|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
1-654 |
0e+00 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 1396.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 1 MNRFIMANSQQCLGCHACEIACVMAHNDEQHVLSQHHFHPRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDDSI 80
Cdd:PRK12769 1 MNRFIMANSQQCLGCHACEIACVMAHNDEQHVLSQHHFHPRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDDSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 81 QVNQQKCIGCKSCVVACPFGTMQIVLTPVAAGKVKATAHKCDLCAGRENGPACVENCPADALQLVTDVALSGMAKSRRLR 160
Cdd:PRK12769 81 QVNQQKCIGCKSCVVACPFGTMQIVLTPVAAGKVKATAHKCDLCAGRENGPACVENCPADALQLVTEQALSGMAKSRRLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 161 TARQEHQPWHASTAAQEMPVMSKVEQMQATPARGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCGEHSVCEWTC 240
Cdd:PRK12769 161 TARQEHQPWHASTAAQEMPAMSKVEQMQATPPRGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCGEHSICEWTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 241 PLHNHIPQWIELVKAGNIDAAVELSHQTNTLPEITGRVCPQDRLCEGACTIRDEHGAVTIGNIERYISDQALAKGWRPDL 320
Cdd:PRK12769 241 PLHNHIPQWIELVKAGNIDAAVELSHQTNSLPEITGRVCPQDRLCEGACTLRDEYGAVTIGNIERYISDQALAKGWRPDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 321 SHVTKVDKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGLLTFGIPSFKLDKSLLARRREIFSAMGIHFELNCEV 400
Cdd:PRK12769 321 SQVTKSDKRVAIIGAGPAGLACADVLARNGVAVTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 401 GKDVSLDSLLEQYDAVFVGVGTYRSMKAGLPNEDAPGVYDALPFLIANTKQVMGLEELPEEPFINTAGLNVVVLGGGDTA 480
Cdd:PRK12769 401 GKDISLESLLEDYDAVFVGVGTYRSMKAGLPNEDAPGVYDALPFLIANTKQVMGLEELPEEPFINTAGLNVVVLGGGDTA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 481 MDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELNEQGHVCGIRFLRTRLGEPDAQGRRR 560
Cdd:PRK12769 481 MDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELNEQGHVCGIRFLRTRLGEPDAQGRRR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 561 PVPVEGSEFVMPADAVIMAFGFNPHGMPWLESHGVTVDKWGRIIADVESQYRYQTTNPKIFAGGDAVRGADLVVTAMAEG 640
Cdd:PRK12769 561 PVPIPGSEFVMPADAVIMAFGFNPHGMPWLESHGVTVDKWGRIIADVESQYRYQTSNPKIFAGGDAVRGADLVVTAMAEG 640
|
650
....*....|....
gi 1352181648 641 RHAAQGIIDWLGVK 654
Cdd:PRK12769 641 RHAAQGIIDWLGVK 654
|
|
| gltD_gamma_fam |
TIGR01318 |
glutamate synthase small subunit family protein, proteobacterial; This model represents one of ... |
186-653 |
0e+00 |
|
glutamate synthase small subunit family protein, proteobacterial; This model represents one of three built for the NADPH-dependent or NADH-dependent glutamate synthase (EC 1.4.1.13 and 1.4.1.14, respectively) small subunit and homologs. TIGR01317 describes the small subunit (or equivalent region from longer forms) in eukaryotes, Gram-positive bacteria, and some other lineages, both NADH and NADPH-dependent. TIGR01316 describes a protein of similar length, from Archaea and a number of bacterial lineages, that forms glutamate synthase homotetramers without a large subunit. This model describes both glutatate synthase small subunit and closely related paralogs of unknown function from a number of gamma and alpha subdivision Proteobacteria, including E. coli.
Pssm-ID: 273553 [Multi-domain] Cd Length: 467 Bit Score: 934.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 186 QMQATPARGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCGEhSVCEWTCPLHNHIPQWIELVKAGNIDAAVELS 265
Cdd:TIGR01318 1 FQFIDLPRQDPDKIPVEERKTDFREIYGPFDKGQAQYQADRCLDCGN-PYCEWKCPVHNAIPQWLQLVQEGRIDEAAELS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 266 HQTNTLPEITGRVCPQDRLCEGACTIRDEHGAVTIGNIERYISDQALAKGWRPDLSHVTKVDKRVAIIGAGPAGLACADV 345
Cdd:TIGR01318 80 HQTNTLPEICGRVCPQDRLCEGACTLNDEGGAVTIGNLERYITDTALAMGWRPDLSHVQPTGKRVAVIGAGPAGLACADI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 346 LTRNGVGVTVYDRHPEIGGLLTFGIPSFKLDKSLLARRREIFSAMGIHFELNCEVGKDVSLDSLLEQYDAVFVGVGTYRS 425
Cdd:TIGR01318 160 LARAGVQVVVFDRHPEIGGLLTFGIPSFKLDKAVLSRRREIFTAMGIEFRLNCEVGRDISLDDLLEDYDAVFLGVGTYRS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 426 MKAGLPNEDAPGVYDALPFLIANTKQVMGLEELPEEPFINTAGLNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEAN 505
Cdd:TIGR01318 240 MRGGLPGEDAPGVLPALPFLIANTRQLMGLPEEPEEPLIDVEGKRVVVLGGGDTAMDCVRTAIRLGATKVTCAYRRDEAN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 506 MPGSKKEVKNAREEGANFEFNVQPVALELNEQGHVCGIRFLRTRLGEPDAQGRRRPVPVEGSEFVMPADAVIMAFGFNPH 585
Cdd:TIGR01318 320 MPGSRREVANAREEGVEFLFNVQPVSIESDEDGQVIGVTVVRTKLGEPDANGRRRPVPVAGSEFVLPADVVIMAFGFSPH 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352181648 586 GMPWLESHGVTVDKWGRIIADVESQYRYQTTNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWLGV 653
Cdd:TIGR01318 400 LMPWLAAHGITLDSWGRIITALSSGLTYQTTNPKIFAGGDAVRGADLVVTAVAEGRDAAQGILDWLGV 467
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
1-648 |
0e+00 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 827.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 1 MNRFIMANSQQCLGCHACEIACVMAHNDEQHVLSQHHFHPRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDDSI 80
Cdd:PRK12809 1 MNKFIAAEAAECIGCHACEIACAVAHNQENWPLSHSDFRPRIHVVGKGQAANPVACHHCNNAPCVTACPVNALTFQSDSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 81 QVNQQKCIGCKSCVVACPFGTMQIVLTpvaagkvkaTAHKCDLCAGRENGP-ACVENCPADALQLVTDVALSGMAKSRRL 159
Cdd:PRK12809 81 QLDEQKCIGCKRCAIACPFGVVEMVDT---------IAQKCDLCNQRSSGTqACIEVCPTQALRLMDDKGLQQIKVARQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 160 RTARQEhqpwhASTAAQEmpvmSKVEQMQATPARGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCGEHSVCEWT 239
Cdd:PRK12809 152 KTAAGK-----ASSDAQP----SRSAALLPVNSRKGADKISASERKTHFGEIYCGLDPQQATYESDRCVYCAEKANCNWH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 240 CPLHNHIPQWIELVKAGNIDAAVELSHQTNTLPEITGRVCPQDRLCEGACTIRDEHGAVTIGNIERYISDQALAKGWRPD 319
Cdd:PRK12809 223 CPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPQDRLCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 320 LSHVTKVDKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGLLTFGIPSFKLDKSLLARRREIFSAMGIHFELNCE 399
Cdd:PRK12809 303 VSKVVPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 400 VGKDVSLDSLLEQYDAVFVGVGTYRSMKAGLPNEDAPGVYDALPFLIANTKQVMGLEELPEEPFINTAGLNVVVLGGGDT 479
Cdd:PRK12809 383 IGRDITFSDLTSEYDAVFIGVGTYGMMRADLPHEDAPGVIQALPFLTAHTRQLMGLPESEEYPLTDVEGKRVVVLGGGDT 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 480 AMDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELNEQGHVCGIRFLRTRLGEPDAQGRR 559
Cdd:PRK12809 463 TMDCLRTSIRLNAASVTCAYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGRR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 560 RPVPVEGSEFVMPADAVIMAFGFNPHGMPWLESHGVTVDKWGRIIADVESQYRYQTTNPKIFAGGDAVRGADLVVTAMAE 639
Cdd:PRK12809 543 RPRPVAGSEFELPADVLIMAFGFQAHAMPWLQGSGIKLDKWGLIQTGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAA 622
|
....*....
gi 1352181648 640 GRHAAQGII 648
Cdd:PRK12809 623 GRQAARDML 631
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
181-656 |
0e+00 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 694.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 181 MSKVEQMQATPaRGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCGEhSVCEWTCPLHNHIPQWIELVKAGNIDA 260
Cdd:PRK12810 1 MGKPTGFLEYD-RVDPKKRPVAERIKDFKEFYEPFSEEQAKIQAARCMDCGI-PFCHWGCPVHNYIPEWNDLVYRGRWEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 261 AVELSHQTNTLPEITGRVCPQDrlCEGACTIRDEHGAVTIGNIERYISDQALAKGWRPDLSHVTKVDKRVAIIGAGPAGL 340
Cdd:PRK12810 79 AAERLHQTNNFPEFTGRVCPAP--CEGACTLNINFGPVTIKNIERYIIDKAFEEGWVKPDPPVKRTGKKVAVVGSGPAGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 341 ACADVLTRNGVGVTVYDRHPEIGGLLTFGIPSFKLDKSLLARRREIFSAMGIHFELNCEVGKDVSLDSLLEQYDAVFVGV 420
Cdd:PRK12810 157 AAADQLARAGHKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAEYDAVFLGT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 421 GTYRSMKAGLPNEDAPGVYDALPFLIANTKQVMGLEelpEEPFINTAGLNVVVLGGGDTAMDCVRTALRHGASNVTcayR 500
Cdd:PRK12810 237 GAYKPRDLGIPGRDLDGVHFAMDFLIQNTRRVLGDE---TEPFISAKGKHVVVIGGGDTGMDCVGTAIRQGAKSVT---Q 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 501 RDEANMPGSKK-------------EVKNAREEGANFEFNVQPVALElNEQGHVCGIRFLRTRLGEPDaqgrrrPVPVEGS 567
Cdd:PRK12810 311 RDIMPMPPSRRnknnpwpywpmklEVSNAHEEGVEREFNVQTKEFE-GENGKVTGVKVVRTELGEGD------FEPVEGS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 568 EFVMPADAVIMAFGFNPHGMPWLESHGVTVDKWGRIIADvesQYRYQTTNPKIFAGGDAVRGADLVVTAMAEGRHAAQGI 647
Cdd:PRK12810 384 EFVLPADLVLLAMGFTGPEAGLLAQFGVELDERGRVAAP---DNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAI 460
|
....*....
gi 1352181648 648 IDWLGVKSV 656
Cdd:PRK12810 461 DAYLMGSTA 469
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
204-650 |
0e+00 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 658.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 204 RKTGFDEIYLPFRADQAQREASRCLKCGeHSVCEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNTLPEITGRVCPqdR 283
Cdd:COG0493 1 RIKDFREVYPGLSEEEAIEQAARCLDCG-DPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCP--A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 284 LCEGACTIRDEHGAVTIGNIERYISDQALAKGWRPDLSHVTKVDKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIG 363
Cdd:COG0493 78 PCEGACVRGIVDEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 364 GLLTFGIPSFKLDKSLLARRREIFSAMGIHFELNCEVGKDVSLDSLLEQYDAVFVGVGTYRSMKAGLPNEDAPGVYDALP 443
Cdd:COG0493 158 GLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKGVHSAMD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 444 FLIANTKQVMgleelpeEPFINTAGLNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEGANF 523
Cdd:COG0493 238 FLTAVNLGEA-------PDTILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKEEVEEALEEGVEF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 524 EFNVQPVALELNEQGHVCGIRFLRTRLGEPDAQGRRRPVPVEGSEFVMPADAVIMAFGFNPHGMPWLESHGVTVDKWGRI 603
Cdd:COG0493 311 LFLVAPVEIIGDENGRVTGLECVRMELGEPDESGRRRPVPIEGSEFTLPADLVILAIGQTPDPSGLEEELGLELDKRGTI 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1352181648 604 IADVESqyrYQTTNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDW 650
Cdd:COG0493 391 VVDEET---YQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
187-657 |
0e+00 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 581.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 187 MQATPARGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCGEhSVCEWTCPLHNHIPQWIELVKAGNIDAAVELSH 266
Cdd:PRK11749 2 KFLTTPRIPMPRQDAEERAQNFDEVAPGYTPEEAIEEASRCLQCKD-APCVKACPVSIDIPEFIRLIAEGNLKGAAETIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 267 QTNTLPEITGRVCPQDRLCEGACTIRDEHGAVTIGNIERYISDQALAKGWRPDLShVTKVDKRVAIIGAGPAGLACADVL 346
Cdd:PRK11749 81 ETNPLPAVCGRVCPQERLCEGACVRGKKGEPVAIGRLERYITDWAMETGWVLFKR-APKTGKKVAVIGAGPAGLTAAHRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 347 TRNGVGVTVYDRHPEIGGLLTFGIPSFKLDKSLLARRREIFSAMGIHFELNCEVGKDVSLDSLLEQYDAVFVGVGTYRSM 426
Cdd:PRK11749 160 ARKGYDVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDELRAGYDAVFIGTGAGLPR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 427 KAGLPNEDAPGVYDALPFLiANTKQVMGLEELPeepfintAGLNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANM 506
Cdd:PRK11749 240 FLGIPGENLGGVYSAVDFL-TRVNQAVADYDLP-------VGKRVVVIGGGNTAMDAARTAKRLGAESVTIVYRRGREEM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 507 PGSKKEVKNAREEGANFEFNVQPVALELNEQGHVcGIRFLRTRLGEPDAQGRRRpVPVEGSEFVMPADAVIMAFGFNPHG 586
Cdd:PRK11749 312 PASEEEVEHAKEEGVEFEWLAAPVEILGDEGRVT-GVEFVRMELGEPDASGRRR-VPIEGSEFTLPADLVIKAIGQTPNP 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352181648 587 MPWLESHGVTVDKWGRIIADVESqyrYQTTNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWLGVKSVK 657
Cdd:PRK11749 390 LILSTTPGLELNRWGTIIADDET---GRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYLEGAASA 457
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
178-655 |
2.40e-136 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 407.48 E-value: 2.40e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 178 MPVMSKVeqmqatPARGEPdklaIEARKTGFDEIYLPFRADQAQREASRCLKCGEHSvCEWTCPLHNHIPQWIELVKAGN 257
Cdd:PRK12831 3 KDRKKRV------PVREQD----PEVRATNFEEVCLGYNEEEAVKEASRCLQCKKPK-CVKGCPVSINIPGFISKLKEGD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 258 IDAAVELSHQTNTLPEITGRVCPQDRLCEGACTIRDEHGAVTIGNIERYISDQALAKGWRPdLSHVTKVDKRVAIIGAGP 337
Cdd:PRK12831 72 FEEAAKIIAKYNALPAVCGRVCPQESQCEGKCVLGIKGEPVAIGKLERFVADWARENGIDL-SETEEKKGKKVAVIGSGP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 338 AGLACADVLTRNGVGVTVYDRHPEIGGLLTFGIPSFKLDKS-LLARRREIFSAMGIHFELNCEVGKDVSLDSLLEQ--YD 414
Cdd:PRK12831 151 AGLTCAGDLAKMGYDVTIFEALHEPGGVLVYGIPEFRLPKEtVVKKEIENIKKLGVKIETNVVVGKTVTIDELLEEegFD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 415 AVFVGVGTYRSMKAGLPNEDAPGVYDALPFLianTKQVMGLEELPE--EPFIntAGLNVVVLGGGDTAMDCVRTALRHGA 492
Cdd:PRK12831 231 AVFIGSGAGLPKFMGIPGENLNGVFSANEFL---TRVNLMKAYKPEydTPIK--VGKKVAVVGGGNVAMDAARTALRLGA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 493 sNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELNEQGHVCGIRFLRTRLGEPDAQGRRRPVPVEGSEFVMP 572
Cdd:PRK12831 306 -EVHIVYRRSEEELPARVEEVHHAKEEGVIFDLLTNPVEILGDENGWVKGMKCIKMELGEPDASGRRRPVEIEGSEFVLE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 573 ADAVIMAFGFNPHGMPWLESHGVTVDKWGRIIADVESQyryQTTNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWLG 652
Cdd:PRK12831 385 VDTVIMSLGTSPNPLISSTTKGLKINKRGCIVADEETG---LTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYLS 461
|
...
gi 1352181648 653 VKS 655
Cdd:PRK12831 462 KKW 464
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
121-651 |
2.85e-126 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 391.03 E-value: 2.85e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 121 CDLCAGRENGPACVENCPADALQLVTDVALSGMAKSRRLRTARQEHQPWHASTAAQEMPVMSKVEQMQATPARGEPDKLA 200
Cdd:PRK12778 225 CRVTVGGKTKFACVDGPEFDGHLVDFDEMLKRMGAYKTIEGEELLKLEERTAAWRAELRKSMKPKERTAIERVPMPELDP 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 201 IEARKTGFDEIYLPFRADQAQREASRCLKCgEHSVCEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNTLPEITGRVCP 280
Cdd:PRK12778 305 EYRAHNRFEEVNLGLTKEQAMTEAKRCLDC-KNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVCGRVCP 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 281 QDRLCEGACTI-RDEHGAVTIGNIERYISDQALAKGwRPDLSHVT-KVDKRVAIIGAGPAGLACADVLTRNGVGVTVYDR 358
Cdd:PRK12778 384 QEKQCESKCIHgKMGEEAVAIGYLERFVADYERESG-NISVPEVAeKNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 359 HPEIGGLLTFGIPSFKLDKSLLARRREIFSAMGIHFELNCEVGKDVSLDSLLEQ-YDAVFVGVGtyrsmkAGLPN----- 432
Cdd:PRK12778 463 LHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELEEEgFKGIFIASG------AGLPNfmnip 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 433 -EDAPGVYDALPFLianTK-QVM-GLEELPEEPFIntAGLNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGS 509
Cdd:PRK12778 537 gENSNGVMSSNEYL---TRvNLMdAASPDSDTPIK--FGKKVAVVGGGNTAMDSARTAKRLGAERVTIVYRRSEEEMPAR 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 510 KKEVKNAREEGANFEFNVQPVALELNEQGHVCGIRFLRTRLGEPDAQGRRRPVPVEGSEFVMPADAVIMAFGFNPHGMPW 589
Cdd:PRK12778 612 LEEVKHAKEEGIEFLTLHNPIEYLADEKGWVKQVVLQKMELGEPDASGRRRPVAIPGSTFTVDVDLVIVSVGVSPNPLVP 691
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352181648 590 LESHGVTVDKWGRIIADVESqyryQTTNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWL 651
Cdd:PRK12778 692 SSIPGLELNRKGTIVVDEEM----QSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYL 749
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
202-651 |
5.83e-117 |
|
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of NADPH and NADH forms of glutamate synthase as found in eukaryotes and some bacteria. This protein is found in numerous species having no homolog of the glutamate synthase large subunit. The prototype of the family, from Pyrococcus sp. KOD1, was shown to be active as a homotetramer and to require NADPH. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130383 [Multi-domain] Cd Length: 449 Bit Score: 357.26 E-value: 5.83e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 202 EARKTGFDEIYLPFRADQAQREASRCLKC-GEHSVCEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNTLPEITGRVCP 280
Cdd:TIGR01316 3 EERSKLFQEAALGYTEQLALVEAQRCLNCkDATKPCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLLPAICGRVCP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 281 QDRLCEGACTI----RDEHGAVTIGNIERYISDQALAKGWRPDLSHVTKVDKRVAIIGAGPAGLACADVLTRNGVGVTVY 356
Cdd:TIGR01316 83 QERQCEGQCTVgkmfKDVGKPVSIGALERFVADWERQHGIETEPEKAPSTHKKVAVIGAGPAGLACASELAKAGHSVTVF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 357 DRHPEIGGLLTFGIPSFKLDKSLLARRREIFSAMGIHFELNCEVGKDVSLDSLLEQYDAVFVGVGTYRSMKAGLPNEDAP 436
Cdd:TIGR01316 163 EALHKPGGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQYDAVFIGTGAGLPKLMNIPGEELC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 437 GVYDALPFLIANTkqVMGLEELPEEPFINTAGLNVVVLGGGDTAMDCVRTALRHGASnVTCAYRRDEANMPGSKKEVKNA 516
Cdd:TIGR01316 243 GVYSANDFLTRAN--LMKAYEFPHADTPVYAGKSVVVIGGGNTAVDSARTALRLGAE-VHCLYRRTREDMTARVEEIAHA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 517 REEGANFEFNVQPVALELNEQGHVCGIRFLRTRLGEPDAQGRRRPVPVEGSEFVMPADAVIMAFGFNPHGMPWlESHGVT 596
Cdd:TIGR01316 320 EEEGVKFHFLCQPVEIIGDEEGNVRAVKFRKMDCQEQIDSGERRFLPCGDAECKLEADAVIVAIGNGSNPIMA-ETTRLK 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1352181648 597 VDKWGRIIADvesqYRYQTTNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWL 651
Cdd:TIGR01316 399 TSERGTIVVD----EDQRTSIPGVFAGGDIILGAATVIRAMGQGKRAAKSINEYL 449
|
|
| GOGAT_sm_gam |
TIGR01317 |
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ... |
193-651 |
2.14e-111 |
|
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for the NADPH-dependent or NADH-dependent glutamate synthase (EC 1.4.1.13 and 1.4.1.14, respectively) small subunit or homologous region. TIGR01316 describes a family in several archaeal and deeply branched bacterial lineages of a homotetrameric form for which there is no large subunit. Another model describes glutamate synthase small subunit from gamma and some alpha subdivision Proteobacteria plus paralogs of unknown function. This model describes the small subunit, or homologous region of longer forms proteins, of eukaryotes, Gram-positive bacteria, cyanobacteria, and some other lineages. All members with known function participate in NADH or NADPH-dependent reactions to interconvert between glutamine plus 2-oxoglutarate and two molecules of glutamate.
Pssm-ID: 162300 [Multi-domain] Cd Length: 485 Bit Score: 344.12 E-value: 2.14e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 193 RGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCGEhSVCEWT--CPLHNHIPQWIELVKAGNIDAAVELSHQTNT 270
Cdd:TIGR01317 10 RRKPTERDPRTRLKDWKEFTNPFDKESAKYQAARCMDCGT-PFCHNDsgCPLNNLIPEFNDLVFRGRWKEALDRLHATNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 271 LPEITGRVCPQDrlCEGACTIRDEHGAVTIGNIERYISDQALAKGWRPDLSHVTKVDKRVAIIGAGPAGLACADVLTRNG 350
Cdd:TIGR01317 89 FPEFTGRVCPAP--CEGACTLGISEDPVGIKSIERIIIDKGFQEGWVQPRPPSKRTGKKVAVVGSGPAGLAAADQLNRAG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 351 VGVTVYDRHPEIGGLLTFGIPSFKLDKSLLARRREIFSAMGIHFELNCEVGKDVSLDSLLEQYDAVFVGVGTYRSMKAGL 430
Cdd:TIGR01317 167 HTVTVFEREDRCGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELKEQFDAVVLAGGATKPRDLPI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 431 PNEDAPGVYDALPFLIANTKQVMGlEELPEEPFINTAGLNVVVLGGGDTAMDCVRTALRHGASNVT-------CAYRRDE 503
Cdd:TIGR01317 247 PGRELKGIHYAMEFLPSATKALLG-KDFKDIIFIKAKGKKVVVIGGGDTGADCVGTSLRHGAASVHqfeimpkPPEARAK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 504 ANM----PgSKKEVKNAREEGANF------EFNVQPVALELNEQGHVCGIRFLRTRLgEPDAQGRRRPVPVEGSEFVMPA 573
Cdd:TIGR01317 326 DNPwpewP-RVYRVDYAHEEAAAHygrdprEYSILTKEFIGDDEGKVTALRTVRVEW-KKSQDGKWQFVEIPGSEEVFEA 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352181648 574 DAVIMAFGFNPHGMPWLESHGVTVDKWGRIIADVESqyrYQTTNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWL 651
Cdd:TIGR01317 404 DLVLLAMGFVGPEQILLDDFGVKKTRRGNISAGYDD---YSTSIPGVFAAGDCRRGQSLIVWAINEGRKAAAAVDRYL 478
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
196-651 |
1.19e-107 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 348.85 E-value: 1.19e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 196 PDKLAIEaRKTGFDEIYLPFRADQAQREASRCLKCGEHSvCEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNTLPEIT 275
Cdd:PRK12775 303 PERDAVE-RARNFKEVNLGYSLEDALQEAERCIQCAKPT-CIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSIC 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 276 GRVCPQDRLCEGACTIRDEHGAVTIGNIERYISDQALAKGWRP-DLShvtKVDKRVAIIGAGPAGLACADVLTRNGVGVT 354
Cdd:PRK12775 381 GRVCPQETQCEAQCIIAKKHESVGIGRLERFVGDNARAKPVKPpRFS---KKLGKVAICGSGPAGLAAAADLVKYGVDVT 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 355 VYDRHPEIGGLLTFGIPSFKLDKSLLARRREIFSAMGIHFELNCEVGKDVSLDSLLEQ--YDAVFVGVGTYRSMKAGLPN 432
Cdd:PRK12775 458 VYEALHVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQLMNDkgFDAVFLGVGAGAPTFLGIPG 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 433 EDAPGVYDALPFLiaNTKQVMGLEELPEEPFINTAGLNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKE 512
Cdd:PRK12775 538 EFAGQVYSANEFL--TRVNLMGGDKFPFLDTPISLGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARIEE 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 513 VKNAREEGANFEFNVQPVALELNEQGHVCGIRFLRTRLGEPDAQGRRRPVPVEgsEFV-MPADAVIMAFGFNPHGMPWLE 591
Cdd:PRK12775 616 IRHAKEEGIDFFFLHSPVEIYVDAEGSVRGMKVEEMELGEPDEKGRRKPMPTG--EFKdLECDTVIYALGTKANPIITQS 693
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352181648 592 SHGVTVDKWGRIIADVESQYRYQTTN-PKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWL 651
Cdd:PRK12775 694 TPGLALNKWGNIAADDGKLESTQSTNlPGVFAGGDIVTGGATVILAMGAGRRAARSIATYL 754
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
236-652 |
8.90e-105 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 329.53 E-value: 8.90e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 236 CEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNTLPEITGRVCPQDrlCEGACTiRDEH-GAVTIGNIERYISDQALAK 314
Cdd:PRK12771 49 CNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCN-RGQVdDAVGINAVERFLGDYAIAN 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 315 GWRPDlshVTKVD--KRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGLLTFGIPSFKLDKSLLARrrEI--FSAM 390
Cdd:PRK12771 126 GWKFP---APAPDtgKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVLDA--EIqrILDL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 391 GIHFELNCEVGKDVSLDSLLEQYDAVFVGVGTYRSMKAGLPNEDAPGVYDALPFLIAntkqvMGLEELPEepfintAGLN 470
Cdd:PRK12771 201 GVEVRLGVRVGEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFLRA-----VGEGEPPF------LGKR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 471 VVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELNEQGhVCGIRFLRTRL 550
Cdd:PRK12771 270 VVVIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIEGDENG-ATGLRVITVEK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 551 GEPDAQGrrRPVPVEGSEFVMPADAVIMAFGFNPHGMPWLESHGVTVdKWGRIIADVESQyryQTTNPKIFAGGDAVRGA 630
Cdd:PRK12771 349 MELDEDG--RPSPVTGEEETLEADLVVLAIGQDIDSAGLESVPGVEV-GRGVVQVDPNFM---MTGRPGVFAGGDMVPGP 422
|
410 420
....*....|....*....|..
gi 1352181648 631 DLVVTAMAEGRHAAQGIIDWLG 652
Cdd:PRK12771 423 RTVTTAIGHGKKAARNIDAFLG 444
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
236-658 |
2.42e-96 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 310.12 E-value: 2.42e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 236 CEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNTLPEITGRVCPQDrlCEGACTirdEHGA---VTIGNIERYISDQAL 312
Cdd:PRK12814 104 CELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAP--CEEACR---RHGVdepVSICALKRYAADRDM 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 313 AKGWRPDLSHVTKVDKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGLLTFGIPSFKLDKSLLARRREIFSAMGI 392
Cdd:PRK12814 179 ESAERYIPERAPKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPESVIDADIAPLRAMGA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 393 HFELNCEVGKDVSLDSLLEQYDAVFVGVGTYRSMKAGLPNEDAPGVYDALPFL--IANTKQVmgleelpeepfinTAGLN 470
Cdd:PRK12814 259 EFRFNTVFGRDITLEELQKEFDAVLLAVGAQKASKMGIPGEELPGVISGIDFLrnVALGTAL-------------HPGKK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 471 VVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELNEQGHVcgIRFLRTRL 550
Cdd:PRK12814 326 VVVIGGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVSIERSEGGLE--LTAIKMQQ 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 551 GEPDAQGRRRPVPVEGSEFVMPADAVIMAFG--FNPhgmPWLESHGVTVDKWGRIIADVESQyryQTTNPKIFAGGDAVR 628
Cdd:PRK12814 404 GEPDESGRRRPVPVEGSEFTLQADTVISAIGqqVDP---PIAEAAGIGTSRNGTVKVDPETL---QTSVAGVFAGGDCVT 477
|
410 420 430
....*....|....*....|....*....|
gi 1352181648 629 GADLVVTAMAEGRHAAQGIIDWLGVKSVKS 658
Cdd:PRK12814 478 GADIAINAVEQGKRAAHAIDLFLNGKPVTA 507
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
75-647 |
2.50e-86 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 282.43 E-value: 2.50e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 75 HVDDsiqvnQQKCIGCKSCVVACPFGTMQIVLTPVAAGKVKATAHK-------CDLCAgrengpACVENCPADALQLVTD 147
Cdd:PRK13984 40 HIND-----WEKCIGCGTCSKICPTDAITMVEVPDLPQEYGKKPQRpvidygrCSFCA------LCVDICTTGSLKMTRE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 148 -VALSGMAKSRRLRTARQEHQPWHAStaaqEMPV-MSKVEQMQATP-ARGEPDKLAIEARKTGFDEIYLPFRADQAQREA 224
Cdd:PRK13984 109 yIHISPDPEDFIFMPTEKGINAKEPD----NAPLgWVRDENSELLDlERVEMEEIPPEERVKSFIEIVKGYSKEQAMQEA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 225 SRCLKCGehsVCEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNTLPEITGRVCPQDrlCEGACTIRDEHGAVTIGNIE 304
Cdd:PRK13984 185 ARCVECG---ICTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVCGRVCTHK--CETVCSIGHRGEPIAIRWLK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 305 RYISDQALAKGWRPDLS-HVTKVDKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGLLTFGIPSFKLDKSLLARR 383
Cdd:PRK13984 260 RYIVDNVPVEKYSEILDdEPEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYGIPSYRLPDEALDKD 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 384 REIFSAMGIHFELNCEVGKDVSLDSLLEQYDAVFVGVGTYRSMKAGLPNEDAPGVYDALPFLIANTKQVMGLEELPEEPf 463
Cdd:PRK13984 340 IAFIEALGVKIHLNTRVGKDIPLEELREKHDAVFLSTGFTLGRSTRIPGTDHPDVIQALPLLREIRDYLRGEGPKPKIP- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 464 intagLNVVVLGGGDTAMDCVRTALR-----HGASNVTC-AYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALeLNEQ 537
Cdd:PRK13984 419 -----RSLVVIGGGNVAMDIARSMARlqkmeYGEVNVKVtSLERTFEEMPADMEEIEEGLEEGVVIYPGWGPMEV-VIEN 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 538 GHVCGIRFLRTrLGEPDAQGRRRPVPVEGSEFVMPADAVIMAFGFNPH----GMPWLESHgvtvdKW--GRIIADvesQY 611
Cdd:PRK13984 493 DKVKGVKFKKC-VEVFDEEGRFNPKFDESDQIIVEADMVVEAIGQAPDysylPEELKSKL-----EFvrGRILTN---EY 563
|
570 580 590
....*....|....*....|....*....|....*.
gi 1352181648 612 RyQTTNPKIFAGGDAVRGADlVVTAMAEGRHAAQGI 647
Cdd:PRK13984 564 G-QTSIPWLFAGGDIVHGPD-IIHGVADGYWAAEGI 597
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
328-651 |
4.28e-82 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 263.00 E-value: 4.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 328 KRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGLLTFGIPSFKLDKS-------LLAR-------RREIFSAMGIH 393
Cdd:PRK12770 19 KKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIErvregvkELEEagvvfhtRTKVCCGEPLH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 394 FELNCE-VGKDVSLDSLLEQYDAVFVGVGTYRSMKAGLPNEDAPGVYDALPFLIANTKQVMGLeeLPEEPFINTAGLNVV 472
Cdd:PRK12770 99 EEEGDEfVERIVSLEELVKKYDAVLIATGTWKSRKLGIPGEDLPGVYSALEYLFRIRAAKLGY--LPWEKVPPVEGKKVV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 473 VLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPValELNEQGHVCGIRFLRTRLGE 552
Cdd:PRK12770 177 VVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPV--RIIGEGRVEGVELAKMRLGE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 553 PDAQGRRRPVPVEGSEFVMPADAVIMAFGFNPHGMPWLESHGVTVDKWGRIIADvesqYRYQTTNPKIFAGGDAVRGADL 632
Cdd:PRK12770 255 PDESGRPRPVPIPGSEFVLEADTVVFAIGEIPTPPFAKECLGIELNRKGEIVVD----EKHMTSREGVFAAGDVVTGPSK 330
|
330
....*....|....*....
gi 1352181648 633 VVTAMAEGRHAAQGIIDWL 651
Cdd:PRK12770 331 IGKAIKSGLRAAQSIHEWL 349
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
240-649 |
2.05e-70 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 246.28 E-value: 2.05e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 240 CPLHNHIPQWIELVKAGNIDAAVELSHQTNTLPEITGRVCPQDRLCEGACTirdeHGA--VTIGNIERYI--------SD 309
Cdd:PRK12779 214 CPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVCT----HTKrpIEIGQLEWYLpqheklvnPN 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 310 QALAKGWRPDlSHVTKVDKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGLLTFGIPSFKLDKSLLARRREIFSA 389
Cdd:PRK12779 290 ANERFAGRIS-PWAAAVKPPIAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIKL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 390 MGIHFELNCEVGKDVSLDSL-LEQYDAVFVGVGtyrsmkAGLPN------EDAPGVYDALPFLiANTKQVMGLEELPEEP 462
Cdd:PRK12779 369 LGGRFVKNFVVGKTATLEDLkAAGFWKIFVGTG------AGLPTfmnvpgEHLLGVMSANEFL-TRVNLMRGLDDDYETP 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 463 FINTAGLNVVVLGGGDTAMDCVRTALRHGAsNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELNEQGH-VC 541
Cdd:PRK12779 442 LPEVKGKEVFVIGGGNTAMDAARTAKRLGG-NVTIVYRRTKSEMPARVEELHHALEEGINLAVLRAPREFIGDDHTHfVT 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 542 GIRFLRTRLGEPDAQGRRRPVPVeGSEFVMPADAVIMAFGFNPHGMPWLESHGVTVDKWGRIIADVESQyryQTTNPKIF 621
Cdd:PRK12779 521 HALLDVNELGEPDKSGRRSPKPT-GEIERVPVDLVIMALGNTANPIMKDAEPGLKTNKWGTIEVEKGSQ---RTSIKGVY 596
|
410 420
....*....|....*....|....*...
gi 1352181648 622 AGGDAVRGADLVVTAMAEGRHAAQGIID 649
Cdd:PRK12779 597 SGGDAARGGSTAIRAAGDGQAAAKEIVG 624
|
|
| HycB_like |
cd10554 |
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ... |
4-145 |
2.75e-70 |
|
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.
Pssm-ID: 319876 [Multi-domain] Cd Length: 149 Bit Score: 224.83 E-value: 2.75e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 4 FIMANSQQCLGCHACEIACVMAHNDEQHV---LSQHHFHPRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDDSI 80
Cdd:cd10554 1 FVIADPDKCIGCRTCEVACAAAHSGKGIFeagTDGLPFLPRLRVVKTGEVTAPVQCRQCEDAPCANVCPVGAISQEDGVV 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352181648 81 QVNQQKCIGCKSCVVACPFGTMQIVLTPVA----AGKVKATAHKCDLCAGRENGPACVENCPADALQLV 145
Cdd:cd10554 81 QVDEERCIGCKLCVLACPFGAIEMAPTTVPgvdwERGPRAVAVKCDLCAGREGGPACVEACPTKALTLV 149
|
|
| HycB |
COG1142 |
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion]; |
1-147 |
5.00e-64 |
|
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
Pssm-ID: 440757 [Multi-domain] Cd Length: 138 Bit Score: 207.97 E-value: 5.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 1 MNRFIMANSQQCLGCHACEIACVMAHNDEQhvlsQHHFHPRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDDSI 80
Cdd:COG1142 1 MNKFIIADPEKCIGCRTCEAACAVAHEGEE----GEPFLPRIRVVRKAGVSAPVQCRHCEDAPCAEVCPVGAITRDDGAV 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352181648 81 QVNQQKCIGCKSCVVACPFGTMQIVLTPvaagkVKATAHKCDLCAGRENGPACVENCPADALQLVTD 147
Cdd:COG1142 77 VVDEEKCIGCGLCVLACPFGAITMVGEK-----SRAVAVKCDLCGGREGGPACVEACPTGALRLVDV 138
|
|
| PRK10330 |
PRK10330 |
electron transport protein HydN; |
1-162 |
1.60e-56 |
|
electron transport protein HydN;
Pssm-ID: 182382 [Multi-domain] Cd Length: 181 Bit Score: 189.72 E-value: 1.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 1 MNRFIMANSQQCLGCHACEIACVMAHNDEQHV--LSQHHFHPRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDD 78
Cdd:PRK10330 1 MNRFIIADASKCIGCRTCEVACVVSHQENQDCasLTPETFLPRIHVIKGVNVSTATVCRQCEDAPCANVCPNGAISRDKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 79 SIQVNQQKCIGCKSCVVACPFGTMQIVLTPV----AAG----KVKATAHKCDLCAGRENGPACVENCPADALQLVTDVAL 150
Cdd:PRK10330 81 FVHVMQERCIGCKTCVVACPYGAMEVVVRPVirnsGAGlnvrAEKAEANKCDLCNHREDGPACMAACPTHALICVDRNKL 160
|
170
....*....|..
gi 1352181648 151 SGMAKSRRLRTA 162
Cdd:PRK10330 161 EQLSAEKRRRAA 172
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
204-316 |
1.01e-50 |
|
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyzes the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds. This domain carries two Fe4-S4 clusters.
Pssm-ID: 434132 [Multi-domain] Cd Length: 113 Bit Score: 171.57 E-value: 1.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 204 RKTGFDEIYLPFRADQAQREASRCLKCGeHSVCEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNTLPEITGRVCPQDR 283
Cdd:pfam14691 1 RIKNFEEVALGYTEEEAIAEASRCLQCK-DPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQER 79
|
90 100 110
....*....|....*....|....*....|....
gi 1352181648 284 LCEGACTI-RDEHGAVTIGNIERYISDQALAKGW 316
Cdd:pfam14691 80 QCEGACVLgKKGFEPVAIGRLERFAADWARENGI 113
|
|
| CooF_like |
cd10563 |
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ... |
5-145 |
1.38e-40 |
|
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the iron-sulfur subunit of carbon monoxide dehydrogenase (CODH), found in anaerobic bacteria and archaea. Carbon monoxide dehydrogenase is a key enzyme for carbon monoxide (CO) metabolism, where CooF is the proposed mediator of electron transfer between CODH and the CO-induced hydrogenase, catalyzing the reaction that uses CO as a single carbon and energy source, and producing only H2 and CO2. The ion-sulfur subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons in the protein complex during reaction.
Pssm-ID: 319885 [Multi-domain] Cd Length: 140 Bit Score: 144.71 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 5 IMANSQQCLGCHACEIACVMAHNDEQHVLSQHHFH----PRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISH--VDD 78
Cdd:cd10563 2 IFIDEEKCLGCKLCEVACAVAHSKSKDLIKAKLEKerprPRIRVEESGGRSFPLQCRHCDEPPCVKACMSGAMHKdpETG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352181648 79 SIQVNQQKCIGCKSCVVACPFGtmqiVLTPVAAGKVkatAHKCDLCAGRENgPACVENCPADALQLV 145
Cdd:cd10563 82 IVIHDEEKCVGCWMCVMVCPYG----AIRPDKERKV---ALKCDLCPDRET-PACVEACPTGALVLE 140
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
12-145 |
6.30e-37 |
|
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319870 [Multi-domain] Cd Length: 136 Bit Score: 134.44 E-value: 6.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 12 CLGCHACEIACVMAHNdeqhvLSQHHFHPRITVIKHQQQRSA---VTCHHCEDAPCARSCPNGAISHVDDSI-QVNQQKC 87
Cdd:cd04410 8 CIGCGTCEVACKQEHG-----LRPGPDWSRIKVIEGGGLERAflpVSCMHCEDPPCVKACPTGAIYKDEDGIvLIDEDKC 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352181648 88 IGCKSCVVACPFGTMQIVLTPVAagkvkatAHKCDLCAGR---ENGPACVENCPADALQLV 145
Cdd:cd04410 83 IGCGSCVEACPYGAIVFDPEPGK-------AVKCDLCGDRldeGLEPACVKACPTGALTFG 136
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
5-145 |
1.35e-36 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319872 [Multi-domain] Cd Length: 130 Bit Score: 133.47 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 5 IMANSQQCLGCHACEIACVMAHNDEqhvlsqhhFHP---RITVIKHQQQR--SAVTCHHCEDAPCARSCPNGAISHVDDS 79
Cdd:cd10550 1 LVVDPEKCTGCRTCELACSLKHEGV--------FNPslsRIRVVRFEPEGldVPVVCRQCEDAPCVEACPVGAISRDEET 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352181648 80 --IQVNQQKCIGCKSCVVACPFGTMQIVltpvaagKVKATAHKCDLCAGrenGPACVENCPADALQLV 145
Cdd:cd10550 73 gaVVVDEDKCIGCGMCVEACPFGAIRVD-------PETGKAIKCDLCGG---DPACVKVCPTGALEFV 130
|
|
| HybA |
COG0437 |
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
1-143 |
4.13e-36 |
|
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];
Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 133.92 E-value: 4.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 1 MNRFIMA-NSQQCLGCHACEIACVMAHNDEQHV-LSQHHFHPRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDD 78
Cdd:COG0437 3 MKRYGMViDLTKCIGCRACVVACKEENNLPVGVtWRRVRRYEEGEFPNVEWLFVPVLCNHCDDPPCVKVCPTGATYKRED 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352181648 79 SI-QVNQQKCIGCKSCVVACPFGTMQIvltpvaaGKVKATAHKCDLCAGR-ENG--PACVENCPADALQ 143
Cdd:COG0437 83 GIvLVDYDKCIGCRYCVAACPYGAPRF-------NPETGVVEKCTFCADRlDEGllPACVEACPTGALV 144
|
|
| DMSOR_beta_like |
cd16374 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
5-151 |
2.08e-34 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319896 [Multi-domain] Cd Length: 139 Bit Score: 127.39 E-value: 2.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 5 IMANSQQCLGCHACEIACVMAHndeqhvlsqhHFHPRITVIKHQQQRSA-VTCHHCEDAPCARSCPNGAISH-VDDSIQV 82
Cdd:cd16374 1 VYVDPERCIGCRACEIACAREH----------SGKPRISVEVVEDLASVpVRCRHCEDAPCMEVCPTGAIYRdEDGAVLV 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352181648 83 NQQKCIGCKSCVVACPFGTMQIVltpvaagKVKATAHKCDLCAGRENG---PACVENCPADALQLVTDVALS 151
Cdd:cd16374 71 DPDKCIGCGMCAMACPFGVPRFD-------PSLKVAVKCDLCIDRRREgklPACVEACPTGALKFGDIEELL 135
|
|
| DMSOR_beta_like |
cd16371 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
8-144 |
1.29e-33 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319893 [Multi-domain] Cd Length: 140 Bit Score: 125.37 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 8 NSQQCLGCHACEIACVMAHNDEQHVLsqhhfhpRITVIKHQQQRS--------AVTCHHCEDAPCARSCPNGAISHVDDS 79
Cdd:cd16371 5 DQERCIGCKACEIACKDKNDLPPGVN-------WRRVYEYEGGEFpevfayflSMSCNHCENPACVKVCPTGAITKREDG 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352181648 80 I-QVNQQKCIGCKSCVVACPFGTMQIvltpvaaGKVKATAHKCDLCAGR-ENG--PACVENCPADALQL 144
Cdd:cd16371 78 IvVVDQDKCIGCGYCVWACPYGAPQY-------NPETGKMDKCDMCVDRlDEGekPACVAACPTRALDF 139
|
|
| PsrB |
cd10551 |
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ... |
12-142 |
2.64e-31 |
|
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.
Pssm-ID: 319873 [Multi-domain] Cd Length: 185 Bit Score: 120.33 E-value: 2.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 12 CLGCHACEIACVMAHNdeqhvLSQHHFHPRITVIKHQQQRSA------VTCHHCEDAPCARSCPNGAISHVDDSI-QVNQ 84
Cdd:cd10551 8 CIGCGACVVACKAENN-----VPPGVFRNRVLEYEVGEYPNVkrtflpVLCNHCENPPCVKVCPTGATYKREDGIvLVDY 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352181648 85 QKCIGCKSCVVACPFG-----TMQIVLTPVAAGKVKATAHKCDLCAGR-ENG--PACVENCPADAL 142
Cdd:cd10551 83 DKCIGCRYCMAACPYGaryfnPEEPHEFGEVPVRPKGVVEKCTFCYHRlDEGllPACVEACPTGAR 148
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
330-651 |
4.00e-28 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 114.83 E-value: 4.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 330 VAIIGAGPAGLACADVLTRNGVGVTVYDRhPEIGGLLT--------FGIPSFKLDKSLLARRREIFSAMGIHFELnCEV- 400
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLAttkeienyPGFPEGISGPELAERLREQAERFGAEILL-EEVt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 401 -------GKDVSLDSlLEQY--DAVFVGVG-TYRsmKAGLPNEDAP---GVY-----DALPFliantkqvmgleelpeep 462
Cdd:COG0492 81 svdkddgPFRVTTDD-GTEYeaKAVIIATGaGPR--KLGLPGEEEFegrGVSycatcDGFFF------------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 463 fintAGLNVVVLGGGDTAMDCVRTaLRHGASNVTCAYRRDEANmpGSKKEVKNAREEgANFEFNVQPVALELNEQGHVCG 542
Cdd:COG0492 140 ----RGKDVVVVGGGDSALEEALY-LTKFASKVTLIHRRDELR--ASKILVERLRAN-PKIEVLWNTEVTEIEGDGRVEG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 543 IRFLRTRLGEpdaqgrrrpvpvegsEFVMPADAVIMAFGFNPHgMPWLESHGVTVDKWGRIIADvesqYRYQTTNPKIFA 622
Cdd:COG0492 212 VTLKNVKTGE---------------EKELEVDGVFVAIGLKPN-TELLKGLGLELDEDGYIVVD----EDMETSVPGVFA 271
|
330 340 350
....*....|....*....|....*....|
gi 1352181648 623 GGDAVRGA-DLVVTAMAEGRHAAQGIIDWL 651
Cdd:COG0492 272 AGDVRDYKyRQAATAAGEGAIAALSAARYL 301
|
|
| PhsB_like |
cd10553 |
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ... |
5-146 |
7.25e-28 |
|
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This family includes beta FeS subunits of anaerobic DMSO reductase (DMSOR) superfamily that have yet to be characterized. DMSOR consists of a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and the tungsten-containing formate dehydrogenase (FDH-T). Examples of heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319875 [Multi-domain] Cd Length: 146 Bit Score: 109.38 E-value: 7.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 5 IMANSQQCLGCHACEIACVMAHNDEQHVLSQHHFHPRITVIKHQQQRSAV--TCHHCEDAPCARSCPNGAIS-HVDDSI- 80
Cdd:cd10553 5 LYHDSKRCIGCLACEVHCKVKNNLPVGPRLCRIFAVGPKMVGGKPRLKFVymSCFHCENPWCVKACPTGAMQkREKDGIv 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352181648 81 QVNQQKCIGCKSCVVACPFGTMQivLTPvAAGKVkataHKCDLCAGR-ENG--PACVENCPADALQLVT 146
Cdd:cd10553 85 YVDQELCIGCKACIEACPWGIPQ--WNP-ATGKV----VKCDYCMDRiDQGlkPACVTGCTTHALSFVR 146
|
|
| FDH_beta_like |
cd16366 |
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ... |
12-143 |
9.40e-28 |
|
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.
Pssm-ID: 319888 [Multi-domain] Cd Length: 156 Bit Score: 109.41 E-value: 9.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 12 CLGCHACEIACVMAHNDEQHVLSQHHFHP-------------RITVIKHQQQR-----SAVTCHHCEDAPCARSCPNGAI 73
Cdd:cd16366 8 CTGCRACQVACKQWNGLPAEKTEFTGSYQnppdltahtwtlvRFYEVEKPGGDlswlfRKDQCMHCTDAGCLAACPTGAI 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352181648 74 SHVD-DSIQVNQQKCIGCKSCVVACPFGTmqivltpVAAGKVKATAHKCDLCAGR-ENG--PACVENCPADALQ 143
Cdd:cd16366 88 IRTEtGTVVVDPETCIGCGYCVNACPFDI-------PRFDEETGRVAKCTLCYDRiSNGlqPACVKTCPTGALT 154
|
|
| FDH_b_like |
cd10562 |
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ... |
5-143 |
1.73e-25 |
|
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.
Pssm-ID: 319884 [Multi-domain] Cd Length: 161 Bit Score: 103.15 E-value: 1.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 5 IMANSQQCLGCHACEIACvMAHNDEQHVLSQ----HHFHPRI-----TVIKHQQQRSAVT----------CHHCEDAPCA 65
Cdd:cd10562 1 MLVDTSKCTACRGCQVAC-KQWNQLPAEKTPftgsYQNPPDLtpntwTLIRFYEHEEDNGgirwlfrkrqCMHCTDAACV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 66 RSCPNGAISHVDD-SIQVNQQKCIGCKSCVVACPFGTMQIvltpvaaGKVKATAHKCDLCAGR-ENG--PACVENCPADA 141
Cdd:cd10562 80 KVCPTGALYKTENgAVVVDEDKCIGCGYCVAACPFDVPRY-------DETTNKITKCTLCFDRiENGmqPACVKTCPTGA 152
|
..
gi 1352181648 142 LQ 143
Cdd:cd10562 153 LT 154
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
328-640 |
9.11e-25 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 105.09 E-value: 9.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 328 KRVAIIGAGPAGLACADVLTRNGVGVTVYDR---HPEIGGLLTFGI-------PSFKLDKSLLARRREIFSAM--GIHFE 395
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDegtCPYGGCVLSKALlgaaeapEIASLWADLYKRKEEVVKKLnnGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 396 LNCEV------GKDVSLDSLLE------QYDAVFVGVGTyRSMKAGLpnedaPGVYDALPFLIAN--TKQVMGLEELPEe 461
Cdd:pfam07992 81 LGTEVvsidpgAKKVVLEELVDgdgetiTYDRLVIATGA-RPRLPPI-----PGVELNVGFLVRTldSAEALRLKLLPK- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 462 pfintaglNVVVLGGGDTAMDCVRTALRHGAsNVTCAYRRDEAnMPGSKKEVKNA-----REEGANFEFNVQPVALELNE 536
Cdd:pfam07992 154 --------RVVVVGGGYIGVELAAALAKLGK-EVTLIEALDRL-LRAFDEEISAAlekalEKNGVEVRLGTSVKEIIGDG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 537 QGhvcgirfLRTRLGepdaqgrrrpvpvEGSEFvmPADAVIMAFGFNPhGMPWLESHGVTVDKWGRIIADVesqyRYQTT 616
Cdd:pfam07992 224 DG-------VEVILK-------------DGTEI--DADLVVVAIGRRP-NTELLEAAGLELDERGGIVVDE----YLRTS 276
|
330 340
....*....|....*....|....*
gi 1352181648 617 NPKIFAGGD-AVRGADLVVTAMAEG 640
Cdd:pfam07992 277 VPGIYAAGDcRVGGPELAQNAVAQG 301
|
|
| FDH-O_like |
cd10560 |
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ... |
12-143 |
1.84e-24 |
|
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes beta subunit of formate dehydrogenase family O (FDH-O), which is highly homologous to formate dehydrogenase N (FDH-N), a member of the DMSO reductase family. In E. coli three formate dehydrogenases are synthesized that are capable of oxidizing formate; Fdh-H, couples formate disproportionation to hydrogen and CO2, and is part of the cytoplasmically oriented formate hydrogenlyase complex, while FDH-N and FDH-O indicate their respective induction after growth with nitrate and oxygen. Little is known about FDH-O, although it shows formate oxidase activity during aerobic growth and is also synthesized during nitrate respiration, similar to FDH-N.
Pssm-ID: 319882 [Multi-domain] Cd Length: 225 Bit Score: 102.08 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 12 CLGCHACEIACV--------------MAHNDEQ--------HVLSQHHFHPRITVIKHQQQR---SAVTCHHCEDAPCAR 66
Cdd:cd10560 9 CIGCKACEVACKqwnqlpadgydfsgMSYDNTGdlsastwrHVKFIERPTEDGPANEGGDLQwlfMSDVCKHCTDAGCLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 67 SCPNGAISHVD-DSIQVNQQKCIGCKSCVVACPFGTMQIvltpvaaGKVKATAHKCDLCAGREN---GPACVENCPADAL 142
Cdd:cd10560 89 ACPTGAIFRTEfGTVYIQPDICNGCGYCVAACPFGVIDR-------NEETGRAHKCTLCYDRLKdglEPACAKACPTGSI 161
|
.
gi 1352181648 143 Q 143
Cdd:cd10560 162 Q 162
|
|
| DMSOR_beta_like |
cd16369 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
10-146 |
6.33e-24 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319891 [Multi-domain] Cd Length: 172 Bit Score: 99.00 E-value: 6.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 10 QQCLGCHACEIACVMAhndeqhvlSQHHFHPRITV--IK--HQQQRSAVTCHHCEDAPCARSCPNGAISHVDDSI--QVN 83
Cdd:cd16369 9 SRCIGCRACVAACREC--------GTHRGKSMIHVdyIDrgESTQTAPTVCMHCEDPTCAEVCPADAIKVTEDGVvqSAL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352181648 84 QQKCIGCKSCVVACPFGTMQIVLTPvaagkvkATAHKCDLCAGREN---GPACVENCPADALQLVT 146
Cdd:cd16369 81 KPRCIGCSNCVNACPFGVPKYDEER-------NLMMKCDMCYDRTSvgkAPMCASVCPSGALFYGT 139
|
|
| HybA_like |
cd10561 |
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ... |
12-143 |
7.92e-22 |
|
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 (Hyd-2), an enzyme that catalyzes the reversible oxidation of H2 to protons and electrons. Hyd-2 is membrane-associated and forms an unusual heterotetrameric [NiFe]-hydrogenase in that it lacks the typical cytochrome b membrane anchor subunit that transfers electrons to the quinone pool. The electron transfer subunit of Hyd-2 (HybA) which is predicted to contain four iron-sulfur clusters, is essential for electron transfer from Hyd-2 to menaquinone/demethylmenaquinone (MQ/DMQ) to couple hydrogen oxidation to fumarate reduction.
Pssm-ID: 319883 [Multi-domain] Cd Length: 196 Bit Score: 93.82 E-value: 7.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 12 CLGCHACEIACVMAHN------------DEQHVLSQHHFhpriTVIK------HQQQRSAVT--CHHCEDAPCARSCPNG 71
Cdd:cd10561 9 CIGCRACEVACKEWNGlpaedtafgpgwDNPRDLSAKTY----TVIKryevetGGKGFVFVKrqCMHCLDPACVSACPVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 72 AISHVDDSIQV-NQQKCIGCKSCVVACPFGtmqivlTPV-----AAGKVKatahKCDLCAGR-ENG--PACVENCPADAL 142
Cdd:cd10561 85 ALRKTPEGPVTyDEDKCIGCRYCMVACPFN------IPKyewdsANPKIR----KCTMCYDRlKEGkqPACVEACPTGAL 154
|
.
gi 1352181648 143 Q 143
Cdd:cd10561 155 L 155
|
|
| DMSOR_beta_like |
cd16367 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
11-145 |
3.55e-21 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319889 [Multi-domain] Cd Length: 138 Bit Score: 90.06 E-value: 3.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 11 QCLGCHACEIACVMAHNDeqhvlsqhhfHPRI--TVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDDSIQVNQQKCI 88
Cdd:cd16367 20 RCIRCDNCEKACADTHDG----------HSRLdrNGLRFGNLLVPTACRHCVDPVCMIGCPTGAIHRDDGGEVVISDACC 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1352181648 89 GCKSCVVACPFGTMQIVLtpvaagkvkatAHKCDLCAGReNGPACVENCPADALQLV 145
Cdd:cd16367 90 GCGNCASACPYGAIQMVR-----------AVKCDLCAGY-AGPACVSACPTGAAIRV 134
|
|
| FDH-N |
cd10558 |
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ... |
12-157 |
2.97e-20 |
|
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS subunit of formate dehydrogenase-N (FDH-N), a member of the DMSO reductase family. FDH-N is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. Thus, FDH-N is a major component of nitrate respiration of Escherichia coli. This integral membrane enzyme forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups.
Pssm-ID: 319880 [Multi-domain] Cd Length: 208 Bit Score: 89.37 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 12 CLGCHACEIACVMAHN---DEQHVLSQHHFHPRI-----TVIK---HQQQRS------AVTCHHCEDAPCARSCP-NGAI 73
Cdd:cd10558 9 CIGCKACQVACKEWNDlraEVGHNVGTYQNPADLspetwTLMKfreVEDNGKlewlirKDGCMHCADPGCLKACPsPGAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 74 SHVDDSI-QVNQQKCIGCKSCVVACPFGTMQIvltpvaaGKVKATAHKCDLCAGR-ENG--PACVENCPADALQLVTDVA 149
Cdd:cd10558 89 VQYANGIvDFQSDKCIGCGYCIKGCPFDIPRI-------SKDDNKMYKCTLCSDRvSVGlePACVKTCPTGALHFGTKED 161
|
....*...
gi 1352181648 150 LSGMAKSR 157
Cdd:cd10558 162 MLALAEKR 169
|
|
| TH_beta_N |
cd10552 |
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ... |
12-165 |
3.66e-17 |
|
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This family includes the beta subunit of pyrogallol-phloroglucinol transhydroxylase (TH), a cytoplasmic molybdenum (Mo) enzyme from anaerobic microorganisms like Pelobacter acidigallici and Desulfitobacterium hafniense which catalyzes the conversion of pyrogallol to phloroglucinol, an important building block of plant polymers. TH belongs to the DMSO reductase (DMSOR) family; it is a heterodimer consisting of a large alpha catalytic subunit and a small beta FeS subunit. The beta subunit has two domains with the N-terminal domain containing three [4Fe-4S] centers and a seven-stranded, mainly antiparallel beta-barrel domain. In the anaerobic bacterium Pelobacter acidigallici, gallic acid, pyrogallol, phloroglucinol, or phloroglucinol carboxylic acid are fermented to three molecules of acetate (plus CO2), and TH is the key enzyme in the fermentation pathway, which converts pyrogallol to phloroglucinol in the absence of O2.
Pssm-ID: 319874 [Multi-domain] Cd Length: 186 Bit Score: 80.06 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 12 CLGCHACEIACVMAH--NDEQHVLSQH----HFHPRITvikhQQQRSAV----------TCHHCEDAPCARSCPNGAISH 75
Cdd:cd10552 8 CNGCYNCFLACKDEHvgNDWPGYAAPQprhgHFWMRIL----RRERGQYpkvdvaylpvPCNHCDNAPCIKAAKDGAVYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 76 VDDSI-QVNQQKCIGCKSCVVACPFGTM------QIvltpvaagkvkatAHKCDLCAGR-ENG---PACVENCPADALQL 144
Cdd:cd10552 84 RDDGIvIIDPEKAKGQKQLVDACPYGAIywneelQV-------------PQKCTFCAHLlDDGwkePRCVQACPTGALRF 150
|
170 180
....*....|....*....|...
gi 1352181648 145 --VTDVALSGMAKSRRLRTARQE 165
Cdd:cd10552 151 gkLEDEEMAAKAAEEGLEVLHPE 173
|
|
| PRK09898 |
PRK09898 |
ferredoxin-like protein; |
5-145 |
8.96e-17 |
|
ferredoxin-like protein;
Pssm-ID: 182135 [Multi-domain] Cd Length: 208 Bit Score: 79.49 E-value: 8.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 5 IMANSQQCLGCHACEIACVMaHNDEqhvlSQHHFHPRITVIKH----------------QQQRSAVTCHHCEDAPCARSC 68
Cdd:PRK09898 61 LVTQRARCTGCHRCEISCTN-FNDG----SVGTFFSRIKIHRNyffgdngvgsggglygDLNYTADTCRQCKEPQCMNVC 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352181648 69 PNGAISHVDD--SIQVNQQKCIGCKSCVVACPFGtmqivLTPVAAGKVKATahKCDLCAgrengpACVENCPADALQLV 145
Cdd:PRK09898 136 PIGAITWQQKegCITVDHKRCIGCSACTTACPWM-----MATVNTESKKSS--KCVLCG------ECANACPTGALKII 201
|
|
| DMSOR_beta_like |
cd16372 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
3-146 |
4.07e-16 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319894 [Multi-domain] Cd Length: 125 Bit Score: 75.06 E-value: 4.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 3 RFIMANSQQCLGCHACEIACVMAHNDEQHV-LSqhhfhpRITVIKHQQQRSAVTCHHCedAPCARSCPNGAISHVDDSI- 80
Cdd:cd16372 1 KLLVTDPEKCIGCLQCEEACSKTFFKEEDReKS------CIRITETEGGYAINVCNQC--GECIDVCPTGAITRDANGVv 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 81 QVNQQKCIGCKSCVVACPFGTMqivltpvaagkVKATAH----KCDLCAgrengpACVENCPADALQLVT 146
Cdd:cd16372 73 MINKKLCVGCLMCVGFCPEGAM-----------FKHEDYpepfKCIACG------ICVKACPTGALELVE 125
|
|
| PLN02852 |
PLN02852 |
ferredoxin-NADP+ reductase |
329-639 |
6.33e-16 |
|
ferredoxin-NADP+ reductase
Pssm-ID: 215457 Cd Length: 491 Bit Score: 80.90 E-value: 6.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 329 RVAIIGAGPAGLACADVLTR--NGVGVTVYDRHPEIGGLLTFGI-PSFKLDKSLLARRREIFSAMGIHFELNCEVGKDVS 405
Cdd:PLN02852 28 HVCVVGSGPAGFYTADKLLKahDGARVDIIERLPTPFGLVRSGVaPDHPETKNVTNQFSRVATDDRVSFFGNVTLGRDVS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 406 LDSLLEQYDAVFVGVGTYRSMKAGLPNEDAPGVYDALPFliantkqVMGLEELPEEPFINTA---GLNVVVLGGGDTAMD 482
Cdd:PLN02852 108 LSELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREF-------VWWYNGHPDCVHLPPDlksSDTAVVLGQGNVALD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 483 CVRTALR--------------------HGASNVTCAYRR-------------------------DEANM---PGSKKEVK 514
Cdd:PLN02852 181 CARILLRptdelastdiaehalealrgSSVRKVYLVGRRgpvqaactakelrellglknvrvriKEADLtlsPEDEEELK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 515 NAR---------------EEGAN--------FEFNVQPVALELNEQG--HVCGIRFLRTRLgEPDAqGRRRPVPVEGSEF 569
Cdd:PLN02852 261 ASRpkrrvyellskaaaaGKCAPsggqrelhFVFFRNPTRFLDSGDGngHVAGVKLERTVL-EGAA-GSGKQVAVGTGEF 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 570 -VMPADAVIMAFGFN--P-HGMPWLESHGVTVDKWGRIIADVESqyryQTTNPKIFAGGDAVRG-----------ADLVV 634
Cdd:PLN02852 339 eDLPCGLVLKSIGYKslPvDGLPFDHKRGVVPNVHGRVLSSASG----ADTEPGLYVVGWLKRGptgiigtnltcAEETV 414
|
....*
gi 1352181648 635 TAMAE 639
Cdd:PLN02852 415 ASIAE 419
|
|
| PRK14993 |
PRK14993 |
tetrathionate reductase subunit TtrB; |
10-137 |
2.14e-14 |
|
tetrathionate reductase subunit TtrB;
Pssm-ID: 184955 [Multi-domain] Cd Length: 244 Bit Score: 73.37 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 10 QQCLGCHACEIACVMahndeQHVLSQHHFhpRITVIKHQ---QQRSAVT-------CHHCEDAPCARSCPNGAISHVDDS 79
Cdd:PRK14993 51 RRCIGCQSCTVSCTI-----ENQTPQGAF--RTTVNQYQvqrEGSQEVTnvllprlCNHCDNPPCVPVCPVQATFQREDG 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352181648 80 IQV-NQQKCIGCKSCVVACPFGTMQIvltpvaaGKVKATAHKCDLCAGR-ENG--PACVENC 137
Cdd:PRK14993 124 IVVvDNKRCVGCAYCVQACPYDARFI-------NHETQTADKCTFCVHRlEAGllPACVESC 178
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
330-644 |
6.33e-14 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 74.35 E-value: 6.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 330 VAIIGAGPAGLACADVLTRNGVGVTVYDRHPeIGG------------LL-------------TFGI----PSFKLDKsLL 380
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKGR-LGGtclnvgcipskaLLhaaevahearhaaEFGIsagaPSVDWAA-LM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 381 ARRREIFSAM--GIHFEL---NCEV----GKDVSLDSLL----EQY--DAVFVGVGTyRSMKAGLPNEDAPGVYDalpfl 445
Cdd:COG1249 84 ARKDKVVDRLrgGVEELLkknGVDVirgrARFVDPHTVEvtggETLtaDHIVIATGS-RPRVPPIPGLDEVRVLT----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 446 ianTKQVMGLEELPEepfintaglNVVVLGGGDTAMD--CVRTALrhGaSNVTCAYRRDEAnMPGSKKEV-----KNARE 518
Cdd:COG1249 158 ---SDEALELEELPK---------SLVVIGGGYIGLEfaQIFARL--G-SEVTLVERGDRL-LPGEDPEIsealeKALEK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 519 EGANFEFNVQPVALELNEQGHVCGIRflrtrlgepdaqgrrrpvpVEGSEFVMPADAVIMAFGFNPH----GmpwLESHG 594
Cdd:COG1249 222 EGIDILTGAKVTSVEKTGDGVTVTLE-------------------DGGGEEAVEADKVLVATGRRPNtdglG---LEAAG 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1352181648 595 VTVDKWGRIIADVesqyRYQTTNPKIFAGGDAVRGADLVVTAMAEGRHAA 644
Cdd:COG1249 280 VELDERGGIKVDE----YLRTSVPGIYAIGDVTGGPQLAHVASAEGRVAA 325
|
|
| Fer4_11 |
pfam13247 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
56-144 |
6.85e-14 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 404184 [Multi-domain] Cd Length: 99 Bit Score: 67.66 E-value: 6.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 56 CHHCEDAPCARSCPNGAISH--VDDSIQVNQQKCIGCKSCVVACPFGTmqivltpVAAGKVKATAHKCDLCAGR-ENG-- 130
Cdd:pfam13247 10 CRHCLNPPCKASCPVGAIYKdeETGAVLLDEKTCRGWRECVSACPYNI-------PRYNDETGKAEKCDMCYDRvEAGll 82
|
90
....*....|....
gi 1352181648 131 PACVENCPADALQL 144
Cdd:pfam13247 83 PACVQTCPTGAMNF 96
|
|
| DMSOR_beta_like |
cd16368 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
56-141 |
2.80e-11 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319890 [Multi-domain] Cd Length: 200 Bit Score: 63.21 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 56 CHHCEDAPCARSCPNGAI-SHVDDSIQVNQQKCIGCKSCVVACPFGTMQ--------IVLTPVAAGkvKATAHKCDLCAG 126
Cdd:cd16368 91 CMHCDNPPCAKLCPFGAArKTPEGAVYIDDDLCFGGAKCRDVCPWHIPQrqagvgiyLHLAPEYAG--GGVMYKCDLCKD 168
|
90
....*....|....*...
gi 1352181648 127 R-ENG--PACVENCPADA 141
Cdd:cd16368 169 LlAQGkpPACIEACPKGA 186
|
|
| PRK10882 |
PRK10882 |
hydrogenase 2 operon protein HybA; |
12-165 |
3.41e-11 |
|
hydrogenase 2 operon protein HybA;
Pssm-ID: 236786 [Multi-domain] Cd Length: 328 Bit Score: 65.08 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 12 CLGCHACEIACVMAHNDEQHV-----------LSQHHFhpriTVIKHQQQRSAVT--------------CHHCEDAPCAR 66
Cdd:PRK10882 47 CVGCQACVTKCQEINFPERNPqgeqtwdnpdkLSPYTN----NIIKVWKSGTGVNkdqeengyayikkqCMHCVDPNCVS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 67 SCPNGAISH--VDDSIQVNQQKCIGCKSCVVACPFGTMQIVLtPVAAGKVkataHKCDLCAGR-----ENG--PACVENC 137
Cdd:PRK10882 123 VCPVSALTKdpKTGIVHYDKDVCTGCRYCMVACPFNVPKYDY-NNPFGAI----HKCELCNQKgverlDKGglPGCVEVC 197
|
170 180
....*....|....*....|....*...
gi 1352181648 138 PADALQLVTDVALSGMAKsRRLRTARQE 165
Cdd:PRK10882 198 PTGAVIFGTREELLAEAK-RRLALKPGS 224
|
|
| EBDH_beta |
cd10555 |
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ... |
56-139 |
6.85e-11 |
|
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene dehydrogenase (EBDH, EC 1.17.99.2), a member of the DMSO reductase family. EBDH oxidizes the hydrocarbon ethylbenzene to (S)-1-phenylethanol. It is a heterotrimer, with the alpha subunit containing the catalytic center with a molybdenum held by two molybdopterin-guanine dinucleotides, the beta subunit containing four iron-sulfur clusters (the electron transfer subunit) and the gamma subunit containing a methionine and a lysine as axial heme ligands. During catalysis, electrons produced by substrate oxidation are transferred to a heme in the gamma subunit and then presumably to a separate cytochrome involved in nitrate respiration.
Pssm-ID: 319877 [Multi-domain] Cd Length: 316 Bit Score: 63.86 E-value: 6.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 56 CHHCEDAPCARSCPNGAI-SHVDDSIQ-VNQQKCIGCKSCVVACPFGtmQIVLTPvaagkVKATAHKCDLCAGR-ENG-- 130
Cdd:cd10555 133 CNHCTNPACLAACPRKAIyKREEDGIVlVDQDRCRGYRYCVEACPYK--KIYFNP-----VEQKSEKCIFCYPRiEKGva 205
|
....*....
gi 1352181648 131 PACVENCPA 139
Cdd:cd10555 206 PACARQCVG 214
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
56-100 |
8.59e-11 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 58.20 E-value: 8.59e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1352181648 56 CHHCEDapCARSCPNGAISHVDDSIQVNQQKCIGCKSCVVACPFG 100
Cdd:COG2768 13 CIGCGA--CVKVCPVGAISIEDGKAVIDPEKCIGCGACIEVCPVG 55
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
9-100 |
1.55e-10 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 63.89 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 9 SQQCLGCHACEIACVmaHNDEQHVLSQHHFHPRITVIKHQQQRSAVTCHHCEdaPCARSCPNGAISHVDDSIQVNQQKCI 88
Cdd:COG4624 48 CSCCPRCCLCCCCCC--RCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCY--PCVRACPVKAIKVDDGKAEIDEEKCI 123
|
90
....*....|..
gi 1352181648 89 GCKSCVVACPFG 100
Cdd:COG4624 124 SCGQCVAVCPFG 135
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
56-142 |
1.62e-10 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 58.95 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 56 CHHCedAPCARSCPNGAISHVDD-----SIQVNQQKCIGCKSCVVACPFGTMQIV----LTPVAAGKVKATAHKCDLCAg 126
Cdd:cd10549 8 CIGC--GICVKACPTDAIELGPNgaiarGPEIDEDKCVFCGACVEVCPTGAIELTpegkEYVPKEKEAEIDEEKCIGCG- 84
|
90
....*....|....*.
gi 1352181648 127 rengpACVENCPADAL 142
Cdd:cd10549 85 -----LCVKVCPVDAI 95
|
|
| DMSOR_beta_like |
cd16370 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
11-145 |
1.33e-09 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319892 [Multi-domain] Cd Length: 131 Bit Score: 56.51 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 11 QCLGCHACEIACVMAHndeqhvlsQHHFHPRITVIK------HQQQRSAVTCHHCEDAPCARSCPNGAIS-HVDDSIQVN 83
Cdd:cd16370 10 RCIGCYSCMLACSRRV--------HKSASLSKSAIRvrtrggLEGGFTVVVCRACEDPPCAEACPTGALEpRKGGGVVLD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352181648 84 QQKCIGCKSCVVACpfgtmqivltPVAAGKVKATAHK---CDLCAgrengpACVENCPADALQLV 145
Cdd:cd16370 82 KEKCIGCGNCVKAC----------IVGAIFWDEETNKpiiCIHCG------YCARYCPHDVLAME 130
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
56-105 |
1.84e-09 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 54.28 E-value: 1.84e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1352181648 56 CHHCEDapCARSCPNGAISHVDDSIQVNQQKCIGCKSCVVACPFGTMQIV 105
Cdd:COG4231 24 CTGCGA--CVKVCPADAIEEGDGKAVIDPDLCIGCGSCVQVCPVDAIKLE 71
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
353-647 |
2.13e-09 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 59.44 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 353 VTVYDRHPEIGG-------LLTFGIPSFKldkSLLARRREIFSAMGIHFELNCEV------GKDVSLDS-LLEQYDAVFV 418
Cdd:COG0446 8 ITVIEKGPHHSYqpcglpyYVGGGIKDPE---DLLVRTPESFERKGIDVRTGTEVtaidpeAKTVTLRDgETLSYDKLVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 419 GVGTyRSMKAGLPNEDAPGVYdalpfliantkQVMGLEELPE--EPFINTAGLNVVVLGGGDTAMDCVRTALRHGAsNVT 496
Cdd:COG0446 85 ATGA-RPRPPPIPGLDLPGVF-----------TLRTLDDADAlrEALKEFKGKRAVVIGGGPIGLELAEALRKRGL-KVT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 497 CAYRRDEAnMPGSKKEV-----KNAREEGANFEFNVQPVALElnEQGHVcGIRFlrtrlgepdaqgrrrpvpVEGSEFvm 571
Cdd:COG0446 152 LVERAPRL-LGVLDPEMaalleEELREHGVELRLGETVVAID--GDDKV-AVTL------------------TDGEEI-- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 572 PADAVIMAFGFNPH-------GMPWLESHGVTVDKWGriiadvesqyryQTTNPKIFAGGDAVRGADLVV---------- 634
Cdd:COG0446 208 PADLVVVAPGVRPNtelakdaGLALGERGWIKVDETL------------QTSDPDVYAAGDCAEVPHPVTgktvyiplas 275
|
330
....*....|...
gi 1352181648 635 TAMAEGRHAAQGI 647
Cdd:COG0446 276 AANKQGRVAAENI 288
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
327-596 |
2.49e-09 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 59.88 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 327 DKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGL--------LTFGIPSFKL---------DKSLLARRREIFS- 388
Cdd:COG2072 6 HVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGTwrdnrypgLRLDTPSHLYslpffpnwsDDPDFPTGDEILAy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 389 --------AMGIHFELNCEVgKDVSLDS-----LLE-------QYDAVFVGVGTYRSMK----AGLpnEDAPGV------ 438
Cdd:COG2072 86 leayadkfGLRRPIRFGTEV-TSARWDEadgrwTVTtddgetlTARFVVVATGPLSRPKipdiPGL--EDFAGEqlhsad 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 439 YD-ALPFliantkqvmgleelpeepfintAGLNVVVLGGGDTAMDCVRTALRHGASnVTCAYRRdeANMPGSKKEVKNAR 517
Cdd:COG2072 163 WRnPVDL----------------------AGKRVLVVGTGASAVQIAPELARVAAH-VTVFQRT--PPWVLPRPNYDPER 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 518 EEGANFEFNVQPVALelnEQGHVCG--IRFLRTRLGEPD--------AQGRRRPVP------------------------ 563
Cdd:COG2072 218 GRPANYLGLEAPPAL---NRRDARAwlRRLLRAQVKDPElglltpdyPPGCKRPLLstdyyealrrgnvelvtggierit 294
|
330 340 350
....*....|....*....|....*....|....*....
gi 1352181648 564 ------VEGSEFvmPADAVIMAFGFNPhGMPWLESHGVT 596
Cdd:COG2072 295 edgvvfADGTEH--EVDVIVWATGFRA-DLPWLAPLDVR 330
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
327-396 |
3.23e-09 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 59.86 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 327 DKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGLLTfgipSFKLDK----------SLLARRREIFSAMGIHFEL 396
Cdd:COG1233 3 MYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRAR----TFERPGfrfdvgpsvlTMPGVLERLFRELGLEDYL 78
|
|
| FeFe_hydrog_B1 |
TIGR04105 |
[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups. |
2-105 |
4.79e-09 |
|
[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.
Pssm-ID: 274983 [Multi-domain] Cd Length: 462 Bit Score: 59.14 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 2 NRFIMANSqqCLGC--HACEIACvmahndeqhvlsqhhfhPR--ITVIKHQ---QQRSAVTCHHCEDA-----------P 63
Cdd:TIGR04105 105 NRYTVTDA--CRGClaHPCIEVC-----------------PKgaISMVNGRayiDQEKCIECGKCKKAcpynaiveierP 165
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1352181648 64 CARSCPNGAISHVDDSIQV-NQQKCIGCKSCVVACPFGTM----QIV 105
Cdd:TIGR04105 166 CEKACPVGAISSDEDGRAViDYDKCISCGACMVACPFGAIsdksQIV 212
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
80-149 |
4.82e-09 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 53.19 E-value: 4.82e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 80 IQVNQQKCIGCKSCVVACPFGtmqiVLTPVAAGKVKATAHKCDLCAgrengpACVENCPADALQLVTDVA 149
Cdd:COG1149 6 PVIDEEKCIGCGLCVEVCPEG----AIKLDDGGAPVVDPDLCTGCG------ACVGVCPTGAITLEEREA 65
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
328-387 |
9.40e-09 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 57.92 E-value: 9.40e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352181648 328 KRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGLL-TFGIPSFKLDK---SLLARRREIF 387
Cdd:COG1232 2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIrTVEVDGFRIDRgphSFLTRDPEVL 65
|
|
| NarH_beta-like |
cd10557 |
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ... |
56-137 |
1.12e-08 |
|
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes nitrate reductase A, a member of the DMSO reductase family. The respiratory nitrate reductase complex (NarGHI) from E. coli is a heterotrimer, with the catalytic subunit (NarG) with a molybdo-bis (molybdopterin guanine dinucleotide) cofactor and an [Fe-S] cluster, the electron transfer subunit (NarH) with four [Fe-S] clusters, and the integral membrane subunit (NarI) with two b-type hemes. Nitrate reductase A often forms a respiratory chain with the formate dehydrogenase via the lipid soluble quinol pool. Electron transfer from formate to nitrate is coupled to proton translocation across the cytoplasmic membrane generating proton motive force by a redox loop mechanism. Demethylmenaquinol (DMKH2) has been shown to be a good substrate for NarGHI in nitrate respiration in E. coli.
Pssm-ID: 319879 [Multi-domain] Cd Length: 363 Bit Score: 57.37 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 56 CHHCEDAPCARSCPNGAI-SHVDDSI-QVNQQKCIGCKSCVVACPFgtmQIVLTPVAAGKvkatAHKCDLCAGR-ENG-- 130
Cdd:cd10557 179 CNHCLNPACVAACPSGAIyKREEDGIvLIDQDRCRGWRMCVSACPY---KKVYYNWKTGK----SEKCIFCYPRlEAGqp 251
|
....*..
gi 1352181648 131 PACVENC 137
Cdd:cd10557 252 TVCSETC 258
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
328-651 |
1.27e-08 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 57.45 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 328 KRVAIIGAGPAGLACADVLTRN---GVGVTVYDRHPE----------IGGLLTFGIPSFKLDKsLLARRREIF---SAMG 391
Cdd:COG1252 2 KRIVIVGGGFAGLEAARRLRKKlggDAEVTLIDPNPYhlfqpllpevAAGTLSPDDIAIPLRE-LLRRAGVRFiqgEVTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 392 IHFE---LNCEVGKDVSldslleqYDAVFVGVGTyRSMKAGLPN--EDAPGVY---DALpfLIANTkqvmgLEELPEEpF 463
Cdd:COG1252 81 IDPEartVTLADGRTLS-------YDYLVIATGS-VTNFFGIPGlaEHALPLKtleDAL--ALRER-----LLAAFER-A 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 464 INTAGLNVVVLGGGDT------AMD------CVRTALRHGASNVTCAYRRDEAnMPGSKKEVKNAreeganfefnvqpVA 531
Cdd:COG1252 145 ERRRLLTIVVVGGGPTgvelagELAellrklLRYPGIDPDKVRITLVEAGPRI-LPGLGEKLSEA-------------AE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 532 LELNEQGhvcgIRF-LRTRLGEPDAQGrrrpVPVEGSEFVmPADAVIMAFGFNPHgmPWLESHGVTVDKWGRIIADvesq 610
Cdd:COG1252 211 KELEKRG----VEVhTGTRVTEVDADG----VTLEDGEEI-PADTVIWAAGVKAP--PLLADLGLPTDRRGRVLVD---- 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1352181648 611 yRYQTT--NPKIFAGGD--AVRGAD------LVVTAMAEGRHAAQGIIDWL 651
Cdd:COG1252 276 -PTLQVpgHPNVFAIGDcaAVPDPDgkpvpkTAQAAVQQAKVLAKNIAALL 325
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
64-149 |
1.46e-08 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 56.48 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 64 CARSCPNGAISHVDDSIQVNQQKCIGCKSCVVACPFGTmqIVLTPVAA---------GKVKATAHKCDlcAGRENGPACV 134
Cdd:PRK07118 147 CVAACPFDAIHIENGLPVVDEDKCTGCGACVKACPRNV--IELIPKSArvfvacnskDKGKAVKKVCE--VGCIGCGKCV 222
|
90
....*....|....*
gi 1352181648 135 ENCPADALQLVTDVA 149
Cdd:PRK07118 223 KACPAGAITMENNLA 237
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
329-377 |
1.52e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 57.20 E-value: 1.52e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1352181648 329 RVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGLL-TFGIPSFKLDK 377
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAaSFEFGGLPIER 50
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
328-365 |
1.54e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 57.59 E-value: 1.54e-08
10 20 30
....*....|....*....|....*....|....*...
gi 1352181648 328 KRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGL 365
Cdd:PRK07208 5 KSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGI 42
|
|
| NarH_like |
cd16365 |
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ... |
8-138 |
2.95e-08 |
|
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several DMSO reductase superfamily, including nitrate reductase A, ethylbenzene dehydrogenase and selenate reductase. DMSO Reductase (DMSOR) family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. . The beta subunits of DMSOR contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Nitrate reductase A contains three subunits (the catalytic subunit NarG, the catalytic subunit NarH with four [Fe-S] clusters, and integral membrane subunit NarI) and often forms a respiratory chain with the formate dehydrogenase via the lipid soluble quinol pool. Ethylbenzene dehydrogenase oxidizes the hydrocarbon ethylbenzene to (S)-1-phenylethanol. Selenate reductase catalyzes reduction of selenate to selenite in bacterial species that can obtain energy by respiring anaerobically with selenate as the terminal electron acceptor.
Pssm-ID: 319887 [Multi-domain] Cd Length: 201 Bit Score: 54.51 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 8 NSQQCLGCHACEIAC--VMAHNDEQHVLSQHHF-------HPRITVIKHQQQRS--------AVTCHHCEDAPCARSCPN 70
Cdd:cd16365 8 NLNKCIGCQTCTVACknAWTYRKGQEYMWWNNVetkpgggYPQDWEVKTIDNGGntrfffylQRLCNHCTNPACLAACPR 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352181648 71 GAISHVDDS--IQVNQQKCIGCKSCVVACPFgtMQIVLTPVAagkvkATAHKCDLCAGRENG---PACVENCP 138
Cdd:cd16365 88 GAIYKREEDgiVLIDQKRCRGYRKCVEQCPY--KKIYFNGLS-----RVSEKCIACYPRIEGgdpTRCMSACV 153
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
12-100 |
3.84e-08 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 52.40 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 12 CLGCHACEIACvmahndEQHVLSQHHFHPRITVIKhqqqRSAV----TCHHCEDapCARSCPNGAISHVDD-SIQVNQQK 86
Cdd:cd10549 42 CVFCGACVEVC------PTGAIELTPEGKEYVPKE----KEAEideeKCIGCGL--CVKVCPVDAITLEDElEIVIDKEK 109
|
90
....*....|....
gi 1352181648 87 CIGCKSCVVACPFG 100
Cdd:cd10549 110 CIGCGICAEVCPVN 123
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
64-100 |
4.49e-08 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 50.43 E-value: 4.49e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1352181648 64 CARSCPNGAISHVDDSIQVNQQKCIGCKSCVVACPFG 100
Cdd:COG2221 23 CVAVCPTGAISLDDGKLVIDEEKCIGCGACIRVCPTG 59
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
328-364 |
4.60e-08 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 55.27 E-value: 4.60e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1352181648 328 KRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGG 364
Cdd:COG3380 4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
328-647 |
4.99e-08 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 55.53 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 328 KRVAIIGAGPAGLACADVLTRNG--VGVTV--------YDRHP---EIGGLLTFgipsfkldKSLLARRREIFSAMGIHF 394
Cdd:COG1251 2 MRIVIIGAGMAGVRAAEELRKLDpdGEITVigaephppYNRPPlskVLAGETDE--------EDLLLRPADFYEENGIDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 395 ELNCEV------GKDVSLDSLLE-QYDAVFVGVGTyRSMKAGLPNEDAPGV--------YDALpfliantkqvmgLEELP 459
Cdd:COG1251 74 RLGTRVtaidraARTVTLADGETlPYDKLVLATGS-RPRVPPIPGADLPGVftlrtlddADAL------------RAALA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 460 eepfintAGLNVVVLGGGDTAMDCVRTALRHGASnVTCAYRRD---EANMP--GSKKEVKNAREEGANFEFNVQPVALEl 534
Cdd:COG1251 141 -------PGKRVVVIGGGLIGLEAAAALRKRGLE-VTVVERAPrllPRQLDeeAGALLQRLLEALGVEVRLGTGVTEIE- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 535 nEQGHVCGIRFlrtrlgepdAQGRrrpvpvegsefVMPADAVIMAFGFNPHgMPWLESHGVTVDkwGRIIADvesqyRY- 613
Cdd:COG1251 212 -GDDRVTGVRL---------ADGE-----------ELPADLVVVAIGVRPN-TELARAAGLAVD--RGIVVD-----DYl 262
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1352181648 614 QTTNPKIFAGGDAVRGAD---------LVVTAMAEGRHAAQGI 647
Cdd:COG1251 263 RTSDPDIYAAGDCAEHPGpvygrrvleLVAPAYEQARVAAANL 305
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
332-376 |
7.46e-08 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 49.45 E-value: 7.46e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1352181648 332 IIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGLL-TFGIPSFKLD 376
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAySYRVPGYVFD 46
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
308-421 |
7.47e-08 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 54.63 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 308 SDQALAKGWRPdlshvtkvdKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIgglltfgipSFKLDKSLLARRREIF 387
Cdd:pfam07992 142 SAEALRLKLLP---------KRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRL---------LRAFDEEISAALEKAL 203
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1352181648 388 SAMGIHFELNCEV----GKDVSLDSLLEQ-----YDAVFVGVG 421
Cdd:pfam07992 204 EKNGVEVRLGTSVkeiiGDGDGVEVILKDgteidADLVVVAIG 246
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
56-105 |
1.11e-07 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 53.19 E-value: 1.11e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1352181648 56 CHHCEdaPCARSCPNGAISHVDDS--IQVNQQKCIGCKSCVVACPFGTMQIV 105
Cdd:COG1145 184 CIGCG--LCVKVCPTGAIRLKDGKpqIVVDPDKCIGCGACVKVCPVGAISLE 233
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
64-114 |
1.64e-07 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 48.57 E-value: 1.64e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1352181648 64 CARSCPNGAISHVDD-SIQVNQQKCIGCKSCVVACPFGTmqIVLTPVAAGKV 114
Cdd:COG1149 19 CVEVCPEGAIKLDDGgAPVVDPDLCTGCGACVGVCPTGA--ITLEEREAGKI 68
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
2-118 |
1.96e-07 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 53.01 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 2 NRFIMANSQQCLGCHACEIAC-----VMAHNDEQ-HVLSQHHFHPRITviKHQQQRSAVTCHHCEDApcarsCPNGAISH 75
Cdd:PRK07118 160 NGLPVVDEDKCTGCGACVKACprnviELIPKSARvFVACNSKDKGKAV--KKVCEVGCIGCGKCVKA-----CPAGAITM 232
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1352181648 76 VDDSIQVNQQKCIGCKSCVVACPFGTMQIVLTPVAAGKVKATA 118
Cdd:PRK07118 233 ENNLAVIDQEKCTSCGKCVEKCPTKAIRILNKPPKVKEPKKAA 275
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
69-142 |
2.03e-07 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 48.51 E-value: 2.03e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352181648 69 PNGAISHVDdsIQVNQQKCIGCKSCVVACPFGTMQIVltpvaAGKVKATAHKCDLCAgrengpACVENCPADAL 142
Cdd:COG2221 1 PYGIIGTWP--PKIDEEKCIGCGLCVAVCPTGAISLD-----DGKLVIDEEKCIGCG------ACIRVCPTGAI 61
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
80-147 |
2.34e-07 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 50.09 E-value: 2.34e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352181648 80 IQVNQQKCIGCKSCVVACPFGTMQIVLTPVAAGKVKATAHKCDLCAgrengpACVENCPADALQLVTD 147
Cdd:cd10549 1 LKYDPEKCIGCGICVKACPTDAIELGPNGAIARGPEIDEDKCVFCG------ACVEVCPTGAIELTPE 62
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
80-149 |
3.55e-07 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 48.12 E-value: 3.55e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 80 IQVNQQKCIGCKSCVVACPFGTMQIVltpvaAGKVKATAHKCDLCAgrengpACVENCPADALQLVTDVA 149
Cdd:COG4231 17 YVIDEDKCTGCGACVKVCPADAIEEG-----DGKAVIDPDLCIGCG------SCVQVCPVDAIKLEKRVP 75
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
56-100 |
4.78e-07 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 47.43 E-value: 4.78e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1352181648 56 CHHCEDapCARSCPNGAISHVDD----SIQVNQQKCIGCKSCVVACPFG 100
Cdd:COG1143 4 CIGCGL--CVRVCPVDAITIEDGepgkVYVIDPDKCIGCGLCVEVCPTG 50
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
329-400 |
5.40e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 47.58 E-value: 5.40e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352181648 329 RVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGlltfgipsfKLDKSLLARRREIFSAMGIHFELNCEV 400
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP---------GFDPEIAKILQEKLEKNGIEFLLNTTV 63
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
80-148 |
5.89e-07 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 47.01 E-value: 5.89e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352181648 80 IQVNQQKCIGCKSCVVACPFGtmqiVLTPVAAGKVKATAH--KCDLCAgrengpACVENCPADALQLVTDV 148
Cdd:COG1146 3 PVIDTDKCIGCGACVEVCPVD----VLELDEEGKKALVINpeECIGCG------ACELVCPVGAITVEDDE 63
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
328-364 |
6.01e-07 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 52.16 E-value: 6.01e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1352181648 328 KRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGG 364
Cdd:COG3349 4 PRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
75-155 |
6.68e-07 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 47.03 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 75 HVDDSIQVNQQKCIGCKSCVVACPFGTMQIVltpvaAGKVKATAHKCDLCagrengPACVENCPADALQLVTDVALSGMA 154
Cdd:COG2768 1 HSLGKPYVDEEKCIGCGACVKVCPVGAISIE-----DGKAVIDPEKCIGC------GACIEVCPVGAIKIEWEEDEEFQE 69
|
.
gi 1352181648 155 K 155
Cdd:COG2768 70 K 70
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
328-421 |
9.20e-07 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 51.35 E-value: 9.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 328 KRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGlltfgipsfKLDKSLLARRREIFSAMGIHFELNCEV----GKD 403
Cdd:COG0446 125 KRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLG---------VLDPEMAALLEEELREHGVELRLGETVvaidGDD 195
|
90 100
....*....|....*....|..
gi 1352181648 404 ---VSLDSLLE-QYDAVFVGVG 421
Cdd:COG0446 196 kvaVTLTDGEEiPADLVVVAPG 217
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
56-139 |
9.57e-07 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 48.79 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 56 CHHCEDApCARSCPNGAISHVDDSIQ--------VNQQKCI------GCKSCVVACPFGTMQIVLTPVaAGKVKATAHKC 121
Cdd:cd16373 55 CDLCCDA-CVEVCPTGALRPLDLEEQkvkmgvavIDKDRCLawqggtDCGVCVEACPTEAIAIVLEDD-VLRPVVDEDKC 132
|
90
....*....|....*...
gi 1352181648 122 DLCaGrengpACVENCPA 139
Cdd:cd16373 133 VGC-G-----LCEYVCPV 144
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
332-625 |
1.02e-06 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 51.74 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 332 IIGAGPAGLACADVLTRNGVGVTVYDRHPeIGG-LLTFG-IPS--------------------------FKLD-KSLLAR 382
Cdd:PRK06370 10 VIGAGQAGPPLAARAAGLGMKVALIERGL-LGGtCVNTGcVPTktliasaraahlarraaeygvsvggpVSVDfKAVMAR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 383 RREIF------SAMGIHFELNCEV--------GKD-VSLDSLLEQYDAVFVGVGTyrsmKAGLPneDAPGVyDALPFLIA 447
Cdd:PRK06370 89 KRRIRarsrhgSEQWLRGLEGVDVfrgharfeSPNtVRVGGETLRAKRIFINTGA----RAAIP--PIPGL-DEVGYLTN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 448 NTkqVMGLEELPEepfintaglNVVVLGGGDTAMDCVRTALRHGaSNVTCAyRRDEANMPGSKKEVKNA-----REEGAN 522
Cdd:PRK06370 162 ET--IFSLDELPE---------HLVIIGGGYIGLEFAQMFRRFG-SEVTVI-ERGPRLLPREDEDVAAAvreilEREGID 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 523 FEFNVQPVALELNEQGHVCGIRFlrtrlgepdAQGRRrpvPVEGSEfvmpadaVIMAFGFNPH----GmpwLESHGVTVD 598
Cdd:PRK06370 229 VRLNAECIRVERDGDGIAVGLDC---------NGGAP---EITGSH-------ILVAVGRVPNtddlG---LEAAGVETD 286
|
330 340
....*....|....*....|....*..
gi 1352181648 599 KWGRIIADvesqYRYQTTNPKIFAGGD 625
Cdd:PRK06370 287 ARGYIKVD----DQLRTTNPGIYAAGD 309
|
|
| NapH |
COG0348 |
Polyferredoxin NapH [Energy production and conversion]; |
68-146 |
1.15e-06 |
|
Polyferredoxin NapH [Energy production and conversion];
Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 50.45 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 68 CPNGAISHV--DDS---IQVNQQKCIGCKSCVVACPfgtMQIVltpVAAGKVKATAhkCDLCAgrengpACVENCPADAL 142
Cdd:COG0348 188 CPYGAFQGLlsDLStlrVRYDRGDCIDCGLCVKVCP---MGID---IRKGEINQSE--CINCG------RCIDACPKDAI 253
|
....
gi 1352181648 143 QLVT 146
Cdd:COG0348 254 RFSS 257
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
331-363 |
1.25e-06 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 51.20 E-value: 1.25e-06
10 20 30
....*....|....*....|....*....|...
gi 1352181648 331 AIIGAGPAGLACADVLTRNGVGVTVYDRHPEIG 363
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
82-145 |
1.32e-06 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440759 [Multi-domain] Cd Length: 84 Bit Score: 46.58 E-value: 1.32e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352181648 82 VNQQKCIGCKSCVVACPFGtmqiVLTPVAAGKVKATAHKCDLCAgrengpACVENCPADALQLV 145
Cdd:COG1144 27 VDEDKCIGCGLCWIVCPDG----AIRVDDGKYYGIDYDYCKGCG------ICAEVCPVKAIEMV 80
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
329-396 |
1.64e-06 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 50.47 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 329 RVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIG--------GLLTFGIPS------FKLDKSLLARRREIFSAMGIHF 394
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasgrnaGLIHPGLRYlepselARLALEALDLWEELEEELGIDC 80
|
..
gi 1352181648 395 EL 396
Cdd:pfam01266 81 GF 82
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
327-363 |
1.78e-06 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 50.32 E-value: 1.78e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1352181648 327 DKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIG 363
Cdd:COG0654 3 RTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
81-144 |
2.30e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 50.63 E-value: 2.30e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352181648 81 QVNQQKCIGCKSCVVACPFGTMQIVLTPVAagKVKATAHK-CDLCAGRengpacvenCPADALQL 144
Cdd:COG1148 492 EVDPEKCTGCGRCVEVCPYGAISIDEKGVA--EVNPALCKgCGTCAAA---------CPSGAISL 545
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
327-364 |
2.35e-06 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 50.30 E-value: 2.35e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1352181648 327 DKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGG 364
Cdd:COG1231 7 GKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
328-625 |
2.64e-06 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 50.42 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 328 KRVAIIGAGPAGLACADVLTRN--GVGVTVYDRHpEIGGLLTFGIPSFKLD-----KSLLARRREIFSAMGIHFELNCEV 400
Cdd:PRK09564 1 MKIIIIGGTAAGMSAAAKAKRLnkELEITVYEKT-DIVSFGACGLPYFVGGffddpNTMIARTPEEFIKSGIDVKTEHEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 401 ------GKDVSLDSLLEQ------YDAVFVGVGTyRSMKAGLPNEDAPGVY------DALpfliaNTKQVMGLEELPeep 462
Cdd:PRK09564 80 vkvdakNKTITVKNLKTGsifndtYDKLMIATGA-RPIIPPIKNINLENVYtlksmeDGL-----ALKELLKDEEIK--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 463 fintaglNVVVLGGGDTAMDCVRTALRHGaSNVTcAYRRDEANMPGS-KKEVKNAREEganfEFNVQPVALELNEqghvc 541
Cdd:PRK09564 151 -------NIVIIGAGFIGLEAVEAAKHLG-KNVR-IIQLEDRILPDSfDKEITDVMEE----ELRENGVELHLNE----- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 542 girflrtRLGEPDAQGRRRPVPVEGSEFVmpADAVIMAFGFNPHgMPWLESHGVTVDKWGRIIADvesqyRY-QTTNPKI 620
Cdd:PRK09564 213 -------FVKSLIGEDKVEGVVTDKGEYE--ADVVIVATGVKPN-TEFLEDTGLKTLKNGAIIVD-----EYgETSIENI 277
|
....*
gi 1352181648 621 FAGGD 625
Cdd:PRK09564 278 YAAGD 282
|
|
| SER_beta |
cd10556 |
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ... |
56-138 |
3.64e-06 |
|
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate reductase (SER), a member of the DMSO reductase family. SER catalyzes the reduction of selenate to selenite in bacterial species that can obtain energy by respiring anaerobically with selenate as the terminal electron acceptor. The enzyme comprises three subunits SerABC, forming a heterotrimer, with the catalytic component (alpha-subunit), iron-sulfur protein (beta-subunit) and monomeric b-type heme-containing gamma subunit. Beta subunit contains coordinating one [3Fe-4S] cluster and three [4Fe-4S] clusters and functions as electron carrier.
Pssm-ID: 319878 [Multi-domain] Cd Length: 287 Bit Score: 49.00 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 56 CHHCEDAPCARSCPNGAI--SHVDDSIQVNQQKCIGCKSCVVACPF-GTMQIVLTPVaagkvkatAHKCDLCAGR-ENG- 130
Cdd:cd10556 141 CNHCTYPACLAACPRKAIykREEDGIVLIDQERCRGYRECVEACPYkKPMYNPTTRV--------SEKCIGCYPRiEEGd 212
|
....*....
gi 1352181648 131 -PACVENCP 138
Cdd:cd10556 213 qTQCVSACI 221
|
|
| flavo_MJ0208 |
TIGR02700 |
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of ... |
56-99 |
3.68e-06 |
|
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of archaealflavoprotein. The other, described by TIGR02699 and typified by the partially characterized AF1518 of Archaeoglobus fulgidus, is a homodimeric FMN-containing flavoprotein that accepts electrons from ferredoxin and can transfer them to various oxidoreductases. The function of this protein family is unknown. [Unknown function, General]
Pssm-ID: 131747 [Multi-domain] Cd Length: 234 Bit Score: 48.72 E-value: 3.68e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1352181648 56 CHHCEDapCARSCPNGAISHVDDSIQVNQQKCIGCKSCVVACPF 99
Cdd:TIGR02700 150 CKGCGI--CVDACPRSAIDMVDGKAFIRLLKCVGCGKCKEACPY 191
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
332-649 |
5.55e-06 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 49.38 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 332 IIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGLLTF-G-IPSFKLDKSLLA----RRREIFSAMGihfelnceVGKDVS 405
Cdd:PRK05249 10 VIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHtGtIPSKALREAVLRligfNQNPLYSSYR--------VKLRIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 406 LDSLLE---------------QYD----AVFVGVGTYRSmkaglPN----EDAPGVYDALP---FLIA------------ 447
Cdd:PRK05249 82 FADLLAradhvinkqvevrrgQYErnrvDLIQGRARFVD-----PHtvevECPDGEVETLTadkIVIAtgsrpyrppdvd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 448 -------NTKQVMGLEELPEEpfintaglnVVVLGGGDTAMD--CVRTALRHgasNVTCAYRRDEAnMPGSKKEVKNA-- 516
Cdd:PRK05249 157 fdhpriyDSDSILSLDHLPRS---------LIIYGAGVIGCEyaSIFAALGV---KVTLINTRDRL-LSFLDDEISDAls 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 517 ---REEGANFEFNVQPVALELNEQGHVcgirflrTRLgepdAQGRRrpvpvegsefvMPADAVIMAFG-------FNphg 586
Cdd:PRK05249 224 yhlRDSGVTIRHNEEVEKVEGGDDGVI-------VHL----KSGKK-----------IKADCLLYANGrtgntdgLN--- 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352181648 587 mpwLESHGVTVDKWGRIiaDVESQYryQTTNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIID 649
Cdd:PRK05249 279 ---LENAGLEADSRGQL--KVNENY--QTAVPHIYAVGDVIGFPSLASASMDQGRIAAQHAVG 334
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
86-144 |
7.98e-06 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 43.97 E-value: 7.98e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1352181648 86 KCIGCKSCVVACPFGTMQIVLTPvAAGKVKATAHKCDLCAgrengpACVENCPADALQL 144
Cdd:COG1143 3 KCIGCGLCVRVCPVDAITIEDGE-PGKVYVIDPDKCIGCG------LCVEVCPTGAISM 54
|
|
| PRK05888 |
PRK05888 |
NADH-quinone oxidoreductase subunit NuoI; |
86-147 |
1.14e-05 |
|
NADH-quinone oxidoreductase subunit NuoI;
Pssm-ID: 235637 [Multi-domain] Cd Length: 164 Bit Score: 46.03 E-value: 1.14e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352181648 86 KCIGCKSCVVACPFGTMQIVLTPVAAGKVKATAH-----KCDLCAgrengpACVENCPADALQLVTD 147
Cdd:PRK05888 59 RCIACKLCAAICPADAITIEAAEREDGRRRTTRYdinfgRCIFCG------FCEEACPTDAIVETPD 119
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
56-148 |
1.17e-05 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 48.10 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 56 CHHCEDAPCARSCPNGAISHVDDSIQVNQQKCIGCKSCVVACPFGTMQIVltpvaAGKVKATAHKCDLCaGRengpaCVE 135
Cdd:COG4624 62 CRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVD-----DGKAEIDEEKCISC-GQ-----CVA 130
|
90
....*....|...
gi 1352181648 136 NCPADALQLVTDV 148
Cdd:COG4624 131 VCPFGAITEKSDI 143
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
86-142 |
1.33e-05 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 42.93 E-value: 1.33e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1352181648 86 KCIGCKSCVVACPFGTMQIVLTPVAAgKVKATAHKCDLCAgrengpACVENCPADAL 142
Cdd:pfam13187 1 KCTGCGACVAACPAGAIVPDLVGQTI-RGDIAGLACIGCG------ACVDACPRGAI 50
|
|
| W-FDH |
cd10559 |
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ... |
11-157 |
1.70e-05 |
|
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit of Tungsten-containing formate dehydrogenase (W-FDH), a member of the DMSO reductase family. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.
Pssm-ID: 319881 [Multi-domain] Cd Length: 200 Bit Score: 46.27 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 11 QCLGCHACEIACVMAHN--DEQHVLSQHHFHPR------ITVIKHQQQRSAV----------TCHHCEDAPCARSCP--N 70
Cdd:cd10559 8 RCTACRGCQVACKQWNQlpAEQTKNTGSHQNPPdlsantYKLVRFNEVRNENgkpdwlffpdQCRHCVTPPCKDAADmvP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 71 GAISHVDDSIQV---NQQKCIGCKSCVVACPFGTmqivltPVAAGKVKATAhKCDLCAGR-ENG--PACVENCPADALQL 144
Cdd:cd10559 88 GAVIQDEATGAVvftEKTAELDFDDVLSACPYNI------PRKNEATGRIV-KCDMCIDRvSNGlqPACVKACPTGAMNF 160
|
170
....*....|...
gi 1352181648 145 VTDVALSGMAKSR 157
Cdd:cd10559 161 GDRDEMLAMASKR 173
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
327-447 |
2.29e-05 |
|
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 47.38 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 327 DKRVAIIGAGPAGLACADVLTRNGVGVTVYDrhpeigglltfgipsfklDKSLLARRREIFSAMGIHFELncevGKDvsL 406
Cdd:COG0771 4 GKKVLVLGLGKSGLAAARLLAKLGAEVTVSD------------------DRPAPELAAAELEAPGVEVVL----GEH--P 59
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1352181648 407 DSLLEQYDAVFVgvgtyrsmkaglpnedAPGVYDALPFLIA 447
Cdd:COG0771 60 EELLDGADLVVK----------------SPGIPPDHPLLKA 84
|
|
| NuoI |
TIGR01971 |
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ... |
86-144 |
2.34e-05 |
|
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]
Pssm-ID: 273902 [Multi-domain] Cd Length: 122 Bit Score: 44.33 E-value: 2.34e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352181648 86 KCIGCKSCVVACPFGTMQIVLTPVAAGKVKATAH-----KCDLCAgrengpACVENCPADALQL 144
Cdd:TIGR01971 44 KCIGCTLCAAVCPADAIRVVPAEGEDGKRRLKFYeinfgRCIFCG------LCEEACPTDAIVL 101
|
|
| FixX |
COG2440 |
Ferredoxin-like protein FixX [Energy production and conversion]; |
58-100 |
2.88e-05 |
|
Ferredoxin-like protein FixX [Energy production and conversion];
Pssm-ID: 441981 [Multi-domain] Cd Length: 87 Bit Score: 42.88 E-value: 2.88e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1352181648 58 HCEDAPCARSCPNGAISHVDD-SIQVNQQKCIGCKSCVVACPFG 100
Cdd:COG2440 26 RCLAKPCTRYCPAGVYEIVGDgRLQINYENCLECGTCRIKCPTQ 69
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
325-648 |
2.99e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 47.09 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 325 KVDkrVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGLLTFG-IPSfkldKSLL-----ARRREIFSAMGIHFElnc 398
Cdd:PRK06292 3 KYD--VIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGcIPS----KALIaaaeaFHEAKHAEEFGIHAD--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 399 evGKDVSLDSLLEQYDAV---FVGvGTYRSMKAgLPNEDA------------------------------------PGVY 439
Cdd:PRK06292 74 --GPKIDFKKVMARVRRErdrFVG-GVVEGLEK-KPKIDKikgtarfvdpntvevngerieakniviatgsrvppiPGVW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 440 DAL-PFLIANTkQVMGLEELPEEpfintaglnVVVLGGG----DTAmdcvrTALRHGASNVTCAYRRDEAnMPGSKKEVK 514
Cdd:PRK06292 150 LILgDRLLTSD-DAFELDKLPKS---------LAVIGGGviglELG-----QALSRLGVKVTVFERGDRI-LPLEDPEVS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 515 NAreegANFEFNVQpVALELNEQghVCGIrflrtrlgEPDAQGRRRPVPVEGSEFVMPADAVIMAFGFNPH----GmpwL 590
Cdd:PRK06292 214 KQ----AQKILSKE-FKIKLGAK--VTSV--------EKSGDEKVEELEKGGKTETIEADYVLVATGRRPNtdglG---L 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1352181648 591 ESHGVTVDKWGRIIADvesqYRYQTTNPKIFAGGDAVRGADLVVTAMAEGRHAAQGII 648
Cdd:PRK06292 276 ENTGIELDERGRPVVD----EHTQTSVPGIYAAGDVNGKPPLLHEAADEGRIAAENAA 329
|
|
| PRK08348 |
PRK08348 |
NADH-plastoquinone oxidoreductase subunit; Provisional |
80-151 |
3.08e-05 |
|
NADH-plastoquinone oxidoreductase subunit; Provisional
Pssm-ID: 181399 [Multi-domain] Cd Length: 120 Bit Score: 43.67 E-value: 3.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352181648 80 IQVNQQKCIGCKSCVVACPFGTmqIVLTPvAAGKVKATAHKCDLCAgrengpACVENCPADALQLVTDVALS 151
Cdd:PRK08348 37 ILYDVDKCVGCRMCVTVCPAGV--FVYLP-EIRKVALWTGRCVFCG------QCVDVCPTGALQMSDDFLLA 99
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
80-146 |
3.11e-05 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 45.87 E-value: 3.11e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352181648 80 IQVNQQKCIGCKSCVVACPFGTMQIVLTPVAagkVKATAHKCDLCagrengPACVENCPADALQLVT 146
Cdd:COG1145 177 AVIDAEKCIGCGLCVKVCPTGAIRLKDGKPQ---IVVDPDKCIGC------GACVKVCPVGAISLEP 234
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
328-365 |
3.77e-05 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 46.78 E-value: 3.77e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1352181648 328 KRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGL 365
Cdd:PLN02172 11 QHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGL 48
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
87-141 |
4.09e-05 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 41.36 E-value: 4.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1352181648 87 CIGCKSCVVACPFGTMQIVLTPVAAGKVKATAH--KCDLCAgrengpACVENCPADA 141
Cdd:pfam12838 1 CIGCGACVAACPVGAITLDEVGEKKGTKTVVIDpeRCVGCG------ACVAVCPTGA 51
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
322-358 |
4.86e-05 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 46.26 E-value: 4.86e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1352181648 322 HVTKVDKRVAIIGAGPAGLACADVLTRNGVGVTVYDR 358
Cdd:COG2509 25 GIPSLKYDVVIVGAGPAGLFAALELAEAGLKPLVLER 61
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
55-100 |
5.17e-05 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440759 [Multi-domain] Cd Length: 84 Bit Score: 41.96 E-value: 5.17e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1352181648 55 TCHHCedAPCARSCPNGAISHVDDS-IQVNQQKCIGCKSCVVACPFG 100
Cdd:COG1144 31 KCIGC--GLCWIVCPDGAIRVDDGKyYGIDYDYCKGCGICAEVCPVK 75
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
56-100 |
5.33e-05 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 40.97 E-value: 5.33e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1352181648 56 CHHCEDapCARSCPNGAISHVD-------DSIQVNQQKCIGCKSCVVACPFG 100
Cdd:pfam12838 1 CIGCGA--CVAACPVGAITLDEvgekkgtKTVVIDPERCVGCGACVAVCPTG 50
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
328-363 |
6.28e-05 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 45.65 E-value: 6.28e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1352181648 328 KRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIG 363
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
12-104 |
6.65e-05 |
|
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319886 [Multi-domain] Cd Length: 139 Bit Score: 43.39 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 12 CLGCHACEIACvmahndEQHVLSQHHFHP---RITVIKHQQQRSAVTCHHCEDApcarsCPNGAIShVDDSI------QV 82
Cdd:cd10564 47 CTFCGACAEAC------PEGALDPAREAPwplRAEIGDSCLALQGVECRSCQDA-----CPTQAIR-FRPRLggialpEL 114
|
90 100
....*....|....*....|..
gi 1352181648 83 NQQKCIGCKSCVVACPFGTMQI 104
Cdd:cd10564 115 DADACTGCGACVSVCPVGAITL 136
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
304-421 |
7.53e-05 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 45.85 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 304 ERYI-SDQALakgwrpdlsHVTKVDKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGlltfgipsfKLDKSLLAR 382
Cdd:COG1249 153 VRVLtSDEAL---------ELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLP---------GEDPEISEA 214
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1352181648 383 RREIFSAMGIHFELNCEV--------GKDVSLDS----LLEQYDAVFVGVG 421
Cdd:COG1249 215 LEKALEKEGIDILTGAKVtsvektgdGVTVTLEDgggeEAVEADKVLVATG 265
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
330-361 |
8.80e-05 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 45.32 E-value: 8.80e-05
10 20 30
....*....|....*....|....*....|..
gi 1352181648 330 VAIIGAGPAGLACADVLTRNGVGVTVYDRHPE 361
Cdd:PRK09126 6 IVVVGAGPAGLSFARSLAGSGLKVTLIERQPL 37
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
470-538 |
9.68e-05 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 41.04 E-value: 9.68e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352181648 470 NVVVLGGGDTAMDCVRTALRHGaSNVTCAYRRDEAnMPGSKKEV-----KNAREEGANFEFNVQPVALELNEQG 538
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLG-SKVTVVERRDRL-LPGFDPEIakilqEKLEKNGIEFLLNTTVEAIEGNGDG 72
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
328-363 |
1.10e-04 |
|
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;
Pssm-ID: 234978 [Multi-domain] Cd Length: 662 Bit Score: 45.22 E-value: 1.10e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1352181648 328 KRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIG 363
Cdd:PRK01747 261 RDAAIIGGGIAGAALALALARRGWQVTLYEADEAPA 296
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
64-113 |
1.48e-04 |
|
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.
Pssm-ID: 349764 [Multi-domain] Cd Length: 246 Bit Score: 43.91 E-value: 1.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1352181648 64 CARSCPNGAISHVDDSIQVNQQKCIGCKSCVVACPFGTmqIVLTPVAAGK 113
Cdd:cd03110 72 CERVCKFGAILEFFQKLIVDESLCEGCGACVIICPRGA--IYLKDRDTGK 119
|
|
| PTZ00188 |
PTZ00188 |
adrenodoxin reductase; Provisional |
329-434 |
1.56e-04 |
|
adrenodoxin reductase; Provisional
Pssm-ID: 240308 Cd Length: 506 Bit Score: 44.87 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 329 RVAIIGAGPAGLACADVLTRN-GVGVTVYDRHPEIGGLLTFGI-PSFKLDKSLLARRREIFSAMGIHFELNCEVGKDVSL 406
Cdd:PTZ00188 41 KVGIIGAGPSALYCCKHLLKHeRVKVDIFEKLPNPYGLIRYGVaPDHIHVKNTYKTFDPVFLSPNYRFFGNVHVGVDLKM 120
|
90 100
....*....|....*....|....*....
gi 1352181648 407 DSLLEQYDAVFVGVGTYR-SMKAGLPNED 434
Cdd:PTZ00188 121 EELRNHYNCVIFCCGASEvSIPIGQQDED 149
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
330-361 |
2.22e-04 |
|
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
Pssm-ID: 396193 [Multi-domain] Cd Length: 348 Bit Score: 43.85 E-value: 2.22e-04
10 20 30
....*....|....*....|....*....|..
gi 1352181648 330 VAIIGAGPAGLACADVLTRNGVGVTVYDRHPE 361
Cdd:pfam01494 4 VLIVGGGPAGLMLALLLARAGVRVVLVERHAT 35
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
306-365 |
2.31e-04 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 44.01 E-value: 2.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 306 YISDQALAkgwrpdlshVTKVDKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGL 365
Cdd:PRK06292 157 LTSDDAFE---------LDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPL 207
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
328-364 |
2.93e-04 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 44.09 E-value: 2.93e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1352181648 328 KRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGG 364
Cdd:PLN02976 694 KKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGG 730
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
326-396 |
2.97e-04 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 43.74 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 326 VDKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHpEIG--------GLLTFGIPSFKLDKSL-LARR-----REIFSAMG 391
Cdd:COG0665 1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLERG-RPGsgasgrnaGQLRPGLAALADRALVrLAREaldlwRELAAELG 79
|
....*
gi 1352181648 392 IHFEL 396
Cdd:COG0665 80 IDCDF 84
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
324-363 |
3.20e-04 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 43.79 E-value: 3.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1352181648 324 TKVDKRVAIIGAGPAGLACADVLTRNGVG---VTVYDRHPEIG 363
Cdd:COG4529 2 TGARKRIAIIGGGASGTALAIHLLRRAPEplrITLFEPRPELG 44
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
64-104 |
4.55e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 43.31 E-value: 4.55e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1352181648 64 CARSCPNGAISHVDDS-IQVNQQKCIGCKSCVVACPFGTMQI 104
Cdd:COG1148 504 CVEVCPYGAISIDEKGvAEVNPALCKGCGTCAAACPSGAISL 545
|
|
| napG |
PRK09476 |
quinol dehydrogenase periplasmic component; Provisional |
86-157 |
5.51e-04 |
|
quinol dehydrogenase periplasmic component; Provisional
Pssm-ID: 236534 [Multi-domain] Cd Length: 254 Bit Score: 42.30 E-value: 5.51e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352181648 86 KCIGCKSCVVACPFGTMQIV--LTPVAAGKVKATAHK--CDLCagrENGPaCVENCPADALqlvtDVALSGMAKSR 157
Cdd:PRK09476 60 ACIRCGLCVQACPYDTLKLAtlASGLSAGTPYFVARDipCEMC---EDIP-CVKACPSGAL----DRELVDIDDAR 127
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
192-241 |
5.69e-04 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 42.94 E-value: 5.69e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1352181648 192 ARGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCG---EHSVCEWTCP 241
Cdd:PRK12771 471 PRAQRPELDADERVGDFDEVLGGLTEEEARQEAARCLSCGncfECDNCYGACP 523
|
|
| napG |
PRK09476 |
quinol dehydrogenase periplasmic component; Provisional |
56-99 |
6.48e-04 |
|
quinol dehydrogenase periplasmic component; Provisional
Pssm-ID: 236534 [Multi-domain] Cd Length: 254 Bit Score: 41.92 E-value: 6.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1352181648 56 CHHCEDAPCARSCPNGAISH----VDDS-----IQVNQQKCIG-----CKSCVVACPF 99
Cdd:PRK09476 99 CEMCEDIPCVKACPSGALDRelvdIDDArmglaVLVDQENCLNfqglrCDVCYRVCPL 156
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
329-362 |
6.96e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 42.37 E-value: 6.96e-04
10 20 30
....*....|....*....|....*....|....
gi 1352181648 329 RVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEI 362
Cdd:PRK06753 2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESV 35
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
455-641 |
7.07e-04 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 42.45 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 455 LEELPEEpfintaglnVVVLGGGDTAMD--CVRTALrhgASNVTCAYRRDEAnMPGSKKEVKNA-----REEGANFEFNV 527
Cdd:PRK06116 163 LEELPKR---------VAVVGAGYIAVEfaGVLNGL---GSETHLFVRGDAP-LRGFDPDIRETlveemEKKGIRLHTNA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 528 QPVALELNEQGHvcgirfLRTRLgepdAQGRrrpvpvegsefVMPADAVIMAFGFNP--HGMPwLESHGVTVDKWGRIIA 605
Cdd:PRK06116 230 VPKAVEKNADGS------LTLTL----EDGE-----------TLTVDCLIWAIGREPntDGLG-LENAGVKLNEKGYIIV 287
|
170 180 190
....*....|....*....|....*....|....*..
gi 1352181648 606 DvesqyRYQTTN-PKIFAGGDAVRGADLVVTAMAEGR 641
Cdd:PRK06116 288 D-----EYQNTNvPGIYAVGDVTGRVELTPVAIAAGR 319
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
55-98 |
7.30e-04 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 38.00 E-value: 7.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1352181648 55 TCHHCedAPCARSCPNGAISHV-------DDSIQVNQQKCIGCKSCVVACP 98
Cdd:pfam13237 8 KCIGC--GRCTAACPAGLTRVGaiverleGEAVRIGVWKCIGCGACVEACP 56
|
|
| crtI_fam |
TIGR02734 |
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ... |
330-391 |
1.15e-03 |
|
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two symmetrical pairs of) sites. This is achieved by two enzymes (crtP and crtQ) in cyanobacteria (Gloeobacter being an exception) and plants, but by a single enzyme in most other bacteria and in fungi. This single enzyme is called the bacterial-type phytoene desaturase, or CrtI. Most members of this family, part of the larger pfam01593, which also contains amino oxidases, are CrtI itself; it is likely that all members act on either phytoene or on related compounds such as dehydrosqualene, for carotenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 274273 [Multi-domain] Cd Length: 495 Bit Score: 41.88 E-value: 1.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352181648 330 VAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGL--------LTF--GiPSFKLDKSLLarrREIFSAMG 391
Cdd:TIGR02734 1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRagvleddgFRFdtG-PTVITMPEAL---EELFALAG 68
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
311-366 |
1.58e-03 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 41.38 E-value: 1.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1352181648 311 ALAKGWRPDLSHVTKVDKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGLL 366
Cdd:COG1148 124 AKAKLLEPLEPIKVPVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRA 179
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
297-361 |
1.63e-03 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 40.82 E-value: 1.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352181648 297 AVTIGNIERYISDQALAKGWRPDLSHVTKVDKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPE 361
Cdd:COG0569 65 TLITFGDAVLFGGLLEALRRRRMERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPE 129
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
330-362 |
1.75e-03 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 41.43 E-value: 1.75e-03
10 20 30
....*....|....*....|....*....|...
gi 1352181648 330 VAIIGAGPAGLACADVLTRNGVGVTVYDRHPEI 362
Cdd:PRK06183 13 VVIVGAGPVGLTLANLLGQYGVRVLVLERWPTL 45
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
328-364 |
1.92e-03 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 41.25 E-value: 1.92e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1352181648 328 KRVAIIGAGPAGLACADVLTRNgVGVTVYDRHPEIGG 364
Cdd:COG2907 4 MRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
10-144 |
2.00e-03 |
|
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319886 [Multi-domain] Cd Length: 139 Bit Score: 39.15 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 10 QQCLGCHACEIACvmahndEQHVLsqhhfhpritvIKHQQQRSAVT-----CHHCEDapCARSCPNGAISHVDDS----- 79
Cdd:cd10564 13 DLCTRCGDCVEAC------PEGII-----------VRGDGGFPELDfsrgeCTFCGA--CAEACPEGALDPAREApwplr 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352181648 80 IQVnQQKC-----IGCKSCVVACPfgTMQIVLTPVAAGKVKAT--AHKCDLCAgrengpACVENCPADALQL 144
Cdd:cd10564 74 AEI-GDSClalqgVECRSCQDACP--TQAIRFRPRLGGIALPEldADACTGCG------ACVSVCPVGAITL 136
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
80-138 |
2.09e-03 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 36.84 E-value: 2.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352181648 80 IQVNQQKCIGCKSCVVACPFGTMQIVLTP--VAAGKVKATAHKCDLCAgrengpACVENCP 138
Cdd:pfam13237 2 VVIDPDKCIGCGRCTAACPAGLTRVGAIVerLEGEAVRIGVWKCIGCG------ACVEACP 56
|
|
| PRK05888 |
PRK05888 |
NADH-quinone oxidoreductase subunit NuoI; |
64-109 |
2.17e-03 |
|
NADH-quinone oxidoreductase subunit NuoI;
Pssm-ID: 235637 [Multi-domain] Cd Length: 164 Bit Score: 39.48 E-value: 2.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1352181648 64 CARSCPNGAIS-----HVD-----DSIQVNQQKCIGCKSCVVACPfgTMQIVLTPV 109
Cdd:PRK05888 66 CAAICPADAITieaaeREDgrrrtTRYDINFGRCIFCGFCEEACP--TDAIVETPD 119
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
330-369 |
2.26e-03 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 41.06 E-value: 2.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1352181648 330 VAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGLLTFG 369
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGMLTSG 41
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
331-363 |
2.46e-03 |
|
flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 272992 [Multi-domain] Cd Length: 400 Bit Score: 40.66 E-value: 2.46e-03
10 20 30
....*....|....*....|....*....|...
gi 1352181648 331 AIIGAGPAGLACADVLTRNGVGVTVYDRHPEIG 363
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIG 33
|
|
| PRK10194 |
PRK10194 |
ferredoxin-type protein NapF; |
11-98 |
2.55e-03 |
|
ferredoxin-type protein NapF;
Pssm-ID: 182296 [Multi-domain] Cd Length: 163 Bit Score: 39.24 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 11 QCLGCHACEIACvmahndeqhvlSQHHFHPR--------ITVIKHQQQRSAVTCHHCEDapcarSCPNGAISHVDD---- 78
Cdd:PRK10194 67 ECSFCYACAQAC-----------PESLFSPRhtrawdlqFTIGDACLAYQSVECRRCQD-----SCEPMAIIFRPTlsgi 130
|
90 100
....*....|....*....|.
gi 1352181648 79 -SIQVNQQKCIGCKSCVVACP 98
Cdd:PRK10194 131 yQPQLNSQLCNGCGACAASCP 151
|
|
| Fer4 |
pfam00037 |
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ... |
80-100 |
2.79e-03 |
|
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 459642 [Multi-domain] Cd Length: 24 Bit Score: 35.69 E-value: 2.79e-03
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
64-98 |
2.89e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 40.75 E-value: 2.89e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1352181648 64 CARSCPNGAISHVD--DSIQVNQQKCIGCKSCVVACP 98
Cdd:PRK13795 589 CVGACPTGAIRIEEgkRKISVDEEKCIHCGKCTEVCP 625
|
|
| PRK08243 |
PRK08243 |
4-hydroxybenzoate 3-monooxygenase; Validated |
329-358 |
2.97e-03 |
|
4-hydroxybenzoate 3-monooxygenase; Validated
Pssm-ID: 236198 [Multi-domain] Cd Length: 392 Bit Score: 40.55 E-value: 2.97e-03
10 20 30
....*....|....*....|....*....|
gi 1352181648 329 RVAIIGAGPAGLACADVLTRNGVGVTVYDR 358
Cdd:PRK08243 4 QVAIIGAGPAGLLLGQLLHLAGIDSVVLER 33
|
|
| Ala_dh_like |
cd01620 |
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ... |
312-380 |
3.01e-03 |
|
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.
Pssm-ID: 240621 [Multi-domain] Cd Length: 317 Bit Score: 40.08 E-value: 3.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352181648 312 LAKGWRPDLSHVTKVDK-RVAIIGAGPAGLACADVLTRNGVGVTVYDRHPE-IGGLLT-FGIPSFKLDKSLL 380
Cdd:cd01620 146 LARIQGGRMGGAGGVPPaKVLIIGAGVVGLGAAKIAKKLGANVLVYDIKEEkLKGVETlGGSRLRYSQKEEL 217
|
|
| PRK07688 |
PRK07688 |
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated |
327-358 |
3.22e-03 |
|
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
Pssm-ID: 181084 [Multi-domain] Cd Length: 339 Bit Score: 40.36 E-value: 3.22e-03
10 20 30
....*....|....*....|....*....|...
gi 1352181648 327 DKRVAIIGAGPAGLACADVLTRNGVG-VTVYDR 358
Cdd:PRK07688 24 EKHVLIIGAGALGTANAEMLVRAGVGkVTIVDR 56
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
310-364 |
3.33e-03 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 39.76 E-value: 3.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1352181648 310 QALAKGWRPDLSHVTKVDkrVAIIGAGPAGLACADVLTRN-GVGVTVYDRHPEIGG 364
Cdd:pfam01946 2 RAMTRRYFEDLDDYAESD--VVIVGAGSSGLTAAYYLAKNrGLKVAIIERSVSPGG 55
|
|
| Fer4_6 |
pfam12837 |
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ... |
80-100 |
3.47e-03 |
|
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 432822 [Multi-domain] Cd Length: 24 Bit Score: 35.28 E-value: 3.47e-03
|
| PLN02576 |
PLN02576 |
protoporphyrinogen oxidase |
321-367 |
3.55e-03 |
|
protoporphyrinogen oxidase
Pssm-ID: 215314 [Multi-domain] Cd Length: 496 Bit Score: 40.38 E-value: 3.55e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1352181648 321 SHVTKVDKRVAIIGAGPAGLACADVL-TRNGVGVTVYDRHPEIGGLLT 367
Cdd:PLN02576 6 GSAAASSKDVAVVGAGVSGLAAAYALaSKHGVNVLVTEARDRVGGNIT 53
|
|
| PRK12387 |
PRK12387 |
formate hydrogenlyase complex iron-sulfur subunit; Provisional |
83-163 |
4.11e-03 |
|
formate hydrogenlyase complex iron-sulfur subunit; Provisional
Pssm-ID: 183492 [Multi-domain] Cd Length: 180 Bit Score: 38.86 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 83 NQQKCIGCKSCVVACPFG--TMQivlTPVAAGKVK--ATAHKCDLCaGRengpaCVENCPADALQLVTDVALSGMAKSRR 158
Cdd:PRK12387 36 NPQQCIGCAACVNACPSNalTVE---TDLATGELAweFNLGRCIFC-GR-----CEEVCPTAAIKLSQEFELAVWKKEDL 106
|
....*
gi 1352181648 159 LRTAR 163
Cdd:PRK12387 107 LQQSE 111
|
|
| ferrodoxin_EFR1 |
NF038196 |
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ... |
75-143 |
4.24e-03 |
|
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).
Pssm-ID: 468407 [Multi-domain] Cd Length: 243 Bit Score: 39.46 E-value: 4.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352181648 75 HVDDsiqvnqqKCIGCKSCVVACPFGTmqIVLTpvaAGKVKAtAHKCDLCAgrengpACVENCPADALQ 143
Cdd:NF038196 182 HVTD-------KCIGCGICAKVCPVNN--IEME---DGKPVW-GHNCTHCL------ACIHRCPKEAIE 231
|
|
| ETF_QO |
pfam05187 |
Electron transfer flavoprotein-ubiquinone oxidoreductase, 4Fe-4S; Electron-transfer ... |
61-93 |
4.59e-03 |
|
Electron transfer flavoprotein-ubiquinone oxidoreductase, 4Fe-4S; Electron-transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO) in the inner mitochondrial membrane accepts electrons from electron-transfer flavoprotein which is located in the mitochondrial matrix and reduces ubiquinone in the mitochondrial membrane. The two redox centres in the protein, FAD and a [4Fe4S] cluster, are present in a 64-kDa monomer.
Pssm-ID: 461576 [Multi-domain] Cd Length: 104 Bit Score: 37.21 E-value: 4.59e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1352181648 61 DAPCARSCPNGAISHVDDS------IQVNQQKCIGCKSC 93
Cdd:pfam05187 43 AGPEQRYCPAGVYEYVEDEepggprLQINAQNCVHCKTC 81
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
87-149 |
4.59e-03 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 39.53 E-value: 4.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352181648 87 CIGCKSCVVACPFGTMQIVltpvaAGKVKATAHKCDLCAgrengpACVENCPADALQLVTDVA 149
Cdd:PRK07118 141 CLGLGSCVAACPFDAIHIE-----NGLPVVDEDKCTGCG------ACVKACPRNVIELIPKSA 192
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
562-644 |
4.66e-03 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 40.13 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 562 VPVEGSEFVMP-------ADAVIMAFGFNPHGMPW-LESHGVTVDKWGRIIADvesqYRYQTTNPKIFAGGDAVRGADLV 633
Cdd:PRK13748 336 VAHVDGEFVLTtghgelrADKLLVATGRAPNTRSLaLDAAGVTVNAQGAIVID----QGMRTSVPHIYAAGDCTDQPQFV 411
|
90
....*....|.
gi 1352181648 634 VTAMAEGRHAA 644
Cdd:PRK13748 412 YVAAAAGTRAA 422
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
328-383 |
4.78e-03 |
|
protoporphyrinogen oxidase; Reviewed
Pssm-ID: 237009 [Multi-domain] Cd Length: 451 Bit Score: 39.83 E-value: 4.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352181648 328 KRVAIIGAGPAGLACADVLTRNG--VGVTVYDRHPEIGGLL-TFGIPSFKLD---KSLLARR 383
Cdd:PRK11883 1 KKVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKIqTVRKDGFPIElgpESFLARK 62
|
|
| PRK12409 |
PRK12409 |
D-amino acid dehydrogenase small subunit; Provisional |
328-359 |
5.41e-03 |
|
D-amino acid dehydrogenase small subunit; Provisional
Pssm-ID: 237093 [Multi-domain] Cd Length: 410 Bit Score: 39.62 E-value: 5.41e-03
10 20 30
....*....|....*....|....*....|..
gi 1352181648 328 KRVAIIGAGPAGLACADVLTRNGVGVTVYDRH 359
Cdd:PRK12409 2 SHIAVIGAGITGVTTAYALAQRGYQVTVFDRH 33
|
|
| PRK06126 |
PRK06126 |
hypothetical protein; Provisional |
326-361 |
5.95e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235704 [Multi-domain] Cd Length: 545 Bit Score: 39.59 E-value: 5.95e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1352181648 326 VDKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPE 361
Cdd:PRK06126 6 SETPVLIVGGGPVGLALALDLGRRGVDSILVERKDG 41
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
85-147 |
6.86e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 37.62 E-value: 6.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352181648 85 QKCIGCKSCVVACPFGTMQ---------IVLTPVAAGKVKAtahkCDLCagrenGPACVENCPADALQLVTD 147
Cdd:cd16373 14 ALCIRCGLCVEACPTGVIQpagledgleGGRTPYLDPREGP----CDLC-----CDACVEVCPTGALRPLDL 76
|
|
| PRK00783 |
PRK00783 |
DNA-directed RNA polymerase subunit D; Provisional |
32-98 |
7.70e-03 |
|
DNA-directed RNA polymerase subunit D; Provisional
Pssm-ID: 234837 [Multi-domain] Cd Length: 263 Bit Score: 38.71 E-value: 7.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352181648 32 VLSQHHFHPRITVIKHqqqrsavtCHHCEDapCARSCPNGAISHVDDSIQV-NQQKCIGCKSCVVACP 98
Cdd:PRK00783 155 SACGYKYYPRIEVSED--------CDECEK--CVEACPRGVLELKEGKLVVtDLLNCSLCKLCERACP 212
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
323-441 |
9.12e-03 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 39.03 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 323 VTKVDKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIgglltfgIPSFKLDKSllARRREIFSAMGIHFELNCEV-- 400
Cdd:PRK06370 167 LDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRL-------LPREDEDVA--AAVREILEREGIDVRLNAECir 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1352181648 401 ------GKDVSLDSLLEQY----DAVFVGVGtyRSmkaglPNED-----APGV-YDA 441
Cdd:PRK06370 238 verdgdGIAVGLDCNGGAPeitgSHILVAVG--RV-----PNTDdlgleAAGVeTDA 287
|
|
| E1_enzyme_family |
cd01483 |
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ... |
329-422 |
9.62e-03 |
|
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS.
Pssm-ID: 238760 [Multi-domain] Cd Length: 143 Bit Score: 37.25 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352181648 329 RVAIIGAGPAGLACADVLTRNGVG-VTVYD----------RHPeIGGLLTFGIPsfkldKSLLARRR--EIFSAMGIHFE 395
Cdd:cd01483 1 RVLLVGLGGLGSEIALNLARSGVGkITLIDfdtvelsnlnRQF-LARQADIGKP-----KAEVAARRlnELNPGVNVTAV 74
|
90 100
....*....|....*....|....*..
gi 1352181648 396 lNCEVGKDvSLDSLLEQYDAVFVGVGT 422
Cdd:cd01483 75 -PEGISED-NLDDFLDGVDLVIDAIDN 99
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
56-105 |
9.80e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 39.00 E-value: 9.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1352181648 56 CHHcedaPCARSCP---NGA----ISHVDDSIQVNQQKCIGCKSCVVACPFGTMQIV 105
Cdd:COG1245 17 CNY----ECIKYCPvnrTGKeaieIDEDDGKPVISEELCIGCGICVKKCPFDAISIV 69
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