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Conserved domains on  [gi|1402624270|ref|NP_001351369|]
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methionine synthase reductase [Homo sapiens]

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 ...
 277-697 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: 620.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 277 PISKAVQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQLEDKREHCVLLKIKADTKKKGATL 356
Cdd:cd06203     1 PISSAKKLTEGDDVKTVVDLTLDLSPTGFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVPNTKKKNAKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 357 PQHIPAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTSDSAEKRRLQELCSKQGAADYSRFVRDACACLLDLLLAFPSCQP 436
Cdd:cd06203    81 PVHIPKVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDFVRKRGLSLLDLLEAFPSCRP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 437 PLSLLLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEFLStattevlrKGVCTGWLALLVASVLQPNihashedsgkal 516
Cdd:cd06203   161 PLSLLIEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPA--------KGLCTSWLESLCLSASSHG------------ 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 517 aPKISISPRTTNSFHLP-DDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPDGNFGAMWLFFGCRHKDRDYLFRKELRH 595
Cdd:cd06203   221 -VKVPFYLRSSSRFRLPpDDLRRPIIMVGPGTGVAPFLGFLQHREKLKESHTETVFGEAWLFFGCRHRDRDYLFRDELEE 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 596 FLKHGILTHLKVSFSRDAPVGeeeAPAKYVQDNIQLHGQQVARILLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVE 675
Cdd:cd06203   300 FLEEGILTRLIVAFSRDENDG---STPKYVQDKLEERGKKLVDLLLNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGLD 376

                         410       420
                  ....*....|....*....|..
gi 1402624270 676 KLEAMKTLATLKEEKRYLQDIW 697
Cdd:cd06203   377 KLEAKKLLARLRKEDRYLEDVW 398
Flavodoxin_1 pfam00258
Flavodoxin;
6-142 6.25e-36

Flavodoxin;


:

Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 132.11  E-value: 6.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270   6 LLYATQQGQAKAIAEEICEQAVVHGFSADLHCISESDK-YDLKTETAPLVVVVSTTGTGDPPDTARKFVKEIQNQ-TLPV 83
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDDVDEtLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFgTLED 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1402624270  84 DFFAHLRYGLLGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADDC---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 ...
 277-697 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: 620.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 277 PISKAVQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQLEDKREHCVLLKIKADTKKKGATL 356
Cdd:cd06203     1 PISSAKKLTEGDDVKTVVDLTLDLSPTGFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVPNTKKKNAKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 357 PQHIPAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTSDSAEKRRLQELCSKQGAADYSRFVRDACACLLDLLLAFPSCQP 436
Cdd:cd06203    81 PVHIPKVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDFVRKRGLSLLDLLEAFPSCRP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 437 PLSLLLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEFLStattevlrKGVCTGWLALLVASVLQPNihashedsgkal 516
Cdd:cd06203   161 PLSLLIEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPA--------KGLCTSWLESLCLSASSHG------------ 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 517 aPKISISPRTTNSFHLP-DDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPDGNFGAMWLFFGCRHKDRDYLFRKELRH 595
Cdd:cd06203   221 -VKVPFYLRSSSRFRLPpDDLRRPIIMVGPGTGVAPFLGFLQHREKLKESHTETVFGEAWLFFGCRHRDRDYLFRDELEE 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 596 FLKHGILTHLKVSFSRDAPVGeeeAPAKYVQDNIQLHGQQVARILLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVE 675
Cdd:cd06203   300 FLEEGILTRLIVAFSRDENDG---STPKYVQDKLEERGKKLVDLLLNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGLD 376

                         410       420
                  ....*....|....*....|..
gi 1402624270 676 KLEAMKTLATLKEEKRYLQDIW 697
Cdd:cd06203   377 KLEAKKLLARLRKEDRYLEDVW 398
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
 2-697 1.33e-133

Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440138 [Multi-domain]  Cd Length: 561  Bit Score: 405.30  E-value: 1.33e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270   2 RRFLLLYATQQGQAKAIAEEICEQAVVHGFSADLHCISESDKYDLKTETApLVVVVSTTGTGDPPDTARKFVKEIQNQTL 81
Cdd:COG0369    27 TPLTILYGSQTGNAEGLAEQLAERAKAAGLAVTLASLDDYKPKDLAKEGL-LLIVTSTYGEGEPPDNARAFYEFLHSKKA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270  82 PVdfFAHLRYGLLGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADdcVGLELVVEPWIAGLWPALRKHFRSSRGQE 161
Cdd:COG0369   106 PK--LDGLRYAVLGLGDSSYETFCQTGKDFDARLEELGATRLLPRVDCD--VDYEEAAEAWLAAVLAALAEALGAAAAAA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 162 EISgalPVASPASSRTDLVKSELLHiesqvellrfddsgrkdsevlkqnavnsNQsnvviedfessltrsvpplsqasln 241
Cdd:COG0369   182 AAA---AAAAPAYSRKNPFPATVLE----------------------------NR------------------------- 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 242 ipglppeylqvhlqeslgqeesqvsvtsadpvfqvpiskavQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSD 321
Cdd:COG0369   206 -----------------------------------------ELTGRGSAKETRHIEIDLPGSGLSYEPGDALGVWPENDP 244

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 322 SEVQSLLQRLQLedKREHCVLLKikadtkkkGATLPqhipagcsLQFIFTWCLEIRAIPKKaFLRALVDYTsDSAEKRRL 401
Cdd:COG0369   245 ALVDELLARLGL--DGDEPVTLD--------GEPLS--------LREALTEHLELTRLTPP-LLEKYAELT-GNAELAAL 304

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 402 QELCSKQGAADYSR------FVRDacaclldlllaFPSCQPPLSLLLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEF 475
Cdd:COG0369   305 LADEDKAALREYLAgrqlldLLRE-----------FPAAELSAEELLELLRPLTPRLYSISSSPKAHPDEVHLTVGVVRY 373

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 476 lstATTEVLRKGVCTGWLALLvasvlqpnihasHEDSgkalapKISISPRTTNSFHLPDDPSIPIIMVGPGTGIAPFIGF 555
Cdd:COG0369   374 ---EASGRERKGVASTYLADL------------EEGD------TVPVFVEPNPNFRLPADPDTPIIMIGPGTGIAPFRAF 432

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 556 LQHREKLQEQhpdgnfGAMWLFFGCRHKDRDYLFRKELRHFLKHGILTHLKVSFSRDapvgeeEAPAKYVQDNIQLHGQQ 635
Cdd:COG0369   433 LQEREARGAS------GKNWLFFGDRHFTTDFLYQTELQAWLKDGVLTRLDLAFSRD------QAEKIYVQHRLLEQGAE 500

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1402624270 636 VARiLLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLEAMKTLATLKEEKRYLQDIW 697
Cdd:COG0369   501 LWA-WLEEGAHVYVCGDASRMAKDVDAALLDIIAEHGGLSEEEAEEYLAELRAEKRYQRDVY 561
cysJ TIGR01931
sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an ...
 2-697 1.20e-83

sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an NADPH-dependent sulfite reductase flavoprotein subunit. Most members of this family are found in Cys biosynthesis gene clusters. The closest homologs below the trusted cutoff are designated as subunits nitrate reductase.


Pssm-ID: 273882 [Multi-domain]  Cd Length: 597  Bit Score: 275.81  E-value: 1.20e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270   2 RRFLLLYATQQGQAKAIAEEICEQAVVHGFSADLhciSESDKY---DLKTETApLVVVVSTTGTGDPPDTARKFVKEIQN 78
Cdd:TIGR01931  59 KRVTILYGSQTGNARRLAKRLAEKLEAAGFSVRL---SSADDYkfkQLKKERL-LLLVISTQGEGEPPEEAISLHKFLHS 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270  79 QTLPVdfFAHLRYGLLGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADdcVGLELVVEPWIAGLWPALRKhfrssr 158
Cdd:TIGR01931 135 KKAPK--LENLRYSVLGLGDSSYEFFCQTGKDFDKRLEELGGKRLLPRVDAD--LDYDANAAEWRAGVLTALNE------ 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 159 gQEEISGALPVASPASsrtdlvksellhiesqvellrfddsgrkdsevlkqnavNSNQSNvviedfESSLTRSVPplsqa 238
Cdd:TIGR01931 205 -QAKGGASTPSASETS--------------------------------------TPLQTS------TSVYSKQNP----- 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 239 slnipgLPPEYLqvhlqeslgqeESQvsvtsadpvfqvpiskavQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICP 318
Cdd:TIGR01931 235 ------FRAEVL-----------ENQ------------------KITGRNSKKDVRHIEIDLEGSGLHYEPGDALGVWYK 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 319 NSDSEVQSLLQrlqledkrehcvLLKIKADTK--KKGATLPqhipagcslqfIFTWCLEIRAIPK--KAFLRALVDYTSD 394
Cdd:TIGR01931 280 NDPALVKEILK------------LLNLDPDEKvtIGGKTIP-----------LFEALITHFELTQntKPLLKAYAELTGN 336

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 395 S------AEKRRLQELCSKQGAADYSRFVrdacaclldlllafpscqpPLSL----LLEHLPKLQPRPYSCASSSLFHPG 464
Cdd:TIGR01931 337 KelkaliADNEKLKAYIQNTPLIDLIRDY-------------------PADLdaeqLISLLRPLTPRLYSISSSQSEVGD 397

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 465 KLHFVFNIVEFLSTATTevlRKGVCTGWLAllvaSVLQPnihashEDSgkalaPKISISPRttNSFHLPDDPSIPIIMVG 544
Cdd:TIGR01931 398 EVHLTVGVVRYQAHGRA---RLGGASGFLA----ERLKE------GDT-----VPVYIEPN--DNFRLPEDPDTPIIMIG 457

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 545 PGTGIAPFIGFLQHREKlqeqhpDGNFGAMWLFFGCRHKDRDYLFRKELRHFLKHGILTHLKVSFSRDapvgeeEAPAKY 624
Cdd:TIGR01931 458 PGTGVAPFRAFMQERAE------DGAKGKNWLFFGNPHFTTDFLYQVEWQNYLKKGVLTKMDLAFSRD------QAEKIY 525

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1402624270 625 VQDNIQLHGQQVARiLLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLEAMKTLATLKEEKRYLQDIW 697
Cdd:TIGR01931 526 VQHRIREQGAELWQ-WLQEGAHIYVCGDAKKMAKDVHQALLDIIAKEGHLDAEEAEEYLTDLRVEKRYQRDVY 597
PRK06214 PRK06214
sulfite reductase subunit alpha;
284-697 5.26e-66

sulfite reductase subunit alpha;


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 226.88  E-value: 5.26e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 284 LTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQledkrehcvllkIKADTKKKGATLPQHIPAG 363
Cdd:PRK06214  179 LNKPGSEKETWHVEIDLAGSGLDYEVGDSLGLFPANDPALVDAVIAALG------------APPEFPIGGKTLREALLED 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 364 CSLQfiftwcleirAIPKKAFlrALVDYTSDSAEKRRLQELCSKQ---GAADYsrfvrdacACLLDLLLAFPSCQPPLSL 440
Cdd:PRK06214  247 VSLG----------PAPDGLF--ELLSYITGGAARKKARALAAGEdpdGDAAT--------LDVLAALEKFPGIRPDPEA 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 441 LLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEFlstATTEVLRKGVCTGWLALLVA--SVLQPNIHASHedsgkalap 518
Cdd:PRK06214  307 FVEALDPLQPRLYSISSSPKATPGRVSLTVDAVRY---EIGSRLRLGVASTFLGERLApgTRVRVYVQKAH--------- 374

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 519 kisisprttnSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEqhPDGNfgamWLFFGCRHKDRDYLFRKELRHFLK 598
Cdd:PRK06214  375 ----------GFALPADPNTPIIMVGPGTGIAPFRAFLHERAATKA--PGRN----WLFFGHQRSATDFFYEDELNGLKA 438

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 599 HGILTHLKVSFSRDapvGEEEApakYVQDNIQLHGQQVARiLLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLE 678
Cdd:PRK06214  439 AGVLTRLSLAWSRD---GEEKT---YVQDRMRENGAELWK-WLEEGAHFYVCGDAKRMAKDVERALVDIVAQFGGRSPDE 511

                         410
                  ....*....|....*....
gi 1402624270 679 AMKTLATLKEEKRYLQDIW 697
Cdd:PRK06214  512 AVAFVAELKKAGRYQADVY 530
FAD_binding_1 pfam00667
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, ...
 273-492 1.82e-46

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


Pssm-ID: 395540 [Multi-domain]  Cd Length: 219  Bit Score: 164.05  E-value: 1.82e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 273 VFQVPISKAVQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQLEDKREHCVLLKIKADTKKK 352
Cdd:pfam00667   7 PFTAPVLSNRELTSPSSDRNCIHVELDISGSGLTYQTGDHLGVYPPNNEELVEELLERLGLDPKPDTVVLLKTLDERVKP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 353 GATLPqhipagCSLQFIFTWCLEIRAIPKKAFLRALVDYTSDSAEKRRLQELCSKQGAADYSRFVRDACACLLDLLLAFP 432
Cdd:pfam00667  87 PRLPP------TTYRQALKYYLDITGPPSKQLLRLLAQFAPEEEEKQRLEFLSSDAGAREYKRWKLNHAPTLLEVLEEFP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 433 SCQPPLSLLLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEFLSTATTEvLRKGVCTGW 492
Cdd:pfam00667 161 SVKLPADFLLTQLPQLQPRYYSISSSSKVHPNEVHLTVVVVEYETDGEGR-IHYGVCSNW 219
Flavodoxin_1 pfam00258
Flavodoxin;
6-142 6.25e-36

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 132.11  E-value: 6.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270   6 LLYATQQGQAKAIAEEICEQAVVHGFSADLHCISESDK-YDLKTETAPLVVVVSTTGTGDPPDTARKFVKEIQNQ-TLPV 83
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDDVDEtLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFgTLED 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1402624270  84 DFFAHLRYGLLGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADDC---VGLELVVEPW 142
Cdd:pfam00258  81 GDLSGLKYAVFGLGDSGYEGFCGAAKKLDEKLSELGASRVGPLGEGDEDpqeDGLEEAFEAW 142
PRK08105 PRK08105
flavodoxin; Provisional
 1-150 1.24e-16

flavodoxin; Provisional


Pssm-ID: 181230 [Multi-domain]  Cd Length: 149  Bit Score: 77.23  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270   1 MRRFLLLYATQQGQAKAIAEEICEQAVVHGFSADL---HCISESDKYDLKTetapLVVVVSTTGTGDPPDTARKFVKEIQ 77
Cdd:PRK08105    1 MAKVGIFVGTVYGNALLVAEEAEAILTAQGHEVTLfedPELSDWQPYQDEL----VLVVTSTTGQGDLPDSIVPLFQALK 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1402624270  78 NQtlpVDFFAHLRYGLLGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADDCVGLELVVE--PWIAGlWPAL 150
Cdd:PRK08105   77 DT---AGYQPNLRYGVIALGDSSYDNFCGAGKQFDALLQEQGAKRVGERLEIDACETPEPEVEanPWVEQ-WGTL 147
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
 5-146 1.79e-12

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


Pssm-ID: 440480 [Multi-domain]  Cd Length: 135  Bit Score: 64.92  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270   5 LLLYATQQGQAKAIAEEICEQAVVHGfsADLHCISESDKYDLKTETApLVVVVSTTGtGDPPDTARKFVKEIQNQtlpvd 84
Cdd:COG0716     2 LIVYGSTTGNTEKVAEAIAEALGAAG--VDLFEIEDADLDDLEDYDL-LILGTPTWA-GELPDDWEDFLEELKED----- 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1402624270  85 fFAHLRYGLLGLGDSEytYFCNGGKIIDKRLQELGAR--HFYDTGH--ADDCVGLELVVEPWIAGL 146
Cdd:COG0716    73 -LSGKKVALFGTGDSS--GYGDALGELKELLEEKGAKvvGGYDFEGskAPDAEDTEERAEEWLKQL 135
 
Name Accession Description Interval E-value
methionine_synthase_red cd06203
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ...
 277-697 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: 620.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 277 PISKAVQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQLEDKREHCVLLKIKADTKKKGATL 356
Cdd:cd06203     1 PISSAKKLTEGDDVKTVVDLTLDLSPTGFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVPNTKKKNAKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 357 PQHIPAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTSDSAEKRRLQELCSKQGAADYSRFVRDACACLLDLLLAFPSCQP 436
Cdd:cd06203    81 PVHIPKVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDFVRKRGLSLLDLLEAFPSCRP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 437 PLSLLLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEFLStattevlrKGVCTGWLALLVASVLQPNihashedsgkal 516
Cdd:cd06203   161 PLSLLIEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPA--------KGLCTSWLESLCLSASSHG------------ 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 517 aPKISISPRTTNSFHLP-DDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPDGNFGAMWLFFGCRHKDRDYLFRKELRH 595
Cdd:cd06203   221 -VKVPFYLRSSSRFRLPpDDLRRPIIMVGPGTGVAPFLGFLQHREKLKESHTETVFGEAWLFFGCRHRDRDYLFRDELEE 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 596 FLKHGILTHLKVSFSRDAPVGeeeAPAKYVQDNIQLHGQQVARILLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVE 675
Cdd:cd06203   300 FLEEGILTRLIVAFSRDENDG---STPKYVQDKLEERGKKLVDLLLNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGLD 376

                         410       420
                  ....*....|....*....|..
gi 1402624270 676 KLEAMKTLATLKEEKRYLQDIW 697
Cdd:cd06203   377 KLEAKKLLARLRKEDRYLEDVW 398
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
 2-697 1.33e-133

Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440138 [Multi-domain]  Cd Length: 561  Bit Score: 405.30  E-value: 1.33e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270   2 RRFLLLYATQQGQAKAIAEEICEQAVVHGFSADLHCISESDKYDLKTETApLVVVVSTTGTGDPPDTARKFVKEIQNQTL 81
Cdd:COG0369    27 TPLTILYGSQTGNAEGLAEQLAERAKAAGLAVTLASLDDYKPKDLAKEGL-LLIVTSTYGEGEPPDNARAFYEFLHSKKA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270  82 PVdfFAHLRYGLLGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADdcVGLELVVEPWIAGLWPALRKHFRSSRGQE 161
Cdd:COG0369   106 PK--LDGLRYAVLGLGDSSYETFCQTGKDFDARLEELGATRLLPRVDCD--VDYEEAAEAWLAAVLAALAEALGAAAAAA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 162 EISgalPVASPASSRTDLVKSELLHiesqvellrfddsgrkdsevlkqnavnsNQsnvviedfessltrsvpplsqasln 241
Cdd:COG0369   182 AAA---AAAAPAYSRKNPFPATVLE----------------------------NR------------------------- 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 242 ipglppeylqvhlqeslgqeesqvsvtsadpvfqvpiskavQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSD 321
Cdd:COG0369   206 -----------------------------------------ELTGRGSAKETRHIEIDLPGSGLSYEPGDALGVWPENDP 244

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 322 SEVQSLLQRLQLedKREHCVLLKikadtkkkGATLPqhipagcsLQFIFTWCLEIRAIPKKaFLRALVDYTsDSAEKRRL 401
Cdd:COG0369   245 ALVDELLARLGL--DGDEPVTLD--------GEPLS--------LREALTEHLELTRLTPP-LLEKYAELT-GNAELAAL 304

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 402 QELCSKQGAADYSR------FVRDacaclldlllaFPSCQPPLSLLLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEF 475
Cdd:COG0369   305 LADEDKAALREYLAgrqlldLLRE-----------FPAAELSAEELLELLRPLTPRLYSISSSPKAHPDEVHLTVGVVRY 373

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 476 lstATTEVLRKGVCTGWLALLvasvlqpnihasHEDSgkalapKISISPRTTNSFHLPDDPSIPIIMVGPGTGIAPFIGF 555
Cdd:COG0369   374 ---EASGRERKGVASTYLADL------------EEGD------TVPVFVEPNPNFRLPADPDTPIIMIGPGTGIAPFRAF 432

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 556 LQHREKLQEQhpdgnfGAMWLFFGCRHKDRDYLFRKELRHFLKHGILTHLKVSFSRDapvgeeEAPAKYVQDNIQLHGQQ 635
Cdd:COG0369   433 LQEREARGAS------GKNWLFFGDRHFTTDFLYQTELQAWLKDGVLTRLDLAFSRD------QAEKIYVQHRLLEQGAE 500

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1402624270 636 VARiLLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLEAMKTLATLKEEKRYLQDIW 697
Cdd:COG0369   501 LWA-WLEEGAHVYVCGDASRMAKDVDAALLDIIAEHGGLSEEEAEEYLAELRAEKRYQRDVY 561
CYPOR cd06204
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 269-697 4.08e-113

NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99801 [Multi-domain]  Cd Length: 416  Bit Score: 347.32  E-value: 4.08e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 269 SADPVFQVPISKAVQLTTNdAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQLEDKREhcvLLKIKAD 348
Cdd:cd06204     1 DAKNPFLAPVAVSRELFTG-SDRSCLHIEFDISGSGIRYQTGDHLAVWPTNPSEEVERLLKVLGLDDRDT---VISLKSL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 349 tkKKGATLPQHIPAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTSDSAEKRRLQELCSkQGAADYSRFVRDACACLLDLL 428
Cdd:cd06204    77 --DEPASKKVPFPCPTTYRTALRHYLDITAPVSRQVLAALAQFAPDPEEKERLLKLAS-EGKDEYAKWIVEPHRNLLEVL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 429 LAFPSCQ---PPLSLLLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEFLSTATTEVlrKGVCTGWL---ALLVASVLQ 502
Cdd:cd06204   154 QDFPSAKptpPPFDFLIELLPRLQPRYYSISSSSKVHPNRIHITAVVVKYPTPTGRII--KGVATNWLlalKPALNGEKP 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 503 PNIHASHEDSGKALAPKISISPRTTNsFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPDgnFGAMWLFFGCRH 582
Cdd:cd06204   232 PTPYYLSGPRKKGGGSKVPVFVRRSN-FRLPTKPSTPVIMIGPGTGVAPFRGFIQERAALKESGKK--VGPTLLFFGCRH 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 583 KDRDYLFRKELRHFLKHGILTHLKVSFSRdapvgeEEAPAKYVQDNIQLHGQQVARiLLQENGHIYVCGDAKNMAKDVHD 662
Cdd:cd06204   309 PDEDFIYKDELEEYAKLGGLLELVTAFSR------EQPKKVYVQHRLAEHAEQVWE-LINEGAYIYVCGDAKNMARDVEK 381

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1402624270 663 ALVQIISKEVGVEKLEAMKTLATLKEEKRYLQDIW 697
Cdd:cd06204   382 TLLEILAEQGGMTETEAEEYVKKLKTRGRYQEDVW 416
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 436-697 1.34e-103

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: 316.97  E-value: 1.34e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 436 PPLSLLLEHLP-KLQPRPYSCASSSLFHPGKLHFVFNIVEFLSTATteVLRKGVCTGWLALLVasvlqpnihashedsgk 514
Cdd:cd06182    33 QPGDHLGVIPPnPLQPRYYSIASSPDVDPGEVHLCVRVVSYEAPAG--RIRKGVCSNFLAGLQ----------------- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 515 aLAPKISISPRTTNSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQeqHPDGNFGAMWLFFGCRHKDRDYLFRKELR 594
Cdd:cd06182    94 -LGAKVTVFIRPAPSFRLPKDPTTPIIMVGPGTGIAPFRGFLQERAALR--ANGKARGPAWLFFGCRNFASDYLYREELQ 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 595 HFLKHGILTHLKVSFSRDAPVgeeeaPAKYVQDNIQLHGQQVARiLLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGV 674
Cdd:cd06182   171 EALKDGALTRLDVAFSREQAE-----PKVYVQDKLKEHAEELRR-LLNEGAHIYVCGDAKSMAKDVEDALVKIIAKAGGV 244

                         250       260
                  ....*....|....*....|...
gi 1402624270 675 EKLEAMKTLATLKEEKRYLQDIW 697
Cdd:cd06182   245 DESDAEEYLKELEDEGRYVEDVW 267
CyPoR_like cd06207
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 277-697 2.11e-98

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: 307.66  E-value: 2.11e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 277 PISKAVQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQLEDKrehcVLLKIKADTKKKGAtl 356
Cdd:cd06207     1 KVTENKRLTPADYDRSTRHIEFDLGGSGLSYETGDNLGIYPENSDALVDEFLARLGLDGD----DVVRVEPNEQQRGK-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 357 pQHIPAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTSDSAEKRRLQELCSKQGAADYSRFVRDACACLLDLllaFPSCQP 436
Cdd:cd06207    75 -PPFPEPISVRQLLKKFLDIFGKPTKKFLKLLSQLATDEEEKEDLYKLASREGRTEYKRYEKYTYLEVLKD---FPSVRP 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 437 PLSLLLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEFLSTATTEvlRKGVCTGWLALLVAsvlQPNIHASHEDSgkal 516
Cdd:cd06207   151 TLEQLLELCPLIKPRYYSISSSPLKNPNEVHLLVSLVSWKTPSGRS--RYGLCSSYLAGLKV---GQRVTVFIKKS---- 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 517 apkisisprttnSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPdgNFGAMWLFFGCRHKDRDYLFRKELRHF 596
Cdd:cd06207   222 ------------SFKLPKDPKKPIIMVGPGTGLAPFRAFLQERAALLAQGP--EIGPVLLYFGCRHEDKDYLYKEELEEY 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 597 LKHGILTHLKVSFSRDAPvgeeeaPAKYVQDNIQLHGQQVARILLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEK 676
Cdd:cd06207   288 EKSGVLTTLGTAFSRDQP------KKVYVQDLIRENSDLVYQLLEEGAGVIYVCGSTWKMPPDVQEAFEEILKKHGGGDE 361

                         410       420
                  ....*....|....*....|.
gi 1402624270 677 LEAMKTLATLKEEKRYLQDIW 697
Cdd:cd06207   362 ELAEKKIEELEERGRYVVEAW 382
Nitric_oxide_synthase cd06202
The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses ...
 283-696 6.17e-88

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: 281.53  E-value: 6.17e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 283 QLTTNDAIKTTLLVELDISNTD-FSYQPGDAFSVICPNSDSEVQSLLQRLQLEDKREHCVLLKIKADTK-----KKGATL 356
Cdd:cd06202     7 NLQSPKSSRSTILVKLDTNGAQeLHYQPGDHVGIFPANRPELVDALLDRLHDAPPPDQVIKLEVLEERStalgiIKTWTP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 357 PQHIPAgCSLQFIFTWCLEIRAIPKKAFLRALVDYTSDSAEKRRLQELCskQGAADYSRFVRDACACLLDLLLAFPSCQP 436
Cdd:cd06202    87 HERLPP-CTLRQALTRYLDITTPPTPQLLQLLATLATDEKDKERLEVLG--KGSSEYEDWKWYKNPNILEVLEEFPSLQV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 437 PLSLLLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEFLSTATTEVLRKGVCTGWLallvaSVLQPNIHAshedsgkal 516
Cdd:cd06202   164 PASLLLTQLPLLQPRYYSISSSPDMYPGEIHLTVAVVSYRTRDGQGPVHHGVCSTWL-----NGLTPGDTV--------- 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 517 apkisisP---RTTNSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHR--EKLQEQHPDGNFGAMWLFFGCRHKDRDYLFRK 591
Cdd:cd06202   230 -------PcfvRSAPSFHLPEDPSVPVIMVGPGTGIAPFRSFWQQRqyDLRMSEDPGKKFGDMTLFFGCRNSTIDDIYKE 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 592 ELRHFLKHGILTHLKVSFSRdapvgEEEAPAKYVQDNIQLHGQQVARILLQENGHIYVCGDAkNMAKDVHDALVQIISKE 671
Cdd:cd06202   303 ETEEAKNKGVLTEVYTALSR-----EPGKPKTYVQDLLKEQAESVYDALVREGGHIYVCGDV-TMAEDVSQTIQRILAEH 376

                         410       420
                  ....*....|....*....|....*
gi 1402624270 672 VGVEKLEAMKTLATLKEEKRYLQDI 696
Cdd:cd06202   377 GNMSAEEAEEFILKLRDENRYHEDI 401
SiR cd06199
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 283-697 2.71e-86

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: 275.26  E-value: 2.71e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 283 QLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQLedKREHCVllkikadTKKKGATLPqhipa 362
Cdd:cd06199     7 LLTGPGSEKETRHIELDLEGSGLSYEPGDALGVYPTNDPALVDELLAALGL--SGDEPV-------STVGGGTLP----- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 363 gcsLQFIFTWCLEIRaipkKAFLRALVDYTSDSAEkrrlQELCSKQGAADYSRF--VRDACACLLDLLLAFPSCQpplsl 440
Cdd:cd06199    73 ---LREALIKHYEIT----TLLLALLESYAADTGA----LELLALAALEAVLAFaeLRDVLDLLPIPPARLTAEE----- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 441 LLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEFLSTATTevlRKGVCTGWLALLVAsvlqpnihashedsgkaLAPKI 520
Cdd:cd06199   137 LLDLLRPLQPRLYSIASSPKAVPDEVHLTVAVVRYESHGRE---RKGVASTFLADRLK-----------------EGDTV 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 521 SISPRTTNSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREklQEQHPdgnfGAMWLFFGCRHKDRDYLFRKELRHFLKHG 600
Cdd:cd06199   197 PVFVQPNPHFRLPEDPDAPIIMVGPGTGIAPFRAFLQERE--ATGAK----GKNWLFFGERHFATDFLYQDELQQWLKDG 270

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 601 ILTHLKVSFSRDapvGEEEApakYVQDNIQLHGQQVARiLLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLEAM 680
Cdd:cd06199   271 VLTRLDTAFSRD---QAEKV---YVQDRMREQGAELWA-WLEEGAHFYVCGDAKRMAKDVDAALLDIIATEGGMDEEEAE 343

                         410
                  ....*....|....*..
gi 1402624270 681 KTLATLKEEKRYLQDIW 697
Cdd:cd06199   344 AYLKELKKEKRYQRDVY 360
cysJ TIGR01931
sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an ...
 2-697 1.20e-83

sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an NADPH-dependent sulfite reductase flavoprotein subunit. Most members of this family are found in Cys biosynthesis gene clusters. The closest homologs below the trusted cutoff are designated as subunits nitrate reductase.


Pssm-ID: 273882 [Multi-domain]  Cd Length: 597  Bit Score: 275.81  E-value: 1.20e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270   2 RRFLLLYATQQGQAKAIAEEICEQAVVHGFSADLhciSESDKY---DLKTETApLVVVVSTTGTGDPPDTARKFVKEIQN 78
Cdd:TIGR01931  59 KRVTILYGSQTGNARRLAKRLAEKLEAAGFSVRL---SSADDYkfkQLKKERL-LLLVISTQGEGEPPEEAISLHKFLHS 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270  79 QTLPVdfFAHLRYGLLGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADdcVGLELVVEPWIAGLWPALRKhfrssr 158
Cdd:TIGR01931 135 KKAPK--LENLRYSVLGLGDSSYEFFCQTGKDFDKRLEELGGKRLLPRVDAD--LDYDANAAEWRAGVLTALNE------ 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 159 gQEEISGALPVASPASsrtdlvksellhiesqvellrfddsgrkdsevlkqnavNSNQSNvviedfESSLTRSVPplsqa 238
Cdd:TIGR01931 205 -QAKGGASTPSASETS--------------------------------------TPLQTS------TSVYSKQNP----- 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 239 slnipgLPPEYLqvhlqeslgqeESQvsvtsadpvfqvpiskavQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICP 318
Cdd:TIGR01931 235 ------FRAEVL-----------ENQ------------------KITGRNSKKDVRHIEIDLEGSGLHYEPGDALGVWYK 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 319 NSDSEVQSLLQrlqledkrehcvLLKIKADTK--KKGATLPqhipagcslqfIFTWCLEIRAIPK--KAFLRALVDYTSD 394
Cdd:TIGR01931 280 NDPALVKEILK------------LLNLDPDEKvtIGGKTIP-----------LFEALITHFELTQntKPLLKAYAELTGN 336

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 395 S------AEKRRLQELCSKQGAADYSRFVrdacaclldlllafpscqpPLSL----LLEHLPKLQPRPYSCASSSLFHPG 464
Cdd:TIGR01931 337 KelkaliADNEKLKAYIQNTPLIDLIRDY-------------------PADLdaeqLISLLRPLTPRLYSISSSQSEVGD 397

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 465 KLHFVFNIVEFLSTATTevlRKGVCTGWLAllvaSVLQPnihashEDSgkalaPKISISPRttNSFHLPDDPSIPIIMVG 544
Cdd:TIGR01931 398 EVHLTVGVVRYQAHGRA---RLGGASGFLA----ERLKE------GDT-----VPVYIEPN--DNFRLPEDPDTPIIMIG 457

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 545 PGTGIAPFIGFLQHREKlqeqhpDGNFGAMWLFFGCRHKDRDYLFRKELRHFLKHGILTHLKVSFSRDapvgeeEAPAKY 624
Cdd:TIGR01931 458 PGTGVAPFRAFMQERAE------DGAKGKNWLFFGNPHFTTDFLYQVEWQNYLKKGVLTKMDLAFSRD------QAEKIY 525

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1402624270 625 VQDNIQLHGQQVARiLLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLEAMKTLATLKEEKRYLQDIW 697
Cdd:TIGR01931 526 VQHRIREQGAELWQ-WLQEGAHIYVCGDAKKMAKDVHQALLDIIAKEGHLDAEEAEEYLTDLRVEKRYQRDVY 597
PRK06214 PRK06214
sulfite reductase subunit alpha;
284-697 5.26e-66

sulfite reductase subunit alpha;


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 226.88  E-value: 5.26e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 284 LTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQledkrehcvllkIKADTKKKGATLPQHIPAG 363
Cdd:PRK06214  179 LNKPGSEKETWHVEIDLAGSGLDYEVGDSLGLFPANDPALVDAVIAALG------------APPEFPIGGKTLREALLED 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 364 CSLQfiftwcleirAIPKKAFlrALVDYTSDSAEKRRLQELCSKQ---GAADYsrfvrdacACLLDLLLAFPSCQPPLSL 440
Cdd:PRK06214  247 VSLG----------PAPDGLF--ELLSYITGGAARKKARALAAGEdpdGDAAT--------LDVLAALEKFPGIRPDPEA 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 441 LLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEFlstATTEVLRKGVCTGWLALLVA--SVLQPNIHASHedsgkalap 518
Cdd:PRK06214  307 FVEALDPLQPRLYSISSSPKATPGRVSLTVDAVRY---EIGSRLRLGVASTFLGERLApgTRVRVYVQKAH--------- 374

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 519 kisisprttnSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEqhPDGNfgamWLFFGCRHKDRDYLFRKELRHFLK 598
Cdd:PRK06214  375 ----------GFALPADPNTPIIMVGPGTGIAPFRAFLHERAATKA--PGRN----WLFFGHQRSATDFFYEDELNGLKA 438

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 599 HGILTHLKVSFSRDapvGEEEApakYVQDNIQLHGQQVARiLLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLE 678
Cdd:PRK06214  439 AGVLTRLSLAWSRD---GEEKT---YVQDRMRENGAELWK-WLEEGAHFYVCGDAKRMAKDVERALVDIVAQFGGRSPDE 511

                         410
                  ....*....|....*....
gi 1402624270 679 AMKTLATLKEEKRYLQDIW 697
Cdd:PRK06214  512 AVAFVAELKKAGRYQADVY 530
cysJ PRK10953
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
6-697 1.40e-63

NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;


Pssm-ID: 182862 [Multi-domain]  Cd Length: 600  Bit Score: 222.29  E-value: 1.40e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270   6 LLYATQQGQAKAIAEEICEQAVVHGFSADLhcISESDkYDLK--TETAPLVVVVSTTGTGDPPDTARKFVKEIQNQTLPV 83
Cdd:PRK10953   66 LISASQTGNARRVAEQLRDDLLAAKLNVNL--VNAGD-YKFKqiAQEKLLIVVTSTQGEGEPPEEAVALHKFLFSKKAPK 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270  84 dfFAHLRYGLLGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADdcVGLELVVEPWIAGLwpalrkhfrssrgqeei 163
Cdd:PRK10953  143 --LENTAFAVFGLGDTSYEFFCQAGKDFDSKLAELGAERLLDRVDAD--VEYQAAASEWRARV----------------- 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 164 sgalpvaspassrTDLVKSELLHIESQVEllrfddsgrkdsevlkqnavnSNQSNVVIEDFESSLTRSVPpLSqASLnip 243
Cdd:PRK10953  202 -------------VDALKSRAPAVAAPSQ---------------------SVATGAVNEIHTSPYSKEAP-LT-ASL--- 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 244 glppeylqvhlqeSLGQeesqvsvtsadpvfqvpiskavQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSE 323
Cdd:PRK10953  243 -------------SVNQ----------------------KITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPAL 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 324 VQSLLQrlqledkrehcvLLKIKAD--TKKKGATLPqhipagcsLQFIFTWCLEIR-----------AIPKKAFLRALVd 390
Cdd:PRK10953  288 VKELVE------------LLWLKGDepVTVDGKTLP--------LAEALQWHFELTvntanivenyaTLTRSETLLPLV- 346

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 391 ytsdsAEKRRLQELCSKQGAADYSRFvrdacaclldlllaFPScQPPLSLLLEHLPKLQPRPYSCASSSLFHPGKLHFVF 470
Cdd:PRK10953  347 -----GDKAALQHYAATTPIVDMVRF--------------APA-QLDAEQLIGLLRPLTPRLYSIASSQAEVENEVHITV 406

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 471 NIVEFlstattEV---LRKGVCTGWLALLVASVLQPNIHASHEDSgkalapkisisprttnsFHLPDDPSIPIIMVGPGT 547
Cdd:PRK10953  407 GVVRY------DIegrARAGGASSFLADRLEEEGEVRVFIEHNDN-----------------FRLPANPETPVIMIGPGT 463

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 548 GIAPFIGFLQHREKlqeqhpDGNFGAMWLFFGCRHKDRDYLFRKELRHFLKHGILTHLKVSFSRDapvgeeEAPAKYVQD 627
Cdd:PRK10953  464 GIAPFRAFMQQRAA------DGAPGKNWLFFGNPHFTEDFLYQVEWQRYVKEGLLTRIDLAWSRD------QKEKIYVQD 531

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 628 NIQLHGQQVARiLLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLEAMKTLATLKEEKRYLQDIW 697
Cdd:PRK10953  532 KLREQGAELWR-WINDGAHIYVCGDANRMAKDVEQALLEVIAEFGGMDTEAADEFLSELRVERRYQRDVY 600
bifunctional_CYPOR cd06206
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ...
 304-697 3.49e-63

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: 215.20  E-value: 3.49e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 304 DFSYQPGDAFSVICPNSDSEVQSLLQRLQLEDKRehcvLLKIKADTKKKGATLPQHIPAGcslqFIFTWCLEIRAIPKKA 383
Cdd:cd06206    27 GMTYRAGDYLAVLPRNPPELVRRALRRFGLAWDT----VLTISASGSATGLPLGTPISVS----ELLSSYVELSQPATRR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 384 FLRALVDYTSDSaEKRRLQELCSKQGaadYSRFVRDACACLLDLLLAFPSCQPPLSLLLEHLPKLQPRPYSCASSSLFHP 463
Cdd:cd06206    99 QLAALAEATRCP-DTKALLERLAGEA---YAAEVLAKRVSVLDLLERFPSIALPLATFLAMLPPMRPRQYSISSSPLVDP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 464 GKLHFVFNIVEFlSTATTEVLRKGVCTGWLallvaSVLQPNIHashedsgkalapkISISPRTTNS-FHLPDDPSIPIIM 542
Cdd:cd06206   175 GHATLTVSVLDA-PALSGQGRYRGVASSYL-----SSLRPGDS-------------IHVSVRPSHSaFRPPSDPSTPLIM 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 543 VGPGTGIAPFIGFLQHREKLQEQhpDGNFGAMWLFFGCRHKDRDYLFRKELRHFLKHGILThLKVSFSRDApvgeeEAPA 622
Cdd:cd06206   236 IAAGTGLAPFRGFLQERAALLAQ--GRKLAPALLFFGCRHPDHDDLYRDELEEWEAAGVVS-VRRAYSRPP-----GGGC 307

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1402624270 623 KYVQDNIQLHGQQVARiLLQENGHIYVCGDAKnMAKDVHDALVQIISKEV----GVEKLEAMKTLATLKEEKRYLQDIW 697
Cdd:cd06206   308 RYVQDRLWAEREEVWE-LWEQGARVYVCGDGR-MAPGVREVLKRIYAEKDerggGSDDEEAEEWLEELRNKGRYATDVF 384
FAD_binding_1 pfam00667
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, ...
 273-492 1.82e-46

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


Pssm-ID: 395540 [Multi-domain]  Cd Length: 219  Bit Score: 164.05  E-value: 1.82e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 273 VFQVPISKAVQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQLEDKREHCVLLKIKADTKKK 352
Cdd:pfam00667   7 PFTAPVLSNRELTSPSSDRNCIHVELDISGSGLTYQTGDHLGVYPPNNEELVEELLERLGLDPKPDTVVLLKTLDERVKP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 353 GATLPqhipagCSLQFIFTWCLEIRAIPKKAFLRALVDYTSDSAEKRRLQELCSKQGAADYSRFVRDACACLLDLLLAFP 432
Cdd:pfam00667  87 PRLPP------TTYRQALKYYLDITGPPSKQLLRLLAQFAPEEEEKQRLEFLSSDAGAREYKRWKLNHAPTLLEVLEEFP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 433 SCQPPLSLLLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEFLSTATTEvLRKGVCTGW 492
Cdd:pfam00667 161 SVKLPADFLLTQLPQLQPRYYSISSSSKVHPNEVHLTVVVVEYETDGEGR-IHYGVCSNW 219
Flavodoxin_1 pfam00258
Flavodoxin;
6-142 6.25e-36

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 132.11  E-value: 6.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270   6 LLYATQQGQAKAIAEEICEQAVVHGFSADLHCISESDK-YDLKTETAPLVVVVSTTGTGDPPDTARKFVKEIQNQ-TLPV 83
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDDVDEtLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFgTLED 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1402624270  84 DFFAHLRYGLLGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADDC---VGLELVVEPW 142
Cdd:pfam00258  81 GDLSGLKYAVFGLGDSGYEGFCGAAKKLDEKLSELGASRVGPLGEGDEDpqeDGLEEAFEAW 142
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 438-667 1.71e-31

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: 122.56  E-value: 1.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 438 LSLLLEHLPKLQPRPYSCASSSlFHPGKLHFVFNIVEflstattevlrKGVCTGWLALLvasvlqpnihashedsgkALA 517
Cdd:cd00322    29 VDLHLPGDGRGLRRAYSIASSP-DEEGELELTVKIVP-----------GGPFSAWLHDL------------------KPG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 518 PKISISPRTtNSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPdgnfgaMWLFFGCRHKDrDYLFRKELRHFL 597
Cdd:cd00322    79 DEVEVSGPG-GDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGE------ITLLYGARTPA-DLLFLDELEELA 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 598 KHGILTHLKVSFSRDAPVGEEEAPAKYVQDNIQlhgqqvARILLQENGHIYVCGDAkNMAKDVHDALVQI 667
Cdd:cd00322   151 KEGPNFRLVLALSRESEAKLGPGGRIDREAEIL------ALLPDDSGALVYICGPP-AMAKAVREALVSL 213
SiR_like1 cd06200
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 441-697 5.50e-30

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: 118.92  E-value: 5.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 441 LLEHLPK--LQPRPYSCASssLFHPGKLHFVfnivefLSTATTEVLRKGVCTGWLALlvasvlqpniHAshedsgkALAP 518
Cdd:cd06200    37 IAEIGPRhpLPHREYSIAS--LPADGALELL------VRQVRHADGGLGLGSGWLTR----------HA-------PIGA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 519 KISISPRTTNSFHLPDDPSiPIIMVGPGTGIAPFIGFLQHREKlQEQHPDgnfgamWLFFGCRHKDRDYLFRKELRHFLK 598
Cdd:cd06200    92 SVALRLRENPGFHLPDDGR-PLILIGNGTGLAGLRSHLRARAR-AGRHRN------WLLFGERQAAHDFFCREELEAWQA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 599 HGILTHLKVSFSRDAPVGeeeapaKYVQDNIQLHGQQVaRILLQENGHIYVCGDAKNMAKDVHDALVQIIskevGVEKLE 678
Cdd:cd06200   164 AGHLARLDLAFSRDQAQK------RYVQDRLRAAADEL-RAWVAEGAAIYVCGSLQGMAPGVDAVLDEIL----GEEAVE 232

                         250
                  ....*....|....*....
gi 1402624270 679 AmktlatLKEEKRYLQDIW 697
Cdd:cd06200   233 A------LLAAGRYRRDVY 245
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 450-692 1.01e-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: 113.57  E-value: 1.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 450 PRPYSCASSSL---FHPGKLHFVFNIVEFLSTATTEVlRKGVCTGWLallvasvlqpnihashedsgKALAP--KISISP 524
Cdd:cd06208    64 LRLYSIASSRYgddGDGKTLSLCVKRLVYTDPETDET-KKGVCSNYL--------------------CDLKPgdDVQITG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 525 RTTNSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHRekLQEQHPDGNF-GAMWLFFGCRHKDrDYLFRKELRHFLK-HGIL 602
Cdd:cd06208   123 PVGKTMLLPEDPNATLIMIATGTGIAPFRSFLRRL--FREKHADYKFtGLAWLFFGVPNSD-SLLYDDELEKYPKqYPDN 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 603 THLKVSFSRDAPvgEEEAPAKYVQDNIQLHGQQVARILLQENGHIYVCGdAKNMAKDVHDALVQIiskevgVEKLEAMKT 682
Cdd:cd06208   200 FRIDYAFSREQK--NADGGKMYVQDRIAEYAEEIWNLLDKDNTHVYICG-LKGMEPGVDDALTSV------AEGGLAWEE 270

                         250
                  ....*....|.
gi 1402624270 683 -LATLKEEKRY 692
Cdd:cd06208   271 fWESLKKKGRW 281
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 450-697 1.76e-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: 99798 [Multi-domain]  Cd Length: 289  Bit Score: 112.81  E-value: 1.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 450 PRPYSCASSSlfhpgklhfVFNIVEFlstatteVLRK---GVCTGWLALL-----VASVLQPNihashedsgkalapkis 521
Cdd:cd06201   100 PRFYSLASSS---------SDGFLEI-------CVRKhpgGLCSGYLHGLkpgdtIKAFIRPN----------------- 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 522 isprttNSFHLPDDPSiPIIMVGPGTGIAPFIGFLQHREKlqeQHPdgnfgaMWLFFGCRHKDRDYLFRKELRHFLKHGI 601
Cdd:cd06201   147 ------PSFRPAKGAA-PVILIGAGTGIAPLAGFIRANAA---RRP------MHLYWGGRDPASDFLYEDELDQYLADGR 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 602 LTHLKVSFSRdapvgeEEAPAkYVQDNIQLHGQQVARiLLQENGHIYVCGdAKNMAKDVHDALVQIIskevGVEKLeamk 681
Cdd:cd06201   211 LTQLHTAFSR------TPDGA-YVQDRLRADAERLRR-LIEDGAQIMVCG-SRAMAQGVAAVLEEIL----APQPL---- 273

                         250
                  ....*....|....*.
gi 1402624270 682 TLATLKEEKRYLQDIW 697
Cdd:cd06201   274 SLDELKLQGRYAEDVY 289
PRK08105 PRK08105
flavodoxin; Provisional
 1-150 1.24e-16

flavodoxin; Provisional


Pssm-ID: 181230 [Multi-domain]  Cd Length: 149  Bit Score: 77.23  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270   1 MRRFLLLYATQQGQAKAIAEEICEQAVVHGFSADL---HCISESDKYDLKTetapLVVVVSTTGTGDPPDTARKFVKEIQ 77
Cdd:PRK08105    1 MAKVGIFVGTVYGNALLVAEEAEAILTAQGHEVTLfedPELSDWQPYQDEL----VLVVTSTTGQGDLPDSIVPLFQALK 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1402624270  78 NQtlpVDFFAHLRYGLLGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADDCVGLELVVE--PWIAGlWPAL 150
Cdd:PRK08105   77 DT---AGYQPNLRYGVIALGDSSYDNFCGAGKQFDALLQEQGAKRVGERLEIDACETPEPEVEanPWVEQ-WGTL 147
PRK09004 PRK09004
FMN-binding protein MioC; Provisional
 13-126 1.83e-16

FMN-binding protein MioC; Provisional


Pssm-ID: 181608 [Multi-domain]  Cd Length: 146  Bit Score: 76.79  E-value: 1.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270  13 GQAKAIAEEICEQAVVHGFSADLHCISESDkyDLKTETAPLVVVvSTTGTGDPPDTARKFVKEIQNQTLPvdfFAHLRYG 92
Cdd:PRK09004   13 GGAEYVADHLAEKLEEAGFSTETLHGPLLD--DLSASGLWLIVT-STHGAGDLPDNLQPFFEELQEQKPD---LSQVRFA 86

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1402624270  93 LLGLGDSEYTYFCNGGKIIDKRLQELGARHFYDT 126
Cdd:PRK09004   87 AIGIGSSEYDTFCGAIDKLEQLLKAKGAKQIGET 120
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 542-662 9.08e-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: 73.45  E-value: 9.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 542 MVGPGTGIAPFIGFLQHRekLQEQHPDGNfgaMWLFFGCRHkDRDYLFRKELRHF-LKHGILTHLKVSFSRDApvGEEEA 620
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAI--LEDPKDPTQ---VVLVFGNRN-EDDILYREELDELaEKHPGRLTVVYVVSRPE--AGWTG 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1402624270 621 PAKYVQDNIqlhgQQVARILLQENGHIYVCGdAKNMAKDVHD 662
Cdd:pfam00175  73 GKGRVQDAL----LEDHLSLPDEETHVYVCG-PPGMIKAVRK 109
PLN03116 PLN03116
ferredoxin--NADP+ reductase; Provisional
 532-681 1.45e-15

ferredoxin--NADP+ reductase; Provisional


Pssm-ID: 215586 [Multi-domain]  Cd Length: 307  Bit Score: 78.22  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 532 LP-DDPSIPIIMVGPGTGIAPFIGFLqhREKLQEQHPDGNF-GAMWLFFGCRHKDRdYLFRKELRHFLKhgiltHLKVSF 609
Cdd:PLN03116  150 LPeEDPNATHIMVATGTGIAPFRGFL--RRMFMEDVPAFKFgGLAWLFLGVANSDS-LLYDDEFERYLK-----DYPDNF 221

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1402624270 610 SRDAPVGEEEAPAK----YVQDNIQLHGQQVARiLLQENGHIYVCGdAKNMAKDVHDALvQIISKEVGV---EKLEAMK 681
Cdd:PLN03116  222 RYDYALSREQKNKKggkmYVQDKIEEYSDEIFK-LLDNGAHIYFCG-LKGMMPGIQDTL-KRVAEERGEsweEKLSGLK 297
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
 451-683 3.51e-15

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 77.73  E-value: 3.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 451 RPYSCASSSLFHPGKLHFVFNIVEFLS-TATTEVLRKGVCTGWLAllvasVLQPnihashedsgkalAPKISISPRTTNS 529
Cdd:PLN03115  146 RLYSIASSALGDFGDSKTVSLCVKRLVyTNDQGEIVKGVCSNFLC-----DLKP-------------GAEVKITGPVGKE 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 530 FHLPDDPSIPIIMVGPGTGIAPFIGFLQhrEKLQEQHPDGNF-GAMWLFFGCRHKDrDYLFRKELRHfLKHGILTHLKVS 608
Cdd:PLN03115  208 MLMPKDPNATIIMLATGTGIAPFRSFLW--KMFFEKHDDYKFnGLAWLFLGVPTSS-SLLYKEEFEK-MKEKAPENFRLD 283

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1402624270 609 FSrdapVGEEEAPAK----YVQDNIQLHGQQVARILLQENGHIYVCGdAKNMAKDVHDALVQIISKEvGVEKLEAMKTL 683
Cdd:PLN03115  284 FA----VSREQTNAKgekmYIQTRMAEYAEELWELLKKDNTYVYMCG-LKGMEKGIDDIMVSLAAKD-GIDWFEYKKQL 356
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
 5-146 1.79e-12

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


Pssm-ID: 440480 [Multi-domain]  Cd Length: 135  Bit Score: 64.92  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270   5 LLLYATQQGQAKAIAEEICEQAVVHGfsADLHCISESDKYDLKTETApLVVVVSTTGtGDPPDTARKFVKEIQNQtlpvd 84
Cdd:COG0716     2 LIVYGSTTGNTEKVAEAIAEALGAAG--VDLFEIEDADLDDLEDYDL-LILGTPTWA-GELPDDWEDFLEELKED----- 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1402624270  85 fFAHLRYGLLGLGDSEytYFCNGGKIIDKRLQELGAR--HFYDTGH--ADDCVGLELVVEPWIAGL 146
Cdd:COG0716    73 -LSGKKVALFGTGDSS--GYGDALGELKELLEEKGAKvvGGYDFEGskAPDAEDTEERAEEWLKQL 135
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
527-676 1.54e-10

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 61.73  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 527 TNSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHrekLQEQHPDGNFgamWLFFGCRHKDrDYLFRKELRHFLKHGILTHLK 606
Cdd:COG1018    98 RGDFVLDPEPARPLLLIAGGIGITPFLSMLRT---LLARGPFRPV---TLVYGARSPA-DLAFRDELEALAARHPRLRLH 170

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1402624270 607 VSFSRdapvgEEEAPAKYVQDniqlhgQQVARILL-QENGHIYVCGDAkNMAKDVHDALvqiisKEVGVEK 676
Cdd:COG1018   171 PVLSR-----EPAGLQGRLDA------ELLAALLPdPADAHVYLCGPP-PMMEAVRAAL-----AELGVPE 224
PRK05723 PRK05723
flavodoxin; Provisional
 53-151 3.01e-08

flavodoxin; Provisional


Pssm-ID: 168208  Cd Length: 151  Bit Score: 53.26  E-value: 3.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270  53 LVVVVSTTGTGDPPDTARKFVKEIQNQtLPVDFFAhLRYGLLGLGDSEY-TYFCNGGKIIDKRLQELGARHFYDTGHAD- 130
Cdd:PRK05723   51 LLAVTSTTGMGELPDNLMPLYSAIRDQ-LPAAWRG-LPGAVIALGDSSYgDTFCGGGEQMRELFAELGVREVQPMLRLDa 128

                          90       100
                  ....*....|....*....|..
gi 1402624270 131 -DCVGLELVVEPWIAGLWPALR 151
Cdd:PRK05723  129 sETVTPETDAEPWLAEFAAALK 150
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 438-666 1.41e-07

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


Pssm-ID: 99792 [Multi-domain]  Cd Length: 241  Bit Score: 52.95  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 438 LSLLLEHLPKLQpRPYSCASsslfHPGKLHFvfnivEFLSTatteVLRKGVCTgwlallvaSVLQpnihashedsgkALA 517
Cdd:cd06195    33 LGLPNDDGKLVR-RAYSIAS----APYEENL-----EFYII----LVPDGPLT--------PRLF------------KLK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 518 P--KISISPRTTNSFHLPDDPSIP-IIMVGPGTGIAPFIGFLQHREKLQEqhpdgnFGAMWLFFGCRHKDrDYLFRKELR 594
Cdd:cd06195    79 PgdTIYVGKKPTGFLTLDEVPPGKrLWLLATGTGIAPFLSMLRDLEIWER------FDKIVLVHGVRYAE-ELAYQDEIE 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1402624270 595 HFLKHgilTHLKVSF----SRDAPVGEEEApakYVQDNIQlHGQQVARI---LLQENGHIYVCGDaKNMAKDVHDALVQ 666
Cdd:cd06195   152 ALAKQ---YNGKFRYvpivSREKENGALTG---RIPDLIE-SGELEEHAglpLDPETSHVMLCGN-PQMIDDTQELLKE 222
PRK09267 PRK09267
flavodoxin FldA; Validated
 1-121 1.57e-07

flavodoxin FldA; Validated


Pssm-ID: 236439 [Multi-domain]  Cd Length: 169  Bit Score: 51.75  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270   1 MRRFLLLYATQQGQAKAIAEEICEQavVHGFSADLHCISESDK-----YDLktetapLVVVVSTTGTGDPPDTARKFVKE 75
Cdd:PRK09267    1 MAKIGIFFGSDTGNTEDIAKMIQKK--LGKDVADVVDIAKASKedfeaYDL------LILGIPTWGYGELQCDWDDFLPE 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1402624270  76 IQNqtlpVDfFAHLRYGLLGLGDSE-YT-YFCNGGKIIDKRLQELGAR 121
Cdd:PRK09267   73 LEE----ID-FSGKKVALFGLGDQEdYAeYFCDAMGTLYDIVEPRGAT 115
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 546-676 2.18e-06

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: 49.16  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 546 GTGIAPFIGFLqhREKLQEQHPDGNFgamwLFFGCRhKDRDYLFRKELRHFLKHG-ILThlkvsfsrdapVGEEEAPAky 624
Cdd:cd06196   108 GAGITPFIAIL--RDLAAKGKLEGNT----LIFANK-TEKDIILKDELEKMLGLKfINV-----------VTDEKDPG-- 167

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1402624270 625 vqdniqLHGQQVARILLQE-----NGHIYVCGDAKnMAKDVHDALvqiisKEVGVEK 676
Cdd:cd06196   168 ------YAHGRIDKAFLKQhvtdfNQHFYVCGPPP-MEEAINGAL-----KELGVPE 212
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 528-666 1.05e-05

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 47.55  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 528 NSFHLPDDPSiPIIMVGPGTGIAPFIGFLQHrekLQEQHPDgnfgaMWLFFGCRHKDrDYLFRKELRHFLKhgilTHLKV 607
Cdd:COG0543    88 NGFPLEDSGR-PVLLVAGGTGLAPLRSLAEA---LLARGRR-----VTLYLGARTPE-DLYLLDELEALAD----FRVVV 153

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 608 SfSRDAPVGEEEapakYVQDniqlhgqQVARILLQENGH-IYVCGdAKNMAKDVHDALVQ 666
Cdd:COG0543   154 T-TDDGWYGRKG----FVTD-------ALKELLAEDSGDdVYACG-PPPMMKAVAELLLE 200
PRK06703 PRK06703
flavodoxin; Provisional
 1-126 1.60e-05

flavodoxin; Provisional


Pssm-ID: 235854 [Multi-domain]  Cd Length: 151  Bit Score: 45.52  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270   1 MRRFLLLYATQQGQAKAIAEEICEQAVVHGFSADLHCISESDKYDLktETAPLVVVVSTT-GTGDPPDTARKFVKEIQNQ 79
Cdd:PRK06703    1 MAKILIAYASMSGNTEDIADLIKVSLDAFDHEVVLQEMDGMDAEEL--LAYDGIILGSYTwGDGDLPYEAEDFHEDLENI 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1402624270  80 TLpvdffAHLRYGLLGLGDSEYTYFCNGGKIIDKRLQELGARHFYDT 126
Cdd:PRK06703   79 DL-----SGKKVAVFGSGDTAYPLFCEAVTIFEERLVERGAELVQEG 120
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 530-676 3.63e-05

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: 46.01  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 530 FHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPdgnfgaMWLFFGCRHKDrDYLFRKELRHFLKHgiLTHLKVSF 609
Cdd:cd06184   106 FVLDEASDRPLVLISAGVGITPMLSMLEALAAEGPGRP------VTFIHAARNSA-VHAFRDELEELAAR--LPNLKLHV 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1402624270 610 SRDAPVGEEEAPAKYVQDNIQLhgQQVARILLQENGHIYVCGDAKNMaKDVHDALvqiisKEVGVEK 676
Cdd:cd06184   177 FYSEPEAGDREEDYDHAGRIDL--ALLRELLLPADADFYLCGPVPFM-QAVREGL-----KALGVPA 235
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 529-651 4.25e-05

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


Pssm-ID: 99805 [Multi-domain]  Cd Length: 228  Bit Score: 45.28  E-value: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 529 SFHLpDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPdgnfgaMWLFFGCRHkDRDYLFRKELRHFLKHgiLTHLKVS 608
Cdd:cd06209    95 SFYL-REVKRPLLMLAGGTGLAPFLSMLDVLAEDGSAHP------VHLVYGVTR-DADLVELDRLEALAER--LPGFSFR 164

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1402624270 609 FSRDAPvgEEEAPAK-YVQDNIQlhgqqvARILLQENGHIYVCG 651
Cdd:cd06209   165 TVVADP--DSWHPRKgYVTDHLE------AEDLNDGDVDVYLCG 200
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 528-653 9.65e-05

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


Pssm-ID: 99791 [Multi-domain]  Cd Length: 222  Bit Score: 44.18  E-value: 9.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 528 NSFHLPDDPSIPIIMVGPGTGIAPFIGFLqhREKLQEQHPdgnfGAMWLFFGCRHKDRDYLFRKELRHFLKHGILTHLKV 607
Cdd:cd06194    88 QAFYRPEYGEGPLLLVGAGTGLAPLWGIA--RAALRQGHQ----GEIRLVHGARDPDDLYLHPALLWLAREHPNFRYIPC 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1402624270 608 SfSRDAPVGEEEAPAKYVQDNIQLHGQQVArillqenghiYVCGDA 653
Cdd:cd06194   162 V-SEGSQGDPRVRAGRIAAHLPPLTRDDVV----------YLCGAP 196
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 534-664 2.03e-04

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


Pssm-ID: 99795 [Multi-domain]  Cd Length: 216  Bit Score: 43.40  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 534 DDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHP-DgnfgamwLFFGCRhKDRDYLFRKELRHfLKHGILTHLKVSFSRD 612
Cdd:cd06198    92 DDRRARQIWIAGGIGITPFLALLEALAARGDARPvT-------LFYCVR-DPEDAVFLDELRA-LAAAAGVVLHVIDSPS 162

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1402624270 613 APVGEEEapakyvqdniQLHGQQVARIllqENGHIYVCGDAKnMAKDVHDAL 664
Cdd:cd06198   163 DGRLTLE----------QLVRALVPDL---ADADVWFCGPPG-MADALEKGL 200
Flavodoxin_5 pfam12724
Flavodoxin domain; This is a family of flavodoxins. Flavodoxins are electron transfer proteins ...
 5-87 2.32e-04

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


Pssm-ID: 463681 [Multi-domain]  Cd Length: 144  Bit Score: 41.86  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270   5 LLLYATQQGQAKAIAEEICEQAVVHGFSADLHCISESDK---YDlktetapLVVVVSTTGTGDPPDTARKFVKEIQNQ-- 79
Cdd:pfam12724   1 LILYSSRDGQTKKIAERIAEELREEGELVDVEDVEAGEDlssYD-------AVVIGASIYYGKHLPELRQFVTKHRDEls 73


                  ....*...
gi 1402624270  80 TLPVDFFA 87
Cdd:pfam12724  74 SKPVAFFS 81
PRK07308 PRK07308
flavodoxin; Validated
 6-140 3.28e-04

flavodoxin; Validated


Pssm-ID: 180922 [Multi-domain]  Cd Length: 146  Bit Score: 41.31  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270   6 LLYATQQGQAKAIAEEICEQAVVHGFSADLHCISESDKYDLktETAPLVVVVSTT-GTGDPPDTARKFVKEIQNqtlpVD 84
Cdd:PRK07308    6 IVYASMTGNTEEIADIVADKLRELGHDVDVDECTTVDASDF--EDADIAIVATYTyGDGELPDEIVDFYEDLAD----LD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1402624270  85 FFAHLrYGLLGLGDSEYTYFCNGGKIIDKRLQELGARhfydtgHADDCVGLELVVE 140
Cdd:PRK07308   80 LSGKI-YGVVGSGDTFYDYFCKSVDDFEAQFALTGAT------KGAESVKVDLAAE 128
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 529-666 3.83e-04

NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD.


Pssm-ID: 99786 [Multi-domain]  Cd Length: 224  Bit Score: 42.54  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 529 SFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPdgnfgaMWLFFGCRHKDRDYLfRKELRHFLKHgiltHLKVS 608
Cdd:cd06189    90 DFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQGSKRP------IHLYWGARTEEDLYL-DELLEAWAEA----HPNFT 158

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1402624270 609 FsrdAPVgEEEAPAK------YVQ-----DNIQLHGQQVarillqenghiYVCGDAkNMAKDVHDALVQ 666
Cdd:cd06189   159 Y---VPV-LSEPEEGwqgrtgLVHeavleDFPDLSDFDV-----------YACGSP-EMVYAARDDFVE 211
HemG COG4635
Protoporphyrinogen IX oxidase, menaquinone-dependent (flavodoxin domain) [Coenzyme transport ...
 3-87 5.15e-04

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


Pssm-ID: 443673  Cd Length: 179  Bit Score: 41.42  E-value: 5.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270   3 RFLLLYATQQGQAKAIAEEICEQAVVHGFSADLHCISESDkyDLKTETAPLVVVVSTTGTGDPPDTARKFVKEIQNQ--T 80
Cdd:COG4635     2 KVLILYASRDGQTRKIAERIAEVLREAGHDVDLVDLEDAP--DLDLAGYDAVVIGASIRYGKWLPEAVRFVRRHRDAlaA 79


                  ....*..
gi 1402624270  81 LPVDFFA 87
Cdd:COG4635    80 RPVAFFS 86
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 529-665 5.48e-04

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


Pssm-ID: 99813 [Multi-domain]  Cd Length: 235  Bit Score: 42.25  E-value: 5.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 529 SFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPdgnfgaMWLFFGCRHKDrDYLFRKELRHF-LKHGILtHLKV 607
Cdd:cd06217    99 TFTWNPLHGDPVVLLAGGSGIVPLMSMIRYRRDLGWPVP------FRLLYSARTAE-DVIFRDELEQLaRRHPNL-HVTE 170

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1402624270 608 SFSRDAPVGEEEAPAkyvqdniQLHGQQVARILLQENGH-IYVCGDAkNMAKDVHDALV 665
Cdd:cd06217   171 ALTRAAPADWLGPAG-------RITADLIAELVPPLAGRrVYVCGPP-AFVEAATRLLL 221
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 529-664 5.71e-04

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: 41.81  E-value: 5.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 529 SFHLPDDPSIPIIMVGPGTGIAPF----IGFLQHREKlQEQHpdgnfgamwLFFGCRHK----DRDYLFRKELRHflkhg 600
Cdd:cd06187    90 TFYLRRDHDRPVLCIAGGTGLAPLraivEDALRRGEP-RPVH---------LFFGARTErdlyDLEGLLALAARH----- 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1402624270 601 ilTHLKVSfsrdaPVGEEEAPAKYVQDNiqLHGQQVARILLQENGH-IYVCGDAKnMAKDVHDAL 664
Cdd:cd06187   155 --PWLRVV-----PVVSHEEGAWTGRRG--LVTDVVGRDGPDWADHdIYICGPPA-MVDATVDAL 209
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 540-612 8.27e-04

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 42.10  E-value: 8.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1402624270 540 IIMVGPGTGIAPFIGFLQH----REKlqeqhpdgnFGAMWLFFGCRHKdRDYLFRKELRHFLKHGILTHLKVSFSRD 612
Cdd:PRK08345  111 LLLIAGGLGMAPLRSVLLYamdnRWK---------YGNITLIYGAKYY-EDLLFYDELIKDLAEAENVKIIQSVTRD 177
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
539-595 2.10e-03

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 41.03  E-value: 2.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1402624270 539 PIIMVGPGTGIAPFIGFLQHrekLQEQHPDGNfgAMWLFFGCRHKDRDYlFRKELRH 595
Cdd:COG4097   320 RQVWIAGGIGITPFLALLRA---LAARPGDQR--PVDLFYCVRDEEDAP-FLEELRA 370
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 530-651 2.81e-03

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 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: 99812 [Multi-domain]  Cd Length: 243  Bit Score: 39.90  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 530 FHLPDDPSIPIIMVGPGTGIAPFIGFLqhREKLQEQHPdGNFgaMWLFFGCRHkdRDYLFRKELRHF-LKHGILThLKVS 608
Cdd:cd06216   115 FVLPDPLPPRLLLIAAGSGITPVMSML--RTLLARGPT-ADV--VLLYYARTR--EDVIFADELRALaAQHPNLR-LHLL 186

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1402624270 609 FSRDAPVGEeeapakyvqdniqLHGQQVARI-LLQENGHIYVCG 651
Cdd:cd06216   187 YTREELDGR-------------LSAAHLDAVvPDLADRQVYACG 217
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 529-588 8.49e-03

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 39.08  E-value: 8.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402624270 529 SFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPdgnfgaMWLFFGCRHKDRDYL 588
Cdd:PRK07609  196 TFFLREDSDKPIVLLASGTGFAPIKSIVEHLRAKGIQRP------VTLYWGARRPEDLYL 249
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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