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Conserved domains on  [gi|1907093293|ref|XP_036013852|]
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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 1907093293 275 PISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHRVILKIKTDTKKKGAAL 354
Cdd:cd06203     1 PISSAKKLTEGDDVKTVVDLTLDLSPTGFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVPNTKKKNAKV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 355 PAHVPEGRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPSCQP 434
Cdd:cd06203    81 PVHIPKVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDFVRKRGLSLLDLLEAFPSCRP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 435 PLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPPsttaaslrKGVCTGWLATLVApflqpntdvsnvdSGDAL 514
Cdd:cd06203   161 PLSLLIEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPA--------KGLCTSWLESLCL-------------SASSH 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 515 APEIRISPRATNAFHLPED-PSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPDGKFGAMWLFFGCRHKDRDYLFREELRH 593
Cdd:cd06203   220 GVKVPFYLRSSSRFRLPPDdLRRPIIMVGPGTGVAPFLGFLQHREKLKESHTETVFGEAWLFFGCRHRDRDYLFRDELEE 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 594 FLKTGVLTHLKVSFSRDAapdGEEAPAKYVQDNLQRHSQQVARTLLQENGYVYVCGDAKNMAKDVNDTLIGIISNEAGVD 673
Cdd:cd06203   300 FLEEGILTRLIVAFSRDE---NDGSTPKYVQDKLEERGKKLVDLLLNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGLD 376
                         410       420
                  ....*....|....*....|..
gi 1907093293 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 1907093293   6 LLYATQRGQAKAIAEEISEQAVSHGFSADLHCISE-SEKYDLKTETGPLVMVVSTTGTGDPPDTARKFVKEIHNKTLPTD 84
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDDvDETLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGTLED 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907093293  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 1907093293 275 PISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHRVILKIKTDTKKKGAAL 354
Cdd:cd06203     1 PISSAKKLTEGDDVKTVVDLTLDLSPTGFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVPNTKKKNAKV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 355 PAHVPEGRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPSCQP 434
Cdd:cd06203    81 PVHIPKVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDFVRKRGLSLLDLLEAFPSCRP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 435 PLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPPsttaaslrKGVCTGWLATLVApflqpntdvsnvdSGDAL 514
Cdd:cd06203   161 PLSLLIEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPA--------KGLCTSWLESLCL-------------SASSH 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 515 APEIRISPRATNAFHLPED-PSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPDGKFGAMWLFFGCRHKDRDYLFREELRH 593
Cdd:cd06203   220 GVKVPFYLRSSSRFRLPPDdLRRPIIMVGPGTGVAPFLGFLQHREKLKESHTETVFGEAWLFFGCRHRDRDYLFRDELEE 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 594 FLKTGVLTHLKVSFSRDAapdGEEAPAKYVQDNLQRHSQQVARTLLQENGYVYVCGDAKNMAKDVNDTLIGIISNEAGVD 673
Cdd:cd06203   300 FLEEGILTRLIVAFSRDE---NDGSTPKYVQDKLEERGKKLVDLLLNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGLD 376
                         410       420
                  ....*....|....*....|..
gi 1907093293 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 1907093293   5 LLLYATQRGQAKAIAEEISEQAVSHGFSADLHCISESEKYDLKTETGpLVMVVSTTGTGDPPDTARKFVKEIHNKTLPTd 84
Cdd:COG0369    51 TVLYGSQTGNAEGLAEELAKELEAAGLQVLVASLDDYKPKDIAEERL-LLFVVSTQGEGEPPDNAVAFHEFLKGKKAPK- 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293  85 yFAHLQYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDTGHADDcVGLELVVEPWIDGLWAALtkhFKSLGGQENms 164
Cdd:COG0369   129 -LDGLRYAVLGLGDSSYEFFCQAGKDFDRRLQELGATRLFPRVEADV-QDFEAAAAPWRDDVLELL---KSKFPGQEA-- 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 165 dtlsrasdaplstamkpellhiqsqvellrledmgerdselreqnetnrgqqgriedfdsslvHSVPPLSQSSLSIPAVP 244
Cdd:COG0369   202 ---------------------------------------------------------------APAQVATSPQSESPYSK 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 245 PEYLEVHLQEslgqeeNQasvpsgdpsfqvpiskaiRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEE 324
Cdd:COG0369   219 PAPSVAILLE------NR------------------KLTGRDSDKDVRHIELDLPDSGLRYEPGDALGVWPENDPELVDE 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 325 LLQRLQLadkrahrvilkiktdtkkKGAALPAHVPEGRSLQFILTWCLEIrAVPKKAFLRALAEHTSSATEKRRLQELCs 404
Cdd:COG0369   275 FLELLGL------------------DPEEPVTVDGETLPLVEALKSHFEF-TSAPKSLLENLAHFAGQEELRRLLEQLD- 334
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 405 kqgAADYNRFIRdaSVCLLDLLLTFPSCQPPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPpstTAASLRK 484
Cdd:COG0369   335 ---IADLQDYAK--RRTLIDVLRDFPPAKLPAEELIDLLPPLKPRLYSIASSPGVSPDEVHLTVGVVRYQ---AEGRERY 406
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 485 GVCTGWLATLVAPflqpntdvsnvdsGDalapEIRISPRATNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQh 564
Cdd:COG0369   407 GVCSGYLADLLEE-------------GD----TIPVFVQPNKNFRLPEDPETPIIMIGPGTGIAPFRAFVQERAANGAE- 468
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 565 pdgkfGAMWLFFGCRHKDRDYLFREELRHFLKTGVLTHLKVSFSRDaapdgeEAPAKYVQDNLQRHSQQVaRTLLQENGY 644
Cdd:COG0369   469 -----GKNWLFFGCRHFTEDFLYQEEWEEYLKDGVLTRLDLAFSRD------QEEKIYVQDRLREQADEL-WEWLEEGAH 536
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907093293 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 1907093293 281 RLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQladKRAHRVIlkiktdtkkkgaalpahvpE 360
Cdd:PRK06214  178 RLNKPGSEKETWHVEIDLAGSGLDYEVGDSLGLFPANDPALVDAVIAALG---APPEFPI-------------------G 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 361 GRSLQFILTWCLEIRAVPKKAFLRaLAEHTSSATEK--RRLQELCSKQGAAdynrfirdASVCLLDLLLTFPSCQPPLSL 438
Cdd:PRK06214  236 GKTLREALLEDVSLGPAPDGLFEL-LSYITGGAARKkaRALAAGEDPDGDA--------ATLDVLAALEKFPGIRPDPEA 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 439 LLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFppsTTAASLRKGVCTGWLATLVAP------FLQPNtdvsnvdsgd 512
Cdd:PRK06214  307 FVEALDPLQPRLYSISSSPKATPGRVSLTVDAVRY---EIGSRLRLGVASTFLGERLAPgtrvrvYVQKA---------- 373
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 513 alapeirispratNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQhpdgkfGAMWLFFGCRHKDRDYLFREELR 592
Cdd:PRK06214  374 -------------HGFALPADPNTPIIMVGPGTGIAPFRAFLHERAATKAP------GRNWLFFGHQRSATDFFYEDELN 434
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 593 HFLKTGVLTHLKVSFSRDaapdGEEApaKYVQDNLQrhsqQVARTL---LQENGYVYVCGDAKNMAKDVNDTLIGIISNE 669
Cdd:PRK06214  435 GLKAAGVLTRLSLAWSRD----GEEK--TYVQDRMR----ENGAELwkwLEEGAHFYVCGDAKRMAKDVERALVDIVAQF 504
                         410       420
                  ....*....|....*....|....*.
gi 1907093293 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 1907093293 272 FQVPISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHRVILKIKTDTKKkg 351
Cdd:pfam00667   8 FTAPVLSNRELTSPSSDRNCIHVELDISGSGLTYQTGDHLGVYPPNNEELVEELLERLGLDPKPDTVVLLKTLDERVK-- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 352 aalpAHVPEGRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPS 431
Cdd:pfam00667  86 ----PPRLPPTTYRQALKYYLDITGPPSKQLLRLLAQFAPEEEEKQRLEFLSSDAGAREYKRWKLNHAPTLLEVLEEFPS 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093293 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 1907093293   6 LLYATQRGQAKAIAEEISEQAVSHGFSADLHCISE-SEKYDLKTETGPLVMVVSTTGTGDPPDTARKFVKEIHNKTLPTD 84
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDDvDETLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGTLED 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907093293  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 1907093293   1 MRRFLLLYATQRGQAKAIAEEISEQAVSHGFSADL---HCISESEKYDLKTetgpLVMVVSTTGTGDPPDTARKFVKEIh 77
Cdd:PRK08105    1 MAKVGIFVGTVYGNALLVAEEAEAILTAQGHEVTLfedPELSDWQPYQDEL----VLVVTSTTGQGDLPDSIVPLFQAL- 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907093293  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 1907093293   1 MRRFLLLYATQRGQAKAIAEEISEQAVSHGFSADLHcISESEKYDLKTETGPLVMVVSTTGTGDPPDTARKFVKEIHNKT 80
Cdd:COG0716     1 MMKILIVYGSRTGNTEKVAEIIAEELGADGFEVDID-IRPGIKDDLLESYDELLLGTPTWGAGELPDDWYDFIEELEPID 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093293  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 1907093293 275 PISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHRVILKIKTDTKKKGAAL 354
Cdd:cd06203     1 PISSAKKLTEGDDVKTVVDLTLDLSPTGFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVPNTKKKNAKV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 355 PAHVPEGRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPSCQP 434
Cdd:cd06203    81 PVHIPKVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDFVRKRGLSLLDLLEAFPSCRP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 435 PLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPPsttaaslrKGVCTGWLATLVApflqpntdvsnvdSGDAL 514
Cdd:cd06203   161 PLSLLIEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPA--------KGLCTSWLESLCL-------------SASSH 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 515 APEIRISPRATNAFHLPED-PSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPDGKFGAMWLFFGCRHKDRDYLFREELRH 593
Cdd:cd06203   220 GVKVPFYLRSSSRFRLPPDdLRRPIIMVGPGTGVAPFLGFLQHREKLKESHTETVFGEAWLFFGCRHRDRDYLFRDELEE 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 594 FLKTGVLTHLKVSFSRDAapdGEEAPAKYVQDNLQRHSQQVARTLLQENGYVYVCGDAKNMAKDVNDTLIGIISNEAGVD 673
Cdd:cd06203   300 FLEEGILTRLIVAFSRDE---NDGSTPKYVQDKLEERGKKLVDLLLNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGLD 376
                         410       420
                  ....*....|....*....|..
gi 1907093293 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 1907093293   5 LLLYATQRGQAKAIAEEISEQAVSHGFSADLHCISESEKYDLKTETGpLVMVVSTTGTGDPPDTARKFVKEIHNKTLPTd 84
Cdd:COG0369    51 TVLYGSQTGNAEGLAEELAKELEAAGLQVLVASLDDYKPKDIAEERL-LLFVVSTQGEGEPPDNAVAFHEFLKGKKAPK- 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293  85 yFAHLQYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDTGHADDcVGLELVVEPWIDGLWAALtkhFKSLGGQENms 164
Cdd:COG0369   129 -LDGLRYAVLGLGDSSYEFFCQAGKDFDRRLQELGATRLFPRVEADV-QDFEAAAAPWRDDVLELL---KSKFPGQEA-- 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 165 dtlsrasdaplstamkpellhiqsqvellrledmgerdselreqnetnrgqqgriedfdsslvHSVPPLSQSSLSIPAVP 244
Cdd:COG0369   202 ---------------------------------------------------------------APAQVATSPQSESPYSK 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 245 PEYLEVHLQEslgqeeNQasvpsgdpsfqvpiskaiRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEE 324
Cdd:COG0369   219 PAPSVAILLE------NR------------------KLTGRDSDKDVRHIELDLPDSGLRYEPGDALGVWPENDPELVDE 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 325 LLQRLQLadkrahrvilkiktdtkkKGAALPAHVPEGRSLQFILTWCLEIrAVPKKAFLRALAEHTSSATEKRRLQELCs 404
Cdd:COG0369   275 FLELLGL------------------DPEEPVTVDGETLPLVEALKSHFEF-TSAPKSLLENLAHFAGQEELRRLLEQLD- 334
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 405 kqgAADYNRFIRdaSVCLLDLLLTFPSCQPPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPpstTAASLRK 484
Cdd:COG0369   335 ---IADLQDYAK--RRTLIDVLRDFPPAKLPAEELIDLLPPLKPRLYSIASSPGVSPDEVHLTVGVVRYQ---AEGRERY 406
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 485 GVCTGWLATLVAPflqpntdvsnvdsGDalapEIRISPRATNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQh 564
Cdd:COG0369   407 GVCSGYLADLLEE-------------GD----TIPVFVQPNKNFRLPEDPETPIIMIGPGTGIAPFRAFVQERAANGAE- 468
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 565 pdgkfGAMWLFFGCRHKDRDYLFREELRHFLKTGVLTHLKVSFSRDaapdgeEAPAKYVQDNLQRHSQQVaRTLLQENGY 644
Cdd:COG0369   469 -----GKNWLFFGCRHFTEDFLYQEEWEEYLKDGVLTRLDLAFSRD------QEEKIYVQDRLREQADEL-WEWLEEGAH 536
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907093293 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 1907093293 272 FQVPISKAIRLTTNdAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADkraHRVILKIKTDTKKKG 351
Cdd:cd06204     6 FLAPVAVSRELFTG-SDRSCLHIEFDISGSGIRYQTGDHLAVWPTNPSEEVERLLKVLGLDD---RDTVISLKSLDEPAS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 352 AALPahVPEGRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSkQGAADYNRFIRDASVCLLDLLLTFPS 431
Cdd:cd06204    82 KKVP--FPCPTTYRTALRHYLDITAPVSRQVLAALAQFAPDPEEKERLLKLAS-EGKDEYAKWIVEPHRNLLEVLQDFPS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 432 CQ---PPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPpsTTAASLRKGVCTGWLATLVAPFLQPNTDVSNV 508
Cdd:cd06204   159 AKptpPPFDFLIELLPRLQPRYYSISSSSKVHPNRIHITAVVVKYP--TPTGRIIKGVATNWLLALKPALNGEKPPTPYY 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 509 DSGDALAPEIRISP---RATNaFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgKFGAMWLFFGCRHKDRDY 585
Cdd:cd06204   237 LSGPRKKGGGSKVPvfvRRSN-FRLPTKPSTPVIMIGPGTGVAPFRGFIQERAALKESGK--KVGPTLLFFGCRHPDEDF 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 586 LFREELRHFLKTGVLTHLKVSFSRdaapdgEEAPAKYVQDNLQRHSQQVARtLLQENGYVYVCGDAKNMAKDVNDTLIGI 665
Cdd:cd06204   314 IYKDELEEYAKLGGLLELVTAFSR------EQPKKVYVQHRLAEHAEQVWE-LINEGAYIYVCGDAKNMARDVEKTLLEI 386
                         410       420       430
                  ....*....|....*....|....*....|
gi 1907093293 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 1907093293 281 RLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHRVILKIKTDTKKkgaalpaHVPE 360
Cdd:cd06207     7 RLTPADYDRSTRHIEFDLGGSGLSYETGDNLGIYPENSDALVDEFLARLGLDGDDVVRVEPNEQQRGKP-------PFPE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 361 GRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSKQGAADYNRFIRdasVCLLDLLLTFPSCQPPLSLLL 440
Cdd:cd06207    80 PISVRQLLKKFLDIFGKPTKKFLKLLSQLATDEEEKEDLYKLASREGRTEYKRYEK---YTYLEVLKDFPSVRPTLEQLL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 441 EHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFppSTTAASLRKGVCTGWLAtlvapflqpntdvsNVDSGDALAPEIRI 520
Cdd:cd06207   157 ELCPLIKPRYYSISSSPLKNPNEVHLLVSLVSW--KTPSGRSRYGLCSSYLA--------------GLKVGQRVTVFIKK 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 521 SpratnAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgKFGAMWLFFGCRHKDRDYLFREELRHFLKTGVL 600
Cdd:cd06207   221 S-----SFKLPKDPKKPIIMVGPGTGLAPFRAFLQERAALLAQGP--EIGPVLLYFGCRHEDKDYLYKEELEEYEKSGVL 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 601 THLKVSFSRDaapdgeEAPAKYVQDNLQRHSQQVARTLLQENGYVYVCGDAKNMAKDVNDTLIGIISNEAGVDKLEAMKT 680
Cdd:cd06207   294 TTLGTAFSRD------QPKKVYVQDLIRENSDLVYQLLEEGAGVIYVCGSTWKMPPDVQEAFEEILKKHGGGDEELAEKK 367
                         410
                  ....*....|....*
gi 1907093293 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 1907093293 423 LDLLLTFPSCQPPLSLLLEHLP-KLQPRPYSCASSSLRHPDKLHFVFNIVEFPpsTTAASLRKGVCTGWLATLVapflqp 501
Cdd:cd06182    22 FDLSGNSVLKYQPGDHLGVIPPnPLQPRYYSIASSPDVDPGEVHLCVRVVSYE--APAGRIRKGVCSNFLAGLQ------ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 502 ntdvsnvdsgdaLAPEIRISPRATNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQeqHPDGKFGAMWLFFGCRHK 581
Cdd:cd06182    94 ------------LGAKVTVFIRPAPSFRLPKDPTTPIIMVGPGTGIAPFRGFLQERAALR--ANGKARGPAWLFFGCRNF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 582 DRDYLFREELRHFLKTGVLTHLKVSFSRDAApdgeeAPAKYVQDNLQRHSQQVARtLLQENGYVYVCGDAKNMAKDVNDT 661
Cdd:cd06182   160 ASDYLYREELQEALKDGALTRLDVAFSREQA-----EPKVYVQDKLKEHAEELRR-LLNEGAHIYVCGDAKSMAKDVEDA 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907093293 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 1907093293 276 ISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLAdkrahrvilkiktdtkkkGAALP 355
Cdd:cd06199     2 VLENRLLTGPGSEKETRHIELDLEGSGLSYEPGDALGVYPTNDPALVDELLAALGLS------------------GDEPV 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 356 AHVPEG-RSLQFILTWCLEIRAVpkkafLRALAEHTSSATEKRRLQELCSKQGAADYNRfirdasvcLLDLLLTFPSCQP 434
Cdd:cd06199    64 STVGGGtLPLREALIKHYEITTL-----LLALLESYAADTGALELLALAALEAVLAFAE--------LRDVLDLLPIPPA 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 435 PLSL--LLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFppsTTAASLRKGVCTGWLATLVAP------FLQPNtdvs 506
Cdd:cd06199   131 RLTAeeLLDLLRPLQPRLYSIASSPKAVPDEVHLTVAVVRY---ESHGRERKGVASTFLADRLKEgdtvpvFVQPN---- 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 507 nvdsgdalapeirispratNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLqeqhpdGKFGAMWLFFGCRHKDRDYL 586
Cdd:cd06199   204 -------------------PHFRLPEDPDAPIIMVGPGTGIAPFRAFLQEREAT------GAKGKNWLFFGERHFATDFL 258
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 587 FREELRHFLKTGVLTHLKVSFSRDaapdGEEapaK-YVQDNLQRHSQQVArTLLQENGYVYVCGDAKNMAKDVNDTLIGI 665
Cdd:cd06199   259 YQDELQQWLKDGVLTRLDTAFSRD----QAE---KvYVQDRMREQGAELW-AWLEEGAHFYVCGDAKRMAKDVDAALLDI 330
                         410       420       430
                  ....*....|....*....|....*....|
gi 1907093293 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 1907093293 281 RLTTNDAVKSTLLLELDISKI-EFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHrvILKIKTDTKKKGAALPAHV- 358
Cdd:cd06202     7 NLQSPKSSRSTILVKLDTNGAqELHYQPGDHVGIFPANRPELVDALLDRLHDAPPPDQ--VIKLEVLEERSTALGIIKTw 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 359 -PEGR----SLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCskQGAADYNRFIRDASVCLLDLLLTFPSCQ 433
Cdd:cd06202    85 tPHERlppcTLRQALTRYLDITTPPTPQLLQLLATLATDEKDKERLEVLG--KGSSEYEDWKWYKNPNILEVLEEFPSLQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 434 PPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPPSTTAASLRKGVCTGWLATLvapflqpntdvsnvDSGDA 513
Cdd:cd06202   163 VPASLLLTQLPLLQPRYYSISSSPDMYPGEIHLTVAVVSYRTRDGQGPVHHGVCSTWLNGL--------------TPGDT 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 514 LAPEIRISPratnAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHR--EKLQEQHPDGKFGAMWLFFGCRHKDRDYLFREEL 591
Cdd:cd06202   229 VPCFVRSAP----SFHLPEDPSVPVIMVGPGTGIAPFRSFWQQRqyDLRMSEDPGKKFGDMTLFFGCRNSTIDDIYKEET 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 592 RHFLKTGVLTHLKVSFSRDaaPDgeeAPAKYVQDNLQRHSQQVARTLLQENGYVYVCGDAkNMAKDVNDTLIGIISNEAG 671
Cdd:cd06202   305 EEAKNKGVLTEVYTALSRE--PG---KPKTYVQDLLKEQAESVYDALVREGGHIYVCGDV-TMAEDVSQTIQRILAEHGN 378
                         410       420
                  ....*....|....*....|...
gi 1907093293 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 1907093293 278 KAIRLTTNDAV-KSTLLLELDISKiEFSHQPGDSFNVTCPNSDREVEELLQRLQLAdkrahrvilkIKTDTKKKGAALPA 356
Cdd:cd06206     3 VENRELTAPGVgPSKRHLELRLPD-GMTYRAGDYLAVLPRNPPELVRRALRRFGLA----------WDTVLTISASGSAT 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 357 HVPEGRSLQF--ILTWCLEIRAVPKKAFLRALAEHTSsATEKRRLQELCSKQGaadYNRFIRDASVCLLDLLLTFPSCQP 434
Cdd:cd06206    72 GLPLGTPISVseLLSSYVELSQPATRRQLAALAEATR-CPDTKALLERLAGEA---YAAEVLAKRVSVLDLLERFPSIAL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 435 PLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPpSTTAASLRKGVCTGWLATLvapflQPntdvsnvdsGDal 514
Cdd:cd06206   148 PLATFLAMLPPMRPRQYSISSSPLVDPGHATLTVSVLDAP-ALSGQGRYRGVASSYLSSL-----RP---------GD-- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 515 apEIRISPRATN-AFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQhpDGKFGAMWLFFGCRHKDRDYLFREELRH 593
Cdd:cd06206   211 --SIHVSVRPSHsAFRPPSDPSTPLIMIAAGTGLAPFRGFLQERAALLAQ--GRKLAPALLFFGCRHPDHDDLYRDELEE 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 594 FLKTGVLThLKVSFSRDAapdgeEAPAKYVQDNLQRHSQQVARtLLQENGYVYVCGDAKnMAKDVNDTLIGIISNE---- 669
Cdd:cd06206   287 WEAAGVVS-VRRAYSRPP-----GGGCRYVQDRLWAEREEVWE-LWEQGARVYVCGDGR-MAPGVREVLKRIYAEKderg 358
                         410       420
                  ....*....|....*....|....*.
gi 1907093293 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 1907093293 281 RLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQladKRAHRVIlkiktdtkkkgaalpahvpE 360
Cdd:PRK06214  178 RLNKPGSEKETWHVEIDLAGSGLDYEVGDSLGLFPANDPALVDAVIAALG---APPEFPI-------------------G 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 361 GRSLQFILTWCLEIRAVPKKAFLRaLAEHTSSATEK--RRLQELCSKQGAAdynrfirdASVCLLDLLLTFPSCQPPLSL 438
Cdd:PRK06214  236 GKTLREALLEDVSLGPAPDGLFEL-LSYITGGAARKkaRALAAGEDPDGDA--------ATLDVLAALEKFPGIRPDPEA 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 439 LLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFppsTTAASLRKGVCTGWLATLVAP------FLQPNtdvsnvdsgd 512
Cdd:PRK06214  307 FVEALDPLQPRLYSISSSPKATPGRVSLTVDAVRY---EIGSRLRLGVASTFLGERLAPgtrvrvYVQKA---------- 373
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 513 alapeirispratNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQhpdgkfGAMWLFFGCRHKDRDYLFREELR 592
Cdd:PRK06214  374 -------------HGFALPADPNTPIIMVGPGTGIAPFRAFLHERAATKAP------GRNWLFFGHQRSATDFFYEDELN 434
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 593 HFLKTGVLTHLKVSFSRDaapdGEEApaKYVQDNLQrhsqQVARTL---LQENGYVYVCGDAKNMAKDVNDTLIGIISNE 669
Cdd:PRK06214  435 GLKAAGVLTRLSLAWSRD----GEEK--TYVQDRMR----ENGAELwkwLEEGAHFYVCGDAKRMAKDVERALVDIVAQF 504
                         410       420
                  ....*....|....*....|....*.
gi 1907093293 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 1907093293   6 LLYATQRGQAKAIAEEISEQAVSHGFSADLhciSESEKYDLK--TETGPLVMVVSTTGTGDPPDTARKFVKEIHNKTLPT 83
Cdd:PRK10953   66 LISASQTGNARRVAEQLRDDLLAAKLNVNL---VNAGDYKFKqiAQEKLLIVVTSTQGEGEPPEEAVALHKFLFSKKAPK 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293  84 dyFAHLQYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDTGHADdcVGLELVVEPWidglWAALTKHFKSlggqenm 163
Cdd:PRK10953  143 --LENTAFAVFGLGDTSYEFFCQAGKDFDSKLAELGAERLLDRVDAD--VEYQAAASEW----RARVVDALKS------- 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 164 sdtlsrasDAPLSTAmkpellhiQSQVellrledmgerdselreqnetnrGQQGRIEDFDSSLVHSVPPLSqSSLSIpav 243
Cdd:PRK10953  208 --------RAPAVAA--------PSQS-----------------------VATGAVNEIHTSPYSKEAPLT-ASLSV--- 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 244 ppeylevhlqeslgqeeNQasvpsgdpsfqvpiskaiRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVE 323
Cdd:PRK10953  245 -----------------NQ------------------KITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVK 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 324 ELLQRLQLadKRAHRVILKIKTdtkkkgaalpahVPEGRSLQfiltWCLEI-----RAVPKKAFLRALAEHTSSATEKRR 398
Cdd:PRK10953  290 ELVELLWL--KGDEPVTVDGKT------------LPLAEALQ----WHFELtvntaNIVENYATLTRSETLLPLVGDKAA 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 399 LQELCSKQGAADYNRFIrdasvclldllltfPScQPPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPPSTT 478
Cdd:PRK10953  352 LQHYAATTPIVDMVRFA--------------PA-QLDAEQLIGLLRPLTPRLYSIASSQAEVENEVHITVGVVRYDIEGR 416
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 479 AaslRKGVCTGWLATLVApflqpntdvsnvDSGdalapEIRISPRATNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHRE 558
Cdd:PRK10953  417 A---RAGGASSFLADRLE------------EEG-----EVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRA 476
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 559 KlqeqhpDGKFGAMWLFFGCRHKDRDYLFREELRHFLKTGVLTHLKVSFSRDaapdgeEAPAKYVQDNLQRHSQQVARtL 638
Cdd:PRK10953  477 A------DGAPGKNWLFFGNPHFTEDFLYQVEWQRYVKEGLLTRIDLAWSRD------QKEKIYVQDKLREQGAELWR-W 543
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907093293 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 1907093293 272 FQVPISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHRVILKIKTDTKKkg 351
Cdd:pfam00667   8 FTAPVLSNRELTSPSSDRNCIHVELDISGSGLTYQTGDHLGVYPPNNEELVEELLERLGLDPKPDTVVLLKTLDERVK-- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 352 aalpAHVPEGRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPS 431
Cdd:pfam00667  86 ----PPRLPPTTYRQALKYYLDITGPPSKQLLRLLAQFAPEEEEKQRLEFLSSDAGAREYKRWKLNHAPTLLEVLEEFPS 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093293 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 1907093293   6 LLYATQRGQAKAIAEEISEQAVSHGFSADLHCISE-SEKYDLKTETGPLVMVVSTTGTGDPPDTARKFVKEIHNKTLPTD 84
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDDvDETLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGTLED 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907093293  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 1907093293 448 PRPYSCASSSLRhpdklhfvfNIVEFppsttaaSLRK---GVCTGWLATLvapflqpntdvsnvDSGDALAPEIRISPRa 524
Cdd:cd06201   100 PRFYSLASSSSD---------GFLEI-------CVRKhpgGLCSGYLHGL--------------KPGDTIKAFIRPNPS- 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 525 tnaFHLPEDpSAPIIMVGPGTGVAPFVGFLQHREKlqeQHPdgkfgaMWLFFGCRHKDRDYLFREELRHFLKTGVLTHLK 604
Cdd:cd06201   149 ---FRPAKG-AAPVILIGAGTGIAPLAGFIRANAA---RRP------MHLYWGGRDPASDFLYEDELDQYLADGRLTQLH 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 605 VSFSRdaAPDGeeapaKYVQDNLQRHSQQVARtLLQENGYVYVCGdAKNMAKDVNDTLIGIIsneagvdkLEAMKTLATL 684
Cdd:cd06201   216 TAFSR--TPDG-----AYVQDRLRADAERLRR-LIEDGAQIMVCG-SRAMAQGVAAVLEEIL--------APQPLSLDEL 278
                         250
                  ....*....|.
gi 1907093293 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 1907093293 436 LSLLLEHLPKLQPRPYSCASSSlRHPDKLHFVFNIVEfppsttaaslrKGVCTGWLATLvapflqpntdvsnvDSGDala 515
Cdd:cd00322    29 VDLHLPGDGRGLRRAYSIASSP-DEEGELELTVKIVP-----------GGPFSAWLHDL--------------KPGD--- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 516 pEIRISPRATNaFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgkfgaMWLFFGCRHKDrDYLFREELRHFL 595
Cdd:cd00322    80 -EVEVSGPGGD-FFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGE------ITLLYGARTPA-DLLFLDELEELA 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907093293 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 1907093293 439 LLEHLPK--LQPRPYSCAS-----------SSLRHPDKLHfvfnivefppsttaaslrkGVCTGWLaTLVAPflqpntdv 505
Cdd:cd06200    37 IAEIGPRhpLPHREYSIASlpadgalellvRQVRHADGGL-------------------GLGSGWL-TRHAP-------- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 506 snvdsgdaLAPEIRISPRATNAFHLPEDpSAPIIMVGPGTGVAPFVGFLQHREKlQEQHPDgkfgamWLFFGCRHKDRDY 585
Cdd:cd06200    89 --------IGASVALRLRENPGFHLPDD-GRPLILIGNGTGLAGLRSHLRARAR-AGRHRN------WLLFGERQAAHDF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 586 LFREELRHFLKTGVLTHLKVSFSRDAapdgeeAPAKYVQDNLQRHSQQVaRTLLQENGYVYVCGDAKNMAKDVNDTLIGI 665
Cdd:cd06200   153 FCREELEAWQAAGHLARLDLAFSRDQ------AQKRYVQDRLRAAADEL-RAWVAEGAAIYVCGSLQGMAPGVDAVLDEI 225
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907093293 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 1907093293 448 PRPYSCASSSL---RHPDKLHFVFNIVEFPPSTTAaSLRKGVCTGWLATLVApflqpntdvsnvdsGDalapEIRISPRA 524
Cdd:cd06208    64 LRLYSIASSRYgddGDGKTLSLCVKRLVYTDPETD-ETKKGVCSNYLCDLKP--------------GD----DVQITGPV 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 525 TNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHRekLQEQHPDGKF-GAMWLFFGCRHKDrDYLFREELRHFLKT-GVLTH 602
Cdd:cd06208   125 GKTMLLPEDPNATLIMIATGTGIAPFRSFLRRL--FREKHADYKFtGLAWLFFGVPNSD-SLLYDDELEKYPKQyPDNFR 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 603 LKVSFSRDaaPDGEEAPAKYVQDNLQRHSQQVARTLLQENGYVYVCGdAKNMAKDVNDTLigiiSNEAGVDKLEAMKtLA 682
Cdd:cd06208   202 IDYAFSRE--QKNADGGKMYVQDRIAEYAEEIWNLLDKDNTHVYICG-LKGMEPGVDDAL----TSVAEGGLAWEEF-WE 273

                  ....*...
gi 1907093293 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 1907093293 484 KGVCTGWLATLvapflQPNTDVSnvdsgdalapeirISPRATNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQhrEKLQEQ 563
Cdd:PLN03115  182 KGVCSNFLCDL-----KPGAEVK-------------ITGPVGKEMLMPKDPNATIIMLATGTGIAPFRSFLW--KMFFEK 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 564 HPDGKF-GAMWLFFGCRHKDrDYLFREELRHfLKTGVLTHLKVSFSRDAAPDGEEAPAKYVQDNLQRHSQQVARTLLQEN 642
Cdd:PLN03115  242 HDDYKFnGLAWLFLGVPTSS-SLLYKEEFEK-MKEKAPENFRLDFAVSREQTNAKGEKMYIQTRMAEYAEELWELLKKDN 319
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907093293 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 1907093293   1 MRRFLLLYATQRGQAKAIAEEISEQAVSHGFSADL---HCISESEKYDLKTetgpLVMVVSTTGTGDPPDTARKFVKEIh 77
Cdd:PRK08105    1 MAKVGIFVGTVYGNALLVAEEAEAILTAQGHEVTLfedPELSDWQPYQDEL----VLVVTSTTGQGDLPDSIVPLFQAL- 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907093293  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 1907093293 448 PRPYSCASSslRHPDKLH------FVFNIVEFPPSTTAA-SLRKGVCTGWLAtlvapflqpntdvsNVDSGDalapEIRI 520
Cdd:PLN03116   81 VRLYSIAST--RYGDDFDgktaslCVRRAVYYDPETGKEdPAKKGVCSNFLC--------------DAKPGD----KVQI 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 521 SPRATNAFHLPE-DPSAPIIMVGPGTGVAPFVGFLqhREKLQEQHPDGKF-GAMWLFFGCRHKDRdYLFREELrhflkTG 598
Cdd:PLN03116  141 TGPSGKVMLLPEeDPNATHIMVATGTGIAPFRGFL--RRMFMEDVPAFKFgGLAWLFLGVANSDS-LLYDDEF-----ER 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 599 VLTHLKVSFSRDAAPDGEEAPAK----YVQDNLQRHSQQVArTLLQENGYVYVCGdAKNMAKDVNDTLIGiISNEAGVDK 674
Cdd:PLN03116  213 YLKDYPDNFRYDYALSREQKNKKggkmYVQDKIEEYSDEIF-KLLDNGAHIYFCG-LKGMMPGIQDTLKR-VAEERGESW 289
                         250
                  ....*....|....*.
gi 1907093293 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 1907093293  13 GQAKAIAEEISEQAVSHGFSADLHCISESEkyDLKTEtGPLVMVVSTTGTGDPPDTARKFVKEIHNKTLPtdyFAHLQYG 92
Cdd:PRK09004   13 GGAEYVADHLAEKLEEAGFSTETLHGPLLD--DLSAS-GLWLIVTSTHGAGDLPDNLQPFFEELQEQKPD---LSQVRFA 86
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907093293  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 1907093293 540 MVGPGTGVAPFVGFLQHRekLQEQHPDGKfgaMWLFFGCRHkDRDYLFREELRHFLKT--GVLTHLKVSFSRDAAPDGEE 617
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAI--LEDPKDPTQ---VVLVFGNRN-EDDILYREELDELAEKhpGRLTVVYVVSRPEAGWTGGK 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907093293 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 1907093293   1 MRRFLLLYATQRGQAKAIAEEISEQAVSHGFSADLHcISESEKYDLKTETGPLVMVVSTTGTGDPPDTARKFVKEIHNKT 80
Cdd:COG0716     1 MMKILIVYGSRTGNTEKVAEIIAEELGADGFEVDID-IRPGIKDDLLESYDELLLGTPTWGAGELPDDWYDFIEELEPID 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093293  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 1907093293 436 LSLLLEHLPKLQpRPYSCASsslrHPDKLHFVFNIVEFPpsttaaslrKGVCTGWLATLvapflQPntdvsnvdsGDala 515
Cdd:cd06195    33 LGLPNDDGKLVR-RAYSIAS----APYEENLEFYIILVP---------DGPLTPRLFKL-----KP---------GD--- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 516 pEIRISPRATNAFHLPEDPSAP-IIMVGPGTGVAPFVGFLQHREKLQeqhpdgKFGAMWLFFGCRHKDrDYLFREELRHF 594
Cdd:cd06195    82 -TIYVGKKPTGFLTLDEVPPGKrLWLLATGTGIAPFLSMLRDLEIWE------RFDKIVLVHGVRYAE-ELAYQDEIEAL 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907093293 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 1907093293 448 PRPYSCASsslrHPDKLHF-VFNIVEFPPsttaaslrkGVCTGWLATLVAPflqpntdvsnvdsGDALapeiRISPRATN 526
Cdd:cd06194    39 ARSYSPTS----LPDGDNElEFHIRRKPN---------GAFSGWLGEEARP-------------GHAL----RLQGPFGQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 527 AFHLPEDPSAPIIMVGPGTGVAPFVGFLqhREKLQEQHPdgkfGAMWLFFGCRHKDRDYLfREELRHF-LKTGVLTHLKV 605
Cdd:cd06194    89 AFYRPEYGEGPLLLVGAGTGLAPLWGIA--RAALRQGHQ----GEIRLVHGARDPDDLYL-HPALLWLaREHPNFRYIPC 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907093293 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 1907093293  53 LVMVVSTTGTGDPPDTARKFVKEIHNkTLPTDYFAhLQYGLLGLGDSEY-TYFCNGGKVIDKRLQELGAQRFYDTGHAD- 130
Cdd:PRK05723   51 LLAVTSTTGMGELPDNLMPLYSAIRD-QLPAAWRG-LPGAVIALGDSSYgDTFCGGGEQMRELFAELGVREVQPMLRLDa 128
                          90       100
                  ....*....|....*....|..
gi 1907093293 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 1907093293   5 LLLYATQRGQAKAIAEEISEQAVSHGFSADLHCISESEK---YDlktetgpLVMVVSTTGTGDPPDTARKFVKEiHNKTL 81
Cdd:pfam12724   1 LILYSSRDGQTKKIAERIAEELREEGELVDVEDVEAGEDlssYD-------AVVIGASIYYGKHLPELRKFVTK-HRDEL 72
                          90       100
                  ....*....|....*....|..
gi 1907093293  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 1907093293   1 MRRFLLLYATQRGQAKAIAEEISEQAVSHgfSADLHCISES-----EKYDLktetgpLVMVVSTTGTGDPPDTARKFVKE 75
Cdd:PRK09267    1 MAKIGIFFGSDTGNTEDIAKMIQKKLGKD--VADVVDIAKAskedfEAYDL------LILGIPTWGYGELQCDWDDFLPE 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907093293  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 1907093293 449 RPYSCASSSlrHPDKLHFVFNIVEfppsttaaslrKGVCTGWLATLVAPflqpntdvsnvdsGDALAPEiriSPRAtnAF 528
Cdd:cd06209    48 RSYSFSSAP--GDPRLEFLIRLLP-----------GGAMSSYLRDRAQP-------------GDRLTLT---GPLG--SF 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 529 HLpEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgkfgaMWLFFGCRHK------DRDYLFREELRHFlktgvlth 602
Cdd:cd06209    97 YL-REVKRPLLMLAGGTGLAPFLSMLDVLAEDGSAHP------VHLVYGVTRDadlvelDRLEALAERLPGF-------- 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907093293 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 1907093293 526 NAFHLPEDPSAPIIMVGPGTGVAPFVG----FLQHREklqeqhpdgKFGAMWLFFGCRHKDrDYLFREELRHFLKtgvLT 601
Cdd:cd06221    89 NGFPVEEMKGKDLLLVAGGLGLAPLRSlinyILDNRE---------DYGKVTLLYGARTPE-DLLFKEELKEWAK---RS 155
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907093293 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 1907093293 500 QPNTDVSN-----VDSGDalapEIRISPRATNaFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgkfgaMWL 574
Cdd:cd06184    78 EPGGLVSNylhdnVKVGD----VLEVSAPAGD-FVLDEASDRPLVLISAGVGITPMLSMLEALAAEGPGRP------VTF 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 575 FFGCRHKDrDYLFREELRHFLKTGVLTHLKVSFSRDAAPDGEEAPAKYVQDNLQRhsqqVARTLLQENGYVYVCGDAKNM 654
Cdd:cd06184   147 IHAARNSA-VHAFRDELEELAARLPNLKLHVFYSEPEAGDREEDYDHAGRIDLAL----LRELLLPADADFYLCGPVPFM 221
                         170       180
                  ....*....|....*....|
gi 1907093293 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 1907093293 442 HLPKLQPRPYSCASSSlRHPDKLHFVFNIVEfppsttaaslrKGVCTGWLATLvapflQPNTDVsnvdsgdalapEIRIs 521
Cdd:COG0543    45 RVPGGVRRPYSLASAP-DDKGELELHIRVYE-----------VGKVTKYIFGL-----KEGDKI-----------RVRG- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 522 PRATnaFHLPEDPSAPIIMVGPGTGVAPFVGFLQHrekLQEQhpdGKFGAMWLFFGCRHKDrDYLFREELRHFlkTGVLT 601
Cdd:COG0543    96 PLGN--GFLREKIGKPVLLIAGGTGIAPLYAIAKE---LKEK---GDANKVTLLYGARTAK-DLLLLDELEEL--AEKEV 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907093293 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 1907093293 511 GD---ALAPEIRISPRAT-----NAFHLPeDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHP-DgkfgamwLFFGCRhK 581
Cdd:cd06198    64 GDytrRLAERLKPGTRVTvegpyGRFTFD-DRRARQIWIAGGIGITPFLALLEALAARGDARPvT-------LFYCVR-D 134
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907093293 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 1907093293 507 NVDSGDalapEIRISPrATNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQhreKLQEQHPDgkfgAMWLFFGCRHKDrDYL 586
Cdd:COG1018    87 HLKVGD----TLEVSA-PAGDFVLDDLPERKLLLLAGGIGITPFLSMLR---TLLDRGPA----DVVLVHAARTPA-DLA 153

                  ....
gi 1907093293 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 1907093293 526 NAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHreklqEQHPDGKFGAMWLFFGCRHKdRDYLFREELRHFLKTGVLTHLKV 605
Cdd:PRK08345   99 NGFPVDEMEGMDLLLIAGGLGMAPLRSVLLY-----AMDNRWKYGNITLIYGAKYY-EDLLFYDELIKDLAEAENVKIIQ 172
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907093293 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 1907093293   1 MRRFLLLYATQRGQAKAIAEEISEQAVSHGFSADLHCISESEKYDLKTETGplVMVVSTT-GTGDPPDTARKFVKEIHNK 79
Cdd:PRK06703    1 MAKILIAYASMSGNTEDIADLIKVSLDAFDHEVVLQEMDGMDAEELLAYDG--IILGSYTwGDGDLPYEAEDFHEDLENI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907093293  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 1907093293 449 RPYSCASSslrhPDKLHFVfnivefppSTTAASLRKGVCTGWLATLVAPflqpntdvsnvdsGDALapEIRiSPRATnaF 528
Cdd:cd06217    51 RSYSIASS----PTQRGRV--------ELTVKRVPGGEVSPYLHDEVKV-------------GDLL--EVR-GPIGT--F 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 529 HLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgkfgaMWLFFGCRHKDrDYLFREELRHF-LKTGVLtHLKVSF 607
Cdd:cd06217   101 TWNPLHGDPVVLLAGGSGIVPLMSMIRYRRDLGWPVP------FRLLYSARTAE-DVIFRDELEQLaRRHPNL-HVTEAL 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907093293 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 1907093293 538 IIMVGPGTGVAPFVGFLQHRekLQEQHPDGKfgaMWLFFGCRHKDrDYLFREELRHFLKTGVlTHLKVSFSRDAAPDGEE 617
Cdd:cd06183   107 IGMIAGGTGITPMLQLIRAI--LKDPEDKTK---ISLLYANRTEE-DILLREELDELAKKHP-DRFKVHYVLSRPPEGWK 179
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907093293 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 1907093293 528 FHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgkfgaMWLFFGCRHKDRDYL------FREELRHFLKTGVLT 601
Cdd:PRK07609  197 FFLREDSDKPIVLLASGTGFAPIKSIVEHLRAKGIQRP------VTLYWGARRPEDLYLsalaeqWAEELPNFRYVPVVS 270
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907093293 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 1907093293 532 EDPSAPIIMVGPGT------GVAPFVGFLQHREKlqeqhpDGKFGAMWLFFGCRhKDRDYLFREELRHFLKTG---VLTH 602
Cdd:cd06196    90 EDPWGAIEYKGPGVfiaggaGITPFIAILRDLAA------KGKLEGNTLIFANK-TEKDIILKDELEKMLGLKfinVVTD 162
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093293 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 1907093293 528 FHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPdgkfgaMWLFFGCRHKDRDYL------FREELRHFLKTGVLT 601
Cdd:cd06189    91 FFLREDSDRPLILIAGGTGFAPIKSILEHLLAQGSKRP------IHLYWGARTEEDLYLdelleaWAEAHPNFTYVPVLS 164
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907093293 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 1907093293 528 FHLPEDPSAPIIMVGPGTGVAPFV----GFLQHREKlQEQHpdgkfgamwLFFGCRHK----DRDYLFREELRH--FLKT 597
Cdd:cd06187    91 FYLRRDHDRPVLCIAGGTGLAPLRaiveDALRRGEP-RPVH---------LFFGARTErdlyDLEGLLALAARHpwLRVV 160
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907093293 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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