|
Name |
Accession |
Description |
Interval |
E-value |
| cysJ |
PRK10953 |
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit; |
1-601 |
0e+00 |
|
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
Pssm-ID: 182862 [Multi-domain] Cd Length: 600 Bit Score: 1342.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 1 MTTQAPPSNLLPLNPEQLARLQAATTDFSPTQLAWVSGYFWGMLNQQPGAVATAPAAVAQPPAITLISASQTGNARRVAE 80
Cdd:PRK10953 1 MTTQAPPSALLPLNPEQLARLQAATTDLSPTQLAWVSGYFWGVLNQQPGAVAATPAPAAEMPGITLISASQTGNARRVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 81 QLRDDLLAAKLNVNLVNAGEYKFKQIASEKLLVVVASTQGEGEPAEEAVALHKFLFSKKAPKLEGTAFAVFGLGDTSYEF 160
Cdd:PRK10953 81 QLRDDLLAAKLNVNLVNAGDYKFKQIAQEKLLIVVTSTQGEGEPPEEAVALHKFLFSKKAPKLENTAFAVFGLGDTSYEF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 161 FCQSGKDFDSRLAELGAERLLDRVDADVEYQPAAAEWRARIVDVLKSRVPQeSPAQAAVTAAGAVNDIHTSPYTKEEPLT 240
Cdd:PRK10953 161 FCQAGKDFDSKLAELGAERLLDRVDADVEYQAAASEWRARVVDALKSRAPA-VAAPSQSVATGAVNEIHTSPYSKEAPLT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 241 ASLSVNQKITGRDSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVNELVELLWLKGDEPVTLDGKTLPLAEALQWH 320
Cdd:PRK10953 240 ASLSVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVKELVELLWLKGDEPVTVDGKTLPLAEALQWH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 321 FELTVNTANIVENYATLTRSESLLPLVGDKAKLQHYAATTPIVDMVRFSPAQLDADALIGLLRPLTPRLYSIASSQAEVE 400
Cdd:PRK10953 320 FELTVNTANIVENYATLTRSETLLPLVGDKAALQHYAATTPIVDMVRFAPAQLDAEQLIGLLRPLTPRLYSIASSQAEVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 401 NEVHVTVGVVRYDIEGRARAGGASSFLADRVEEEGDVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADE 480
Cdd:PRK10953 400 NEVHITVGVVRYDIEGRARAGGASSFLADRLEEEGEVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 481 APGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLSRIDLAWSRDQKEKVYVQDKLREQGAELWRWINDGAHIYVCGDANRM 560
Cdd:PRK10953 480 APGKNWLFFGNPHFTEDFLYQVEWQRYVKEGLLTRIDLAWSRDQKEKIYVQDKLREQGAELWRWINDGAHIYVCGDANRM 559
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 493179527 561 AKDVEQALLEVIAEFGGMDVETADEFLSELRVERRYQRDVY 601
Cdd:PRK10953 560 AKDVEQALLEVIAEFGGMDTEAADEFLSELRVERRYQRDVY 600
|
|
| cysJ |
TIGR01931 |
sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an ... |
8-601 |
0e+00 |
|
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: 993.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 8 SNLLPLNPEQLARLQAATTDFSPTQLAWVSGYFWGMLNQQ----PGAVATAPAAVAQPPAITLISASQTGNARRVAEQLR 83
Cdd:TIGR01931 1 SPNSPLNQEQLDLLNRLLPTLTEAQLAWLSGYLWALANQTpaalSVAPNEAEEPAAQEKRVTILYGSQTGNARRLAKRLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 84 DDLLAAKLNVNLVNAGEYKFKQIASEKLLVVVASTQGEGEPAEEAVALHKFLFSKKAPKLEGTAFAVFGLGDTSYEFFCQ 163
Cdd:TIGR01931 81 EKLEAAGFSVRLSSADDYKFKQLKKERLLLLVISTQGEGEPPEEAISLHKFLHSKKAPKLENLRYSVLGLGDSSYEFFCQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 164 SGKDFDSRLAELGAERLLDRVDADVEYQPAAAEWRARIVDVLKSRVPQeSPAQAAVTAAGAVNDIHTSPYTKEEPLTASL 243
Cdd:TIGR01931 161 TGKDFDKRLEELGGKRLLPRVDADLDYDANAAEWRAGVLTALNEQAKG-GASTPSASETSTPLQTSTSVYSKQNPFRAEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 244 SVNQKITGRDSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVNELVELLWLKGDEPVTLDGKTLPLAEALQWHFEL 323
Cdd:TIGR01931 240 LENQKITGRNSKKDVRHIEIDLEGSGLHYEPGDALGVWYKNDPALVKEILKLLNLDPDEKVTIGGKTIPLFEALITHFEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 324 TVNTANIVENYATLTRSESLLPLVGDKAKLQHYAATTPIVDMVRFSPAQLDADALIGLLRPLTPRLYSIASSQAEVENEV 403
Cdd:TIGR01931 320 TQNTKPLLKAYAELTGNKELKALIADNEKLKAYIQNTPLIDLIRDYPADLDAEQLISLLRPLTPRLYSISSSQSEVGDEV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 404 HVTVGVVRYDIEGRARAGGASSFLADRVEEEGDVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADEAPG 483
Cdd:TIGR01931 400 HLTVGVVRYQAHGRARLGGASGFLAERLKEGDTVPVYIEPNDNFRLPEDPDTPIIMIGPGTGVAPFRAFMQERAEDGAKG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 484 KNWLFFGNPHFTEDFLYQVEWQRYVKEGVLSRIDLAWSRDQKEKVYVQDKLREQGAELWRWINDGAHIYVCGDANRMAKD 563
Cdd:TIGR01931 480 KNWLFFGNPHFTTDFLYQVEWQNYLKKGVLTKMDLAFSRDQAEKIYVQHRIREQGAELWQWLQEGAHIYVCGDAKKMAKD 559
|
570 580 590
....*....|....*....|....*....|....*...
gi 493179527 564 VEQALLEVIAEFGGMDVETADEFLSELRVERRYQRDVY 601
Cdd:TIGR01931 560 VHQALLDIIAKEGHLDAEEAEEYLTDLRVEKRYQRDVY 597
|
|
| CysJ |
COG0369 |
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ... |
35-601 |
0e+00 |
|
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: 930.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 35 WVSGYFWGMLNQQPGAVATAPAAVAQPPaITLISASQTGNARRVAEQLRDDLLAAKLNVNLVNAGEYKFKQIASEKLLVV 114
Cdd:COG0369 1 WLSGYLAGLASRAAAAAAAAAAAAAGTP-LTILYGSQTGNAEGLAEQLAERAKAAGLAVTLASLDDYKPKDLAKEGLLLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 115 VASTQGEGEPAEEAVALHKFLFSKKAPKLEGTAFAVFGLGDTSYEFFCQSGKDFDSRLAELGAERLLDRVDADVEYQPAA 194
Cdd:COG0369 80 VTSTYGEGEPPDNARAFYEFLHSKKAPKLDGLRYAVLGLGDSSYETFCQTGKDFDARLEELGATRLLPRVDCDVDYEEAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 195 AEWRARIVDVLKSRVPQESPAQAavtaagaVNDIHTSPYTKEEPLTASLSVNQKITGRDSEKDVRHIEIDLGDSGLRYQP 274
Cdd:COG0369 160 EAWLAAVLAALAEALGAAAAAAA-------AAAAAAPAYSRKNPFPATVLENRELTGRGSAKETRHIEIDLPGSGLSYEP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 275 GDALGVWYQNDPALVNELVELLWLKGDEPVTLDGKTLPLAEALQWHFELTVNTANIVENYATLTRSESLLPLV--GDKAK 352
Cdd:COG0369 233 GDALGVWPENDPALVDELLARLGLDGDEPVTLDGEPLSLREALTEHLELTRLTPPLLEKYAELTGNAELAALLadEDKAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 353 LQHYAATTPIVDMVR-FSPAQLDADALIGLLRPLTPRLYSIASSQAEVENEVHVTVGVVRYDIEGRARAGGASSFLADRv 431
Cdd:COG0369 313 LREYLAGRQLLDLLReFPAAELSAEELLELLRPLTPRLYSISSSPKAHPDEVHLTVGVVRYEASGRERKGVASTYLADL- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 432 EEEGDVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADEAPGKNWLFFGNPHFTEDFLYQVEWQRYVKEG 511
Cdd:COG0369 392 EEGDTVPVFVEPNPNFRLPADPDTPIIMIGPGTGIAPFRAFLQEREARGASGKNWLFFGDRHFTTDFLYQTELQAWLKDG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 512 VLSRIDLAWSRDQKEKVYVQDKLREQGAELWRWINDGAHIYVCGDANRMAKDVEQALLEVIAEFGGMDVETADEFLSELR 591
Cdd:COG0369 472 VLTRLDLAFSRDQAEKIYVQHRLLEQGAELWAWLEEGAHVYVCGDASRMAKDVDAALLDIIAEHGGLSEEEAEEYLAELR 551
|
570
....*....|
gi 493179527 592 VERRYQRDVY 601
Cdd:COG0369 552 AEKRYQRDVY 561
|
|
| SiR |
cd06199 |
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
243-601 |
0e+00 |
|
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: 590.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 243 LSVNQKITGRDSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVNELVELLWLKGDEPVTL-DGKTLPLAEALQWHF 321
Cdd:cd06199 2 VLENRLLTGPGSEKETRHIELDLEGSGLSYEPGDALGVYPTNDPALVDELLAALGLSGDEPVSTvGGGTLPLREALIKHY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 322 ELTVNTANIVENYATLTRSESLLPLvGDKAKLQHYAATTPIVDMVRFSPAQLDADALIGLLRPLTPRLYSIASSQAEVEN 401
Cdd:cd06199 82 EITTLLLALLESYAADTGALELLAL-AALEAVLAFAELRDVLDLLPIPPARLTAEELLDLLRPLQPRLYSIASSPKAVPD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 402 EVHVTVGVVRYDIEGRARAGGASSFLADRVEEEGDVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADEA 481
Cdd:cd06199 161 EVHLTVAVVRYESHGRERKGVASTFLADRLKEGDTVPVFVQPNPHFRLPEDPDAPIIMVGPGTGIAPFRAFLQEREATGA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 482 PGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLSRIDLAWSRDQKEKVYVQDKLREQGAELWRWINDGAHIYVCGDANRMA 561
Cdd:cd06199 241 KGKNWLFFGERHFATDFLYQDELQQWLKDGVLTRLDTAFSRDQAEKVYVQDRMREQGAELWAWLEEGAHFYVCGDAKRMA 320
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 493179527 562 KDVEQALLEVIAEFGGMDVETADEFLSELRVERRYQRDVY 601
Cdd:cd06199 321 KDVDAALLDIIATEGGMDEEEAEAYLKELKKEKRYQRDVY 360
|
|
| PRK06214 |
PRK06214 |
sulfite reductase subunit alpha; |
233-601 |
2.07e-150 |
|
sulfite reductase subunit alpha;
Pssm-ID: 235745 [Multi-domain] Cd Length: 530 Bit Score: 443.75 E-value: 2.07e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 233 YTKEEPLTASLSVNQKITGRDSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVNELVELLWLKGDEPVtldgKTLP 312
Cdd:PRK06214 163 TSRDNPVEATFLSRRRLNKPGSEKETWHVEIDLAGSGLDYEVGDSLGLFPANDPALVDAVIAALGAPPEFPI----GGKT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 313 LAEALQWHFELTVNTANIVENYATLTRS----------ESLLPlVGDKAKLQHYAATTpivdmvRFSPAQLDADALIGLL 382
Cdd:PRK06214 239 LREALLEDVSLGPAPDGLFELLSYITGGaarkkaralaAGEDP-DGDAATLDVLAALE------KFPGIRPDPEAFVEAL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 383 RPLTPRLYSIASSQAEVENEVHVTVGVVRYDIEGRARAGGASSFLADRVEEEGDVRVFIEHNDNFRLPANPETPVIMIGP 462
Cdd:PRK06214 312 DPLQPRLYSISSSPKATPGRVSLTVDAVRYEIGSRLRLGVASTFLGERLAPGTRVRVYVQKAHGFALPADPNTPIIMVGP 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 463 GTGIAPFRAFMQQRAADEAPGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLSRIDLAWSRDQKEKVYVQDKLREQGAELW 542
Cdd:PRK06214 392 GTGIAPFRAFLHERAATKAPGRNWLFFGHQRSATDFFYEDELNGLKAAGVLTRLSLAWSRDGEEKTYVQDRMRENGAELW 471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 493179527 543 RWINDGAHIYVCGDANRMAKDVEQALLEVIAEFGGMDVETADEFLSELRVERRYQRDVY 601
Cdd:PRK06214 472 KWLEEGAHFYVCGDAKRMAKDVERALVDIVAQFGGRSPDEAVAFVAELKKAGRYQADVY 530
|
|
| CYPOR_like |
cd06182 |
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
242-601 |
1.60e-114 |
|
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: 342.01 E-value: 1.60e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 242 SLSVNQKITGRDSEKDVRHIEIDL-GDSGLRYQPGDALGVWYQNdpalvnelvellwlkgdepvtldgktlplaealqwh 320
Cdd:cd06182 1 AITVNRKLTPPDSPRSTRHLEFDLsGNSVLKYQPGDHLGVIPPN------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 321 feltvntanivenyatltrsesllplvgdkaklqhyaattpivdmvrfspaqldadaligllrPLTPRLYSIASSQAEVE 400
Cdd:cd06182 45 ---------------------------------------------------------------PLQPRYYSIASSPDVDP 61
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 401 NEVHVTVGVVRY-DIEGRARAGGASSFLADRVEEEGdVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAA- 478
Cdd:cd06182 62 GEVHLCVRVVSYeAPAGRIRKGVCSNFLAGLQLGAK-VTVFIRPAPSFRLPKDPTTPIIMVGPGTGIAPFRGFLQERAAl 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 479 ---DEAPGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLSRIDLAWSRDQ-KEKVYVQDKLREQGAELWRWINDGAHIYVC 554
Cdd:cd06182 141 ranGKARGPAWLFFGCRNFASDYLYREELQEALKDGALTRLDVAFSREQaEPKVYVQDKLKEHAEELRRLLNEGAHIYVC 220
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 493179527 555 GDANRMAKDVEQALLEVIAEFGGMDVETADEFLSELRVERRYQRDVY 601
Cdd:cd06182 221 GDAKSMAKDVEDALVKIIAKAGGVDESDAEEYLKELEDEGRYVEDVW 267
|
|
| CYPOR |
cd06204 |
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
238-600 |
6.40e-105 |
|
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: 323.05 E-value: 6.40e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 238 PLTASLSVNQKITGrDSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVNELVELLWLKGDEPV----TLDGKTL-- 311
Cdd:cd06204 5 PFLAPVAVSRELFT-GSDRSCLHIEFDISGSGIRYQTGDHLAVWPTNPSEEVERLLKVLGLDDRDTVislkSLDEPASkk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 312 -----P--LAEALQWHFELT--VNTANIVE--NYATLTRSESLLPLVGDKAKlQHYA-----ATTPIVD-MVRFSPAQLD 374
Cdd:cd06204 84 vpfpcPttYRTALRHYLDITapVSRQVLAAlaQFAPDPEEKERLLKLASEGK-DEYAkwivePHRNLLEvLQDFPSAKPT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 375 A---DALIGLLRPLTPRLYSIASSQAEVENEVHVTVGVVRYDI-EGRARAGGASSFLADRVEEEGDVR------------ 438
Cdd:cd06204 163 PppfDFLIELLPRLQPRYYSISSSSKVHPNRIHITAVVVKYPTpTGRIIKGVATNWLLALKPALNGEKpptpyylsgprk 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 439 --------VFIEHNdNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADEAPGKNW----LFFGNPHFTEDFLYQVEWQR 506
Cdd:cd06204 243 kgggskvpVFVRRS-NFRLPTKPSTPVIMIGPGTGVAPFRGFIQERAALKESGKKVgptlLFFGCRHPDEDFIYKDELEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 507 YVKEGVLSRIDLAWSRDQKEKVYVQDKLREQGAELWRWINDGAHIYVCGDANRMAKDVEQALLEVIAEFGGMDVETADEF 586
Cdd:cd06204 322 YAKLGGLLELVTAFSREQPKKVYVQHRLAEHAEQVWELINEGAYIYVCGDAKNMARDVEKTLLEILAEQGGMTETEAEEY 401
|
410
....*....|....
gi 493179527 587 LSELRVERRYQRDV 600
Cdd:cd06204 402 VKKLKTRGRYQEDV 415
|
|
| CyPoR_like |
cd06207 |
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
242-601 |
1.06e-97 |
|
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. 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: 303.04 E-value: 1.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 242 SLSVNQKITGRDSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVNELVELLWLKGDEPVTLDGKTLPLAEALQWHf 321
Cdd:cd06207 1 KVTENKRLTPADYDRSTRHIEFDLGGSGLSYETGDNLGIYPENSDALVDEFLARLGLDGDDVVRVEPNEQQRGKPPFPE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 322 ELTVNTAnIVEN---YATLTRS--ESLLPLVGD---KAKLQHYAA-----TTPIVDMVR-------FSPAQLDADALIGL 381
Cdd:cd06207 80 PISVRQL-LKKFldiFGKPTKKflKLLSQLATDeeeKEDLYKLASregrtEYKRYEKYTylevlkdFPSVRPTLEQLLEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 382 LRPLTPRLYSIASSQAEVENEVHVTVGVVRY-DIEGRARAGGASSFLAdRVEEEGDVRVFIeHNDNFRLPANPETPVIMI 460
Cdd:cd06207 159 CPLIKPRYYSISSSPLKNPNEVHLLVSLVSWkTPSGRSRYGLCSSYLA-GLKVGQRVTVFI-KKSSFKLPKDPKKPIIMV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 461 GPGTGIAPFRAFMQQRAA----DEAPGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLSRIDLAWSRDQKEKVYVQDKLRE 536
Cdd:cd06207 237 GPGTGLAPFRAFLQERAAllaqGPEIGPVLLYFGCRHEDKDYLYKEELEEYEKSGVLTTLGTAFSRDQPKKVYVQDLIRE 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493179527 537 QGAELWRWINDGAH-IYVCGDANRMAKDVEQALLEVIAEFGGMDVETADEFLSELRVERRYQRDVY 601
Cdd:cd06207 317 NSDLVYQLLEEGAGvIYVCGSTWKMPPDVQEAFEEILKKHGGGDEELAEKKIEELEERGRYVVEAW 382
|
|
| Nitric_oxide_synthase |
cd06202 |
The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses ... |
266-601 |
1.26e-72 |
|
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: 238.77 E-value: 1.26e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 266 GDSGLRYQPGDALGVWYQNDPALVNELVELLWLK--GDEPVTL-----------------DGKTLP---LAEALQWHFEL 323
Cdd:cd06202 26 GAQELHYQPGDHVGIFPANRPELVDALLDRLHDAppPDQVIKLevleerstalgiiktwtPHERLPpctLRQALTRYLDI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 324 T-VNTANIVENYATLTRSESllplvgDKAKLQ-------------HYAATTpIVDMVR-FSPAQLDADALIGLLRPLTPR 388
Cdd:cd06202 106 TtPPTPQLLQLLATLATDEK------DKERLEvlgkgsseyedwkWYKNPN-ILEVLEeFPSLQVPASLLLTQLPLLQPR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 389 LYSIASSQAEVENEVHVTVGVVRY---DIEGRARAGGASSFLaDRVEEEGDVRVFIEHNDNFRLPANPETPVIMIGPGTG 465
Cdd:cd06202 179 YYSISSSPDMYPGEIHLTVAVVSYrtrDGQGPVHHGVCSTWL-NGLTPGDTVPCFVRSAPSFHLPEDPSVPVIMVGPGTG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 466 IAPFRAFMQQRAAD--------EAPGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLSRIDLAWSRDQ-KEKVYVQDKLRE 536
Cdd:cd06202 258 IAPFRSFWQQRQYDlrmsedpgKKFGDMTLFFGCRNSTIDDIYKEETEEAKNKGVLTEVYTALSREPgKPKTYVQDLLKE 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493179527 537 QGAELWRWI-NDGAHIYVCGDANrMAKDVEQALLEVIAEFGGMDVETADEFLSELRVERRYQRDVY 601
Cdd:cd06202 338 QAESVYDALvREGGHIYVCGDVT-MAEDVSQTIQRILAEHGNMSAEEAEEFILKLRDENRYHEDIF 402
|
|
| methionine_synthase_red |
cd06203 |
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ... |
247-601 |
3.78e-68 |
|
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: 226.43 E-value: 3.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 247 QKITGRDSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVNELVELLWL--KGDEPVTL--DGKTLPLAEALQWHFE 322
Cdd:cd06203 6 KKLTEGDDVKTVVDLTLDLSPTGFDYQPGDTIGILPPNTASEVESLLKRLGLleQADQPCEVkvVPNTKKKNAKVPVHIP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 323 LTVNTANIVENYATLTRS------ESLLPLVGD---KAKLQHYA---ATTPIVDMVRFSPAQ----LDA--------DAL 378
Cdd:cd06203 86 KVVTLRTILTWCLDIRAIpkkpllRALAEFTSDdneKRRLEELCskqGSEDYTDFVRKRGLSlldlLEAfpscrpplSLL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 379 IGLLRPLTPRLYSIASSQAEVENEVHVTVGVVRYDIEGRaraggASSFLADRV----EEEGDVRVFIEHNDNFRLPA-NP 453
Cdd:cd06203 166 IEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPAKGL-----CTSWLESLClsasSHGVKVPFYLRSSSRFRLPPdDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 454 ETPVIMIGPGTGIAPFRAFMQQRAA-----DEAP-GKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLSRIDLAWSRDQ--- 524
Cdd:cd06203 241 RRPIIMVGPGTGVAPFLGFLQHREKlkeshTETVfGEAWLFFGCRHRDRDYLFRDELEEFLEEGILTRLIVAFSRDEndg 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493179527 525 KEKVYVQDKLREQGAELWRWI-NDGAHIYVCGDANRMAKDVEQALLEVIAEFGGMDVETADEFLSELRVERRYQRDVY 601
Cdd:cd06203 321 STPKYVQDKLEERGKKLVDLLlNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGLDKLEAKKLLARLRKEDRYLEDVW 398
|
|
| bifunctional_CYPOR |
cd06206 |
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ... |
259-601 |
2.28e-66 |
|
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase (CYPOR). NADPH cytochrome p450 reductase serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99802 [Multi-domain] Cd Length: 384 Bit Score: 221.36 E-value: 2.28e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 259 RHIEIDLGDsGLRYQPGDALGVWYQNDPALVNELVELLWLKGDEPVTLD----------GKTLPLAEALQWHFEL-TVNT 327
Cdd:cd06206 18 RHLELRLPD-GMTYRAGDYLAVLPRNPPELVRRALRRFGLAWDTVLTISasgsatglplGTPISVSELLSSYVELsQPAT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 328 ANIVENYATLTRSESLLPLVGDKAKlQHYAA-----TTPIVDMV-RFSPAQLDADALIGLLRPLTPRLYSIASSQAEVEN 401
Cdd:cd06206 97 RRQLAALAEATRCPDTKALLERLAG-EAYAAevlakRVSVLDLLeRFPSIALPLATFLAMLPPMRPRQYSISSSPLVDPG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 402 EVHVTVGVVR---YDIEGRARaGGASSFLADRveEEGD-VRVFI-EHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQR 476
Cdd:cd06206 176 HATLTVSVLDapaLSGQGRYR-GVASSYLSSL--RPGDsIHVSVrPSHSAFRPPSDPSTPLIMIAAGTGLAPFRGFLQER 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 477 AA----DEAPGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLSrIDLAWSRDQKEKV-YVQDKLREQGAELWRWINDGAHI 551
Cdd:cd06206 253 AAllaqGRKLAPALLFFGCRHPDHDDLYRDELEEWEAAGVVS-VRRAYSRPPGGGCrYVQDRLWAEREEVWELWEQGARV 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 493179527 552 YVCGDAnRMAKDVEQALLEVIAE----FGGMDVETADEFLSELRVERRYQRDVY 601
Cdd:cd06206 332 YVCGDG-RMAPGVREVLKRIYAEkderGGGSDDEEAEEWLEELRNKGRYATDVF 384
|
|
| SiR_like1 |
cd06200 |
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
384-601 |
1.30e-50 |
|
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: 175.16 E-value: 1.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 384 PLTPRLYSIASSQAEVENEVhvtvgVVRYDIEGRARAGGASSFLADRVEEEGDVRVFIEHNDNFRLPAnPETPVIMIGPG 463
Cdd:cd06200 45 PLPHREYSIASLPADGALEL-----LVRQVRHADGGLGLGSGWLTRHAPIGASVALRLRENPGFHLPD-DGRPLILIGNG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 464 TGIAPFRAFMQQRAADEApGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLSRIDLAWSRDQKEKVYVQDKLREQGAELWR 543
Cdd:cd06200 119 TGLAGLRSHLRARARAGR-HRNWLLFGERQAAHDFFCREELEAWQAAGHLARLDLAFSRDQAQKRYVQDRLRAAADELRA 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493179527 544 WINDGAHIYVCGDANRMAKDVEQALLEVIAEfggmdvetadEFLSELRVERRYQRDVY 601
Cdd:cd06200 198 WVAEGAAIYVCGSLQGMAPGVDAVLDEILGE----------EAVEALLAAGRYRRDVY 245
|
|
| CYPOR_like_FNR |
cd06208 |
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ... |
376-601 |
2.26e-39 |
|
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: 145.93 E-value: 2.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 376 DALIGllRPLTPRLYSIASSqAEVENEVHVTVG-----VVRYDIEG-RARAGGASSFLADRVEEEgDVRVFIEHNDNFRL 449
Cdd:cd06208 55 DAKNG--KPHKLRLYSIASS-RYGDDGDGKTLSlcvkrLVYTDPETdETKKGVCSNYLCDLKPGD-DVQITGPVGKTMLL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 450 PANPETPVIMIGPGTGIAPFRAFMQQRAADEAP-----GKNWLFFGNPhfTED-FLYQVEWQRYVK-EGVLSRIDLAWSR 522
Cdd:cd06208 131 PEDPNATLIMIATGTGIAPFRSFLRRLFREKHAdykftGLAWLFFGVP--NSDsLLYDDELEKYPKqYPDNFRIDYAFSR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 523 DQK----EKVYVQDKLREQGAELWRWIN-DGAHIYVCGDANrMAKDVEQALLEViAEFGgmdvETADEFLSELRVERRYQ 597
Cdd:cd06208 209 EQKnadgGKMYVQDRIAEYAEEIWNLLDkDNTHVYICGLKG-MEPGVDDALTSV-AEGG----LAWEEFWESLKKKGRWH 282
|
....
gi 493179527 598 RDVY 601
Cdd:cd06208 283 VEVY 286
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
358-574 |
6.23e-39 |
|
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: 142.59 E-value: 6.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 358 ATTPIVDMVRFSPAQLDADA------LIGLLRP----LTPRLYSIASSQAEvENEVHVTVGVVRydiegrarAGGASSFL 427
Cdd:cd00322 2 ATEDVTDDVRLFRLQLPNGFsfkpgqYVDLHLPgdgrGLRRAYSIASSPDE-EGELELTVKIVP--------GGPFSAWL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 428 ADRveEEGD-VRVFIEHNDnFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADEAPGKNWLFFGNPHfTEDFLYQVEWQR 506
Cdd:cd00322 73 HDL--KPGDeVEVSGPGGD-FFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGART-PADLLFLDELEE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493179527 507 YVKEGVLSRIDLAWSRDQKEKVYVQDKLREQGAELWR-WINDGAHIYVCGDANrMAKDVEQALLEVIAE 574
Cdd:cd00322 149 LAKEGPNFRLVLALSRESEAKLGPGGRIDREAEILALlPDDSGALVYICGPPA-MAKAVREALVSLGVP 216
|
|
| SiR_like2 |
cd06201 |
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
344-601 |
2.09e-34 |
|
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: 132.07 E-value: 2.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 344 LPLVGDKAKLQHYAATTPIVdmvRFSPAQLDADA----------LIGLLRPLT--PRLYSIASSQAEvenevhvtvGVVr 411
Cdd:cd06201 48 LELVERKDYGAAVQAPTAIL---RFKPAKRKLSGkglpsfeagdLLGILPPGSdvPRFYSLASSSSD---------GFL- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 412 yDIEGRARAGG-ASSFLADRveEEGD-VRVFIEHNDNFRLPANpETPVIMIGPGTGIAPFRAFMQQraaDEAPGKNWLFF 489
Cdd:cd06201 115 -EICVRKHPGGlCSGYLHGL--KPGDtIKAFIRPNPSFRPAKG-AAPVILIGAGTGIAPLAGFIRA---NAARRPMHLYW 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 490 GNPHFTEDFLYQVEWQRYVKEGVLSRIDLAWSRDQkEKVYVQDKLREQGAELWRWINDGAHIYVCGdANRMAKDVEQALL 569
Cdd:cd06201 188 GGRDPASDFLYEDELDQYLADGRLTQLHTAFSRTP-DGAYVQDRLRADAERLRRLIEDGAQIMVCG-SRAMAQGVAAVLE 265
|
250 260 270
....*....|....*....|....*....|..
gi 493179527 570 EVIAefggmdveTADEFLSELRVERRYQRDVY 601
Cdd:cd06201 266 EILA--------PQPLSLDELKLQGRYAEDVY 289
|
|
| PLN03116 |
PLN03116 |
ferredoxin--NADP+ reductase; Provisional |
383-601 |
7.74e-33 |
|
ferredoxin--NADP+ reductase; Provisional
Pssm-ID: 215586 [Multi-domain] Cd Length: 307 Bit Score: 128.29 E-value: 7.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 383 RPLTPRLYSIASSQAEVENEVHVTVGVVR----YDIEGR----ARAGGASSFLADRveEEGD-VRVFIEHNDNFRLPA-N 452
Cdd:PLN03116 77 APHNVRLYSIASTRYGDDFDGKTASLCVRravyYDPETGkedpAKKGVCSNFLCDA--KPGDkVQITGPSGKVMLLPEeD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 453 PETPVIMIGPGTGIAPFRAFMQQRAADEAP-----GKNWLFFGNPHfTEDFLYQVEWQRYVKEGVLS-RIDLAWSRDQKE 526
Cdd:PLN03116 155 PNATHIMVATGTGIAPFRGFLRRMFMEDVPafkfgGLAWLFLGVAN-SDSLLYDDEFERYLKDYPDNfRYDYALSREQKN 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493179527 527 ----KVYVQDKLREQGAELWRWINDGAHIYVCGdANRMAKDVEQALLEVIAEFGgmdvETADEFLSELRVERRYQRDVY 601
Cdd:PLN03116 234 kkggKMYVQDKIEEYSDEIFKLLDNGAHIYFCG-LKGMMPGIQDTLKRVAEERG----ESWEEKLSGLKKNKQWHVEVY 307
|
|
| FAD_binding_1 |
pfam00667 |
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, ... |
232-426 |
4.40e-31 |
|
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: 120.52 E-value: 4.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 232 PYTKEEPLTASLSVNQKITGRDSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVNELVELLWL--KGDEPV---TL 306
Cdd:pfam00667 1 PFDAKKPFTAPVLSNRELTSPSSDRNCIHVELDISGSGLTYQTGDHLGVYPPNNEELVEELLERLGLdpKPDTVVllkTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 307 DGKTLP-------LAEALQWHFELT-VNTANIVENYATLTRSES----LLPLVGDKAK-----LQHYAATTPIVDMVRFS 369
Cdd:pfam00667 81 DERVKPprlppttYRQALKYYLDITgPPSKQLLRLLAQFAPEEEekqrLEFLSSDAGAreykrWKLNHAPTLLEVLEEFP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493179527 370 PAQLDADALIGLLRPLTPRLYSIASSQAEVENEVHVTVGVVRY--DIEGRARAGGASSF 426
Cdd:pfam00667 161 SVKLPADFLLTQLPQLQPRYYSISSSSKVHPNEVHLTVVVVEYetDGEGRIHYGVCSNW 219
|
|
| Flavodoxin_1 |
pfam00258 |
Flavodoxin; |
66-196 |
1.04e-30 |
|
Flavodoxin;
Pssm-ID: 425562 [Multi-domain] Cd Length: 142 Bit Score: 117.09 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 66 LISASQTGNARRVAEQLRDDLLAAKLNVNLVNAGEYK--FKQIASEKLLVVVASTQGEGEPAEEAVALHKFLFSK---KA 140
Cdd:pfam00258 1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDDVDetLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFgtlED 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 493179527 141 PKLEGTAFAVFGLGDTSYEFFCQSGKDFDSRLAELGAERLLDRVDADVEYQPAAAE 196
Cdd:pfam00258 81 GDLSGLKYAVFGLGDSGYEGFCGAAKKLDEKLSELGASRVGPLGEGDEDPQEDGLE 136
|
|
| NAD_binding_1 |
pfam00175 |
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ... |
459-566 |
5.49e-25 |
|
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: 99.64 E-value: 5.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 459 MIGPGTGIAPFRAFMQQRAAD-EAPGKNWLFFGNPHfTEDFLYQVEWQRYVKEGVLSRIDLAW-SRDQKE----KVYVQD 532
Cdd:pfam00175 1 MIAGGTGIAPVRSMLRAILEDpKDPTQVVLVFGNRN-EDDILYREELDELAEKHPGRLTVVYVvSRPEAGwtggKGRVQD 79
|
90 100 110
....*....|....*....|....*....|....
gi 493179527 533 KLREQGAELwrwINDGAHIYVCGdANRMAKDVEQ 566
Cdd:pfam00175 80 ALLEDHLSL---PDEETHVYVCG-PPGMIKAVRK 109
|
|
| PLN03115 |
PLN03115 |
ferredoxin--NADP(+) reductase; Provisional |
383-601 |
1.52e-20 |
|
ferredoxin--NADP(+) reductase; Provisional
Pssm-ID: 215585 [Multi-domain] Cd Length: 367 Bit Score: 93.53 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 383 RPLTPRLYSIASSQ-AEVENEVHVTVGVVRY---DIEGRARAGGASSFLADrVEEEGDVRVFIEHNDNFRLPANPETPVI 458
Cdd:PLN03115 141 KPHKLRLYSIASSAlGDFGDSKTVSLCVKRLvytNDQGEIVKGVCSNFLCD-LKPGAEVKITGPVGKEMLMPKDPNATII 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 459 MIGPGTGIAPFRAFMQQRAADEAP-----GKNWLFFGNPHfTEDFLYQVEWQRyVKEGVLS--RIDLAWSRDQK----EK 527
Cdd:PLN03115 220 MLATGTGIAPFRSFLWKMFFEKHDdykfnGLAWLFLGVPT-SSSLLYKEEFEK-MKEKAPEnfRLDFAVSREQTnakgEK 297
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493179527 528 VYVQDKLREQGAELWRWI-NDGAHIYVCGdanrmAKDVEQALLEVIAEFGGMDVETADEFLSELRVERRYQRDVY 601
Cdd:PLN03115 298 MYIQTRMAEYAEELWELLkKDNTYVYMCG-----LKGMEKGIDDIMVSLAAKDGIDWFEYKKQLKKAEQWNVEVY 367
|
|
| PRK09004 |
PRK09004 |
FMN-binding protein MioC; Provisional |
64-197 |
3.57e-18 |
|
FMN-binding protein MioC; Provisional
Pssm-ID: 181608 [Multi-domain] Cd Length: 146 Bit Score: 81.42 E-value: 3.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 64 ITLISASQTGNARRVAEQLRDDLLAAKLNVNLVNAGEykFKQIASEKLLVVVASTQGEGEPAEEAVALHKFLFSKKaPKL 143
Cdd:PRK09004 4 ITLISGSTLGGAEYVADHLAEKLEEAGFSTETLHGPL--LDDLSASGLWLIVTSTHGAGDLPDNLQPFFEELQEQK-PDL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 493179527 144 EGTAFAVFGLGDTSYEFFCQSGKDFDSRLAELGAERLLDRVDADVEYQP----AAAEW 197
Cdd:PRK09004 81 SQVRFAAIGIGSSEYDTFCGAIDKLEQLLKAKGAKQIGETLKIDVLQHPipedPAEEW 138
|
|
| PRK08105 |
PRK08105 |
flavodoxin; Provisional |
73-201 |
3.46e-16 |
|
flavodoxin; Provisional
Pssm-ID: 181230 [Multi-domain] Cd Length: 149 Bit Score: 75.69 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 73 GNARRVAEQLRDDLLAAKLNVNLVNAGEYKFKQIASEKLLVVVASTQGEGEPAEEAVALHKFLFSKkAPKLEGTAFAVFG 152
Cdd:PRK08105 13 GNALLVAEEAEAILTAQGHEVTLFEDPELSDWQPYQDELVLVVTSTTGQGDLPDSIVPLFQALKDT-AGYQPNLRYGVIA 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 493179527 153 LGDTSYEFFCQSGKDFDSRLAELGAERLLDR--VDA------DVEYQPAAAEWRARI 201
Cdd:PRK08105 92 LGDSSYDNFCGAGKQFDALLQEQGAKRVGERleIDAcetpepEVEANPWVEQWGTLL 148
|
|
| Fpr |
COG1018 |
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
388-570 |
7.88e-14 |
|
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 71.36 E-value: 7.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 388 RLYSIASSqaevENEVHVTVGVVRydIEGraraGGASSFLADRVEEeGDvRVFIE--HNDnFRLPANPETPVIMIGPGTG 465
Cdd:COG1018 53 RAYSLSSA----PGDGRLEITVKR--VPG----GGGSNWLHDHLKV-GD-TLEVSgpRGD-FVLDPEPARPLLLIAGGIG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 466 IAPFRAFMQQRAADEAPGKNWLFFGNPHfTEDFLYQVEWQRYVKEgvLSRIDLAWsrdqkekVYVQDKLREQG----AEL 541
Cdd:COG1018 120 ITPFLSMLRTLLARGPFRPVTLVYGARS-PADLAFRDELEALAAR--HPRLRLHP-------VLSREPAGLQGrldaELL 189
|
170 180 190
....*....|....*....|....*....|.
gi 493179527 542 WRWIND--GAHIYVCGDAnRMAKDVEQALLE 570
Cdd:COG1018 190 AALLPDpaDAHVYLCGPP-PMMEAVRAALAE 219
|
|
| FldA |
COG0716 |
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ... |
64-180 |
3.13e-13 |
|
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440480 [Multi-domain] Cd Length: 135 Bit Score: 66.85 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 64 ITLISASQTGNARRVAEQLRDDLlaAKLNVNLVNAGEYKFKQIASEKLLVVVASTQGeGEPAEEAVAlhkfLFSKKAPKL 143
Cdd:COG0716 1 ILIVYGSTTGNTEKVAEAIAEAL--GAAGVDLFEIEDADLDDLEDYDLLILGTPTWA-GELPDDWED----FLEELKEDL 73
|
90 100 110
....*....|....*....|....*....|....*..
gi 493179527 144 EGTAFAVFGLGDTSyeFFCQSGKDFDSRLAELGAERL 180
Cdd:COG0716 74 SGKKVALFGTGDSS--GYGDALGELKELLEEKGAKVV 108
|
|
| PRK07308 |
PRK07308 |
flavodoxin; Validated |
66-188 |
1.51e-09 |
|
flavodoxin; Validated
Pssm-ID: 180922 [Multi-domain] Cd Length: 146 Bit Score: 56.72 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 66 LISASQTGNARRVAEQLRDDLLAAKLNVNL-----VNAGEYKFKQIAsekllVVVASTQGEGEPAEEAVALHKFLfskKA 140
Cdd:PRK07308 6 IVYASMTGNTEEIADIVADKLRELGHDVDVdecttVDASDFEDADIA-----IVATYTYGDGELPDEIVDFYEDL---AD 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 493179527 141 PKLEGTAFAVFGLGDTSYEFFCQSGKDFDSRLAELGAERLLDRVDADV 188
Cdd:PRK07308 78 LDLSGKIYGVVGSGDTFYDYFCKSVDDFEAQFALTGATKGAESVKVDL 125
|
|
| flav_short |
TIGR01753 |
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ... |
64-197 |
2.29e-09 |
|
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin mononucleotide (FMN) prosthetic group. They can act in nitrogen fixation by nitrogenase, in sulfite reduction, and light-dependent NADP+ reduction in during photosynthesis, among other roles. This model describes the short chain type. Many of these are involved in sulfite reduction. [Energy metabolism, Electron transport]
Pssm-ID: 273789 [Multi-domain] Cd Length: 140 Bit Score: 56.19 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 64 ITLISASQTGNARRVAEQLRDDLLAAKLNVNLVNAGEYKFKQIASEKLLVVVASTQGEGE-PAEEAValhKFLFSKKAPK 142
Cdd:TIGR01753 1 ILIVYASMTGNTEEMANIIAEGLKEAGAEVDLLEVADADAEDLLSYDAVLLGCSTWGDEDlEQDDFE---PFFEELEDID 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 493179527 143 LEGTAFAVFGLGDTSYEfFCQSGKDFDSRLAELGAERLLDRV----DADVEYQPAAAEW 197
Cdd:TIGR01753 78 LGGKKVALFGSGDWGYE-FCEAVDDWEERLKEAGATIIAEGLkvdgDPEEEDLDKCREF 135
|
|
| PRK06703 |
PRK06703 |
flavodoxin; Provisional |
69-178 |
5.04e-09 |
|
flavodoxin; Provisional
Pssm-ID: 235854 [Multi-domain] Cd Length: 151 Bit Score: 55.15 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 69 ASQTGNARRVAEQLRDDLLAAKLNVNLVNAGEYKFKQIASEKLLVVVASTQGEGEPAEEAVALHKFLfskKAPKLEGTAF 148
Cdd:PRK06703 9 ASMSGNTEDIADLIKVSLDAFDHEVVLQEMDGMDAEELLAYDGIILGSYTWGDGDLPYEAEDFHEDL---ENIDLSGKKV 85
|
90 100 110
....*....|....*....|....*....|
gi 493179527 149 AVFGLGDTSYEFFCQSGKDFDSRLAELGAE 178
Cdd:PRK06703 86 AVFGSGDTAYPLFCEAVTIFEERLVERGAE 115
|
|
| flavin_oxioreductase |
cd06189 |
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
388-570 |
1.05e-08 |
|
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: 56.02 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 388 RLYSIASSQAEVEN-EVHVtvgvvrydiegRARAGGASSFLA-DRVEEEGDVRVFIEHNDnFRLPANPETPVIMIGPGTG 465
Cdd:cd06189 42 RPFSIASAPHEDGEiELHI-----------RAVPGGSFSDYVfEELKENGLVRIEGPLGD-FFLREDSDRPLILIAGGTG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 466 IAPFRAFMQQRAADEAPGKNWLFFGNPhfTEDFLYQVEWQR----------YVKegVLSRIDLAWsrdQKEKVYVQDKLR 535
Cdd:cd06189 110 FAPIKSILEHLLAQGSKRPIHLYWGAR--TEEDLYLDELLEawaeahpnftYVP--VLSEPEEGW---QGRTGLVHEAVL 182
|
170 180 190
....*....|....*....|....*....|....*
gi 493179527 536 EQGAELwrwinDGAHIYVCGDANrMAKDVEQALLE 570
Cdd:cd06189 183 EDFPDL-----SDFDVYACGSPE-MVYAARDDFVE 211
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
387-570 |
2.15e-08 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 55.25 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 387 PRLYSIASSQAEvENEVHVTVGVVrydiegraraGGASSFLADRveEEGDvRVFIE--HNDNFRLPANPEtPVIMIGPGT 464
Cdd:COG0543 42 RRPFSIASAPRE-DGTIELHIRVV----------GKGTRALAEL--KPGD-ELDVRgpLGNGFPLEDSGR-PVLLVAGGT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 465 GIAPFRAFMqqRAADEAPGKNWLFFG----NPHFTEDFLYQVEWQRYVkegVLSriDLAWsrdQKEKVYVQDKLREQGAE 540
Cdd:COG0543 107 GLAPLRSLA--EALLARGRRVTLYLGartpEDLYLLDELEALADFRVV---VTT--DDGW---YGRKGFVTDALKELLAE 176
|
170 180 190
....*....|....*....|....*....|
gi 493179527 541 lwrwiNDGAHIYVCGdANRMAKDVEQALLE 570
Cdd:COG0543 177 -----DSGDDVYACG-PPPMMKAVAELLLE 200
|
|
| O2ase_reductase_like |
cd06187 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
383-569 |
2.36e-08 |
|
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: 54.91 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 383 RPLTPRLYSIASSQAEV-ENEVHVtvgvvrydiegRARAGGASSFLADRVEEEGDvRVFIEHN-DNFRLPANPETPVIMI 460
Cdd:cd06187 37 RPRTWRAYSPANPPNEDgEIEFHV-----------RAVPGGRVSNALHDELKVGD-RVRLSGPyGTFYLRRDHDRPVLCI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 461 GPGTGIAPFRAFMQQRAADEAPGKNWLFFGNPhfTEDFLYQVE----------WQRYVKegVLSRIDLAWSRdqkEKVYV 530
Cdd:cd06187 105 AGGTGLAPLRAIVEDALRRGEPRPVHLFFGAR--TERDLYDLEgllalaarhpWLRVVP--VVSHEEGAWTG---RRGLV 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 493179527 531 QDKLREQGAELwrwinDGAHIYVCGDANrMAKDVEQALL 569
Cdd:cd06187 178 TDVVGRDGPDW-----ADHDIYICGPPA-MVDATVDALL 210
|
|
| FNR_iron_sulfur_binding_2 |
cd06216 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
388-555 |
1.61e-06 |
|
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: 49.53 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 388 RLYSIASSQAEVENEVHVTVgvvrydiegRARAGGA-SSFLADRVEEeGDVrVFIEH-NDNFRLPANPETPVIMIGPGTG 465
Cdd:cd06216 65 RSYSLSSSPTQEDGTITLTV---------KAQPDGLvSNWLVNHLAP-GDV-VELSQpQGDFVLPDPLPPRLLLIAAGSG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 466 IAPFRAFMQQRAADEAPGKNWLFFGNPHfTEDFLYQVEWQRYVKEGVLSRIDLAWSRDQKEkvyvQDKLREQGAELWRWI 545
Cdd:cd06216 134 ITPVMSMLRTLLARGPTADVVLLYYART-REDVIFADELRALAAQHPNLRLHLLYTREELD----GRLSAAHLDAVVPDL 208
|
170
....*....|
gi 493179527 546 NDgAHIYVCG 555
Cdd:cd06216 209 AD-RQVYACG 217
|
|
| PRK05723 |
PRK05723 |
flavodoxin; Provisional |
64-206 |
6.42e-06 |
|
flavodoxin; Provisional
Pssm-ID: 168208 Cd Length: 151 Bit Score: 46.33 E-value: 6.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 64 ITLISASQTGNARRVAEQLRDDLLAAKLNV-NLVNAGEYKFKQIASEKLLVVvASTQGEGEPAEEAVALHKFLFSKKAPK 142
Cdd:PRK05723 3 VAILSGSVYGTAEEVARHAESLLKAAGFEAwHNPRASLQDLQAFAPEALLAV-TSTTGMGELPDNLMPLYSAIRDQLPAA 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493179527 143 LEGTAFAVFGLGDTSY-EFFCQSGKDFDSRLAELGAERLLD--RVDADVEYQPA--AAEWRARIVDVLK 206
Cdd:PRK05723 82 WRGLPGAVIALGDSSYgDTFCGGGEQMRELFAELGVREVQPmlRLDASETVTPEtdAEPWLAEFAAALK 150
|
|
| FNR1 |
cd06195 |
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ... |
367-570 |
1.51e-05 |
|
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: 46.79 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 367 RFSPAQLdadALIGLLRPLTPRL---YSIASSQAEVENEVHVTvgvvrydiegRARAGGASSFLADRveEEGDvRVFIEH 443
Cdd:cd06195 24 RFQAGQF---TKLGLPNDDGKLVrraYSIASAPYEENLEFYII----------LVPDGPLTPRLFKL--KPGD-TIYVGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 444 NDNFRLPANPETP---VIMIGPGTGIAPFRAFMQQRAADEAPGKNWLFFG---------NPHFTEdFLYQVEWQ-RYVKe 510
Cdd:cd06195 88 KPTGFLTLDEVPPgkrLWLLATGTGIAPFLSMLRDLEIWERFDKIVLVHGvryaeelayQDEIEA-LAKQYNGKfRYVP- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 511 gVLSRIDLAWSRDQKEKVYVQDKLREQGAELwRWINDGAHIYVCGDANrMAKDVEQALLE 570
Cdd:cd06195 166 -IVSREKENGALTGRIPDLIESGELEEHAGL-PLDPETSHVMLCGNPQ-MIDDTQELLKE 222
|
|
| FNR_N-term_Iron_sulfur_binding |
cd06194 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
366-468 |
4.71e-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: 44.95 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 366 VRFSPAQLdadalIGLLRP-LTPRLYSIASSQAE-VENEVHVTvgvvrydiegRARAGGASSFLADRVEEEGDVRVFIEH 443
Cdd:cd06194 22 LPYLPGQY-----VNLRRAgGLARSYSPTSLPDGdNELEFHIR----------RKPNGAFSGWLGEEARPGHALRLQGPF 86
|
90 100
....*....|....*....|....*
gi 493179527 444 NDNFRLPANPETPVIMIGPGTGIAP 468
Cdd:cd06194 87 GQAFYRPEYGEGPLLLVGAGTGLAP 111
|
|
| FNR_iron_sulfur_binding_3 |
cd06217 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
388-570 |
5.52e-05 |
|
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99813 [Multi-domain] Cd Length: 235 Bit Score: 44.95 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 388 RLYSIASSQAEvenEVHVTVGVVRYDiegrarAGGASSFLADRVEEeGDvRVFIEH-NDNFRLPANPETPVIMIGPGTGI 466
Cdd:cd06217 51 RSYSIASSPTQ---RGRVELTVKRVP------GGEVSPYLHDEVKV-GD-LLEVRGpIGTFTWNPLHGDPVVLLAGGSGI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 467 APFRAFMQQRAADEAPGKNWLFFGNPHfTEDFLYQVEWQRYVKEGVLSRIDLAWSRdqkekVYVQDKLREQG-------A 539
Cdd:cd06217 120 VPLMSMIRYRRDLGWPVPFRLLYSART-AEDVIFRDELEQLARRHPNLHVTEALTR-----AAPADWLGPAGritadliA 193
|
170 180 190
....*....|....*....|....*....|.
gi 493179527 540 ELWRWInDGAHIYVCGdANRMAKDVEQALLE 570
Cdd:cd06217 194 ELVPPL-AGRRVYVCG-PPAFVEAATRLLLE 222
|
|
| PRK09267 |
PRK09267 |
flavodoxin FldA; Validated |
64-162 |
1.49e-04 |
|
flavodoxin FldA; Validated
Pssm-ID: 236439 [Multi-domain] Cd Length: 169 Bit Score: 42.51 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 64 ITLISASQTGNARRVAEQLRDDLlaAKLNVNLVNAGEYKFKQIASEKLLVVVASTQGEGEPA---EEavalhkFLFSKKA 140
Cdd:PRK09267 4 IGIFFGSDTGNTEDIAKMIQKKL--GKDVADVVDIAKASKEDFEAYDLLILGIPTWGYGELQcdwDD------FLPELEE 75
|
90 100
....*....|....*....|....
gi 493179527 141 PKLEGTAFAVFGLGD-TSY-EFFC 162
Cdd:PRK09267 76 IDFSGKKVALFGLGDqEDYaEYFC 99
|
|
| phenol_2-monooxygenase_like |
cd06211 |
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ... |
386-515 |
2.09e-04 |
|
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use molecular oxygen as a substrate in the microbial degredation of phenol. This protein is encoded by a single gene and uses a tightly bound FAD cofactor in the NAD(P)H dependent conversion of phenol and O2 to catechol and H2O. This group is related to the NAD binding ferredoxin reductases.
Pssm-ID: 99807 Cd Length: 238 Bit Score: 43.08 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 386 TPRLYSIASSQAEvENEVHVTVGVVrydiegrarAGGASSFLADRVEEEGDVRVFIEHNDNFRLPANPETPVIMIGPGTG 465
Cdd:cd06211 51 GTRAFSIASSPSD-AGEIELHIRLV---------PGGIATTYVHKQLKEGDELEISGPYGDFFVRDSDQRPIIFIAGGSG 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 493179527 466 IAPFRAFMQQRAADEAPGKNWLFFG--NPH--FTEDFLYQVEWQ----RYVKegVLSR 515
Cdd:cd06211 121 LSSPRSMILDLLERGDTRKITLFFGarTRAelYYLDEFEALEKDhpnfKYVP--ALSR 176
|
|
| PRK07609 |
PRK07609 |
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated |
381-591 |
1.26e-03 |
|
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
Pssm-ID: 181058 [Multi-domain] Cd Length: 339 Bit Score: 41.39 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 381 LLRPLTPRLYSIASS-QAEVENEVHVtvgvvrydiegRARAGGASS-FLADRVEEEGDVRVFIEHNDnFRLPANPETPVI 458
Cdd:PRK07609 141 ILKDGKRRSYSIANApHSGGPLELHI-----------RHMPGGVFTdHVFGALKERDILRIEGPLGT-FFLREDSDKPIV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 459 MIGPGTGIAPFRAFMQQRAADEAPGKNWLFFGNPhfTEDFLYQVEWQ----------RYVKegVLS--RIDLAWsrdQKE 526
Cdd:PRK07609 209 LLASGTGFAPIKSIVEHLRAKGIQRPVTLYWGAR--RPEDLYLSALAeqwaeelpnfRYVP--VVSdaLDDDAW---TGR 281
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493179527 527 KVYVQDKLREQGAELwrwinDGAHIYVCGdANRMakdVEQALLEVIAEfgGMDVET--ADEFLSELR 591
Cdd:PRK07609 282 TGFVHQAVLEDFPDL-----SGHQVYACG-SPVM---VYAARDDFVAA--GLPAEEffADAFTYAAD 337
|
|
| FNR_like_1 |
cd06196 |
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ... |
456-570 |
1.55e-03 |
|
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal region may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99793 [Multi-domain] Cd Length: 218 Bit Score: 40.30 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 456 PVIMIGPGTGIAPFRAFMQQRAADEAPGKNWLFFGNPhfTE-DFLYQVEWQRYVKEGVlsriDLAWSRDQKEKVYVQdkl 534
Cdd:cd06196 101 PGVFIAGGAGITPFIAILRDLAAKGKLEGNTLIFANK--TEkDIILKDELEKMLGLKF----INVVTDEKDPGYAHG--- 171
|
90 100 110
....*....|....*....|....*....|....*...
gi 493179527 535 REQGAELWRWINDGA-HIYVCG-DAnrMAKDVEQALLE 570
Cdd:cd06196 172 RIDKAFLKQHVTDFNqHFYVCGpPP--MEEAINGALKE 207
|
|
| oxygenase_e_transfer_subunit |
cd06213 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
387-555 |
3.14e-03 |
|
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. 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 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: 99809 Cd Length: 227 Bit Score: 39.60 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 387 PRLYSIASSQAEvENEVHVTVgvvrydiegRARAGGASS---FLADRVEEEGDVRVfiEHNDnFRL-PANpeTPVIMIGP 462
Cdd:cd06213 44 ARSYSFANAPQG-DGQLSFHI---------RKVPGGAFSgwlFGADRTGERLTVRG--PFGD-FWLrPGD--APILCIAG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 463 GTGIAPFRAFMQQRAADEAPGKNWLFFGNPhfTEDFLYQVE---------WQRYVKEGVLSR--IDLAWsrdQKEKVYVQ 531
Cdd:cd06213 109 GSGLAPILAILEQARAAGTKRDVTLLFGAR--TQRDLYALDeiaaiaarwRGRFRFIPVLSEepADSSW---KGARGLVT 183
|
170 180
....*....|....*....|....
gi 493179527 532 DKLREQGAElwrwindGAHIYVCG 555
Cdd:cd06213 184 EHIAEVLLA-------ATEAYLCG 200
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
451-570 |
4.64e-03 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 39.88 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493179527 451 ANPETPVIMIGPGTGIAPFRAFMQQRAADEAPGKN-WLFFGNPHfTEDFLYQVEWQRYVKEgvLSRIDLaWSRDQKEKVY 529
Cdd:COG4097 315 RDTAPRQVWIAGGIGITPFLALLRALAARPGDQRPvDLFYCVRD-EEDAPFLEELRALAAR--LAGLRL-HLVVSDEDGR 390
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 493179527 530 V-QDKLREQGAELwrwinDGAHIYVCGDAnRMAKDVEQALLE 570
Cdd:COG4097 391 LtAERLRRLVPDL-----AEADVFFCGPP-GMMDALRRDLRA 426
|
|
| |
