|
Name |
Accession |
Description |
Interval |
E-value |
| cysJ |
PRK10953 |
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit; |
1-599 |
0e+00 |
|
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
Pssm-ID: 182862 [Multi-domain] Cd Length: 600 Bit Score: 1355.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 1 MTTPAPLTGLLPLNPEQLARLQAATTDLTPEQLAWVSGYFWGVLNPRSGAVAVTPVPERKMLGVTLISASQTGNARRVAE 80
Cdd:PRK10953 1 MTTQAPPSALLPLNPEQLARLQAATTDLSPTQLAWVSGYFWGVLNQQPGAVAATPAPAAEMPGITLISASQTGNARRVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 81 ALRDDLLAANLNVTLVNAGDYKFKQIASEKLLVIVTSTQGEGEPPEEAVALHKFLFSKKAPKLTDTAFAVFSLGDTSYEF 160
Cdd:PRK10953 81 QLRDDLLAAKLNVNLVNAGDYKFKQIAQEKLLIVVTSTQGEGEPPEEAVALHKFLFSKKAPKLENTAFAVFGLGDTSYEF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 161 FCQSGKDFDSKLAELGGERLLDRVDADVEYQAAASEWRARVVDVLKSRVP-VAAPSQSVATGAVNDIHTSPYTKDAPLTA 239
Cdd:PRK10953 161 FCQAGKDFDSKLAELGAERLLDRVDADVEYQAAASEWRARVVDALKSRAPaVAAPSQSVATGAVNEIHTSPYSKEAPLTA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 240 TLAVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVKEIVELLWLKGDEPVTVDGKTLPLAEALEWHF 319
Cdd:PRK10953 241 SLSVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVKELVELLWLKGDEPVTVDGKTLPLAEALQWHF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 320 ELTVNTANIVENYATLTRSESLLPLVGDKAQLQHYAATTPIVDMVRFSPAQLDAEALIGLLRPLTPRLYSIASAQAEVES 399
Cdd:PRK10953 321 ELTVNTANIVENYATLTRSETLLPLVGDKAALQHYAATTPIVDMVRFAPAQLDAEQLIGLLRPLTPRLYSIASSQAEVEN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 400 EVHVTVGVVRYDIEGRARAGGASSFLADRVEEEGEVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADGA 479
Cdd:PRK10953 401 EVHITVGVVRYDIEGRARAGGASSFLADRLEEEGEVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADGA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 480 EGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLNRIDLAWSRDQKEKIYVQDKLREQGAELWRWINDGAHIYVCGDARRMA 559
Cdd:PRK10953 481 PGKNWLFFGNPHFTEDFLYQVEWQRYVKEGLLTRIDLAWSRDQKEKIYVQDKLREQGAELWRWINDGAHIYVCGDANRMA 560
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2070305039 560 ADVEKALLEVIAEFGAMDIEAADEFLSELRVERRYQRDVY 599
Cdd:PRK10953 561 KDVEQALLEVIAEFGGMDTEAADEFLSELRVERRYQRDVY 600
|
|
| cysJ |
TIGR01931 |
sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an ... |
10-599 |
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: 1027.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 10 LLPLNPEQLARLQAATTDLTPEQLAWVSGYFWGVLNPRSGAVAVTPVPERKMLG----VTLISASQTGNARRVAEALRDD 85
Cdd:TIGR01931 3 NSPLNQEQLDLLNRLLPTLTEAQLAWLSGYLWALANQTPAALSVAPNEAEEPAAqekrVTILYGSQTGNARRLAKRLAEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 86 LLAANLNVTLVNAGDYKFKQIASEKLLVIVTSTQGEGEPPEEAVALHKFLFSKKAPKLTDTAFAVFSLGDTSYEFFCQSG 165
Cdd:TIGR01931 83 LEAAGFSVRLSSADDYKFKQLKKERLLLLVISTQGEGEPPEEAISLHKFLHSKKAPKLENLRYSVLGLGDSSYEFFCQTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 166 KDFDSKLAELGGERLLDRVDADVEYQAAASEWRARVVDVLKSRVPV--AAPSQSVaTGAVNDIHTSPYTKDAPLTATLAV 243
Cdd:TIGR01931 163 KDFDKRLEELGGKRLLPRVDADLDYDANAAEWRAGVLTALNEQAKGgaSTPSASE-TSTPLQTSTSVYSKQNPFRAEVLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 244 NQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVKEIVELLWLKGDEPVTVDGKTLPLAEALEWHFELTV 323
Cdd:TIGR01931 242 NQKITGRNSKKDVRHIEIDLEGSGLHYEPGDALGVWYKNDPALVKEILKLLNLDPDEKVTIGGKTIPLFEALITHFELTQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 324 NTANIVENYATLTRSESLLPLVGDKAQLQHYAATTPIVDMVRFSPAQLDAEALIGLLRPLTPRLYSIASAQAEVESEVHV 403
Cdd:TIGR01931 322 NTKPLLKAYAELTGNKELKALIADNEKLKAYIQNTPLIDLIRDYPADLDAEQLISLLRPLTPRLYSISSSQSEVGDEVHL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 404 TVGVVRYDIEGRARAGGASSFLADRVEEEGEVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADGAEGKN 483
Cdd:TIGR01931 402 TVGVVRYQAHGRARLGGASGFLAERLKEGDTVPVYIEPNDNFRLPEDPDTPIIMIGPGTGVAPFRAFMQERAEDGAKGKN 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 484 WLFFGNPHFTEDFLYQVEWQRYVKEGVLNRIDLAWSRDQKEKIYVQDKLREQGAELWRWINDGAHIYVCGDARRMAADVE 563
Cdd:TIGR01931 482 WLFFGNPHFTTDFLYQVEWQNYLKKGVLTKMDLAFSRDQAEKIYVQHRIREQGAELWQWLQEGAHIYVCGDAKKMAKDVH 561
|
570 580 590
....*....|....*....|....*....|....*.
gi 2070305039 564 KALLEVIAEFGAMDIEAADEFLSELRVERRYQRDVY 599
Cdd:TIGR01931 562 QALLDIIAKEGHLDAEEAEEYLTDLRVEKRYQRDVY 597
|
|
| CysJ |
COG0369 |
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ... |
35-599 |
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: 930.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 35 WVSGYFWGVLNpRSGAVAVTPVPERKMLGVTLISASQTGNARRVAEALRDDLLAANLNVTLVNAGDYKFKQIASEKLLVI 114
Cdd:COG0369 1 WLSGYLAGLAS-RAAAAAAAAAAAAAGTPLTILYGSQTGNAEGLAEQLAERAKAAGLAVTLASLDDYKPKDLAKEGLLLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 115 VTSTQGEGEPPEEAVALHKFLFSKKAPKLTDTAFAVFSLGDTSYEFFCQSGKDFDSKLAELGGERLLDRVDADVEYQAAA 194
Cdd:COG0369 80 VTSTYGEGEPPDNARAFYEFLHSKKAPKLDGLRYAVLGLGDSSYETFCQTGKDFDARLEELGATRLLPRVDCDVDYEEAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 195 SEWRARVVDVLKSRVPVAAPSQSVATGAvndihTSPYTKDAPLTATLAVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGD 274
Cdd:COG0369 160 EAWLAAVLAALAEALGAAAAAAAAAAAA-----APAYSRKNPFPATVLENRELTGRGSAKETRHIEIDLPGSGLSYEPGD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 275 ALGVWYQNDPALVKEIVELLWLKGDEPVTVDGKTLPLAEALEWHFELTVNTANIVENYATLTRSESLLPLV--GDKAQLQ 352
Cdd:COG0369 235 ALGVWPENDPALVDELLARLGLDGDEPVTLDGEPLSLREALTEHLELTRLTPPLLEKYAELTGNAELAALLadEDKAALR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 353 HYAATTPIVDMVR-FSPAQLDAEALIGLLRPLTPRLYSIASAQAEVESEVHVTVGVVRYDIEGRARAGGASSFLADRvEE 431
Cdd:COG0369 315 EYLAGRQLLDLLReFPAAELSAEELLELLRPLTPRLYSISSSPKAHPDEVHLTVGVVRYEASGRERKGVASTYLADL-EE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 432 EGEVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADGAEGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVL 511
Cdd:COG0369 394 GDTVPVFVEPNPNFRLPADPDTPIIMIGPGTGIAPFRAFLQEREARGASGKNWLFFGDRHFTTDFLYQTELQAWLKDGVL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 512 NRIDLAWSRDQKEKIYVQDKLREQGAELWRWINDGAHIYVCGDARRMAADVEKALLEVIAEFGAMDIEAADEFLSELRVE 591
Cdd:COG0369 474 TRLDLAFSRDQAEKIYVQHRLLEQGAELWAWLEEGAHVYVCGDASRMAKDVDAALLDIIAEHGGLSEEEAEEYLAELRAE 553
|
....*...
gi 2070305039 592 RRYQRDVY 599
Cdd:COG0369 554 KRYQRDVY 561
|
|
| SiR |
cd06199 |
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
240-599 |
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: 588.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 240 TLAVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVKEIVELLWLKGDEPV-TVDGKTLPLAEALEWH 318
Cdd:cd06199 1 TVLENRLLTGPGSEKETRHIELDLEGSGLSYEPGDALGVYPTNDPALVDELLAALGLSGDEPVsTVGGGTLPLREALIKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 319 FELTVNTANIVENYATLTRSESLLPLvGDKAQLQHYAATTPIVDMVRFSPAQLDAEALIGLLRPLTPRLYSIASAQAEVE 398
Cdd:cd06199 81 YEITTLLLALLESYAADTGALELLAL-AALEAVLAFAELRDVLDLLPIPPARLTAEELLDLLRPLQPRLYSIASSPKAVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 399 SEVHVTVGVVRYDIEGRARAGGASSFLADRVEEEGEVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADG 478
Cdd:cd06199 160 DEVHLTVAVVRYESHGRERKGVASTFLADRLKEGDTVPVFVQPNPHFRLPEDPDAPIIMVGPGTGIAPFRAFLQEREATG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 479 AEGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLNRIDLAWSRDQKEKIYVQDKLREQGAELWRWINDGAHIYVCGDARRM 558
Cdd:cd06199 240 AKGKNWLFFGERHFATDFLYQDELQQWLKDGVLTRLDTAFSRDQAEKVYVQDRMREQGAELWAWLEEGAHFYVCGDAKRM 319
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2070305039 559 AADVEKALLEVIAEFGAMDIEAADEFLSELRVERRYQRDVY 599
Cdd:cd06199 320 AKDVDAALLDIIATEGGMDEEEAEAYLKELKKEKRYQRDVY 360
|
|
| PRK06214 |
PRK06214 |
sulfite reductase subunit alpha; |
10-599 |
7.52e-150 |
|
sulfite reductase subunit alpha;
Pssm-ID: 235745 [Multi-domain] Cd Length: 530 Bit Score: 442.20 E-value: 7.52e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 10 LLPLNPEqlarlqaaTTDLTPEQLAWVSGYFWGVLNPRSGavavtpvperkmlGVTLISASQTGNARRVAEALRDDLLAA 89
Cdd:PRK06214 1 LISLIPE--------SAPFSEEQRAWLNGFFAGLLGPDVE-------------GATALSPGEAPALLAAPPAAADDDDAP 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 90 NLNVTLvnagdykfkqiasekllvivtstqgegePPEEAVALHKflfSKKAPKLTDTAFAVFSLGDTSYEffCQ------ 163
Cdd:PRK06214 60 WHDPSL----------------------------PIDERMALAE---GRPLPRKLMAAMAQQDCGQCGYN--CQdyaeai 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 164 -SGKDFDSKLAELGGE---RLLDRVDAdvEYQAAasewrarvvdvlksrvPVAAPSQSVATGAVNDIHTSP---YTKDAP 236
Cdd:PRK06214 107 aSGEEKRLNLCAPGGKetaRMLKKLAE--EFGAA----------------PAAAAPAAAAADAAPAAAALGplgTSRDNP 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 237 LTATLAVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVKEIVELLWLKGDEPVtvdgKTLPLAEALE 316
Cdd:PRK06214 169 VEATFLSRRRLNKPGSEKETWHVEIDLAGSGLDYEVGDSLGLFPANDPALVDAVIAALGAPPEFPI----GGKTLREALL 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 317 WHFELTVNTANIVENYATLTRS----------ESLLPlVGDKAQLQHYAATTpivdmvRFSPAQLDAEALIGLLRPLTPR 386
Cdd:PRK06214 245 EDVSLGPAPDGLFELLSYITGGaarkkaralaAGEDP-DGDAATLDVLAALE------KFPGIRPDPEAFVEALDPLQPR 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 387 LYSIASAQAEVESEVHVTVGVVRYDIEGRARAGGASSFLADRVEEEGEVRVFIEHNDNFRLPANPETPVIMIGPGTGIAP 466
Cdd:PRK06214 318 LYSISSSPKATPGRVSLTVDAVRYEIGSRLRLGVASTFLGERLAPGTRVRVYVQKAHGFALPADPNTPIIMVGPGTGIAP 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 467 FRAFMQQRAADGAEGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLNRIDLAWSRDQKEKIYVQDKLREQGAELWRWINDG 546
Cdd:PRK06214 398 FRAFLHERAATKAPGRNWLFFGHQRSATDFFYEDELNGLKAAGVLTRLSLAWSRDGEEKTYVQDRMRENGAELWKWLEEG 477
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2070305039 547 AHIYVCGDARRMAADVEKALLEVIAEFGAMDIEAADEFLSELRVERRYQRDVY 599
Cdd:PRK06214 478 AHFYVCGDAKRMAKDVERALVDIVAQFGGRSPDEAVAFVAELKKAGRYQADVY 530
|
|
| CYPOR_like |
cd06182 |
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
240-599 |
2.57e-109 |
|
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: 328.91 E-value: 2.57e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 240 TLAVNQKITGRNSEKDVRHIEIDL-GDSGLRYQPGDALGVWYQNdpalvkeivellwlkgdepvtvdgktlplaealewh 318
Cdd:cd06182 1 AITVNRKLTPPDSPRSTRHLEFDLsGNSVLKYQPGDHLGVIPPN------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 319 feltvntanivenyatltrsesllplvgdkaqlqhyaattpivdmvrfspaqldaealigllrPLTPRLYSIASAQAEVE 398
Cdd:cd06182 45 ---------------------------------------------------------------PLQPRYYSIASSPDVDP 61
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 399 SEVHVTVGVVRY-DIEGRARAGGASSFLADRVEEeGEVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAA- 476
Cdd:cd06182 62 GEVHLCVRVVSYeAPAGRIRKGVCSNFLAGLQLG-AKVTVFIRPAPSFRLPKDPTTPIIMVGPGTGIAPFRGFLQERAAl 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 477 ---DGAEGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLNRIDLAWSRDQ-KEKIYVQDKLREQGAELWRWINDGAHIYVC 552
Cdd:cd06182 141 ranGKARGPAWLFFGCRNFASDYLYREELQEALKDGALTRLDVAFSREQaEPKVYVQDKLKEHAEELRRLLNEGAHIYVC 220
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2070305039 553 GDARRMAADVEKALLEVIAEFGAMDIEAADEFLSELRVERRYQRDVY 599
Cdd:cd06182 221 GDAKSMAKDVEDALVKIIAKAGGVDESDAEEYLKELEDEGRYVEDVW 267
|
|
| CYPOR |
cd06204 |
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
236-598 |
2.39e-99 |
|
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: 308.42 E-value: 2.39e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 236 PLTATLAVNQKITGrNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVKEIVELLWLKGDEPV----TVDGKTL-- 309
Cdd:cd06204 5 PFLAPVAVSRELFT-GSDRSCLHIEFDISGSGIRYQTGDHLAVWPTNPSEEVERLLKVLGLDDRDTVislkSLDEPASkk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 310 -----P--LAEALEWHFELT--VNTANIVE--NYATLTRSESLLPLVGDKAQlQHYA-----ATTPIVD-MVRFSPAQLD 372
Cdd:cd06204 84 vpfpcPttYRTALRHYLDITapVSRQVLAAlaQFAPDPEEKERLLKLASEGK-DEYAkwivePHRNLLEvLQDFPSAKPT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 373 A---EALIGLLRPLTPRLYSIASAQAEVESEVHVTVGVVRYDI-EGRARAGGASSFLADRVEEE---------------- 432
Cdd:cd06204 163 PppfDFLIELLPRLQPRYYSISSSSKVHPNRIHITAVVVKYPTpTGRIIKGVATNWLLALKPALngekpptpyylsgprk 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 433 ----GEVRVFIEHNdNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADGAEGKNW----LFFGNPHFTEDFLYQVEWQR 504
Cdd:cd06204 243 kgggSKVPVFVRRS-NFRLPTKPSTPVIMIGPGTGVAPFRGFIQERAALKESGKKVgptlLFFGCRHPDEDFIYKDELEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 505 YVKEGVLNRIDLAWSRDQKEKIYVQDKLREQGAELWRWINDGAHIYVCGDARRMAADVEKALLEVIAEFGAMDIEAADEF 584
Cdd:cd06204 322 YAKLGGLLELVTAFSREQPKKVYVQHRLAEHAEQVWELINEGAYIYVCGDAKNMARDVEKTLLEILAEQGGMTETEAEEY 401
|
410
....*....|....
gi 2070305039 585 LSELRVERRYQRDV 598
Cdd:cd06204 402 VKKLKTRGRYQEDV 415
|
|
| CyPoR_like |
cd06207 |
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
244-599 |
6.91e-95 |
|
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: 295.72 E-value: 6.91e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 244 NQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVKEIVELLWLKGDEPVTVDGKTLPLAEALEWHfELTV 323
Cdd:cd06207 5 NKRLTPADYDRSTRHIEFDLGGSGLSYETGDNLGIYPENSDALVDEFLARLGLDGDDVVRVEPNEQQRGKPPFPE-PISV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 324 NTAnIVEN---YATLTRS--ESLLPLVGD---KAQLQHYAA-----TTPIVDMVR-------FSPAQLDAEALIGLLRPL 383
Cdd:cd06207 84 RQL-LKKFldiFGKPTKKflKLLSQLATDeeeKEDLYKLASregrtEYKRYEKYTylevlkdFPSVRPTLEQLLELCPLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 384 TPRLYSIASAQAEVESEVHVTVGVVRY-DIEGRARAGGASSFLAdRVEEEGEVRVFIeHNDNFRLPANPETPVIMIGPGT 462
Cdd:cd06207 163 KPRYYSISSSPLKNPNEVHLLVSLVSWkTPSGRSRYGLCSSYLA-GLKVGQRVTVFI-KKSSFKLPKDPKKPIIMVGPGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 463 GIAPFRAFMQQRAADGAEGKN----WLFFGNPHFTEDFLYQVEWQRYVKEGVLNRIDLAWSRDQKEKIYVQDKLREQGAE 538
Cdd:cd06207 241 GLAPFRAFLQERAALLAQGPEigpvLLYFGCRHEDKDYLYKEELEEYEKSGVLTTLGTAFSRDQPKKVYVQDLIRENSDL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070305039 539 LWRWINDGAH-IYVCGDARRMAADVEKALLEVIAEFGAMDIEAADEFLSELRVERRYQRDVY 599
Cdd:cd06207 321 VYQLLEEGAGvIYVCGSTWKMPPDVQEAFEEILKKHGGGDEELAEKKIEELEERGRYVVEAW 382
|
|
| Nitric_oxide_synthase |
cd06202 |
The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses ... |
245-599 |
1.11e-69 |
|
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: 230.68 E-value: 1.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 245 QKITGRNSEKDVRHIEIDL-GDSGLRYQPGDALGVWYQNDPALVKEIVELLWLK--GDEPVTV----------------- 304
Cdd:cd06202 6 QNLQSPKSSRSTILVKLDTnGAQELHYQPGDHVGIFPANRPELVDALLDRLHDAppPDQVIKLevleerstalgiiktwt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 305 DGKTLP---LAEALEWHFELT-VNTANIVENYATLTRSESllplvgDKAQLQ-------------HYAATTpIVDMVR-F 366
Cdd:cd06202 86 PHERLPpctLRQALTRYLDITtPPTPQLLQLLATLATDEK------DKERLEvlgkgsseyedwkWYKNPN-ILEVLEeF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 367 SPAQLDAEALIGLLRPLTPRLYSIASAQAEVESEVHVTVGVVRY---DIEGRARAGGASSFLaDRVEEEGEVRVFIEHND 443
Cdd:cd06202 159 PSLQVPASLLLTQLPLLQPRYYSISSSPDMYPGEIHLTVAVVSYrtrDGQGPVHHGVCSTWL-NGLTPGDTVPCFVRSAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 444 NFRLPANPETPVIMIGPGTGIAPFRAFMQQRAAD----GAEGKNW----LFFGNPHFTEDFLYQVEWQRYVKEGVLNRID 515
Cdd:cd06202 238 SFHLPEDPSVPVIMVGPGTGIAPFRSFWQQRQYDlrmsEDPGKKFgdmtLFFGCRNSTIDDIYKEETEEAKNKGVLTEVY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 516 LAWSRDQ-KEKIYVQDKLREQGAELWRWI-NDGAHIYVCGDArRMAADVEKALLEVIAEFGAMDIEAADEFLSELRVERR 593
Cdd:cd06202 318 TALSREPgKPKTYVQDLLKEQAESVYDALvREGGHIYVCGDV-TMAEDVSQTIQRILAEHGNMSAEEAEEFILKLRDENR 396
|
....*.
gi 2070305039 594 YQRDVY 599
Cdd:cd06202 397 YHEDIF 402
|
|
| methionine_synthase_red |
cd06203 |
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ... |
245-599 |
1.40e-65 |
|
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: 219.89 E-value: 1.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 245 QKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVKEIVELLWL--KGDEPVTV--DGKTLPLAEALEWHFE 320
Cdd:cd06203 6 KKLTEGDDVKTVVDLTLDLSPTGFDYQPGDTIGILPPNTASEVESLLKRLGLleQADQPCEVkvVPNTKKKNAKVPVHIP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 321 LTVNTANIVENYATLTRS------ESLLPLVGDKAQ------LQHYAATTPIVDMVRFSPAQ----LDA--------EAL 376
Cdd:cd06203 86 KVVTLRTILTWCLDIRAIpkkpllRALAEFTSDDNEkrrleeLCSKQGSEDYTDFVRKRGLSlldlLEAfpscrpplSLL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 377 IGLLRPLTPRLYSIASAQAEVESEVHVTVGVVRYDIEGRaraggASSFLADRV----EEEGEVRVFIEHNDNFRLPA-NP 451
Cdd:cd06203 166 IEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPAKGL-----CTSWLESLClsasSHGVKVPFYLRSSSRFRLPPdDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 452 ETPVIMIGPGTGIAPFRAFMQQRAA------DGAEGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLNRIDLAWSRDQ--- 522
Cdd:cd06203 241 RRPIIMVGPGTGVAPFLGFLQHREKlkeshtETVFGEAWLFFGCRHRDRDYLFRDELEEFLEEGILTRLIVAFSRDEndg 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2070305039 523 KEKIYVQDKLREQGAELWRWI-NDGAHIYVCGDARRMAADVEKALLEVIAEFGAMDIEAADEFLSELRVERRYQRDVY 599
Cdd:cd06203 321 STPKYVQDKLEERGKKLVDLLlNSNAKIYVCGDAKGMAKDVRDTFVDILSKELGLDKLEAKKLLARLRKEDRYLEDVW 398
|
|
| bifunctional_CYPOR |
cd06206 |
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ... |
257-599 |
8.93e-62 |
|
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: 209.04 E-value: 8.93e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 257 RHIEIDLGDsGLRYQPGDALGVWYQNDPALVKEIVELLWLKGDEPVTVD----------GKTLPLAEALEWHFEL-TVNT 325
Cdd:cd06206 18 RHLELRLPD-GMTYRAGDYLAVLPRNPPELVRRALRRFGLAWDTVLTISasgsatglplGTPISVSELLSSYVELsQPAT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 326 ANIVENYATLTRSESLLPLVGDkAQLQHYAA-----TTPIVDMV-RFSPAQLDAEALIGLLRPLTPRLYSIASAQAEVES 399
Cdd:cd06206 97 RRQLAALAEATRCPDTKALLER-LAGEAYAAevlakRVSVLDLLeRFPSIALPLATFLAMLPPMRPRQYSISSSPLVDPG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 400 EVHVTVGVVR---YDIEGRARaGGASSFLAdRVEEEGEVRVFI-EHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRA 475
Cdd:cd06206 176 HATLTVSVLDapaLSGQGRYR-GVASSYLS-SLRPGDSIHVSVrPSHSAFRPPSDPSTPLIMIAAGTGLAPFRGFLQERA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 476 A---DGAE-GKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLnRIDLAWSRD-QKEKIYVQDKLREQGAELWRWINDGAHIY 550
Cdd:cd06206 254 AllaQGRKlAPALLFFGCRHPDHDDLYRDELEEWEAAGVV-SVRRAYSRPpGGGCRYVQDRLWAEREEVWELWEQGARVY 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2070305039 551 VCGDaRRMAADVEKALLEVIAE----FGAMDIEAADEFLSELRVERRYQRDVY 599
Cdd:cd06206 333 VCGD-GRMAPGVREVLKRIYAEkderGGGSDDEEAEEWLEELRNKGRYATDVF 384
|
|
| SiR_like1 |
cd06200 |
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
382-599 |
2.12e-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: 174.39 E-value: 2.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 382 PLTPRLYSIASAQAEVESEVhvtvgVVRYDIEGRARAGGASSFLADRVEEEGEVRVFIEHNDNFRLPAnPETPVIMIGPG 461
Cdd:cd06200 45 PLPHREYSIASLPADGALEL-----LVRQVRHADGGLGLGSGWLTRHAPIGASVALRLRENPGFHLPD-DGRPLILIGNG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 462 TGIAPFRAFMQQRAADGAEGkNWLFFGNPHFTEDFLYQVEWQRYVKEGVLNRIDLAWSRDQKEKIYVQDKLREQGAELWR 541
Cdd:cd06200 119 TGLAGLRSHLRARARAGRHR-NWLLFGERQAAHDFFCREELEAWQAAGHLARLDLAFSRDQAQKRYVQDRLRAAADELRA 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2070305039 542 WINDGAHIYVCGDARRMAADVEKALLEVIAEfgamdieaadEFLSELRVERRYQRDVY 599
Cdd:cd06200 198 WVAEGAAIYVCGSLQGMAPGVDAVLDEILGE----------EAVEALLAAGRYRRDVY 245
|
|
| CYPOR_like_FNR |
cd06208 |
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ... |
381-599 |
6.61e-38 |
|
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: 141.69 E-value: 6.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 381 RPLTPRLYSIASAqAEVESEVHVTVG-----VVRYDIEG-RARAGGASSFLADRVEEEgEVRVFIEHNDNFRLPANPETP 454
Cdd:cd06208 60 KPHKLRLYSIASS-RYGDDGDGKTLSlcvkrLVYTDPETdETKKGVCSNYLCDLKPGD-DVQITGPVGKTMLLPEDPNAT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 455 VIMIGPGTGIAPFRAFMQQRAADGAE-----GKNWLFFGNPhfTED-FLYQVEWQRYVKEGVLN-RIDLAWSRDQK---- 523
Cdd:cd06208 138 LIMIATGTGIAPFRSFLRRLFREKHAdykftGLAWLFFGVP--NSDsLLYDDELEKYPKQYPDNfRIDYAFSREQKnadg 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070305039 524 EKIYVQDKLREQGAELWRWIN-DGAHIYVCGdARRMAADVEKALLEViaefgAMDIEAADEFLSELRVERRYQRDVY 599
Cdd:cd06208 216 GKMYVQDRIAEYAEEIWNLLDkDNTHVYICG-LKGMEPGVDDALTSV-----AEGGLAWEEFWESLKKKGRWHVEVY 286
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
356-572 |
6.90e-37 |
|
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: 136.81 E-value: 6.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 356 ATTPIVDMVRFSPAQLDAEA------LIGLLRP----LTPRLYSIASAQAEvESEVHVTVGVVRydiegrarAGGASSFL 425
Cdd:cd00322 2 ATEDVTDDVRLFRLQLPNGFsfkpgqYVDLHLPgdgrGLRRAYSIASSPDE-EGELELTVKIVP--------GGPFSAWL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 426 ADRvEEEGEVRVFIEHNDnFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADGAEGKNWLFFGNPHfTEDFLYQVEWQRY 505
Cdd:cd00322 73 HDL-KPGDEVEVSGPGGD-FFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGART-PADLLFLDELEEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2070305039 506 VKEGVLNRIDLAWSRDQKEKIYVQDKLREQGAELWR-WINDGAHIYVCGDArRMAADVEKALLEVIAE 572
Cdd:cd00322 150 AKEGPNFRLVLALSRESEAKLGPGGRIDREAEILALlPDDSGALVYICGPP-AMAKAVREALVSLGVP 216
|
|
| SiR_like2 |
cd06201 |
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
342-599 |
4.19e-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: 131.30 E-value: 4.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 342 LPLVGDKAQLQHYAATTPIVdmvRFSPAQLDAEA----------LIGLLRPLT--PRLYSIASAQAEvesevhvtvGVVr 409
Cdd:cd06201 48 LELVERKDYGAAVQAPTAIL---RFKPAKRKLSGkglpsfeagdLLGILPPGSdvPRFYSLASSSSD---------GFL- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 410 yDIEGRARAGG-ASSFLADrVEEEGEVRVFIEHNDNFRLPANpETPVIMIGPGTGIAPFRAFMQQRAAdgaEGKNWLFFG 488
Cdd:cd06201 115 -EICVRKHPGGlCSGYLHG-LKPGDTIKAFIRPNPSFRPAKG-AAPVILIGAGTGIAPLAGFIRANAA---RRPMHLYWG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 489 NPHFTEDFLYQVEWQRYVKEGVLNRIDLAWSRDQkEKIYVQDKLREQGAELWRWINDGAHIYVCGdARRMAADVEKALLE 568
Cdd:cd06201 189 GRDPASDFLYEDELDQYLADGRLTQLHTAFSRTP-DGAYVQDRLRADAERLRRLIEDGAQIMVCG-SRAMAQGVAAVLEE 266
|
250 260 270
....*....|....*....|....*....|.
gi 2070305039 569 VIAefgamdieAADEFLSELRVERRYQRDVY 599
Cdd:cd06201 267 ILA--------PQPLSLDELKLQGRYAEDVY 289
|
|
| PLN03116 |
PLN03116 |
ferredoxin--NADP+ reductase; Provisional |
381-599 |
5.96e-32 |
|
ferredoxin--NADP+ reductase; Provisional
Pssm-ID: 215586 [Multi-domain] Cd Length: 307 Bit Score: 125.60 E-value: 5.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 381 RPLTPRLYSIASAQAEVESEVHVTVGVVR----YDIEGR----ARAGGASSFLADRVEEEgEVRVFIEHNDNFRLPA-NP 451
Cdd:PLN03116 77 APHNVRLYSIASTRYGDDFDGKTASLCVRravyYDPETGkedpAKKGVCSNFLCDAKPGD-KVQITGPSGKVMLLPEeDP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 452 ETPVIMIGPGTGIAPFRA-----FMQQRAADGAEGKNWLFFGNPHfTEDFLYQVEWQRYVKEGVLN-RIDLAWSRDQKE- 524
Cdd:PLN03116 156 NATHIMVATGTGIAPFRGflrrmFMEDVPAFKFGGLAWLFLGVAN-SDSLLYDDEFERYLKDYPDNfRYDYALSREQKNk 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2070305039 525 ---KIYVQDKLREQGAELWRWINDGAHIYVCGdARRMAADVEKALLEVIAEFGamdiEAADEFLSELRVERRYQRDVY 599
Cdd:PLN03116 235 kggKMYVQDKIEEYSDEIFKLLDNGAHIYFCG-LKGMMPGIQDTLKRVAEERG----ESWEEKLSGLKKNKQWHVEVY 307
|
|
| Flavodoxin_1 |
pfam00258 |
Flavodoxin; |
66-197 |
7.60e-31 |
|
Flavodoxin;
Pssm-ID: 425562 [Multi-domain] Cd Length: 142 Bit Score: 117.47 E-value: 7.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 66 LISASQTGNARRVAEALRDDLLAANLNVTLVNAGDYK--FKQIASEKLLVIVTSTQGEGEPPEEAVALHKFLFSK---KA 140
Cdd:pfam00258 1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDDVDetLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFgtlED 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070305039 141 PKLTDTAFAVFSLGDTSYEFFCQSGKDFDSKLAELGGERLLDRVDADV-----EYQAAASEW 197
Cdd:pfam00258 81 GDLSGLKYAVFGLGDSGYEGFCGAAKKLDEKLSELGASRVGPLGEGDEdpqedGLEEAFEAW 142
|
|
| FAD_binding_1 |
pfam00667 |
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, ... |
230-424 |
5.07e-27 |
|
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: 108.97 E-value: 5.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 230 PYTKDAPLTATLAVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVKEIVELLWL--KGDEPVTV--- 304
Cdd:pfam00667 1 PFDAKKPFTAPVLSNRELTSPSSDRNCIHVELDISGSGLTYQTGDHLGVYPPNNEELVEELLERLGLdpKPDTVVLLktl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 305 DGKTLP-------LAEALEWHFELT-VNTANIVENYATLTRSES----LLPLVGDKAQ-----LQHYAATTPIVDMVRFS 367
Cdd:pfam00667 81 DERVKPprlppttYRQALKYYLDITgPPSKQLLRLLAQFAPEEEekqrLEFLSSDAGAreykrWKLNHAPTLLEVLEEFP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2070305039 368 PAQLDAEALIGLLRPLTPRLYSIASAQAEVESEVHVTVGVVRY--DIEGRARAGGASSF 424
Cdd:pfam00667 161 SVKLPADFLLTQLPQLQPRYYSISSSSKVHPNEVHLTVVVVEYetDGEGRIHYGVCSNW 219
|
|
| NAD_binding_1 |
pfam00175 |
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ... |
457-564 |
2.20e-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: 100.80 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 457 MIGPGTGIAPFRAFMQQRAAD-GAEGKNWLFFGNPHfTEDFLYQVEWQRYVKEGVLNRIDLAW-SRDQKE----KIYVQD 530
Cdd:pfam00175 1 MIAGGTGIAPVRSMLRAILEDpKDPTQVVLVFGNRN-EDDILYREELDELAEKHPGRLTVVYVvSRPEAGwtggKGRVQD 79
|
90 100 110
....*....|....*....|....*....|....
gi 2070305039 531 KLREQGAELwrwINDGAHIYVCGdARRMAADVEK 564
Cdd:pfam00175 80 ALLEDHLSL---PDEETHVYVCG-PPGMIKAVRK 109
|
|
| PLN03115 |
PLN03115 |
ferredoxin--NADP(+) reductase; Provisional |
381-599 |
8.04e-21 |
|
ferredoxin--NADP(+) reductase; Provisional
Pssm-ID: 215585 [Multi-domain] Cd Length: 367 Bit Score: 94.68 E-value: 8.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 381 RPLTPRLYSIAS-AQAEVESEVHVTVGVVRY---DIEGRARAGGASSFLADrVEEEGEVRVFIEHNDNFRLPANPETPVI 456
Cdd:PLN03115 141 KPHKLRLYSIASsALGDFGDSKTVSLCVKRLvytNDQGEIVKGVCSNFLCD-LKPGAEVKITGPVGKEMLMPKDPNATII 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 457 MIGPGTGIAPFRAFMQQRAADGAE-----GKNWLFFGNPHfTEDFLYQVEWQRYVKEGVLN-RIDLAWSRDQK----EKI 526
Cdd:PLN03115 220 MLATGTGIAPFRSFLWKMFFEKHDdykfnGLAWLFLGVPT-SSSLLYKEEFEKMKEKAPENfRLDFAVSREQTnakgEKM 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070305039 527 YVQDKLREQGAELWRWI-NDGAHIYVCGdarrmAADVEKALLEVIAEFGAMDIEAADEFLSELRVERRYQRDVY 599
Cdd:PLN03115 299 YIQTRMAEYAEELWELLkKDNTYVYMCG-----LKGMEKGIDDIMVSLAAKDGIDWFEYKKQLKKAEQWNVEVY 367
|
|
| PRK09004 |
PRK09004 |
FMN-binding protein MioC; Provisional |
61-205 |
2.84e-19 |
|
FMN-binding protein MioC; Provisional
Pssm-ID: 181608 [Multi-domain] Cd Length: 146 Bit Score: 84.50 E-value: 2.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 61 MLGVTLISASQTGNARRVAEALRDDLLAANLNVTLVNAGdyKFKQIASEKLLVIVTSTQGEGEPPEEAVALHKFLFSKKa 140
Cdd:PRK09004 1 MADITLISGSTLGGAEYVADHLAEKLEEAGFSTETLHGP--LLDDLSASGLWLIVTSTHGAGDLPDNLQPFFEELQEQK- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070305039 141 PKLTDTAFAVFSLGDTSYEFFCQSGKDFDSKLAELGGERLLDRVDADVEYQA----AASEWRARVVDVL 205
Cdd:PRK09004 78 PDLSQVRFAAIGIGSSEYDTFCGAIDKLEQLLKAKGAKQIGETLKIDVLQHPipedPAEEWLKSWINLL 146
|
|
| PRK08105 |
PRK08105 |
flavodoxin; Provisional |
73-197 |
3.56e-18 |
|
flavodoxin; Provisional
Pssm-ID: 181230 [Multi-domain] Cd Length: 149 Bit Score: 81.47 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 73 GNARRVAEALRDDLLAANLNVTLVNAGDYKFKQIASEKLLVIVTSTQGEGEPPEEAVALHKFLFSKkAPKLTDTAFAVFS 152
Cdd:PRK08105 13 GNALLVAEEAEAILTAQGHEVTLFEDPELSDWQPYQDELVLVVTSTTGQGDLPDSIVPLFQALKDT-AGYQPNLRYGVIA 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2070305039 153 LGDTSYEFFCQSGKDFDSKLAELGGERLLDR--VDA--DVEYQAAASEW 197
Cdd:PRK08105 92 LGDSSYDNFCGAGKQFDALLQEQGAKRVGERleIDAceTPEPEVEANPW 140
|
|
| FldA |
COG0716 |
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ... |
64-180 |
2.52e-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: 67.24 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 64 VTLISASQTGNARRVAEALRDDLLAAnlNVTLVNAGDYKFKQIASEKLLVIVTSTQGeGEPPEEAVAlhkfLFSKKAPKL 143
Cdd:COG0716 1 ILIVYGSTTGNTEKVAEAIAEALGAA--GVDLFEIEDADLDDLEDYDLLILGTPTWA-GELPDDWED----FLEELKEDL 73
|
90 100 110
....*....|....*....|....*....|....*..
gi 2070305039 144 TDTAFAVFSLGDTSyeFFCQSGKDFDSKLAELGGERL 180
Cdd:COG0716 74 SGKKVALFGTGDSS--GYGDALGELKELLEEKGAKVV 108
|
|
| Fpr |
COG1018 |
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
386-568 |
2.60e-13 |
|
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 69.82 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 386 RLYSIASAqaevESEVHVTVGVVRydIEGraraGGASSFLADRVEEEGEVRVFIEHNDnFRLPANPETPVIMIGPGTGIA 465
Cdd:COG1018 53 RAYSLSSA----PGDGRLEITVKR--VPG----GGGSNWLHDHLKVGDTLEVSGPRGD-FVLDPEPARPLLLIAGGIGIT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 466 PFRAFMQQRAADGAEGKNWLFFGNPHfTEDFLYQVEWQRYVKEgvLNRIDLAWsrdqkekIYVQDKLREQG----AELWR 541
Cdd:COG1018 122 PFLSMLRTLLARGPFRPVTLVYGARS-PADLAFRDELEALAAR--HPRLRLHP-------VLSREPAGLQGrldaELLAA 191
|
170 180
....*....|....*....|....*....
gi 2070305039 542 WIND--GAHIYVCGDArRMAADVEKALLE 568
Cdd:COG1018 192 LLPDpaDAHVYLCGPP-PMMEAVRAALAE 219
|
|
| PRK06703 |
PRK06703 |
flavodoxin; Provisional |
61-178 |
3.06e-10 |
|
flavodoxin; Provisional
Pssm-ID: 235854 [Multi-domain] Cd Length: 151 Bit Score: 59.00 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 61 MLGVTLISASQTGNARRVAEALRDDLLAANLNVTLVNAGDYKFKQIASEKLLVIVTSTQGEGEPPEEAVALHKFLfskKA 140
Cdd:PRK06703 1 MAKILIAYASMSGNTEDIADLIKVSLDAFDHEVVLQEMDGMDAEELLAYDGIILGSYTWGDGDLPYEAEDFHEDL---EN 77
|
90 100 110
....*....|....*....|....*....|....*...
gi 2070305039 141 PKLTDTAFAVFSLGDTSYEFFCQSGKDFDSKLAELGGE 178
Cdd:PRK06703 78 IDLSGKKVAVFGSGDTAYPLFCEAVTIFEERLVERGAE 115
|
|
| PRK07308 |
PRK07308 |
flavodoxin; Validated |
61-188 |
5.64e-10 |
|
flavodoxin; Validated
Pssm-ID: 180922 [Multi-domain] Cd Length: 146 Bit Score: 57.88 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 61 MLGVTLISASQTGNARRVAEALRDDLLAANLNV-----TLVNAGDYKFKQIAsekllVIVTSTQGEGEPPEEAVALHKFL 135
Cdd:PRK07308 1 MALAKIVYASMTGNTEEIADIVADKLRELGHDVdvdecTTVDASDFEDADIA-----IVATYTYGDGELPDEIVDFYEDL 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2070305039 136 fskKAPKLTDTAFAVFSLGDTSYEFFCQSGKDFDSKLAELGGERLLDRVDADV 188
Cdd:PRK07308 76 ---ADLDLSGKIYGVVGSGDTFYDYFCKSVDDFEAQFALTGATKGAESVKVDL 125
|
|
| flav_short |
TIGR01753 |
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ... |
64-202 |
3.52e-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: 55.42 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 64 VTLISASQTGNARRVAEALRDDLLAANLNVTLVNAGDYKFKQIASEKLLVIVTSTQGEGEPPEEAVA-----LHKFLFSK 138
Cdd:TIGR01753 1 ILIVYASMTGNTEEMANIIAEGLKEAGAEVDLLEVADADAEDLLSYDAVLLGCSTWGDEDLEQDDFEpffeeLEDIDLGG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2070305039 139 KApkltdtaFAVFSLGDTSYEfFCQSGKDFDSKLAELG----GERLLDRVDADVEYQAAASEWRARVV 202
Cdd:TIGR01753 81 KK-------VALFGSGDWGYE-FCEAVDDWEERLKEAGatiiAEGLKVDGDPEEEDLDKCREFAKDLA 140
|
|
| flavin_oxioreductase |
cd06189 |
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
386-568 |
4.16e-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: 54.09 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 386 RLYSIASAQAEVES-EVHVtvgvvrydiegRARAGGASSFLA-DRVEEEGEVRVFIEHNDnFRLPANPETPVIMIGPGTG 463
Cdd:cd06189 42 RPFSIASAPHEDGEiELHI-----------RAVPGGSFSDYVfEELKENGLVRIEGPLGD-FFLREDSDRPLILIAGGTG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 464 IAPFRAFMQQRAADGAEGKNWLFFGNPhfTEDFLYQVEWQR----------YVKegVLNRIDLAWsrdQKEKIYVQDKLR 533
Cdd:cd06189 110 FAPIKSILEHLLAQGSKRPIHLYWGAR--TEEDLYLDELLEawaeahpnftYVP--VLSEPEEGW---QGRTGLVHEAVL 182
|
170 180 190
....*....|....*....|....*....|....*
gi 2070305039 534 EQGAELwrwinDGAHIYVCGDArRMAADVEKALLE 568
Cdd:cd06189 183 EDFPDL-----SDFDVYACGSP-EMVYAARDDFVE 211
|
|
| O2ase_reductase_like |
cd06187 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
381-567 |
6.07e-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: 53.75 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 381 RPLTPRLYSIASAQAEV-ESEVHVTvgvvrydiegRARAGGASSFLADRVEEEGEVRVFIEHNDnFRLPANPETPVIMIG 459
Cdd:cd06187 37 RPRTWRAYSPANPPNEDgEIEFHVR----------AVPGGRVSNALHDELKVGDRVRLSGPYGT-FYLRRDHDRPVLCIA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 460 PGTGIAPFRAFMQQRAADGAEGKNWLFFGNPhfTEDFLYQVE----------WQRYVKegVLNRIDLAWSRdqkEKIYVQ 529
Cdd:cd06187 106 GGTGLAPLRAIVEDALRRGEPRPVHLFFGAR--TERDLYDLEgllalaarhpWLRVVP--VVSHEEGAWTG---RRGLVT 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 2070305039 530 DKLREQGAELwrwinDGAHIYVCGDArRMAADVEKALL 567
Cdd:cd06187 179 DVVGRDGPDW-----ADHDIYICGPP-AMVDATVDALL 210
|
|
| PRK05723 |
PRK05723 |
flavodoxin; Provisional |
64-206 |
4.49e-06 |
|
flavodoxin; Provisional
Pssm-ID: 168208 Cd Length: 151 Bit Score: 46.71 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 64 VTLISASQTGNARRVAEALRDDLLAANLNvTLVN--AGDYKFKQIASEKLLViVTSTQGEGEPPEEAVALHKFLFSKKAP 141
Cdd:PRK05723 3 VAILSGSVYGTAEEVARHAESLLKAAGFE-AWHNprASLQDLQAFAPEALLA-VTSTTGMGELPDNLMPLYSAIRDQLPA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 142 KLTDTAFAVFSLGDTSY-EFFCQSGKDFDSKLAELGGERLLD--RVDAD--VEYQAAASEWRARVVDVLK 206
Cdd:PRK05723 81 AWRGLPGAVIALGDSSYgDTFCGGGEQMRELFAELGVREVQPmlRLDASetVTPETDAEPWLAEFAAALK 150
|
|
| FNR_iron_sulfur_binding_2 |
cd06216 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
386-568 |
2.13e-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 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: 46.06 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 386 RLYSIASAQAEVESEVHVTVgvvrydiegRARAGGA-SSFLADRVEEeGEVrVFIEH-NDNFRLPANPETPVIMIGPGTG 463
Cdd:cd06216 65 RSYSLSSSPTQEDGTITLTV---------KAQPDGLvSNWLVNHLAP-GDV-VELSQpQGDFVLPDPLPPRLLLIAAGSG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 464 IAPFRAFMQQRAADGAEGKNWLFFGNPHfTEDFLYQVEWQRYVKEGVLNRIDLAWSRDQKEkiyvQDKLREQGAELWRWI 543
Cdd:cd06216 134 ITPVMSMLRTLLARGPTADVVLLYYART-REDVIFADELRALAAQHPNLRLHLLYTREELD----GRLSAAHLDAVVPDL 208
|
170 180
....*....|....*....|....*
gi 2070305039 544 NDgAHIYVCGdARRMAADVEKALLE 568
Cdd:cd06216 209 AD-RQVYACG-PPGFLDAAEELLEA 231
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
385-568 |
7.92e-05 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 44.47 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 385 PRLYSIASAQAEvESEVHVTVGVVrydiegraraGGASSFLADRveEEGEvRVFIE--HNDNFRLPANPEtPVIMIGPGT 462
Cdd:COG0543 42 RRPFSIASAPRE-DGTIELHIRVV----------GKGTRALAEL--KPGD-ELDVRgpLGNGFPLEDSGR-PVLLVAGGT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 463 GIAPFRAFMQQRAADGaeGKNWLFFG----NPHFTEDFLYQVEWQRYVkegVLnrIDLAWsrdQKEKIYVQDKLREQGAE 538
Cdd:COG0543 107 GLAPLRSLAEALLARG--RRVTLYLGartpEDLYLLDELEALADFRVV---VT--TDDGW---YGRKGFVTDALKELLAE 176
|
170 180 190
....*....|....*....|....*....|
gi 2070305039 539 lwrwiNDGAHIYVCGdARRMAADVEKALLE 568
Cdd:COG0543 177 -----DSGDDVYACG-PPPMMKAVAELLLE 200
|
|
| FNR_N-term_Iron_sulfur_binding |
cd06194 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
364-466 |
1.04e-04 |
|
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: 43.80 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 364 VRFSPAQLdaealIGLLRP-LTPRLYSIASAQAE-VESEVHVTvgvvrydiegRARAGGASSFLADRVEEEGEVRVFIEH 441
Cdd:cd06194 22 LPYLPGQY-----VNLRRAgGLARSYSPTSLPDGdNELEFHIR----------RKPNGAFSGWLGEEARPGHALRLQGPF 86
|
90 100
....*....|....*....|....*
gi 2070305039 442 NDNFRLPANPETPVIMIGPGTGIAP 466
Cdd:cd06194 87 GQAFYRPEYGEGPLLLVGAGTGLAP 111
|
|
| PRK09267 |
PRK09267 |
flavodoxin FldA; Validated |
61-162 |
1.10e-04 |
|
flavodoxin FldA; Validated
Pssm-ID: 236439 [Multi-domain] Cd Length: 169 Bit Score: 42.90 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 61 MLGVTLISASQTGNARRVAEALRDDLLAAnlNVTLVNAGDYKFKQIASEKLLVIVTSTQGEGEPP---EEavalhkFLFS 137
Cdd:PRK09267 1 MAKIGIFFGSDTGNTEDIAKMIQKKLGKD--VADVVDIAKASKEDFEAYDLLILGIPTWGYGELQcdwDD------FLPE 72
|
90 100
....*....|....*....|....*..
gi 2070305039 138 KKAPKLTDTAFAVFSLGD-TSY-EFFC 162
Cdd:PRK09267 73 LEEIDFSGKKVALFGLGDqEDYaEYFC 99
|
|
| FNR_like_1 |
cd06196 |
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ... |
454-568 |
4.53e-04 |
|
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: 41.84 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 454 PVIMIGPGTGIAPFRAFMQQRAADGAEGKNWLFFGNPhfTE-DFLYQVEWQRYVKEGVLNRIdlawSRDQKEKIYVQdkl 532
Cdd:cd06196 101 PGVFIAGGAGITPFIAILRDLAAKGKLEGNTLIFANK--TEkDIILKDELEKMLGLKFINVV----TDEKDPGYAHG--- 171
|
90 100 110
....*....|....*....|....*....|....*..
gi 2070305039 533 REQGAELWRWINDGA-HIYVCGdARRMAADVEKALLE 568
Cdd:cd06196 172 RIDKAFLKQHVTDFNqHFYVCG-PPPMEEAINGALKE 207
|
|
| FNR_iron_sulfur_binding_3 |
cd06217 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
386-568 |
5.65e-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: 41.87 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 386 RLYSIASAQAEvesEVHVTVGVVRYDiegrarAGGASSFLADRVEE--EGEVRVFIEHndnFRLPANPETPVIMIGPGTG 463
Cdd:cd06217 51 RSYSIASSPTQ---RGRVELTVKRVP------GGEVSPYLHDEVKVgdLLEVRGPIGT---FTWNPLHGDPVVLLAGGSG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 464 IAPFRAFMQQRAADGAEGKNWLFFGNPHfTEDFLYQVEWQRYVKEGVLNRIDLAWSRDQkekiyVQDKLREQG------- 536
Cdd:cd06217 119 IVPLMSMIRYRRDLGWPVPFRLLYSART-AEDVIFRDELEQLARRHPNLHVTEALTRAA-----PADWLGPAGritadli 192
|
170 180 190
....*....|....*....|....*....|..
gi 2070305039 537 AELWRWInDGAHIYVCGdARRMAADVEKALLE 568
Cdd:cd06217 193 AELVPPL-AGRRVYVCG-PPAFVEAATRLLLE 222
|
|
| phenol_2-monooxygenase_like |
cd06211 |
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ... |
384-569 |
1.08e-03 |
|
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: 41.16 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 384 TPRLYSIASAQAEV-ESEVHVtvgvvRYdIEGraraGGASSFLADRVEEEGEVRVFIEHNDnFRLPANPETPVIMIGPGT 462
Cdd:cd06211 51 GTRAFSIASSPSDAgEIELHI-----RL-VPG----GIATTYVHKQLKEGDELEISGPYGD-FFVRDSDQRPIIFIAGGS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 463 GIAPFRAFMQQRAADGAEGKNWLFFG--NPH--FTEDFLYQVEWQ----RYVKegVLNRI--DLAWsrdQKEKIYVQDKL 532
Cdd:cd06211 120 GLSSPRSMILDLLERGDTRKITLFFGarTRAelYYLDEFEALEKDhpnfKYVP--ALSREppESNW---KGFTGFVHDAA 194
|
170 180 190
....*....|....*....|....*....|....*..
gi 2070305039 533 REQGAELWRwindGAHIYVCGDARRMAADVeKALLEV 569
Cdd:cd06211 195 KKHFKNDFR----GHKAYLCGPPPMIDACI-KTLMQG 226
|
|
| PRK07609 |
PRK07609 |
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated |
379-553 |
4.48e-03 |
|
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
Pssm-ID: 181058 [Multi-domain] Cd Length: 339 Bit Score: 39.47 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 379 LLRPLTPRLYSIASA-QAEVESEVHVtvgvvrydiegRARAGGASS-FLADRVEEEGEVRVFIEHNDnFRLPANPETPVI 456
Cdd:PRK07609 141 ILKDGKRRSYSIANApHSGGPLELHI-----------RHMPGGVFTdHVFGALKERDILRIEGPLGT-FFLREDSDKPIV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 457 MIGPGTGIAPFRAFMQQRAADGAEGKNWLFFGNPhfTEDFLYQVEWQ----------RYVKegVLN--RIDLAWsrdQKE 524
Cdd:PRK07609 209 LLASGTGFAPIKSIVEHLRAKGIQRPVTLYWGAR--RPEDLYLSALAeqwaeelpnfRYVP--VVSdaLDDDAW---TGR 281
|
170 180
....*....|....*....|....*....
gi 2070305039 525 KIYVQDKLREQGAELwrwinDGAHIYVCG 553
Cdd:PRK07609 282 TGFVHQAVLEDFPDL-----SGHQVYACG 305
|
|
| oxygenase_e_transfer_subunit |
cd06213 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
385-553 |
5.48e-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: 38.83 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 385 PRLYSIASA-QAEVESEVHVtvgvvrydiegRARAGGASS---FLADRVEEEGEVRVfiEHNDnFRL-PANpeTPVIMIG 459
Cdd:cd06213 44 ARSYSFANApQGDGQLSFHI-----------RKVPGGAFSgwlFGADRTGERLTVRG--PFGD-FWLrPGD--APILCIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 460 PGTGIAPFRAFMQQRAADGAEGKNWLFFGNPhfTEDFLYQVE---------WQRYVKEGVLNR--IDLAWsrdQKEKIYV 528
Cdd:cd06213 108 GGSGLAPILAILEQARAAGTKRDVTLLFGAR--TQRDLYALDeiaaiaarwRGRFRFIPVLSEepADSSW---KGARGLV 182
|
170 180
....*....|....*....|....*
gi 2070305039 529 QDKLREQGAElwrwindGAHIYVCG 553
Cdd:cd06213 183 TEHIAEVLLA-------ATEAYLCG 200
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
449-568 |
9.73e-03 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 38.72 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070305039 449 ANPETPVIMIGPGTGIAPFRAFMQQRAADGAEGKN-WLFFGNPHfTEDFLYQVEWQRYVKEgvLNRIDLaWSRDQKEKIY 527
Cdd:COG4097 315 RDTAPRQVWIAGGIGITPFLALLRALAARPGDQRPvDLFYCVRD-EEDAPFLEELRALAAR--LAGLRL-HLVVSDEDGR 390
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2070305039 528 V-QDKLREQGAELwrwinDGAHIYVCGdARRMAADVEKALLE 568
Cdd:COG4097 391 LtAERLRRLVPDL-----AEADVFFCG-PPGMMDALRRDLRA 426
|
|
| |
