATFLAMLPPMRPRQYSISSSPLVDPGHATLTVSVLDAP-ALSGQGRYRGVASSYLSSL-----RP---------GD-- 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 515 apEIRISPRATN-AFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQhpDGKFGAMWLFFGCRHKDRDYLFREELRH 593
Cdd:cd06206  211 --SIHVSVRPSHsAFRPPSDPSTPLIMIAAGTGLAPFRGFLQERAALLAQ--GRKLAPALLFFGCRHPDHDDLYRDELEE 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 594 FLKTGVLThLKVSFSRDAapdgeEAPAKYVQDNLQRHSQQVARtLLQENGYVYVCGDAKnMAKDVNDTLIGIISNE---- 669
Cdd:cd06206  287 WEAAGVVS-VRRAYSRPP-----GGGCRYVQDRLWAEREEVWE-LWEQGARVYVCGDGR-MAPGVREVLKRIYAEKderg 358
                        410       420
                 ....*....|....*....|....*.
gi 568983212 670 AGVDKLEAMKTLATLKQEKRYLQDIW 695
Cdd:cd06206  359 GGSDDEEAEEWLEELRNKGRYATDVF 384
PRK06214 PRK06214
sulfite reductase subunit alpha;
281-695 4.86e-66

sulfite reductase subunit alpha;


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 226.88  E-value: 4.86e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 281 RLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQladKRAHRVIlkiktdtkkkgaalpahvpE 360
Cdd:PRK06214 178 RLNKPGSEKETWHVEIDLAGSGLDYEVGDSLGLFPANDPALVDAVIAALG---APPEFPI-------------------G 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 361 GRSLQFILTWCLEIRAVPKKAFLRaLAEHTSSATEK--RRLQELCSKQGAAdynrfirdASVCLLDLLLTFPSCQPPLSL 438
Cdd:PRK06214 236 GKTLREALLEDVSLGPAPDGLFEL-LSYITGGAARKkaRALAAGEDPDGDA--------ATLDVLAALEKFPGIRPDPEA 306
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 439 LLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFppsTTAASLRKGVCTGWLATLVAP------FLQPNtdvsnvdsgd 512
Cdd:PRK06214 307 FVEALDPLQPRLYSISSSPKATPGRVSLTVDAVRY---EIGSRLRLGVASTFLGERLAPgtrvrvYVQKA---------- 373
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 513 alapeirispratNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQhpdgkfGAMWLFFGCRHKDRDYLFREELR 592
Cdd:PRK06214 374 -------------HGFALPADPNTPIIMVGPGTGIAPFRAFLHERAATKAP------GRNWLFFGHQRSATDFFYEDELN 434
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 593 HFLKTGVLTHLKVSFSRDaapdGEEApaKYVQDNLQrhsqQVARTL---LQENGYVYVCGDAKNMAKDVNDTLIGIISNE 669
Cdd:PRK06214 435 GLKAAGVLTRLSLAWSRD----GEEK--TYVQDRMR----ENGAELwkwLEEGAHFYVCGDAKRMAKDVERALVDIVAQF 504
                        410       420
                 ....*....|....*....|....*.
gi 568983212 670 AGVDKLEAMKTLATLKQEKRYLQDIW 695
Cdd:PRK06214 505 GGRSPDEAVAFVAELKKAGRYQADVY 530
cysJ PRK10953
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
6-695 9.10e-64

NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;


Pssm-ID: 182862 [Multi-domain]  Cd Length: 600  Bit Score: 222.67  E-value: 9.10e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212   6 LLYATQRGQAKAIAEEISEQAVSHGFSADLhciSESEKYDLK--TETGPLVMVVSTTGTGDPPDTARKFVKEIHNKTLPT 83
Cdd:PRK10953  66 LISASQTGNARRVAEQLRDDLLAAKLNVNL---VNAGDYKFKqiAQEKLLIVVTSTQGEGEPPEEAVALHKFLFSKKAPK 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212  84 dyFAHLQYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDTGHADdcVGLELVVEPWidglWAALTKHFKSlggqenm 163
Cdd:PRK10953 143 --LENTAFAVFGLGDTSYEFFCQAGKDFDSKLAELGAERLLDRVDAD--VEYQAAASEW----RARVVDALKS------- 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 164 sdtlsrasDAPLSTAmkpellhiQSQVellrledmgerdselreqnetnrGQQGRIEDFDSSLVHSVPPLSqSSLSIpav 243
Cdd:PRK10953 208 --------RAPAVAA--------PSQS-----------------------VATGAVNEIHTSPYSKEAPLT-ASLSV--- 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 244 ppeylevhlqeslgqeeNQasvpsgdpsfqvpiskaiRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVE 323
Cdd:PRK10953 245 -----------------NQ------------------KITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVK 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 324 ELLQRLQLadKRAHRVILKIKTdtkkkgaalpahVPEGRSLQfiltWCLEI-----RAVPKKAFLRALAEHTSSATEKRR 398
Cdd:PRK10953 290 ELVELLWL--KGDEPVTVDGKT------------LPLAEALQ----WHFELtvntaNIVENYATLTRSETLLPLVGDKAA 351
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 399 LQELCSKQGAADYNRFIrdasvclldllltfPScQPPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPPSTT 478
Cdd:PRK10953 352 LQHYAATTPIVDMVRFA--------------PA-QLDAEQLIGLLRPLTPRLYSIASSQAEVENEVHITVGVVRYDIEGR 416
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 479 AaslRKGVCTGWLATLVApflqpntdvsnvDSGdalapEIRISPRATNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHRE 558
Cdd:PRK10953 417 A---RAGGASSFLADRLE------------EEG-----EVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRA 476
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 559 KlqeqhpDGKFGAMWLFFGCRHKDRDYLFREELRHFLKTGVLTHLKVSFSRDaapdgeEAPAKYVQDNLQRHSQQVARtL 638
Cdd:PRK10953 477 A------DGAPGKNWLFFGNPHFTEDFLYQVEWQRYVKEGLLTRIDLAWSRD------QKEKIYVQDKLREQGAELWR-W 543
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568983212 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 1.54e-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  Cd Length: 219  Bit Score: 169.83  E-value: 1.54e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212  272 FQVPISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHRVILKIKTDTKKkg 351
Cdd:pfam00667   8 FTAPVLSNRELTSPSSDRNCIHVELDISGSGLTYQTGDHLGVYPPNNEELVEELLERLGLDPKPDTVVLLKTLDERVK-- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212  352 aalpAHVPEGRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPS 431
Cdd:pfam00667  86 ----PPRLPPTTYRQALKYYLDITGPPSKQLLRLLAQFAPEEEEKQRLEFLSSDAGAREYKRWKLNHAPTLLEVLEEFPS 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568983212  432 CQPPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFpPSTTAASLRKGVCTGW 490
Cdd:pfam00667 162 VKLPADFLLTQLPQLQPRYYSISSSSKVHPNEVHLTVVVVEY-ETDGEGRIHYGVCSNW 219
Flavodoxin_1 pfam00258
Flavodoxin;
6-142 1.66e-33

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 125.17  E-value: 1.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212    6 LLYATQRGQAKAIAEEISEQAVSHGFSADLHCISE-SEKYDLKTETGPLVMVVSTTGTGDPPDTARKFVKEIHNKTLPTD 84
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDDvDETLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGTLED 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568983212   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 3.30e-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: 3.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 448 PRPYSCASSSLRhpdklhfvfNIVEFppsttaaSLRK---GVCTGWLATLvapflqpntdvsnvDSGDALAPEIRISPRa 524
Cdd:cd06201  100 PRFYSLASSSSD---------GFLEI-------CVRKhpgGLCSGYLHGL--------------KPGDTIKAFIRPNPS- 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 525 tnaFHLPEDpSAPIIMVGPGTGVAPFVGFLQHREKlqeQHPdgkfgaMWLFFGCRHKDRDYLFREELRHFLKTGVLTHLK 604
Cdd:cd06201  149 ---FRPAKG-AAPVILIGAGTGIAPLAGFIRANAA---RRP------MHLYWGGRDPASDFLYEDELDQYLADGRLTQLH 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 605 VSFSRdaAPDGeeapaKYVQDNLQRHSQQVARtLLQENGYVYVCGdAKNMAKDVNDTLIGIIsneagvdkLEAMKTLATL 684
Cdd:cd06201  216 TAFSR--TPDG-----AYVQDRLRADAERLRR-LIEDGAQIMVCG-SRAMAQGVAAVLEEIL--------APQPLSLDEL 278
                        250
                 ....*....|.
gi 568983212 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 1.26e-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: 1.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 436 LSLLLEHLPKLQPRPYSCASSSlRHPDKLHFVFNIVEfppsttaaslrKGVCTGWLATLvapflqpntdvsnvDSGDala 515
Cdd:cd00322   29 VDLHLPGDGRGLRRAYSIASSP-DEEGELELTVKIVP-----------GGPFSAWLHDL--------------KPGD--- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 516 pEIRISPRATNaFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgkfgaMWLFFGCRHKDrDYLFREELRHFL 595
Cdd:cd00322   80 -EVEVSGPGGD-FFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGE------ITLLYGARTPA-DLLFLDELEELA 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568983212 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 1.06e-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: 1.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 439 LLEHLPK--LQPRPYSCAS-----------SSLRHPDKLHfvfnivefppsttaaslrkGVCTGWLaTLVAPflqpntdv 505
Cdd:cd06200   37 IAEIGPRhpLPHREYSIASlpadgalellvRQVRHADGGL-------------------GLGSGWL-TRHAP-------- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 506 snvdsgdaLAPEIRISPRATNAFHLPEDpSAPIIMVGPGTGVAPFVGFLQHREKlQEQHPDgkfgamWLFFGCRHKDRDY 585
Cdd:cd06200   89 --------IGASVALRLRENPGFHLPDD-GRPLILIGNGTGLAGLRSHLRARAR-AGRHRN------WLLFGERQAAHDF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 586 LFREELRHFLKTGVLTHLKVSFSRDAapdgeeAPAKYVQDNLQRHSQQVaRTLLQENGYVYVCGDAKNMAKDVNDTLIGI 665
Cdd:cd06200  153 FCREELEAWQAAGHLARLDLAFSRDQ------AQKRYVQDRLRAAADEL-RAWVAEGAAIYVCGSLQGMAPGVDAVLDEI 225
                        250       260       270
                 ....*....|....*....|....*....|
gi 568983212 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 1.44e-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: 1.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 448 PRPYSCASSSL---RHPDKLHFVFNIVEFPPSTTAaSLRKGVCTGWLATLVApflqpntdvsnvdsGDalapEIRISPRA 524
Cdd:cd06208   64 LRLYSIASSRYgddGDGKTLSLCVKRLVYTDPETD-ETKKGVCSNYLCDLKP--------------GD----DVQITGPV 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 525 TNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHRekLQEQHPDGKF-GAMWLFFGCRHKDrDYLFREELRHFLKT-GVLTH 602
Cdd:cd06208  125 GKTMLLPEDPNATLIMIATGTGIAPFRSFLRRL--FREKHADYKFtGLAWLFFGVPNSD-SLLYDDELEKYPKQyPDNFR 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 603 LKVSFSRDaaPDGEEAPAKYVQDNLQRHSQQVARTLLQENGYVYVCGdAKNMAKDVNDTLigiiSNEAGVDKLEAMKtLA 682
Cdd:cd06208  202 IDYAFSRE--QKNADGGKMYVQDRIAEYAEEIWNLLDKDNTHVYICG-LKGMEPGVDDAL----TSVAEGGLAWEEF-WE 273

                 ....*...
gi 568983212 683 TLKQEKRY 690
Cdd:cd06208  274 SLKKKGRW 281
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
484-686 5.08e-20

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 92.37  E-value: 5.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 484 KGVCTGWLATLvapflQPNTDVSnvdsgdalapeirISPRATNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQhrEKLQEQ 563
Cdd:PLN03115 182 KGVCSNFLCDL-----KPGAEVK-------------ITGPVGKEMLMPKDPNATIIMLATGTGIAPFRSFLW--KMFFEK 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 564 HPDGKF-GAMWLFFGCRHKDrDYLFREELRHfLKTGVLTHLKVSFSRDAAPDGEEAPAKYVQDNLQRHSQQVARTLLQEN 642
Cdd:PLN03115 242 HDDYKFnGLAWLFLGVPTSS-SLLYKEEFEK-MKEKAPENFRLDFAVSREQTNAKGEKMYIQTRMAEYAEELWELLKKDN 319
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568983212 643 GYVYVCGdAKNMAKDVNDTLIGIISNEaGVDKLEAMKTLATLKQ 686
Cdd:PLN03115 320 TYVYMCG-LKGMEKGIDDIMVSLAAKD-GIDWFEYKKQLKKAEQ 361
PRK08105 PRK08105
flavodoxin; Provisional
1-150 2.19e-18

flavodoxin; Provisional


Pssm-ID: 181230 [Multi-domain]  Cd Length: 149  Bit Score: 82.24  E-value: 2.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212   1 MRRFLLLYATQRGQAKAIAEEISEQAVSHGFSADL---HCISESEKYDLKTetgpLVMVVSTTGTGDPPDTARKFVKEIh 77
Cdd:PRK08105   1 MAKVGIFVGTVYGNALLVAEEAEAILTAQGHEVTLfedPELSDWQPYQDEL----VLVVTSTTGQGDLPDSIVPLFQAL- 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568983212  78 NKTLPtdYFAHLQYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDTGHADDCVGLELVVE--PWIDGlWAAL 150
Cdd:PRK08105  76 KDTAG--YQPNLRYGVIALGDSSYDNFCGAGKQFDALLQEQGAKRVGERLEIDACETPEPEVEanPWVEQ-WGTL 147
PLN03116 PLN03116
ferredoxin--NADP+ reductase; Provisional
448-690 2.54e-18

ferredoxin--NADP+ reductase; Provisional


Pssm-ID: 215586 [Multi-domain]  Cd Length: 307  Bit Score: 86.31  E-value: 2.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 448 PRPYSCASSslRHPDKLH------FVFNIVEFPPSTTAA-SLRKGVCTGWLAtlvapflqpntdvsNVDSGDalapEIRI 520
Cdd:PLN03116  81 VRLYSIAST--RYGDDFDgktaslCVRRAVYYDPETGKEdPAKKGVCSNFLC--------------DAKPGD----KVQI 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 521 SPRATNAFHLPE-DPSAPIIMVGPGTGVAPFVGFLqhREKLQEQHPDGKF-GAMWLFFGCRHKDRdYLFREELrhflkTG 598
Cdd:PLN03116 141 TGPSGKVMLLPEeDPNATHIMVATGTGIAPFRGFL--RRMFMEDVPAFKFgGLAWLFLGVANSDS-LLYDDEF-----ER 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 599 VLTHLKVSFSRDAAPDGEEAPAK----YVQDNLQRHSQQVArTLLQENGYVYVCGdAKNMAKDVNDTLIGiISNEAGVDK 674
Cdd:PLN03116 213 YLKDYPDNFRYDYALSREQKNKKggkmYVQDKIEEYSDEIF-KLLDNGAHIYFCG-LKGMMPGIQDTLKR-VAEERGESW 289
                        250
                 ....*....|....*.
gi 568983212 675 LEamkTLATLKQEKRY 690
Cdd:PLN03116 290 EE---KLSGLKKNKQW 302
PRK09004 PRK09004
FMN-binding protein MioC; Provisional
13-126 2.27e-16

FMN-binding protein MioC; Provisional


Pssm-ID: 181608 [Multi-domain]  Cd Length: 146  Bit Score: 76.41  E-value: 2.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212  13 GQAKAIAEEISEQAVSHGFSADLHCISESEkyDLKTEtGPLVMVVSTTGTGDPPDTARKFVKEIHNKTLPtdyFAHLQYG 92
Cdd:PRK09004  13 GGAEYVADHLAEKLEEAGFSTETLHGPLLD--DLSAS-GLWLIVTSTHGAGDLPDNLQPFFEELQEQKPD---LSQVRFA 86
                         90       100       110
                 ....*....|....*....|....*....|....
gi 568983212  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 7.36e-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: 7.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212  540 MVGPGTGVAPFVGFLQHRekLQEQHPDGKfgaMWLFFGCRHkDRDYLFREELRHFLKT--GVLTHLKVSFSRDAAPDGEE 617
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAI--LEDPKDPTQ---VVLVFGNRN-EDDILYREELDELAEKhpGRLTVVYVVSRPEAGWTGGK 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568983212  618 apaKYVQDNLQRHSQQvartLLQENGYVYVCGdAKNMAKDV 658
Cdd:pfam00175  75 ---GRVQDALLEDHLS----LPDEETHVYVCG-PPGMIKAV 107
FldA COG0716
Flavodoxin [Energy production and conversion];
1-150 1.68e-13

Flavodoxin [Energy production and conversion];


Pssm-ID: 223788 [Multi-domain]  Cd Length: 151  Bit Score: 68.56  E-value: 1.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212   1 MRRFLLLYATQRGQAKAIAEEISEQAVSHGFSADLHcISESEKYDLKTETGPLVMVVSTTGTGDPPDTARKFVKEIHNKT 80
Cdd:COG0716    1 MMKILIVYGSRTGNTEKVAEIIAEELGADGFEVDID-IRPGIKDDLLESYDELLLGTPTWGAGELPDDWYDFIEELEPID 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568983212  81 LPTdyfahLQYGLLGLGDSEY-TYFCNGGKVIDKRLQELGAQ--------RFYDTGHADDcvGLELVVEPWIDGLWAAL 150
Cdd:COG0716   80 FKG-----KLVAVFGLGDQSYyGYFCEAGGNFEDILEEKGAKavgiletlGYIFDASPNE--EDEKRIKEWVKQILNEL 151
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
436-662 2.67e-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: 2.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 436 LSLLLEHLPKLQpRPYSCASsslrHPDKLHFVFNIVEFPpsttaaslrKGVCTGWLATLvapflQPntdvsnvdsGDala 515
Cdd:cd06195   33 LGLPNDDGKLVR-RAYSIAS----APYEENLEFYIILVP---------DGPLTPRLFKL-----KP---------GD--- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 516 pEIRISPRATNAFHLPEDPSAP-IIMVGPGTGVAPFVGFLQHREKLQeqhpdgKFGAMWLFFGCRHKDrDYLFREELRHF 594
Cdd:cd06195   82 -TIYVGKKPTGFLTLDEVPPGKrLWLLATGTGIAPFLSMLRDLEIWE------RFDKIVLVHGVRYAE-ELAYQDEIEAL 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568983212 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 6.34e-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  Cd Length: 222  Bit Score: 56.89  E-value: 6.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 448 PRPYSCASsslrHPDKLHF-VFNIVEFPPsttaaslrkGVCTGWLATLVAPflqpntdvsnvdsGDALapeiRISPRATN 526
Cdd:cd06194   39 ARSYSPTS----LPDGDNElEFHIRRKPN---------GAFSGWLGEEARP-------------GHAL----RLQGPFGQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 527 AFHLPEDPSAPIIMVGPGTGVAPFVGFLqhREKLQEQHPdgkfGAMWLFFGCRHKDRDYLfREELRHF-LKTGVLTHLKV 605
Cdd:cd06194   89 AFYRPEYGEGPLLLVGAGTGLAPLWGIA--RAALRQGHQ----GEIRLVHGARDPDDLYL-HPALLWLaREHPNFRYIPC 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568983212 606 SfSRDAAPDGEEAPAKYVQDNLQRHSQQVartllqengyVYVCGDA 651
Cdd:cd06194  162 V-SEGSQGDPRVRAGRIAAHLPPLTRDDV----------VYLCGAP 196
PRK05723 PRK05723
flavodoxin; Provisional
53-151 2.97e-06

flavodoxin; Provisional


Pssm-ID: 168208  Cd Length: 151  Bit Score: 47.48  E-value: 2.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212  53 LVMVVSTTGTGDPPDTARKFVKEIHNkTLPTDYFAhLQYGLLGLGDSEY-TYFCNGGKVIDKRLQELGAQRFYDTGHAD- 130
Cdd:PRK05723  51 LLAVTSTTGMGELPDNLMPLYSAIRD-QLPAAWRG-LPGAVIALGDSSYgDTFCGGGEQMRELFAELGVREVQPMLRLDa 128
                         90       100
                 ....*....|....*....|..
gi 568983212 131 -DCVGLELVVEPWIDGLWAALT 151
Cdd:PRK05723 129 sETVTPETDAEPWLAEFAAALK 150
Flavodoxin_5 pfam12724
Flavodoxin domain; This is a family of flavodoxins. Flavodoxins are electron transfer proteins ...
5-103 4.48e-06

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


Pssm-ID: 432744  Cd Length: 144  Bit Score: 46.87  E-value: 4.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212    5 LLLYATQRGQAKAIAEEISEQAVSHGFSADLHCISESEK---YDlktetgpLVMVVSTTGTGDPPDTARKFVKEiHNKTL 81
Cdd:pfam12724   1 LILYSSRDGQTKKIAERIAEELREEGELVDVEDVEAGEDlssYD-------AVVIGASIYYGKHLPELRKFVTK-HRDEL 72
                          90       100
                  ....*....|....*....|..
gi 568983212   82 PTDYFAHLQYGLLGLGDSEYTY 103
Cdd:pfam12724  73 SSKPVAFFSVNLTARKPEKNPY 94
PRK09267 PRK09267
flavodoxin FldA; Validated
1-120 4.77e-06

flavodoxin FldA; Validated


Pssm-ID: 236439 [Multi-domain]  Cd Length: 169  Bit Score: 47.13  E-value: 4.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212   1 MRRFLLLYATQRGQAKAIAEEISEQAVSHgfSADLHCISES-----EKYDLktetgpLVMVVSTTGTGDPPDTARKFVKE 75
Cdd:PRK09267   1 MAKIGIFFGSDTGNTEDIAKMIQKKLGKD--VADVVDIAKAskedfEAYDL------LILGIPTWGYGELQCDWDDFLPE 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568983212  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 6.59e-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: 6.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 449 RPYSCASSSlrHPDKLHFVFNIVEfppsttaaslrKGVCTGWLATLVAPflqpntdvsnvdsGDALAPEiriSPRAtnAF 528
Cdd:cd06209   48 RSYSFSSAP--GDPRLEFLIRLLP-----------GGAMSSYLRDRAQP-------------GDRLTLT---GPLG--SF 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 529 HLpEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgkfgaMWLFFGCRHK------DRDYLFREELRHFlktgvlth 602
Cdd:cd06209   97 YL-REVKRPLLMLAGGTGLAPFLSMLDVLAEDGSAHP------VHLVYGVTRDadlvelDRLEALAERLPGF-------- 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568983212 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 7.56e-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: 7.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 526 NAFHLPEDPSAPIIMVGPGTGVAPFVG----FLQHREklqeqhpdgKFGAMWLFFGCRHKDrDYLFREELRHFLKtgvLT 601
Cdd:cd06221   89 NGFPVEEMKGKDLLLVAGGLGLAPLRSlinyILDNRE---------DYGKVTLLYGARTPE-DLLFKEELKEWAK---RS 155
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568983212 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 8.87e-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: 8.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 500 QPNTDVSN-----VDSGDalapEIRISPRATNaFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgkfgaMWL 574
Cdd:cd06184   78 EPGGLVSNylhdnVKVGD----VLEVSAPAGD-FVLDEASDRPLVLISAGVGITPMLSMLEALAAEGPGRP------VTF 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 575 FFGCRHKDrDYLFREELRHFLKTGVLTHLKVSFSRDAAPDGEEAPAKYVQDNLQRhsqqVARTLLQENGYVYVCGDAKNM 654
Cdd:cd06184  147 IHAARNSA-VHAFRDELEELAARLPNLKLHVFYSEPEAGDREEDYDHAGRIDLAL----LRELLLPADADFYLCGPVPFM 221
                        170       180
                 ....*....|....*....|
gi 568983212 655 aKDVNDTLIgiisnEAGVDK 674
Cdd:cd06184  222 -QAVREGLK-----ALGVPA 235
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
442-664 1.87e-05

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


Pssm-ID: 223617 [Multi-domain]  Cd Length: 252  Bit Score: 46.63  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 442 HLPKLQPRPYSCASSSlRHPDKLHFVFNIVEfppsttaaslrKGVCTGWLATLvapflQPNTDVsnvdsgdalapEIRIs 521
Cdd:COG0543   45 RVPGGVRRPYSLASAP-DDKGELELHIRVYE-----------VGKVTKYIFGL-----KEGDKI-----------RVRG- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 522 PRATnaFHLPEDPSAPIIMVGPGTGVAPFVGFLQHrekLQEQhpdGKFGAMWLFFGCRHKDrDYLFREELRHFlkTGVLT 601
Cdd:COG0543   96 PLGN--GFLREKIGKPVLLIAGGTGIAPLYAIAKE---LKEK---GDANKVTLLYGARTAK-DLLLLDELEEL--AEKEV 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568983212 602 HLKVSfsrdaapDGEEAPAKYV-QDNLQRHsqqvartLLQENGYVYVCGdAKNMAKDVNDTLIG 664
Cdd:COG0543  165 HPVTD-------DGWKGRKGFVtTDVLKEL-------LDLEVDDVYICG-PPAMVKAVREKLKE 213
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
511-649 2.42e-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: 2.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 511 GD---ALAPEIRISPRAT-----NAFHLPeDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHP-DgkfgamwLFFGCRhK 581
Cdd:cd06198   64 GDytrRLAERLKPGTRVTvegpyGRFTFD-DRRARQIWIAGGIGITPFLALLEALAARGDARPvT-------LFYCVR-D 134
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568983212 582 DRDYLFREELRHfLKTGVLTHLKVSFSRDAAPDGEEAPAKYVQDNLQRHSqqvartllqengyVYVCG 649
Cdd:cd06198  135 PEDAVFLDELRA-LAAAAGVVLHVIDSPSDGRLTLEQLVRALVPDLADAD-------------VWFCG 188
Fpr COG1018
Ferredoxin-NADP reductase [Energy production and conversion];
507-590 3.34e-05

Ferredoxin-NADP reductase [Energy production and conversion];


Pssm-ID: 223949 [Multi-domain]  Cd Length: 266  Bit Score: 46.12  E-value: 3.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 507 NVDSGDalapEIRISPrATNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQhreKLQEQHPDgkfgAMWLFFGCRHKDrDYL 586
Cdd:COG1018   87 HLKVGD----TLEVSA-PAGDFVLDDLPERKLLLLAGGIGITPFLSMLR---TLLDRGPA----DVVLVHAARTPA-DLA 153

                 ....
gi 568983212 587 FREE 590
Cdd:COG1018  154 FRDE 157
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
526-663 3.52e-05

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 46.34  E-value: 3.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 526 NAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHreklqEQHPDGKFGAMWLFFGCRHKdRDYLFREELRHFLKTGVLTHLKV 605
Cdd:PRK08345  99 NGFPVDEMEGMDLLLIAGGLGMAPLRSVLLY-----AMDNRWKYGNITLIYGAKYY-EDLLFYDELIKDLAEAENVKIIQ 172
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568983212 606 SFSRDA-APDGEEAPAKYVqdnlQRHSQQVARTLLQE------NGYVYVCGDAKnMAKDVNDTLI 663
Cdd:PRK08345 173 SVTRDPeWPGCHGLPQGFI----ERVCKGVVTDLFREantdpkNTYAAICGPPV-MYKFVFKELI 232
PRK06703 PRK06703
flavodoxin; Provisional
1-126 4.54e-05

flavodoxin; Provisional


Pssm-ID: 235854 [Multi-domain]  Cd Length: 151  Bit Score: 43.98  E-value: 4.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212   1 MRRFLLLYATQRGQAKAIAEEISEQAVSHGFSADLHCISESEKYDLKTETGplVMVVSTT-GTGDPPDTARKFVKEIHNK 79
Cdd:PRK06703   1 MAKILIAYASMSGNTEDIADLIKVSLDAFDHEVVLQEMDGMDAEELLAYDG--IILGSYTwGDGDLPYEAEDFHEDLENI 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568983212  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 8.51e-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: 8.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 449 RPYSCASSslrhPDKLHFVfnivefppSTTAASLRKGVCTGWLATLVAPflqpntdvsnvdsGDALapEIRiSPRATnaF 528
Cdd:cd06217   51 RSYSIASS----PTQRGRV--------ELTVKRVPGGEVSPYLHDEVKV-------------GDLL--EVR-GPIGT--F 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 529 HLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgkfgaMWLFFGCRHKDrDYLFREELRHF-LKTGVLtHLKVSF 607
Cdd:cd06217  101 TWNPLHGDPVVLLAGGSGIVPLMSMIRYRRDLGWPVP------FRLLYSARTAE-DVIFRDELEQLaRRHPNL-HVTEAL 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568983212 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 1.05e-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: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 538 IIMVGPGTGVAPFVGFLQHRekLQEQHPDGKfgaMWLFFGCRHKDrDYLFREELRHFLKTGVlTHLKVSFSRDAAPDGEE 617
Cdd:cd06183  107 IGMIAGGTGITPMLQLIRAI--LKDPEDKTK---ISLLYANRTEE-DILLREELDELAKKHP-DRFKVHYVLSRPPEGWK 179
                         90       100       110
                 ....*....|....*....|....*....|...
gi 568983212 618 APAKYV-QDNLQRHSQQVARtllqENGYVYVCG 649
Cdd:cd06183  180 GGVGFItKEMIKEHLPPPPS----EDTLVLVCG 208
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
528-649 1.87e-03

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 41.01  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 528 FHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgkfgaMWLFFGCRHKDRDYL------FREELRHFLKTGVLT 601
Cdd:PRK07609 197 FFLREDSDKPIVLLASGTGFAPIKSIVEHLRAKGIQRP------VTLYWGARRPEDLYLsalaeqWAEELPNFRYVPVVS 270
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568983212 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 2.02e-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: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 532 EDPSAPIIMVGPGT------GVAPFVGFLQHREKlqeqhpDGKFGAMWLFFGCRhKDRDYLFREELRHFLKTG---VLTH 602
Cdd:cd06196   90 EDPWGAIEYKGPGVfiaggaGITPFIAILRDLAA------KGKLEGNTLIFANK-TEKDIILKDELEKMLGLKfinVVTD 162
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 603 LKVSFSRDAAPDGEeapakYVQDNLQRHSQQvartllqengyVYVCGDAKnMAKDVNDTLIGIISNEAGV 672
Cdd:cd06196  163 EKDPGYAHGRIDKA-----FLKQHVTDFNQH-----------FYVCGPPP-MEEAINGALKELGVPEDSI 215
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
528-663 3.69e-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: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 528 FHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgkfgaMWLFFGCRHKDRDYL------FREELRHFLKTGVLT 601
Cdd:cd06189   91 FFLREDSDRPLILIAGGTGFAPIKSILEHLLAQGSKRP------IHLYWGARTEEDLYLdelleaWAEAHPNFTYVPVLS 164
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568983212 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 8.47e-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: 8.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983212 528 FHLPEDPSAPIIMVGPGTGVAPFV----GFLQHREKlQEQHpdgkfgamwLFFGCRHK----DRDYLFREELRH--FLKT 597
Cdd:cd06187   91 FYLRRDHDRPVLCIAGGTGLAPLRaiveDALRRGEP-RPVH---------LFFGARTErdlyDLEGLLALAARHpwLRVV 160
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568983212 598 GVLTHlkvsfsrdaAPDGEEAPAKYVQDnlqrhsqQVARTLLQENGY-VYVCGDAKnMAKDVNDTLI 663
Cdd:cd06187  161 PVVSH---------EEGAWTGRRGLVTD-------VVGRDGPDWADHdIYICGPPA-MVDATVDALL 210
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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