|
Name |
Accession |
Description |
Interval |
E-value |
| SiR_like1 |
cd06200 |
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
575-872 |
1.18e-127 |
|
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: 383.17 E-value: 1.18e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 575 WTLQQRDLLNPNSLGAPAFNIELLAQ-HDVHWSAGDIAEIQPENstarihaflkqhqldantiladgqqtlvqaladkdl 653
Cdd:cd06200 1 WRLQARVLLNPGSQGAPLWRLRLTPPdAGAQWQAGDIAEIGPRH------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 654 tapiqtfktadellaqlsPLPSREYSIASIPSQQVLRLVVRQKFDAQGELGLGSGWLTAHAALGQNIALRIRNNPSFHLI 733
Cdd:cd06200 45 ------------------PLPHREYSIASLPADGALELLVRQVRHADGGLGLGSGWLTRHAPIGASVALRLRENPGFHLP 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 734 DDDRPIICIGNGTGLAGLMSLLHARTRLNYTQNWLFFGERQQAHDYFYQHTIEAWQSTGMLQRLDLAFSRDQAGKVYVHH 813
Cdd:cd06200 107 DDGRPLILIGNGTGLAGLRSHLRARARAGRHRNWLLFGERQAAHDFFCREELEAWQAAGHLARLDLAFSRDQAQKRYVQD 186
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1872063922 814 KLREQAEELKRWIEQNAVIYVCGSIQGMASDVDQALKDILGETQLEQLRQQGRYRRDVY 872
Cdd:cd06200 187 RLRAAADELRAWVAEGAAIYVCGSLQGMAPGVDAVLDEILGEEAVEALLAAGRYRRDVY 245
|
|
| CysJ |
COG0369 |
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ... |
401-872 |
1.56e-101 |
|
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: 326.72 E-value: 1.56e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 401 AARQNQTQFKIDPNAEHWLIVYASQTGTAEQLAWRTATSLQEAHQPVTVKALQHLSLEDLKNTTQLLCIASTYGTGDAPD 480
Cdd:COG0369 12 RAAAAAAAAAAAAAGTPLTILYGSQTGNAEGLAEQLAERAKAAGLAVTLASLDDYKPKDLAKEGLLLIVTSTYGEGEPPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 481 LTSSFVKKIL-PQTCDLSHLRYAVLALGSREYaDHYCRFGHTIAAWLQRNQAHALFNTIEvnnanpADI------QRWNQ 553
Cdd:COG0369 92 NARAFYEFLHsKKAPKLDGLRYAVLGLGDSSY-ETFCQTGKDFDARLEELGATRLLPRVD------CDVdyeeaaEAWLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 554 ALVQ--------------VTQLDLPSMHIEKTFDTWTLQQRDLLNPNSLGApAFNIEL-LAQHDVHWSAGDIAEIQPENS 618
Cdd:COG0369 165 AVLAalaealgaaaaaaaAAAAAAPAYSRKNPFPATVLENRELTGRGSAKE-TRHIEIdLPGSGLSYEPGDALGVWPEND 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 619 TARIHAFLKQHQLDANT--ILADGQQTLVQALADK-DLTAP--------------------------------------- 656
Cdd:COG0369 244 PALVDELLARLGLDGDEpvTLDGEPLSLREALTEHlELTRLtppllekyaeltgnaelaalladedkaalreylagrqll 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 657 --IQTFK----TADELLAQLSPLPSREYSIASipSQQV----LRL---VVRqkFDAQGE--LGLGSGWLtAHAALGQNIA 721
Cdd:COG0369 324 dlLREFPaaelSAEELLELLRPLTPRLYSISS--SPKAhpdeVHLtvgVVR--YEASGRerKGVASTYL-ADLEEGDTVP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 722 LRIRNNPSFHL-IDDDRPIICIGNGTGLAGLMSLLHARTRLNYT-QNWLFFGERQQAHDYFYQHTIEAWQSTGMLQRLDL 799
Cdd:COG0369 399 VFVEPNPNFRLpADPDTPIIMIGPGTGIAPFRAFLQEREARGASgKNWLFFGDRHFTTDFLYQTELQAWLKDGVLTRLDL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 800 AFSRDQAGKVYVHHKLREQAEELKRWIEQNAVIYVCGSIQGMASDVDQALKDIL----------GETQLEQLRQQGRYRR 869
Cdd:COG0369 479 AFSRDQAEKIYVQHRLLEQGAELWAWLEEGAHVYVCGDASRMAKDVDAALLDIIaehgglseeeAEEYLAELRAEKRYQR 558
|
...
gi 1872063922 870 DVY 872
Cdd:COG0369 559 DVY 561
|
|
| PiuB |
COG3182 |
PepSY-associated TM region [Function unknown]; |
1-404 |
5.09e-88 |
|
PepSY-associated TM region [Function unknown];
Pssm-ID: 442415 [Multi-domain] Cd Length: 379 Bit Score: 284.55 E-value: 5.09e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 1 MLKKAFFQIHWFLGITAGLILSLMGVTGAIYSYEQEILKWMNPNSYQVQVeQKAKLSPAEIYQHFQRTQPDYKINSITVA 80
Cdd:COG3182 2 SLRKLLRRLHLWLGLLAGLFLLILALTGALLVFKPEIDRWLNPELLAVAP-GGPPLSLDELLAAARAAYPGARVTSITLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 81 KDPAASSSINIaKEGAKRGQNILINPYSAAVLPEI-RGREFFQFIQQLHRNLTVGPIGKQITAACTLMLLFFVLSGIYLR 159
Cdd:COG3182 81 AEPDRAARVRV-RDPEGEGRTVYVDPYTGEVLGTRdEGSTFFRFLYRLHRSLLLGDTGRLIVGLAALLLLVLLISGLVLW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 160 WPKRHSFKQWFAIKPQLKGRNFIWDLHAVVGTWVVIFYLVLACTGLYWSYEWWRNGMFKVMGVERPQAQLQADGRNKPvn 239
Cdd:COG3182 160 WPRRRRWKDFFTFRWGAGGRRFWLDLHNVLGVWALPFLLVIALTGLVWSLADWLRAALAALGGGTPAAEAEPPASASA-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 240 snaqalhqaaqtqtagrrantTKPAKQNTLDQaqinlALTKAWQHFPqqlgqDYSSITFNVPKHANSEIEINFVDVIPQH 319
Cdd:COG3182 238 ---------------------PAGAPPLSLDA-----ALAAARAALP-----DAEPRRISLPGDPGGVYTVRGRDPGELT 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 320 ERARNNATFDYQQARITQLELYANKQLNEKIMSSMLPVHRGSFFGPVYQFLAMLAALMMPLFFVTGWMLYLKRRKQKRLT 399
Cdd:COG3182 287 PRGRDTVYFDPYTGEVLAVRDFADYSAGAKLLEWLYPLHTGRFGGLPGRILYFLLGLALALLIVTGLLLWWKRRRKKRAP 366
|
....*
gi 1872063922 400 LAARQ 404
Cdd:COG3182 367 PAARA 371
|
|
| cysJ |
TIGR01931 |
sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an ... |
406-872 |
3.10e-67 |
|
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: 235.36 E-value: 3.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 406 QTQFKIDPNAEHWLIVYASQTGTAEQLAWRTATSLQEAHQPVTVKALQHLSLEDLKNTTQLLCIASTYGTGDAPDLTSSF 485
Cdd:TIGR01931 49 NEAEEPAAQEKRVTILYGSQTGNARRLAKRLAEKLEAAGFSVRLSSADDYKFKQLKKERLLLLVISTQGEGEPPEEAISL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 486 VK----KILPQtcdLSHLRYAVLALGSREYADhYCRFGHTIAAWLQRNQAHALFNTIEVN-----NANP--ADIQRWNQA 554
Cdd:TIGR01931 129 HKflhsKKAPK---LENLRYSVLGLGDSSYEF-FCQTGKDFDKRLEELGGKRLLPRVDADldydaNAAEwrAGVLTALNE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 555 LVQVTQLDLPSMHIEKTFDT----WTLQQ---RDLLNPNSLGAPAFN-----IEL-LAQHDVHWSAGDIAEIQPENSTAR 621
Cdd:TIGR01931 205 QAKGGASTPSASETSTPLQTstsvYSKQNpfrAEVLENQKITGRNSKkdvrhIEIdLEGSGLHYEPGDALGVWYKNDPAL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 622 IHAFLKQHQLDANTILADGQQT--LVQALADK----DLTAPI----------QTFK------------------------ 661
Cdd:TIGR01931 285 VKEILKLLNLDPDEKVTIGGKTipLFEALITHfeltQNTKPLlkayaeltgnKELKaliadneklkayiqntplidlird 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 662 -----TADELLAQLSPLPSREYSIASipSQ-----QVLRLVVRQKFDAQGE--LGLGSGWLTAHAALGQNIALRIRNNPS 729
Cdd:TIGR01931 365 ypadlDAEQLISLLRPLTPRLYSISS--SQsevgdEVHLTVGVVRYQAHGRarLGGASGFLAERLKEGDTVPVYIEPNDN 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 730 FHL-IDDDRPIICIGNGTGLAGLMSLLHARTRLNYT-QNWLFFGERQQAHDYFYQHTIEAWQSTGMLQRLDLAFSRDQAG 807
Cdd:TIGR01931 443 FRLpEDPDTPIIMIGPGTGVAPFRAFMQERAEDGAKgKNWLFFGNPHFTTDFLYQVEWQNYLKKGVLTKMDLAFSRDQAE 522
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1872063922 808 KVYVHHKLREQAEELKRWIEQNAVIYVCGSIQGMASDVDQALKDIL----------GETQLEQLRQQGRYRRDVY 872
Cdd:TIGR01931 523 KIYVQHRIREQGAELWQWLQEGAHIYVCGDAKKMAKDVHQALLDIIakeghldaeeAEEYLTDLRVEKRYQRDVY 597
|
|
| PepSY_TM |
pfam03929 |
PepSY-associated TM region; The PepSY_TM family is so named because it is an alignment of up ... |
7-392 |
7.21e-61 |
|
PepSY-associated TM region; The PepSY_TM family is so named because it is an alignment of up to five transmembranes helices found in bacterial species some of which carry a nested PepSY domain, pfam03413.
Pssm-ID: 427595 [Multi-domain] Cd Length: 355 Bit Score: 210.50 E-value: 7.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 7 FQIHWFLGITAGLILSLMGVTGAIYSYEQEILKWMNPNSYQVQV-EQKAKLSPAEIYQHFQRTQPDYKINSITVAKDPAA 85
Cdd:pfam03929 1 FRLHFWAGLLVGPFLLILALTGALLVFRPEIDRWLNPELLTVPPpGAPAPLAALRAPAAAAAAAAAAAADPGTVAVVPPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 86 SSSINIAKEGAKRGQnILINPYSAAVLPEIRGREFFQFIQQLHRNLTVG-PIGKQITAACTLMLLFFVLSGIYLRWPKRH 164
Cdd:pfam03929 81 PAPADVGLGEGERRA-VFVDPYTGEVLGEYGGSLPFRFLYRLHRGLLLGeLWGRLIVGLAALLLLVLLVSGLVLWWPRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 165 sfKQWFAIKPQLKGRNFIWDLHAVVGTWVVIFYLVLACTGLYWSYEWWRNGMFKVMGverpqaqlqadgrnkpvnsnAQA 244
Cdd:pfam03929 160 --KWLFFRFRPGGGRRFWLDLHNVLGVWALPFLLVLALTGLTWSLAAVWGAAVTALF--------------------SAG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 245 LHQAAQTQTAGRRANTTKPAKQNTLDQAqinlaltkAWQHFPQQLGQDYSSITFNVPKHANSEIEINFVDVIPQHERARN 324
Cdd:pfam03929 218 AAAPAAPAAPAPPAAAAAAPASAAAAAA--------AAAAAAAAAGAAAVAPAPPAPGTAATVVEVYRADPDGRDTVAVD 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1872063922 325 NATFDYQQARITQLELYANkqLNEKIMSSMLPVHRGSFFGPVYQFLAMLAALMMPLFFVTGWMLYLKR 392
Cdd:pfam03929 290 QYSGAVLDGVLFADYPPGD--AGAKLLAWGYPLHFGRFFGLPNRILYFLLGLALALLIVTGLLLWWKR 355
|
|
| PRK06214 |
PRK06214 |
sulfite reductase subunit alpha; |
633-872 |
1.61e-50 |
|
sulfite reductase subunit alpha;
Pssm-ID: 235745 [Multi-domain] Cd Length: 530 Bit Score: 186.43 E-value: 1.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 633 ANTILADGQQTLVQALADKDLTAPIQTfkTADELLAQLSPLPSREYSIASIPSQQVLRL-----VVRQKFDAQGELGLGS 707
Cdd:PRK06214 276 AAGEDPDGDAATLDVLAALEKFPGIRP--DPEAFVEALDPLQPRLYSISSSPKATPGRVsltvdAVRYEIGSRLRLGVAS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 708 GWLTAHAALGQNIALRIRNNPSFHLIDD-DRPIICIGNGTGLAGLMSLLHARTRLNYT-QNWLFFGERQQAHDYFYQHTI 785
Cdd:PRK06214 354 TFLGERLAPGTRVRVYVQKAHGFALPADpNTPIIMVGPGTGIAPFRAFLHERAATKAPgRNWLFFGHQRSATDFFYEDEL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 786 EAWQSTGMLQRLDLAFSRDQAGKVYVHHKLREQAEELKRWIEQNAVIYVCGSIQGMASDVDQALKDILGE---------- 855
Cdd:PRK06214 434 NGLKAAGVLTRLSLAWSRDGEEKTYVQDRMRENGAELWKWLEEGAHFYVCGDAKRMAKDVERALVDIVAQfggrspdeav 513
|
250
....*....|....*..
gi 1872063922 856 TQLEQLRQQGRYRRDVY 872
Cdd:PRK06214 514 AFVAELKKAGRYQADVY 530
|
|
| Flavodoxin_1 |
pfam00258 |
Flavodoxin; |
420-550 |
2.17e-18 |
|
Flavodoxin;
Pssm-ID: 425562 [Multi-domain] Cd Length: 142 Bit Score: 82.42 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 420 IVYASQTGTAEQLAWRTATSLQEAHQPVTVKALQHL--SLEDLKNTTQLLCIASTYGTGDAPDLTSSFVKKILPQT---- 493
Cdd:pfam00258 1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDDVdeTLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGtled 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1872063922 494 CDLSHLRYAVLALGSREYAdHYCRFGHTIAAWLQRNQAHALFNTIEVNNANPADIQR 550
Cdd:pfam00258 81 GDLSGLKYAVFGLGDSGYE-GFCGAAKKLDEKLSELGASRVGPLGEGDEDPQEDGLE 136
|
|
| PRK09004 |
PRK09004 |
FMN-binding protein MioC; Provisional |
427-541 |
1.59e-12 |
|
FMN-binding protein MioC; Provisional
Pssm-ID: 181608 [Multi-domain] Cd Length: 146 Bit Score: 65.62 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 427 GTAEQLAWRTATSLQEAHQPVTVkaLQHLSLEDLKNTTQLLCIASTYGTGDAPDLTSSFVKKILPQTCDLSHLRYAVLAL 506
Cdd:PRK09004 13 GGAEYVADHLAEKLEEAGFSTET--LHGPLLDDLSASGLWLIVTSTHGAGDLPDNLQPFFEELQEQKPDLSQVRFAAIGI 90
|
90 100 110
....*....|....*....|....*....|....*
gi 1872063922 507 GSREYaDHYCRFGHTIAAWLQRNQAHALFNTIEVN 541
Cdd:PRK09004 91 GSSEY-DTFCGAIDKLEQLLKAKGAKQIGETLKID 124
|
|
| NAD_binding_1 |
pfam00175 |
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ... |
742-847 |
3.84e-10 |
|
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: 57.65 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 742 IGNGTGLAGLMSLLHARTRL--NYTQNWLFFGERQQaHDYFYQHTIEAWQstgmlQRLDLAF------SRDQAG----KV 809
Cdd:pfam00175 2 IAGGTGIAPVRSMLRAILEDpkDPTQVVLVFGNRNE-DDILYREELDELA-----EKHPGRLtvvyvvSRPEAGwtggKG 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 1872063922 810 YVHHKLREQAEELKrwiEQNAVIYVCGSIqGMASDVDQ 847
Cdd:pfam00175 76 RVQDALLEDHLSLP---DEETHVYVCGPP-GMIKAVRK 109
|
|
| FldA |
COG0716 |
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ... |
419-513 |
4.29e-08 |
|
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440480 [Multi-domain] Cd Length: 135 Bit Score: 52.60 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 419 LIVYASQTGTAEQLAWRTATSLQEAHqpVTVKALQHLSLEDLKNTTQLLCIASTYGtGDAPDLTSSFVKKILPqtcDLSH 498
Cdd:COG0716 2 LIVYGSTTGNTEKVAEAIAEALGAAG--VDLFEIEDADLDDLEDYDLLILGTPTWA-GELPDDWEDFLEELKE---DLSG 75
|
90
....*....|....*.
gi 1872063922 499 LRYAVLALG-SREYAD 513
Cdd:COG0716 76 KKVALFGTGdSSGYGD 91
|
|
| flav_short |
TIGR01753 |
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ... |
419-518 |
7.73e-06 |
|
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: 46.56 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 419 LIVYASQTGTAEQLAWRTATSLQEAHQPVTVKALQHLSLEDLKNTTQLLCIASTYGTGDAP-DLTSSFVKKIlpQTCDLS 497
Cdd:TIGR01753 2 LIVYASMTGNTEEMANIIAEGLKEAGAEVDLLEVADADAEDLLSYDAVLLGCSTWGDEDLEqDDFEPFFEEL--EDIDLG 79
|
90 100
....*....|....*....|.
gi 1872063922 498 HLRYAVlaLGSREYADHYCRF 518
Cdd:TIGR01753 80 GKKVAL--FGSGDWGYEFCEA 98
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SiR_like1 |
cd06200 |
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
575-872 |
1.18e-127 |
|
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: 383.17 E-value: 1.18e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 575 WTLQQRDLLNPNSLGAPAFNIELLAQ-HDVHWSAGDIAEIQPENstarihaflkqhqldantiladgqqtlvqaladkdl 653
Cdd:cd06200 1 WRLQARVLLNPGSQGAPLWRLRLTPPdAGAQWQAGDIAEIGPRH------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 654 tapiqtfktadellaqlsPLPSREYSIASIPSQQVLRLVVRQKFDAQGELGLGSGWLTAHAALGQNIALRIRNNPSFHLI 733
Cdd:cd06200 45 ------------------PLPHREYSIASLPADGALELLVRQVRHADGGLGLGSGWLTRHAPIGASVALRLRENPGFHLP 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 734 DDDRPIICIGNGTGLAGLMSLLHARTRLNYTQNWLFFGERQQAHDYFYQHTIEAWQSTGMLQRLDLAFSRDQAGKVYVHH 813
Cdd:cd06200 107 DDGRPLILIGNGTGLAGLRSHLRARARAGRHRNWLLFGERQAAHDFFCREELEAWQAAGHLARLDLAFSRDQAQKRYVQD 186
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1872063922 814 KLREQAEELKRWIEQNAVIYVCGSIQGMASDVDQALKDILGETQLEQLRQQGRYRRDVY 872
Cdd:cd06200 187 RLRAAADELRAWVAEGAAIYVCGSLQGMAPGVDAVLDEILGEEAVEALLAAGRYRRDVY 245
|
|
| CysJ |
COG0369 |
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ... |
401-872 |
1.56e-101 |
|
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: 326.72 E-value: 1.56e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 401 AARQNQTQFKIDPNAEHWLIVYASQTGTAEQLAWRTATSLQEAHQPVTVKALQHLSLEDLKNTTQLLCIASTYGTGDAPD 480
Cdd:COG0369 12 RAAAAAAAAAAAAAGTPLTILYGSQTGNAEGLAEQLAERAKAAGLAVTLASLDDYKPKDLAKEGLLLIVTSTYGEGEPPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 481 LTSSFVKKIL-PQTCDLSHLRYAVLALGSREYaDHYCRFGHTIAAWLQRNQAHALFNTIEvnnanpADI------QRWNQ 553
Cdd:COG0369 92 NARAFYEFLHsKKAPKLDGLRYAVLGLGDSSY-ETFCQTGKDFDARLEELGATRLLPRVD------CDVdyeeaaEAWLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 554 ALVQ--------------VTQLDLPSMHIEKTFDTWTLQQRDLLNPNSLGApAFNIEL-LAQHDVHWSAGDIAEIQPENS 618
Cdd:COG0369 165 AVLAalaealgaaaaaaaAAAAAAPAYSRKNPFPATVLENRELTGRGSAKE-TRHIEIdLPGSGLSYEPGDALGVWPEND 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 619 TARIHAFLKQHQLDANT--ILADGQQTLVQALADK-DLTAP--------------------------------------- 656
Cdd:COG0369 244 PALVDELLARLGLDGDEpvTLDGEPLSLREALTEHlELTRLtppllekyaeltgnaelaalladedkaalreylagrqll 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 657 --IQTFK----TADELLAQLSPLPSREYSIASipSQQV----LRL---VVRqkFDAQGE--LGLGSGWLtAHAALGQNIA 721
Cdd:COG0369 324 dlLREFPaaelSAEELLELLRPLTPRLYSISS--SPKAhpdeVHLtvgVVR--YEASGRerKGVASTYL-ADLEEGDTVP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 722 LRIRNNPSFHL-IDDDRPIICIGNGTGLAGLMSLLHARTRLNYT-QNWLFFGERQQAHDYFYQHTIEAWQSTGMLQRLDL 799
Cdd:COG0369 399 VFVEPNPNFRLpADPDTPIIMIGPGTGIAPFRAFLQEREARGASgKNWLFFGDRHFTTDFLYQTELQAWLKDGVLTRLDL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 800 AFSRDQAGKVYVHHKLREQAEELKRWIEQNAVIYVCGSIQGMASDVDQALKDIL----------GETQLEQLRQQGRYRR 869
Cdd:COG0369 479 AFSRDQAEKIYVQHRLLEQGAELWAWLEEGAHVYVCGDASRMAKDVDAALLDIIaehgglseeeAEEYLAELRAEKRYQR 558
|
...
gi 1872063922 870 DVY 872
Cdd:COG0369 559 DVY 561
|
|
| PiuB |
COG3182 |
PepSY-associated TM region [Function unknown]; |
1-404 |
5.09e-88 |
|
PepSY-associated TM region [Function unknown];
Pssm-ID: 442415 [Multi-domain] Cd Length: 379 Bit Score: 284.55 E-value: 5.09e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 1 MLKKAFFQIHWFLGITAGLILSLMGVTGAIYSYEQEILKWMNPNSYQVQVeQKAKLSPAEIYQHFQRTQPDYKINSITVA 80
Cdd:COG3182 2 SLRKLLRRLHLWLGLLAGLFLLILALTGALLVFKPEIDRWLNPELLAVAP-GGPPLSLDELLAAARAAYPGARVTSITLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 81 KDPAASSSINIaKEGAKRGQNILINPYSAAVLPEI-RGREFFQFIQQLHRNLTVGPIGKQITAACTLMLLFFVLSGIYLR 159
Cdd:COG3182 81 AEPDRAARVRV-RDPEGEGRTVYVDPYTGEVLGTRdEGSTFFRFLYRLHRSLLLGDTGRLIVGLAALLLLVLLISGLVLW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 160 WPKRHSFKQWFAIKPQLKGRNFIWDLHAVVGTWVVIFYLVLACTGLYWSYEWWRNGMFKVMGVERPQAQLQADGRNKPvn 239
Cdd:COG3182 160 WPRRRRWKDFFTFRWGAGGRRFWLDLHNVLGVWALPFLLVIALTGLVWSLADWLRAALAALGGGTPAAEAEPPASASA-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 240 snaqalhqaaqtqtagrrantTKPAKQNTLDQaqinlALTKAWQHFPqqlgqDYSSITFNVPKHANSEIEINFVDVIPQH 319
Cdd:COG3182 238 ---------------------PAGAPPLSLDA-----ALAAARAALP-----DAEPRRISLPGDPGGVYTVRGRDPGELT 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 320 ERARNNATFDYQQARITQLELYANKQLNEKIMSSMLPVHRGSFFGPVYQFLAMLAALMMPLFFVTGWMLYLKRRKQKRLT 399
Cdd:COG3182 287 PRGRDTVYFDPYTGEVLAVRDFADYSAGAKLLEWLYPLHTGRFGGLPGRILYFLLGLALALLIVTGLLLWWKRRRKKRAP 366
|
....*
gi 1872063922 400 LAARQ 404
Cdd:COG3182 367 PAARA 371
|
|
| cysJ |
TIGR01931 |
sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an ... |
406-872 |
3.10e-67 |
|
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: 235.36 E-value: 3.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 406 QTQFKIDPNAEHWLIVYASQTGTAEQLAWRTATSLQEAHQPVTVKALQHLSLEDLKNTTQLLCIASTYGTGDAPDLTSSF 485
Cdd:TIGR01931 49 NEAEEPAAQEKRVTILYGSQTGNARRLAKRLAEKLEAAGFSVRLSSADDYKFKQLKKERLLLLVISTQGEGEPPEEAISL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 486 VK----KILPQtcdLSHLRYAVLALGSREYADhYCRFGHTIAAWLQRNQAHALFNTIEVN-----NANP--ADIQRWNQA 554
Cdd:TIGR01931 129 HKflhsKKAPK---LENLRYSVLGLGDSSYEF-FCQTGKDFDKRLEELGGKRLLPRVDADldydaNAAEwrAGVLTALNE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 555 LVQVTQLDLPSMHIEKTFDT----WTLQQ---RDLLNPNSLGAPAFN-----IEL-LAQHDVHWSAGDIAEIQPENSTAR 621
Cdd:TIGR01931 205 QAKGGASTPSASETSTPLQTstsvYSKQNpfrAEVLENQKITGRNSKkdvrhIEIdLEGSGLHYEPGDALGVWYKNDPAL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 622 IHAFLKQHQLDANTILADGQQT--LVQALADK----DLTAPI----------QTFK------------------------ 661
Cdd:TIGR01931 285 VKEILKLLNLDPDEKVTIGGKTipLFEALITHfeltQNTKPLlkayaeltgnKELKaliadneklkayiqntplidlird 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 662 -----TADELLAQLSPLPSREYSIASipSQ-----QVLRLVVRQKFDAQGE--LGLGSGWLTAHAALGQNIALRIRNNPS 729
Cdd:TIGR01931 365 ypadlDAEQLISLLRPLTPRLYSISS--SQsevgdEVHLTVGVVRYQAHGRarLGGASGFLAERLKEGDTVPVYIEPNDN 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 730 FHL-IDDDRPIICIGNGTGLAGLMSLLHARTRLNYT-QNWLFFGERQQAHDYFYQHTIEAWQSTGMLQRLDLAFSRDQAG 807
Cdd:TIGR01931 443 FRLpEDPDTPIIMIGPGTGVAPFRAFMQERAEDGAKgKNWLFFGNPHFTTDFLYQVEWQNYLKKGVLTKMDLAFSRDQAE 522
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1872063922 808 KVYVHHKLREQAEELKRWIEQNAVIYVCGSIQGMASDVDQALKDIL----------GETQLEQLRQQGRYRRDVY 872
Cdd:TIGR01931 523 KIYVQHRIREQGAELWQWLQEGAHIYVCGDAKKMAKDVHQALLDIIakeghldaeeAEEYLTDLRVEKRYQRDVY 597
|
|
| SiR |
cd06199 |
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
595-872 |
1.89e-66 |
|
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: 225.95 E-value: 1.89e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 595 IEL-LAQHDVHWSAGDIAEIQPENSTARIHAFLKQHQLDANTILA---DGQQTLVQALADK-DLTAPIQ----------- 658
Cdd:cd06199 20 IELdLEGSGLSYEPGDALGVYPTNDPALVDELLAALGLSGDEPVStvgGGTLPLREALIKHyEITTLLLallesyaadtg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 659 ------------------------------TFKTADELLAQLSPLPSREYSIASIPS---QQVlRLVVRQ-KFDAQGE-- 702
Cdd:cd06199 100 alellalaaleavlafaelrdvldllpippARLTAEELLDLLRPLQPRLYSIASSPKavpDEV-HLTVAVvRYESHGRer 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 703 LGLGSGWLTAHAALGQNIALRIRNNPSFHL-IDDDRPIICIGNGTGLAGLMSLLHARTRLNYT-QNWLFFGERQQAHDYF 780
Cdd:cd06199 179 KGVASTFLADRLKEGDTVPVFVQPNPHFRLpEDPDAPIIMVGPGTGIAPFRAFLQEREATGAKgKNWLFFGERHFATDFL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 781 YQHTIEAWQSTGMLQRLDLAFSRDQAGKVYVHHKLREQAEELKRWIEQNAVIYVCGSIQGMASDVDQALKDIL------- 853
Cdd:cd06199 259 YQDELQQWLKDGVLTRLDTAFSRDQAEKVYVQDRMREQGAELWAWLEEGAHFYVCGDAKRMAKDVDAALLDIIateggmd 338
|
330 340
....*....|....*....|..
gi 1872063922 854 ---GETQLEQLRQQGRYRRDVY 872
Cdd:cd06199 339 eeeAEAYLKELKKEKRYQRDVY 360
|
|
| PepSY_TM |
pfam03929 |
PepSY-associated TM region; The PepSY_TM family is so named because it is an alignment of up ... |
7-392 |
7.21e-61 |
|
PepSY-associated TM region; The PepSY_TM family is so named because it is an alignment of up to five transmembranes helices found in bacterial species some of which carry a nested PepSY domain, pfam03413.
Pssm-ID: 427595 [Multi-domain] Cd Length: 355 Bit Score: 210.50 E-value: 7.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 7 FQIHWFLGITAGLILSLMGVTGAIYSYEQEILKWMNPNSYQVQV-EQKAKLSPAEIYQHFQRTQPDYKINSITVAKDPAA 85
Cdd:pfam03929 1 FRLHFWAGLLVGPFLLILALTGALLVFRPEIDRWLNPELLTVPPpGAPAPLAALRAPAAAAAAAAAAAADPGTVAVVPPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 86 SSSINIAKEGAKRGQnILINPYSAAVLPEIRGREFFQFIQQLHRNLTVG-PIGKQITAACTLMLLFFVLSGIYLRWPKRH 164
Cdd:pfam03929 81 PAPADVGLGEGERRA-VFVDPYTGEVLGEYGGSLPFRFLYRLHRGLLLGeLWGRLIVGLAALLLLVLLVSGLVLWWPRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 165 sfKQWFAIKPQLKGRNFIWDLHAVVGTWVVIFYLVLACTGLYWSYEWWRNGMFKVMGverpqaqlqadgrnkpvnsnAQA 244
Cdd:pfam03929 160 --KWLFFRFRPGGGRRFWLDLHNVLGVWALPFLLVLALTGLTWSLAAVWGAAVTALF--------------------SAG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 245 LHQAAQTQTAGRRANTTKPAKQNTLDQAqinlaltkAWQHFPQQLGQDYSSITFNVPKHANSEIEINFVDVIPQHERARN 324
Cdd:pfam03929 218 AAAPAAPAAPAPPAAAAAAPASAAAAAA--------AAAAAAAAAGAAAVAPAPPAPGTAATVVEVYRADPDGRDTVAVD 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1872063922 325 NATFDYQQARITQLELYANkqLNEKIMSSMLPVHRGSFFGPVYQFLAMLAALMMPLFFVTGWMLYLKR 392
Cdd:pfam03929 290 QYSGAVLDGVLFADYPPGD--AGAKLLAWGYPLHFGRFFGLPNRILYFLLGLALALLIVTGLLLWWKR 355
|
|
| CYPOR_like |
cd06182 |
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
672-872 |
3.81e-59 |
|
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: 202.57 E-value: 3.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 672 PLPSREYSIASIPSQQ--VLRLVVRQ-KFDA-QGELGLG--SGWLTAhAALGQNIALRIRNNPSFHLIDD-DRPIICIGN 744
Cdd:cd06182 45 PLQPRYYSIASSPDVDpgEVHLCVRVvSYEApAGRIRKGvcSNFLAG-LQLGAKVTVFIRPAPSFRLPKDpTTPIIMVGP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 745 GTGLAGLMSLLHARTRL-----NYTQNWLFFGERQQAHDYFYQHTIEAWQSTGMLQRLDLAFSRDQAG-KVYVHHKLREQ 818
Cdd:cd06182 124 GTGIAPFRGFLQERAALrangkARGPAWLFFGCRNFASDYLYREELQEALKDGALTRLDVAFSREQAEpKVYVQDKLKEH 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1872063922 819 AEELKRWIEQNAVIYVCGSIQGMASDVDQALKDIL----------GETQLEQLRQQGRYRRDVY 872
Cdd:cd06182 204 AEELRRLLNEGAHIYVCGDAKSMAKDVEDALVKIIakaggvdesdAEEYLKELEDEGRYVEDVW 267
|
|
| PRK06214 |
PRK06214 |
sulfite reductase subunit alpha; |
633-872 |
1.61e-50 |
|
sulfite reductase subunit alpha;
Pssm-ID: 235745 [Multi-domain] Cd Length: 530 Bit Score: 186.43 E-value: 1.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 633 ANTILADGQQTLVQALADKDLTAPIQTfkTADELLAQLSPLPSREYSIASIPSQQVLRL-----VVRQKFDAQGELGLGS 707
Cdd:PRK06214 276 AAGEDPDGDAATLDVLAALEKFPGIRP--DPEAFVEALDPLQPRLYSISSSPKATPGRVsltvdAVRYEIGSRLRLGVAS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 708 GWLTAHAALGQNIALRIRNNPSFHLIDD-DRPIICIGNGTGLAGLMSLLHARTRLNYT-QNWLFFGERQQAHDYFYQHTI 785
Cdd:PRK06214 354 TFLGERLAPGTRVRVYVQKAHGFALPADpNTPIIMVGPGTGIAPFRAFLHERAATKAPgRNWLFFGHQRSATDFFYEDEL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 786 EAWQSTGMLQRLDLAFSRDQAGKVYVHHKLREQAEELKRWIEQNAVIYVCGSIQGMASDVDQALKDILGE---------- 855
Cdd:PRK06214 434 NGLKAAGVLTRLSLAWSRDGEEKTYVQDRMRENGAELWKWLEEGAHFYVCGDAKRMAKDVERALVDIVAQfggrspdeav 513
|
250
....*....|....*..
gi 1872063922 856 TQLEQLRQQGRYRRDVY 872
Cdd:PRK06214 514 AFVAELKKAGRYQADVY 530
|
|
| cysJ |
PRK10953 |
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit; |
420-872 |
1.71e-49 |
|
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
Pssm-ID: 182862 [Multi-domain] Cd Length: 600 Bit Score: 184.92 E-value: 1.71e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 420 IVYASQTGTAEQLAWRTATSLQEAHQPVT-VKA----LQHLSLEDLknttqLLCIASTYGTGDAPDLTSSFVK----KIL 490
Cdd:PRK10953 66 LISASQTGNARRVAEQLRDDLLAAKLNVNlVNAgdykFKQIAQEKL-----LIVVTSTQGEGEPPEEAVALHKflfsKKA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 491 PQtcdLSHLRYAVLALGSREYaDHYCRFGHTIAAWLQRNQAHALFNTIEVNNANPADIQRWNQALVQVTQLDLPSMHIEK 570
Cdd:PRK10953 141 PK---LENTAFAVFGLGDTSY-EFFCQAGKDFDSKLAELGAERLLDRVDADVEYQAAASEWRARVVDALKSRAPAVAAPS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 571 TFDTWTLQQRDLLNPNSLGAP-----AFN--------------IEL-LAQHDVHWSAGDIAEIQPENSTARI-------- 622
Cdd:PRK10953 217 QSVATGAVNEIHTSPYSKEAPltaslSVNqkitgrnsekdvrhIEIdLGDSGLRYQPGDALGVWYQNDPALVkelvellw 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 623 -----------------HAFLKQHQLDANTILADGQ-------QTLVQALADK-------------DLT--APIQTfkTA 663
Cdd:PRK10953 297 lkgdepvtvdgktlplaEALQWHFELTVNTANIVENyatltrsETLLPLVGDKaalqhyaattpivDMVrfAPAQL--DA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 664 DELLAQLSPLPSREYSIASipSQ-------QVLRLVVRQKFDAQGELGLGSGWLTAHAALGQNIALRIRNNPSFHLIDD- 735
Cdd:PRK10953 375 EQLIGLLRPLTPRLYSIAS--SQaevenevHITVGVVRYDIEGRARAGGASSFLADRLEEEGEVRVFIEHNDNFRLPANp 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 736 DRPIICIGNGTGLAGLMSLLHARTRLNYT-QNWLFFGERQQAHDYFYQhtIEaWQS---TGMLQRLDLAFSRDQAGKVYV 811
Cdd:PRK10953 453 ETPVIMIGPGTGIAPFRAFMQQRAADGAPgKNWLFFGNPHFTEDFLYQ--VE-WQRyvkEGLLTRIDLAWSRDQKEKIYV 529
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1872063922 812 HHKLREQAEELKRWIEQNAVIYVCGSIQGMASDVDQALKDILGETQ----------LEQLRQQGRYRRDVY 872
Cdd:PRK10953 530 QDKLREQGAELWRWINDGAHIYVCGDANRMAKDVEQALLEVIAEFGgmdteaadefLSELRVERRYQRDVY 600
|
|
| methionine_synthase_red |
cd06203 |
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ... |
666-872 |
7.43e-44 |
|
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: 164.03 E-value: 7.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 666 LLAQLSPLPSREYSIASIPSQQVLRLVVRQKFDAQGELGLGSGWLTAH----AALGQNIALRIRNNPSFHLIDDD--RPI 739
Cdd:cd06203 165 LIEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPAKGLCTSWLESLclsaSSHGVKVPFYLRSSSRFRLPPDDlrRPI 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 740 ICIGNGTGLAGLMSLLHARTRL-------NYTQNWLFFGERQQAHDYFYQHTIEAWQSTGMLQRLDLAFSRDQ---AGKV 809
Cdd:cd06203 245 IMVGPGTGVAPFLGFLQHREKLkeshtetVFGEAWLFFGCRHRDRDYLFRDELEEFLEEGILTRLIVAFSRDEndgSTPK 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1872063922 810 YVHHKLREQAEELKRWI-EQNAVIYVCGSIQGMASDVDQALKDILGE----------TQLEQLRQQGRYRRDVY 872
Cdd:cd06203 325 YVQDKLEERGKKLVDLLlNSNAKIYVCGDAKGMAKDVRDTFVDILSKelgldkleakKLLARLRKEDRYLEDVW 398
|
|
| SiR_like2 |
cd06201 |
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
646-872 |
8.68e-41 |
|
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: 151.71 E-value: 8.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 646 QALADKDLTAPIQTFKTADEL--LAQLSPLPsREYSIASIPSQQVLRLVVRQKfdaqgELGLGSGWLTAhAALGQNIALR 723
Cdd:cd06201 70 KPAKRKLSGKGLPSFEAGDLLgiLPPGSDVP-RFYSLASSSSDGFLEICVRKH-----PGGLCSGYLHG-LKPGDTIKAF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 724 IRNNPSFHLIDDDRPIICIGNGTGLAGLMSLLHARTRlnYTQNWLFFGERQQAHDYFYQHTIEAWQSTGMLQRLDLAFSR 803
Cdd:cd06201 143 IRPNPSFRPAKGAAPVILIGAGTGIAPLAGFIRANAA--RRPMHLYWGGRDPASDFLYEDELDQYLADGRLTQLHTAFSR 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1872063922 804 DQaGKVYVHHKLREQAEELKRWIEQNAVIYVCGSiQGMASDVDQALKDILGETQL--EQLRQQGRYRRDVY 872
Cdd:cd06201 221 TP-DGAYVQDRLRADAERLRRLIEDGAQIMVCGS-RAMAQGVAAVLEEILAPQPLslDELKLQGRYAEDVY 289
|
|
| CyPoR_like |
cd06207 |
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
593-872 |
7.62e-38 |
|
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: 145.88 E-value: 7.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 593 FNIEL-LAQHDVHWSAGDIAEIQPENSTARIHAFLKQHQLDANTIL-----------------ADGQQTLVQALadkDLT 654
Cdd:cd06207 18 RHIEFdLGGSGLSYETGDNLGIYPENSDALVDEFLARLGLDGDDVVrvepneqqrgkppfpepISVRQLLKKFL---DIF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 655 AP---------------------------------------------IQTFKTADELLAQL----SPLPSREYSIASIPS 685
Cdd:cd06207 95 GKptkkflkllsqlatdeeekedlyklasregrteykryekytylevLKDFPSVRPTLEQLlelcPLIKPRYYSISSSPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 686 QQVLR------LVVRQKFDAQGELGLGSGWLtAHAALGQNIALRIRNNpSFHLIDDDR-PIICIGNGTGLAGLMSLLHAR 758
Cdd:cd06207 175 KNPNEvhllvsLVSWKTPSGRSRYGLCSSYL-AGLKVGQRVTVFIKKS-SFKLPKDPKkPIIMVGPGTGLAPFRAFLQER 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 759 TRLNyTQNW------LFFGERQQAHDYFYQHTIEAWQSTGMLQRLDLAFSRDQAGKVYVHHKLREQAEELKRWIEQNA-V 831
Cdd:cd06207 253 AALL-AQGPeigpvlLYFGCRHEDKDYLYKEELEEYEKSGVLTTLGTAFSRDQPKKVYVQDLIRENSDLVYQLLEEGAgV 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1872063922 832 IYVCGSIQGMASDVDQALKDILGETQ----------LEQLRQQGRYRRDVY 872
Cdd:cd06207 332 IYVCGSTWKMPPDVQEAFEEILKKHGggdeelaekkIEELEERGRYVVEAW 382
|
|
| CYPOR |
cd06204 |
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
634-871 |
1.10e-37 |
|
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: 146.25 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 634 NTILADGQQTLVQALAD----KDLTAPIQTFKtadELLAQLSPlpsREYSIASIPSQQ-----VLRLVVRQKFDAQGEL- 703
Cdd:cd06204 139 AKWIVEPHRNLLEVLQDfpsaKPTPPPFDFLI---ELLPRLQP---RYYSISSSSKVHpnrihITAVVVKYPTPTGRIIk 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 704 GLGSGWLTAHAALGQNIALRIRNNPS-------------------FHL-IDDDRPIICIGNGTGLAGLMSLLHARTRLNY 763
Cdd:cd06204 213 GVATNWLLALKPALNGEKPPTPYYLSgprkkgggskvpvfvrrsnFRLpTKPSTPVIMIGPGTGVAPFRGFIQERAALKE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 764 T-----QNWLFFGERQQAHDYFYQHTIEAWQSTGMLQRLDLAFSRDQAGKVYVHHKLREQAEELKRWIEQNAVIYVCGSI 838
Cdd:cd06204 293 SgkkvgPTLLFFGCRHPDEDFIYKDELEEYAKLGGLLELVTAFSREQPKKVYVQHRLAEHAEQVWELINEGAYIYVCGDA 372
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1872063922 839 QGMASDVDQALKDILGE------TQLEQ----LRQQGRYRRDV 871
Cdd:cd06204 373 KNMARDVEKTLLEILAEqggmteTEAEEyvkkLKTRGRYQEDV 415
|
|
| bifunctional_CYPOR |
cd06206 |
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ... |
627-872 |
2.70e-34 |
|
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: 135.46 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 627 KQHQLDANTILADGQQTLVQALADKDLTAPIQT-----------FKTAD----ELLAQLSPLPSREYSIASIP--SQQVL 689
Cdd:cd06206 98 RQLAALAEATRCPDTKALLERLAGEAYAAEVLAkrvsvldllerFPSIAlplaTFLAMLPPMRPRQYSISSSPlvDPGHA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 690 RL---VVRQ-KFDAQGE-LGLGSGWLTAHAAlGQNIALRIR-NNPSFHLIDD-DRPIICIGNGTGLAGLMSLLHAR---- 758
Cdd:cd06206 178 TLtvsVLDApALSGQGRyRGVASSYLSSLRP-GDSIHVSVRpSHSAFRPPSDpSTPLIMIAAGTGLAPFRGFLQERaall 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 759 ---TRLNYTQnwLFFGERQQAHDYFYQHTIEAWQSTGMLQrLDLAFSRDQAGKV-YVHHKLREQAEELKRWIEQNAVIYV 834
Cdd:cd06206 257 aqgRKLAPAL--LFFGCRHPDHDDLYRDELEEWEAAGVVS-VRRAYSRPPGGGCrYVQDRLWAEREEVWELWEQGARVYV 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1872063922 835 CGSiQGMASDVDQALKDILGETQ--------------LEQLRQQGRYRRDVY 872
Cdd:cd06206 334 CGD-GRMAPGVREVLKRIYAEKDergggsddeeaeewLEELRNKGRYATDVF 384
|
|
| Nitric_oxide_synthase |
cd06202 |
The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses ... |
662-872 |
3.22e-33 |
|
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: 132.84 E-value: 3.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 662 TADELLAQLSPLPSREYSIASIPSQ-----QVLRLVVR-QKFDAQGEL--GLGSGWLTAhAALGQNIALRIRNNPSFHLI 733
Cdd:cd06202 164 PASLLLTQLPLLQPRYYSISSSPDMypgeiHLTVAVVSyRTRDGQGPVhhGVCSTWLNG-LTPGDTVPCFVRSAPSFHLP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 734 DD-DRPIICIGNGTGLAGLMSLLHART---------RLNYTQNWLFFGERQQAHDYFYQHTIEAWQSTGMLQRLDLAFSR 803
Cdd:cd06202 243 EDpSVPVIMVGPGTGIAPFRSFWQQRQydlrmsedpGKKFGDMTLFFGCRNSTIDDIYKEETEEAKNKGVLTEVYTALSR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 804 DQA-GKVYVHHKLREQAEELKRWI-EQNAVIYVCGSIQgMASDVDQALKDIL----------GETQLEQLRQQGRYRRDV 871
Cdd:cd06202 323 EPGkPKTYVQDLLKEQAESVYDALvREGGHIYVCGDVT-MAEDVSQTIQRILaehgnmsaeeAEEFILKLRDENRYHEDI 401
|
.
gi 1872063922 872 Y 872
Cdd:cd06202 402 F 402
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
675-855 |
2.22e-27 |
|
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: 111.00 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 675 SREYSIASIPS-QQVLRLVVRQKfdaqgELGLGSGWLTAHAaLGQNIALRIRNNPSFHLIDDDRPIICIGNGTGLAGLMS 753
Cdd:cd00322 41 RRAYSIASSPDeEGELELTVKIV-----PGGPFSAWLHDLK-PGDEVEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 754 LLHARTRLNY-TQNWLFFGERQQAhDYFYQHTIEAWQSTGMLQRLDLAFSRDQAGKVYVHHKLREQAEELKR-WIEQNAV 831
Cdd:cd00322 115 MLRHLAADKPgGEITLLYGARTPA-DLLFLDELEELAKEGPNFRLVLALSRESEAKLGPGGRIDREAEILALlPDDSGAL 193
|
170 180
....*....|....*....|....
gi 1872063922 832 IYVCGSiQGMASDVDQALKDILGE 855
Cdd:cd00322 194 VYICGP-PAMAKAVREALVSLGVP 216
|
|
| Flavodoxin_1 |
pfam00258 |
Flavodoxin; |
420-550 |
2.17e-18 |
|
Flavodoxin;
Pssm-ID: 425562 [Multi-domain] Cd Length: 142 Bit Score: 82.42 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 420 IVYASQTGTAEQLAWRTATSLQEAHQPVTVKALQHL--SLEDLKNTTQLLCIASTYGTGDAPDLTSSFVKKILPQT---- 493
Cdd:pfam00258 1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDDVdeTLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGtled 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1872063922 494 CDLSHLRYAVLALGSREYAdHYCRFGHTIAAWLQRNQAHALFNTIEVNNANPADIQR 550
Cdd:pfam00258 81 GDLSGLKYAVFGLGDSGYE-GFCGAAKKLDEKLSELGASRVGPLGEGDEDPQEDGLE 136
|
|
| CYPOR_like_FNR |
cd06208 |
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ... |
672-872 |
1.28e-15 |
|
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: 78.13 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 672 PLPSREYSIAS-----IPSQQVLRLVVRQKFDAQGEL-----GLGSGWLtAHAALGQNIALrirNNPS--FHLIDDDR-- 737
Cdd:cd06208 61 PHKLRLYSIASsrygdDGDGKTLSLCVKRLVYTDPETdetkkGVCSNYL-CDLKPGDDVQI---TGPVgkTMLLPEDPna 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 738 PIICIGNGTGLA---GLMSLLHARTRLNYTQN---WLFFGERQQAhDYFYQHTIEAWQSTGMLQ-RLDLAFSRDQ----A 806
Cdd:cd06208 137 TLIMIATGTGIApfrSFLRRLFREKHADYKFTglaWLFFGVPNSD-SLLYDDELEKYPKQYPDNfRIDYAFSREQknadG 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1872063922 807 GKVYVHHKLREQAEELKRWIEQ-NAVIYVCGsIQGMASDVDQALKDILG-----ETQLEQLRQQGRYRRDVY 872
Cdd:cd06208 216 GKMYVQDRIAEYAEEIWNLLDKdNTHVYICG-LKGMEPGVDDALTSVAEgglawEEFWESLKKKGRWHVEVY 286
|
|
| Fpr |
COG1018 |
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
676-851 |
6.90e-13 |
|
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 69.05 E-value: 6.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 676 REYSIASIPSQQVLRLVVRQKFDaqgelGLGSGWLTAHAALGQNIALR-IRNNpsFHL-IDDDRPIICIGNGTGLAGLMS 753
Cdd:COG1018 53 RAYSLSSAPGDGRLEITVKRVPG-----GGGSNWLHDHLKVGDTLEVSgPRGD--FVLdPEPARPLLLIAGGIGITPFLS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 754 LLHARTRLNYTQNW-LFFGERQQAHDYFYQHtIEAWQSTGMLQRLDLAFSRDQAGkvyvhHKLREQAEELKRWIE--QNA 830
Cdd:COG1018 126 MLRTLLARGPFRPVtLVYGARSPADLAFRDE-LEALAARHPRLRLHPVLSREPAG-----LQGRLDAELLAALLPdpADA 199
|
170 180
....*....|....*....|.
gi 1872063922 831 VIYVCGSiQGMASDVDQALKD 851
Cdd:COG1018 200 HVYLCGP-PPMMEAVRAALAE 219
|
|
| PRK09004 |
PRK09004 |
FMN-binding protein MioC; Provisional |
427-541 |
1.59e-12 |
|
FMN-binding protein MioC; Provisional
Pssm-ID: 181608 [Multi-domain] Cd Length: 146 Bit Score: 65.62 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 427 GTAEQLAWRTATSLQEAHQPVTVkaLQHLSLEDLKNTTQLLCIASTYGTGDAPDLTSSFVKKILPQTCDLSHLRYAVLAL 506
Cdd:PRK09004 13 GGAEYVADHLAEKLEEAGFSTET--LHGPLLDDLSASGLWLIVTSTHGAGDLPDNLQPFFEELQEQKPDLSQVRFAAIGI 90
|
90 100 110
....*....|....*....|....*....|....*
gi 1872063922 507 GSREYaDHYCRFGHTIAAWLQRNQAHALFNTIEVN 541
Cdd:PRK09004 91 GSSEY-DTFCGAIDKLEQLLKAKGAKQIGETLKID 124
|
|
| PLN03116 |
PLN03116 |
ferredoxin--NADP+ reductase; Provisional |
734-872 |
6.73e-11 |
|
ferredoxin--NADP+ reductase; Provisional
Pssm-ID: 215586 [Multi-domain] Cd Length: 307 Bit Score: 64.35 E-value: 6.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 734 DDDRPIICIGNGTGLAGLMSLLHartRL------NYT---QNWLFFG----ERQQAHDYFyQHTIEAWQSTgmlQRLDLA 800
Cdd:PLN03116 154 DPNATHIMVATGTGIAPFRGFLR---RMfmedvpAFKfggLAWLFLGvansDSLLYDDEF-ERYLKDYPDN---FRYDYA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 801 FSRDQ----AGKVYVHHKLREQAEELKRWIEQNAVIYVCGsIQGMASDVDQALKDILG------ETQLEQLRQQGRYRRD 870
Cdd:PLN03116 227 LSREQknkkGGKMYVQDKIEEYSDEIFKLLDNGAHIYFCG-LKGMMPGIQDTLKRVAEergeswEEKLSGLKKNKQWHVE 305
|
..
gi 1872063922 871 VY 872
Cdd:PLN03116 306 VY 307
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
676-851 |
2.50e-10 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 61.80 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 676 REYSIASIPSQQ-VLRLVVRqkfdaqgELGLGSGWLtAHAALGQniALRIR---NNPsFHLIDDDRPIICIGNGTGLAGL 751
Cdd:COG0543 43 RPFSIASAPREDgTIELHIR-------VVGKGTRAL-AELKPGD--ELDVRgplGNG-FPLEDSGRPVLLVAGGTGLAPL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 752 MSLL-HARTRLNYTQnwLFFGERQQAhDYFYQHTIEAWQSTgmlqRLDLAFSRDQAGKV-YVHHKLREQAEElkrwiEQN 829
Cdd:COG0543 112 RSLAeALLARGRRVT--LYLGARTPE-DLYLLDELEALADF----RVVVTTDDGWYGRKgFVTDALKELLAE-----DSG 179
|
170 180
....*....|....*....|..
gi 1872063922 830 AVIYVCGSIqGMASDVDQALKD 851
Cdd:COG0543 180 DDVYACGPP-PMMKAVAELLLE 200
|
|
| T4MO_e_transfer_like |
cd06190 |
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ... |
676-836 |
3.48e-10 |
|
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates toluene and forms p-cresol as part of a three component toluene-4-monoxygenase system. Electron transfer is from NADH to an NADH:ferredoxin oxidoreductase (TmoF in P. mendocina) to ferredoxin to an iron-containing oxygenase. TmoF is homologous to other mono- and dioxygenase systems within the ferredoxin reductase family.
Pssm-ID: 99787 Cd Length: 232 Bit Score: 61.11 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 676 REYSIASIPSQQ-VLRLVVRQKFDaqgelGLGSGWLTAHAALGQNIALR-------IRNnpsfhliDDDRPIICIGNGTG 747
Cdd:cd06190 41 RAYSMANLANASgEWEFIIKRKPG-----GAASNALFDNLEPGDELELDgpyglayLRP-------DEDRDIVCIAGGSG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 748 LAGLMSLLH--ARTRLNYTQN-WLFFGERQQAhDYFYQHTIEAWQSTGMLQRLDLAFSRDQAGKV--------YVHhklr 816
Cdd:cd06190 109 LAPMLSILRgaARSPYLSDRPvDLFYGGRTPS-DLCALDELSALVALGARLRVTPAVSDAGSGSAagwdgptgFVH---- 183
|
170 180
....*....|....*....|...
gi 1872063922 817 eqaEELKRWIE---QNAVIYVCG 836
Cdd:cd06190 184 ---EVVEATLGdrlAEFEFYFAG 203
|
|
| NAD_binding_1 |
pfam00175 |
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ... |
742-847 |
3.84e-10 |
|
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: 57.65 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 742 IGNGTGLAGLMSLLHARTRL--NYTQNWLFFGERQQaHDYFYQHTIEAWQstgmlQRLDLAF------SRDQAG----KV 809
Cdd:pfam00175 2 IAGGTGIAPVRSMLRAILEDpkDPTQVVLVFGNRNE-DDILYREELDELA-----EKHPGRLtvvyvvSRPEAGwtggKG 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 1872063922 810 YVHHKLREQAEELKrwiEQNAVIYVCGSIqGMASDVDQ 847
Cdd:pfam00175 76 RVQDALLEDHLSLP---DEETHVYVCGPP-GMIKAVRK 109
|
|
| O2ase_reductase_like |
cd06187 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
672-850 |
1.72e-09 |
|
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: 58.76 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 672 PLPSREYSIASIPS-QQVLRLVVRQkfdaqGELGLGSGWLTAHAALGQNIALrirNNP--SFHLIDD-DRPIICIGNGTG 747
Cdd:cd06187 38 PRTWRAYSPANPPNeDGEIEFHVRA-----VPGGRVSNALHDELKVGDRVRL---SGPygTFYLRRDhDRPVLCIAGGTG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 748 LAGLMSLLHARTRLNYTQN-WLFFGERQQAhDYFYQHTIEAWQSTgmLQRLDL--AFSRDQAGKV----YVHHKLREQAE 820
Cdd:cd06187 110 LAPLRAIVEDALRRGEPRPvHLFFGARTER-DLYDLEGLLALAAR--HPWLRVvpVVSHEEGAWTgrrgLVTDVVGRDGP 186
|
170 180 190
....*....|....*....|....*....|
gi 1872063922 821 ELKRWieqnaVIYVCGSiQGMASDVDQALK 850
Cdd:cd06187 187 DWADH-----DIYICGP-PAMVDATVDALL 210
|
|
| BenDO_FAD_NAD |
cd06209 |
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ... |
676-836 |
7.37e-09 |
|
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. As a Class I bacterial dioxygenases, benzoate dioxygenase like proteins combine an [2Fe-2S] cluster containing N-terminal ferredoxin at the end fused to an FAD/NADP(P) domain. In dioxygenase FAD/NAD(P) binding domain, the reductase transfers 2 electrons from NAD(P)H to the oxygenase which insert into an aromatic substrate, an initial step in microbial aerobic degradation of aromatic rings. Flavin oxidoreductases use flavins as substrates, unlike flavoenzymes which have a flavin prosthetic group.
Pssm-ID: 99805 [Multi-domain] Cd Length: 228 Bit Score: 57.22 E-value: 7.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 676 REYSIASIPSQQVLRLVVRQKFDaqgelGLGSGWLTAHAALGQNIALRirnNP--SFHLIDDDRPIICIGNGTGLAGLMS 753
Cdd:cd06209 48 RSYSFSSAPGDPRLEFLIRLLPG-----GAMSSYLRDRAQPGDRLTLT---GPlgSFYLREVKRPLLMLAGGTGLAPFLS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 754 LLH--ARTRlnytQNW---LFFGERqQAHDYFYQHTIEAWQstgmlQRL-----DLAFSRDQAG---KVYVHHKLreQAE 820
Cdd:cd06209 120 MLDvlAEDG----SAHpvhLVYGVT-RDADLVELDRLEALA-----ERLpgfsfRTVVADPDSWhprKGYVTDHL--EAE 187
|
170
....*....|....*.
gi 1872063922 821 ELKrwiEQNAVIYVCG 836
Cdd:cd06209 188 DLN---DGDVDVYLCG 200
|
|
| oxygenase_e_transfer_subunit |
cd06213 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
675-790 |
8.63e-09 |
|
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: 56.94 E-value: 8.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 675 SREYSIASIPS-QQVLRLVVRQKfdAQGELglgSGWLTAHAALGQNIALRirnNP--SFHLIDDDRPIICIGNGTGLAGL 751
Cdd:cd06213 44 ARSYSFANAPQgDGQLSFHIRKV--PGGAF---SGWLFGADRTGERLTVR---GPfgDFWLRPGDAPILCIAGGSGLAPI 115
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1872063922 752 MSLLH----ARTRLNYTqnwLFFGERQQaHDYFYQHTIEAWQS 790
Cdd:cd06213 116 LAILEqaraAGTKRDVT---LLFGARTQ-RDLYALDEIAAIAA 154
|
|
| FldA |
COG0716 |
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ... |
419-513 |
4.29e-08 |
|
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440480 [Multi-domain] Cd Length: 135 Bit Score: 52.60 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 419 LIVYASQTGTAEQLAWRTATSLQEAHqpVTVKALQHLSLEDLKNTTQLLCIASTYGtGDAPDLTSSFVKKILPqtcDLSH 498
Cdd:COG0716 2 LIVYGSTTGNTEKVAEAIAEALGAAG--VDLFEIEDADLDDLEDYDLLILGTPTWA-GELPDDWEDFLEELKE---DLSG 75
|
90
....*....|....*.
gi 1872063922 499 LRYAVLALG-SREYAD 513
Cdd:COG0716 76 KKVALFGTGdSSGYGD 91
|
|
| PRK09267 |
PRK09267 |
flavodoxin FldA; Validated |
420-516 |
4.83e-07 |
|
flavodoxin FldA; Validated
Pssm-ID: 236439 [Multi-domain] Cd Length: 169 Bit Score: 50.60 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 420 IVYASQTGTAEQLAWRTATSLQEAHqpVTVKALQHLSLEDLKNTTQLLCIASTYGTGDAPDLTSSFVKKIlpQTCDLSHL 499
Cdd:PRK09267 6 IFFGSDTGNTEDIAKMIQKKLGKDV--ADVVDIAKASKEDFEAYDLLILGIPTWGYGELQCDWDDFLPEL--EEIDFSGK 81
|
90
....*....|....*...
gi 1872063922 500 RYAVLALGSRE-YADHYC 516
Cdd:PRK09267 82 KVALFGLGDQEdYAEYFC 99
|
|
| PRK08105 |
PRK08105 |
flavodoxin; Provisional |
421-555 |
6.07e-07 |
|
flavodoxin; Provisional
Pssm-ID: 181230 [Multi-domain] Cd Length: 149 Bit Score: 49.89 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 421 VYASQTGTAEQLAwrtATSLQEAHQpvtVKALQHLSLEDLKNTTQ--LLCIASTYGTGDAPDLTSSF---VKKILPQtcd 495
Cdd:PRK08105 11 VYGNALLVAEEAE---AILTAQGHE---VTLFEDPELSDWQPYQDelVLVVTSTTGQGDLPDSIVPLfqaLKDTAGY--- 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1872063922 496 LSHLRYAVLALGSREYaDHYCRFGHTIAAWLQRNQAHALFNTIEVN---NANPAD-----IQRWNQAL 555
Cdd:PRK08105 82 QPNLRYGVIALGDSSY-DNFCGAGKQFDALLQEQGAKRVGERLEIDaceTPEPEVeanpwVEQWGTLL 148
|
|
| flavin_oxioreductase |
cd06189 |
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
675-851 |
1.04e-06 |
|
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: 50.63 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 675 SREYSIASIPSQqvlrlvvrqkfDAQGEL--GLGSGWLTA---HAALGQNIALRIRN-NPSFHL-IDDDRPIICIGNGTG 747
Cdd:cd06189 41 KRPFSIASAPHE-----------DGEIELhiRAVPGGSFSdyvFEELKENGLVRIEGpLGDFFLrEDSDRPLILIAGGTG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 748 LAGLMSLLHARTRLNYTQN-WLFFGERQQAHDYfYQHTIEAWQS-------TGMLQRLDlafsRDQAGKV-YVHHKLREQ 818
Cdd:cd06189 110 FAPIKSILEHLLAQGSKRPiHLYWGARTEEDLY-LDELLEAWAEahpnftyVPVLSEPE----EGWQGRTgLVHEAVLED 184
|
170 180 190
....*....|....*....|....*....|...
gi 1872063922 819 AEELKRWieqnaVIYVCGSiQGMasdVDQALKD 851
Cdd:cd06189 185 FPDLSDF-----DVYACGS-PEM---VYAARDD 208
|
|
| monooxygenase_like |
cd06212 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
674-787 |
1.07e-06 |
|
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. These flavoprotein monooxygenases use molecular oxygen as a substrate and require reduced FAD. One atom of oxygen is incorportated into the aromatic compond, while the other is used to form a molecule of water. In contrast dioxygenases add both atoms of oxygen to the substrate.
Pssm-ID: 99808 [Multi-domain] Cd Length: 232 Bit Score: 50.79 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 674 PSREYSIASIPSQ-QVLRLVVRQKFDaqgelGLGSGWLTAHAALGQNIALR-------IRNNpsfhlidDDRPIICIGNG 745
Cdd:cd06212 45 ETRSFSMANTPADpGRLEFIIKKYPG-----GLFSSFLDDGLAVGDPVTVTgpygtctLRES-------RDRPIVLIGGG 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1872063922 746 TGLAGLMSLL--HARTRLNYTQNwLFFGERQQAhDYFYQHTIEA 787
Cdd:cd06212 113 SGMAPLLSLLrdMAASGSDRPVR-FFYGARTAR-DLFYLEEIAA 154
|
|
| MMO_FAD_NAD_binding |
cd06210 |
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ... |
675-837 |
1.43e-06 |
|
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent hydroxylation of methane to methanol. This multicomponent enzyme mediates electron transfer via a hydroxylase (MMOH), a coupling protein, and a reductase which is comprised of an N-terminal [2Fe-2S] ferredoxin domain, an FAD binding subdomain, and an NADH binding subdomain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. Dioxygenases add both atom of oxygen to the substrate, while mono-oxygenases add one atom to the substrate and one atom to water.
Pssm-ID: 99806 Cd Length: 236 Bit Score: 50.42 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 675 SREYSIASIPSQQ-----VLRLVVRQKFdaqgelglgSGWLTAHAALGQNIALRirnNP--SFHLIDDD-RPIICIGNGT 746
Cdd:cd06210 51 RRSYSLANTPNWDgrlefLIRLLPGGAF---------STYLETRAKVGQRLNLR---GPlgAFGLRENGlRPRWFVAGGT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 747 GLAGLMSLLHartrlnYTQNW-------LFFGERQQaHDYFYQHTIEAWQSTGMLQRLDLAFSRDQA------GKVyvhh 813
Cdd:cd06210 119 GLAPLLSMLR------RMAEWgepqearLFFGVNTE-AELFYLDELKRLADSLPNLTVRICVWRPGGewegyrGTV---- 187
|
170 180
....*....|....*....|....*..
gi 1872063922 814 klreqAEELKRWIEQNAV---IYVCGS 837
Cdd:cd06210 188 -----VDALREDLASSDAkpdIYLCGP 209
|
|
| FNR_iron_sulfur_binding_3 |
cd06217 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
676-852 |
3.92e-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 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: 48.80 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 676 REYSIASIPSQQV-LRLVVRQKfdAQGELglgSGWLTAHAALGQNIALRirnNP--SFHLID-DDRPIICIGNGTGLAGL 751
Cdd:cd06217 51 RSYSIASSPTQRGrVELTVKRV--PGGEV---SPYLHDEVKVGDLLEVR---GPigTFTWNPlHGDPVVLLAGGSGIVPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 752 MSLLHARTRLNYTQN-WLFFGERqQAHDYFYQHTIEAwqstgmLQRLDLAFSRD-----QAGKVYVHHKLREQAEELKRW 825
Cdd:cd06217 123 MSMIRYRRDLGWPVPfRLLYSAR-TAEDVIFRDELEQ------LARRHPNLHVTealtrAAPADWLGPAGRITADLIAEL 195
|
170 180
....*....|....*....|....*....
gi 1872063922 826 IEQNA--VIYVCGSiQGMASDVDQALKDI 852
Cdd:cd06217 196 VPPLAgrRVYVCGP-PAFVEAATRLLLEL 223
|
|
| PLN03115 |
PLN03115 |
ferredoxin--NADP(+) reductase; Provisional |
734-872 |
6.13e-06 |
|
ferredoxin--NADP(+) reductase; Provisional
Pssm-ID: 215585 [Multi-domain] Cd Length: 367 Bit Score: 49.23 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 734 DDDRPIICIGNGTGLAGLMSLL-------HARTRLNyTQNWLFFGErQQAHDYFYQHTIEAWQSTGMLQ-RLDLAFSRDQ 805
Cdd:PLN03115 213 DPNATIIMLATGTGIAPFRSFLwkmffekHDDYKFN-GLAWLFLGV-PTSSSLLYKEEFEKMKEKAPENfRLDFAVSREQ 290
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1872063922 806 AG----KVYVHHKLREQAEELKRWIEQ-NAVIYVCGsIQGMASDVDQALKDILGETQLE------QLRQQGRYRRDVY 872
Cdd:PLN03115 291 TNakgeKMYIQTRMAEYAEELWELLKKdNTYVYMCG-LKGMEKGIDDIMVSLAAKDGIDwfeykkQLKKAEQWNVEVY 367
|
|
| flav_short |
TIGR01753 |
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ... |
419-518 |
7.73e-06 |
|
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: 46.56 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 419 LIVYASQTGTAEQLAWRTATSLQEAHQPVTVKALQHLSLEDLKNTTQLLCIASTYGTGDAP-DLTSSFVKKIlpQTCDLS 497
Cdd:TIGR01753 2 LIVYASMTGNTEEMANIIAEGLKEAGAEVDLLEVADADAEDLLSYDAVLLGCSTWGDEDLEqDDFEPFFEEL--EDIDLG 79
|
90 100
....*....|....*....|.
gi 1872063922 498 HLRYAVlaLGSREYADHYCRF 518
Cdd:TIGR01753 80 GKKVAL--FGSGDWGYEFCEA 98
|
|
| phenol_2-monooxygenase_like |
cd06211 |
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ... |
659-781 |
9.41e-06 |
|
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: 47.70 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 659 TFKTADELLAQLSPLP-SREYSIASIPSQQ-----VLRLVvrqkfdaqgELGLGSGWLtaHAALGQNIALRIrNNP--SF 730
Cdd:cd06211 35 EFQAGQYVNLQAPGYEgTRAFSIASSPSDAgeielHIRLV---------PGGIATTYV--HKQLKEGDELEI-SGPygDF 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1872063922 731 HLID-DDRPIICIGNGTGLAGLMS-LLHARTRLNYTQNWLFFGERQQAhDYFY 781
Cdd:cd06211 103 FVRDsDQRPIIFIAGGSGLSSPRSmILDLLERGDTRKITLFFGARTRA-ELYY 154
|
|
| PRK07308 |
PRK07308 |
flavodoxin; Validated |
420-517 |
1.95e-05 |
|
flavodoxin; Validated
Pssm-ID: 180922 [Multi-domain] Cd Length: 146 Bit Score: 45.55 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 420 IVYASQTGTAEQLAWRTATSLQEAHQPVTVKALQHLSLEDLKNTTQLLCIASTYGTGDAPDLTSSFVKKIlpQTCDLSHL 499
Cdd:PRK07308 6 IVYASMTGNTEEIADIVADKLRELGHDVDVDECTTVDASDFEDADIAIVATYTYGDGELPDEIVDFYEDL--ADLDLSGK 83
|
90
....*....|....*...
gi 1872063922 500 RYAVLALGSREYaDHYCR 517
Cdd:PRK07308 84 IYGVVGSGDTFY-DYFCK 100
|
|
| FNR_N-term_Iron_sulfur_binding |
cd06194 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
669-760 |
8.24e-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: 8.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 669 QLSPLPSREYSIASIPSQQ-VLRLVVRQKFDaqgelGLGSGWLTAHAALGQniALRIRNnPS---FHLID-DDRPIICIG 743
Cdd:cd06194 33 RRAGGLARSYSPTSLPDGDnELEFHIRRKPN-----GAFSGWLGEEARPGH--ALRLQG-PFgqaFYRPEyGEGPLLLVG 104
|
90
....*....|....*...
gi 1872063922 744 NGTGLAGLMSLL-HARTR 760
Cdd:cd06194 105 AGTGLAPLWGIArAALRQ 122
|
|
| PRK05723 |
PRK05723 |
flavodoxin; Provisional |
420-522 |
1.05e-04 |
|
flavodoxin; Provisional
Pssm-ID: 168208 Cd Length: 151 Bit Score: 43.25 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 420 IVYASQTGTAEQLAWRTATSLQEAHQPVTVKAlqHLSLEDLKN--TTQLLCIASTYGTGDAPD----LTSSfVKKILPQT 493
Cdd:PRK05723 5 ILSGSVYGTAEEVARHAESLLKAAGFEAWHNP--RASLQDLQAfaPEALLAVTSTTGMGELPDnlmpLYSA-IRDQLPAA 81
|
90 100
....*....|....*....|....*....
gi 1872063922 494 cdLSHLRYAVLALGSREYADHYCRFGHTI 522
Cdd:PRK05723 82 --WRGLPGAVIALGDSSYGDTFCGGGEQM 108
|
|
| flavohem_like_fad_nad_binding |
cd06184 |
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ... |
675-855 |
1.28e-04 |
|
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling.
Pssm-ID: 99781 Cd Length: 247 Bit Score: 44.47 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 675 SREYSIASIPSQQVLRLVVRQkfDAQGELglgSGWLTAHAALGQNIALRirnNPS--FHLIDD-DRPIICIGNGTGLAGL 751
Cdd:cd06184 57 IRQYSLSDAPNGDYYRISVKR--EPGGLV---SNYLHDNVKVGDVLEVS---APAgdFVLDEAsDRPLVLISAGVGITPM 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 752 MSLLHARTRLNYTQN-WLFFGERQQAHDYFYQHTIEAWQSTGMLQRLdLAFSRDQAGKVYVHHKL--REQAEELKRW-IE 827
Cdd:cd06184 129 LSMLEALAAEGPGRPvTFIHAARNSAVHAFRDELEELAARLPNLKLH-VFYSEPEAGDREEDYDHagRIDLALLRELlLP 207
|
170 180
....*....|....*....|....*...
gi 1872063922 828 QNAVIYVCGSIQGMasdvdQALKDILGE 855
Cdd:cd06184 208 ADADFYLCGPVPFM-----QAVREGLKA 230
|
|
| FNR_iron_sulfur_binding_2 |
cd06216 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
676-851 |
2.27e-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 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: 43.75 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 676 REYSIASIPSQQ--VLRLVVRQKFDaqgelGLGSGWLTAHAALGQNIALrirNNPS--FHLIDDDR-PIICIGNGTGLAG 750
Cdd:cd06216 65 RSYSLSSSPTQEdgTITLTVKAQPD-----GLVSNWLVNHLAPGDVVEL---SQPQgdFVLPDPLPpRLLLIAAGSGITP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 751 LMSLLHARTRLNYTQN--WLFFGeRQQAHDYFyqhtieawqsTGMLQRLDLAFSRDQagkVYVHHKLREQ-----AEELK 823
Cdd:cd06216 137 VMSMLRTLLARGPTADvvLLYYA-RTREDVIF----------ADELRALAAQHPNLR---LHLLYTREELdgrlsAAHLD 202
|
170 180 190
....*....|....*....|....*....|
gi 1872063922 824 RW--IEQNAVIYVCGSiQGMASDVDQALKD 851
Cdd:cd06216 203 AVvpDLADRQVYACGP-PGFLDAAEELLEA 231
|
|
| NADH_quinone_reductase |
cd06188 |
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ... |
675-846 |
5.74e-04 |
|
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) provides a means of storing redox reaction energy via the transmembrane translocation of Na2+ ions. The C-terminal domain resembles ferredoxin:NADP+ oxidoreductase, and has NADH and FAD binding sites. (Na+-NQR) is distinct from H+-translocating NADH:quinone oxidoreductases and noncoupled NADH:quinone oxidoreductases. The NAD(P) binding domain of 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 vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain of this group typically contains an iron-sulfur cluster binding domain.
Pssm-ID: 99785 [Multi-domain] Cd Length: 283 Bit Score: 42.68 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 675 SREYSIASIPSQQ-VLRLVVRQ---KFDAQG-ELGLGSGWLtAHAALGQNIALrirNNP--SFHLIDDDRPIICIGNGTG 747
Cdd:cd06188 86 SRAYSLANYPAEEgELKLNVRIatpPPGNSDiPPGIGSSYI-FNLKPGDKVTA---SGPfgEFFIKDTDREMVFIGGGAG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 748 LAGLMSLL-------HARTRLNYtqnwlFFGERQQAhDYFYQHTIE--AWQSTGMlqRLDLAFSRDQA-----GKV-YVH 812
Cdd:cd06188 162 MAPLRSHIfhllktlKSKRKISF-----WYGARSLK-ELFYQEEFEalEKEFPNF--KYHPVLSEPQPednwdGYTgFIH 233
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1872063922 813 HKLREQAEELKRWIEqNAVIYVCG------SIQGMASDVD 846
Cdd:cd06188 234 QVLLENYLKKHPAPE-DIEFYLCGpppmnsAVIKMLDDLG 272
|
|
| PRK06703 |
PRK06703 |
flavodoxin; Provisional |
419-531 |
1.09e-03 |
|
flavodoxin; Provisional
Pssm-ID: 235854 [Multi-domain] Cd Length: 151 Bit Score: 40.51 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872063922 419 LIVYASQTGTAEQLAWRTATSLQEAHQPVTVKALQHLSLEDLKNTTQLLCIASTYGTGDAPDLTSSFVKKILpqTCDLSH 498
Cdd:PRK06703 5 LIAYASMSGNTEDIADLIKVSLDAFDHEVVLQEMDGMDAEELLAYDGIILGSYTWGDGDLPYEAEDFHEDLE--NIDLSG 82
|
90 100 110
....*....|....*....|....*....|...
gi 1872063922 499 LRYAVLALGSREYaDHYCRFGHTIAAWLQRNQA 531
Cdd:PRK06703 83 KKVAVFGSGDTAY-PLFCEAVTIFEERLVERGA 114
|
|
| |
