|
Name |
Accession |
Description |
Interval |
E-value |
| formate-DH-alph |
TIGR01553 |
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase ... |
1-803 |
0e+00 |
|
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase alpha chains found mainly in proteobacteria but also in Aquifex. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits of 32 and 20 kDa. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The electrons are utilized mainly in the nitrate respiration by nitrate reductase. In E. coli and Salmonella, there are two forms of the formate dehydrogenase, one induced by nitrate which is strictly anaerobic (fdn), and one incuced during the transition from aerobic to anaerobic growth (fdo). This subunit is one of only three proteins in E. coli which contain selenocysteine. This model is well-defined, with a large, unpopulated trusted/noise gap. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]
Pssm-ID: 273689 [Multi-domain] Cd Length: 1009 Bit Score: 1165.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 1 MTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLL 80
Cdd:TIGR01553 212 MTNNWVDIKNSDLILVMGGNPAENHPIGFKWAIRAK-KKGAKIIHIDPRFNRTATVADLYAPIRSGSDIAFLNGMIKYIL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 81 NNEKFNREYTEAYTNASLIVREDYGFEDGLFTGYDAEKRKYDKSSWTYELDENGFAKRDTTLQHPRCVWNLLKQHVSRYT 160
Cdd:TIGR01553 291 EKELYQKEYVVNYTNASFIVGEGFAFEDGLFAGYNKETRKYDKSKWGYEFDENGNPKRDETLKHPRCVFNILKEHYSRYT 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 161 PDVVENICGTPKDAFLKVCEYIAETSAHDKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQ 240
Cdd:TIGR01553 371 PEKVSAICGTPKELFLKVYEEYCKTGKPNKAMTILYALGWTQHSVGTQNIRAMSINQLLLGNIGVPGGGINALRGHSNVQ 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 241 GLTDLGLLSQSLPGYMTLPSEKQTDLQTYLTANTPKPLLEGQVNYWGNYPKFFVSMMKAFFGDKATAENSWGFDWLPKWD 320
Cdd:TIGR01553 451 GSTDHGLLMHILPGYLGTPRASIPTYEQYTKKFTPVSKDPQSANYWSNFPKFFASYIKSMWGDAATNENGWAYDYLPKGE 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 321 KGYD-VLQYFEMMKEGKVNGYICQGFNPVASFPNKNKVIGCLSKLKFLVTIDPLNTETSNFWQNHGelneVDSSKIQTEV 399
Cdd:TIGR01553 531 DGYDsWLTLFDDMFQGKIKGFFAWGQNPLNSGPNSNKTREALTKLKWMVVMDPFDNETGSFWRGPG----MDPKEIKTEV 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 400 FRLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIALTDGEILSGIFLRLRKMYAEQGGANPDQVLNMTWNYAIPHEPSSE 479
Cdd:TIGR01553 607 FFLPTAVFIEKEGSISNSGRWMQWRYKGPDPPGNAIPDGDIIVELAKRVQELYAKEGGKLAEPVTKLKWDYWVPDHPDAH 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 480 EVAMESNGKALADITDPatgAVIVKKGQQLSSFAQLRDDGTTSCGCWIFAGSWTPEGNQMARRDNADPSGLGNTLGWAWA 559
Cdd:TIGR01553 687 EIAKEINGYALKDFKVG---DVEYKKGQQIATFGHLRDDGSTTSGCWLYTGSYTEKGNMAARRDKSDPAGLGLYPGWTWA 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 560 WPLNRRILYNRASADPQGNPWDPKRQLLKWDGTKWTgW--DIPDYSA-APPGSGVGPFIMQQEGMGRLFALDKMAEGPFP 636
Cdd:TIGR01553 764 WPANRRVLYNRASVDLNGKPWDPERALVEWNAAEKK-WvgDIPDYPPtAPPEKGKGAFIMKPEGYGRLFAPGKREDGPLP 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 637 EHYEPFETPLGTNPLHPNVISNPAARIFKDDAEALGKADKFPYVGTTYRLTEHFHYWTKHALLNAILQPEQFVEIGESLA 716
Cdd:TIGR01553 843 EHYEPMESPVITNPFHPNVLHNPTALHYKTDEKAVGDPKRYPFVATTYRLTEHWHTWTRNTPWLLEAEPQMFCEISEELA 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 717 NKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTLKANGKDIDTIGIPIHWGYEGVAKKGFIANTLTPFVGDANTQTPEFKS 796
Cdd:TIGR01553 923 TEKGIQNGDKVILESVRGKIWAKAIVTKRIKPLAIQGQQVHMIGIPIHWGWSFLKNGGDATNILTPSVGDPNTGTPETKA 1002
|
....*..
gi 535687910 797 FLVNVEK 803
Cdd:TIGR01553 1003 FLVNIEK 1009
|
|
| formate_DH_Act |
NF041513 |
formate dehydrogenase; Members of this family are the enzyme formate dehydrogenase, of a type ... |
7-801 |
0e+00 |
|
formate dehydrogenase; Members of this family are the enzyme formate dehydrogenase, of a type found in the Actinomycetota, as in the genera Streptomyces, Nocardiopsis, Gordonia, and Saccharomonospora. Many are selenoproteins.
Pssm-ID: 469399 [Multi-domain] Cd Length: 1066 Bit Score: 775.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 7 DIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLLNNEKFN 86
Cdd:NF041513 209 DLANSDCIVIQGSNMAEAHPVGFQWVMEAK-ARGATVIHVDPRFTRTSALADLHVPIRAGSDIAFLGGLINHVLSNELYF 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 87 REYTEAYTNASLIVREDY-GFED--GLFTGYDAEKRKYDKSSWTYELDEN------------------------------ 133
Cdd:NF041513 288 REYVLAYTNAATIVSEDFrDTEDldGLFSGFDPETGSYDPASWQYEGVEVaaaagqrdqlydsrggahesargeehgsgg 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 134 ----GFAKRDTTLQHPRCVWNLLKQHVSRYTPDVVENICGTPKDAFLKVCEYIAETSAHDKTASFLYALGWTQHSIGAQN 209
Cdd:NF041513 368 apvaGAPRRDETLQDPRCVFQILKRHFARYTPEMVEEICGIPRELFLKVADALTANSGRERTTAFCYAVGWTQHTVGVQY 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 210 IRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLLSQSLPGYMTLP-SEKQTDLQTYLTANTPkpllegQVNYWGN 288
Cdd:NF041513 448 IRAASILQLLLGNIGRPGGGIMALRGHASIQGSTDIPTLFNLLPGYLPMPhAHKHEDLDSYVEANAS------QKGFWAN 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 289 YPKFFVSMMKAFFGDKATAENSWGFDWLPKWDKGYDVLQYFEMMKEGKVNGYICQGFNP-VASFPNKNKVIGcLSKLKFL 367
Cdd:NF041513 522 MRAYTVSLLKAWWGDAATAENDFCFDYLPRLTGDHSTYQTVMAMLDGKVKGYFLMGENPaVGSANGRLQRLG-MANLDWL 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 368 VTIDPLNTETSNFWQNHGELN--EVDSSKIQTEVFRLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIALTDGEILSGIF 445
Cdd:NF041513 601 VVRDFSLIESATFWKDGPEIEtgELRTEDIGTEVFFFPAAAHTEKSGTFTNTQRLLQWRHQAVEPPGDARSDLWFFYHLG 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 446 LRLRKMYAEQGGANPDQVLNMTWNYAI--PH-EPSSEEVAMESNGKALAditdpatgavivkkGQQLSSFAQLRDDGTTS 522
Cdd:NF041513 681 RRIREKLAGSTDPRDRPLLDLTWDYPTegPHgEPDAEAVLAEINGYDLS--------------GRPLSAYTELKDDGSTS 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 523 CGCWIFAGSWTPEGNQMARRDnadPSGLGNTLG--WAWAWPLNRRILYNRASADPQGNPWDPKRQLLKWDGTK--WTGWD 598
Cdd:NF041513 747 CGCWIYCGVYADGVNQAARRK---PGREQDWVAaeWGWAWPANRRILYNRASADPEGRPWSERKKYVWWDAEAgrWTGYD 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 599 IPDYSAA-------PPG-------SGVGPFIMQQEGMGRLFALDKMAEGPFPEHYEPFETPLGtNPLHPNViSNPAARIF 664
Cdd:NF041513 824 VPDFPVDkppdyrpPPGatgpaalSGDDPFIMQADGKGWLFAPAGLVDGPLPTHYEPQESPVR-NPLYGQQ-RNPARKVY 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 665 KDDAEALGK------ADKFPYVGTTYRLTEHF-----HYWTKHAllnAILQPEQFVEIGESLANKLGIAQGDTVKVSSNR 733
Cdd:NF041513 902 PREDNRYHPsggepgAEVYPYVFTTYRLTEHHtaggmSRWLPYL---AELQPEMFCEVSPELAAERGLENGGWATIVTAR 978
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 535687910 734 GYIKAKAVVTKRIRTLKANGKDIDTIGIPIHWGYEGVAkKGFIANTLTPFVGDANTQTPEFKSFLVNV 801
Cdd:NF041513 979 GAIEARVLVTDRMTPLRVQGRTVHQIGLPYHWGPNGLV-TGDAANELLGITLDPNVHIQESKALTCDI 1045
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
1-662 |
0e+00 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. Members of the MopB_Formate-Dh-Na-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239153 [Multi-domain] Cd Length: 649 Bit Score: 703.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 1 MTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKIHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLL 80
Cdd:cd02752 160 MTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEKNGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGGMINYII 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 81 nnekfnreyteaytnaslivredygfedglftgydaekrkydksswtyeldengfakrdttlqhprcvwnllkqhvsRYT 160
Cdd:cd02752 240 -----------------------------------------------------------------------------RYT 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 161 PDVVENICGTPKDAFLKVCEYIAETSAHDKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQ 240
Cdd:cd02752 243 PEEVEDICGVPKEDFLKVAEMFAATGRPDKPGTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALRGHSNVQ 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 241 GLTDLGLLSQSLPGYMTlpsekqtdlqtyltantpkpllegqvnywgnypkffvsmmkaffgdkataenswgfdwlpkwd 320
Cdd:cd02752 323 GATDLGLLSHNLPGYLG--------------------------------------------------------------- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 321 kgydvlqyfemmkegkvngyicqGFNPVASFPNKNKVIGCLSKLKFLVTIDPLNTETSNFWQNHGelneVDSSKIQTEVF 400
Cdd:cd02752 340 -----------------------GQNPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKNPG----MDPKSIQTEVF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 401 RLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIALTDGEILSGIFLRLRKMYAEQGGANPDQVLNmtWNYAIPHEPSSEE 480
Cdd:cd02752 393 LLPAACQYEKEGSITNSGRWLQWRYKVVEPPGEAKSDGDILVELAKRLGFLYEKEGGAFPEPITK--WNYGYGDEPTPEE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 481 VAMESNGKALADITDPATGAVIVKKGQQLSSFAQLRDDGTTSCGCWIFAGSWTPEGNqMARRDNADPSGLGNTLGWAWAW 560
Cdd:cd02752 471 IAREINGGALTDGYTGQSPERLKAHGQNVHTFDTLRDDGSTACGCWIYSGSYTEEGR-MARRDTSDPDGLGLYPGWPWPW 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 561 PLNRRILYNRASADPQGNPWDPKRQLLKWDGTK-WTGWDIPDYSA-APPGSGVGPFIMQQEGMGRLFALDKmaEGPFPEH 638
Cdd:cd02752 550 PVNRRILYNRASVDMEGKPGYPERPLVEWDGLGwWWKGDVPDGPWpAAKEHGCGPFIMAPEGQARLFVWNF--DGPFPEH 627
|
650 660
....*....|....*....|....
gi 535687910 639 YEPFETPLGTNplHPNVISNPAAR 662
Cdd:cd02752 628 YEPLESPRPDL--HSKVAKNPTYK 649
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
1-804 |
1.78e-98 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 320.68 E-value: 1.78e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 1 MTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLL 80
Cdd:COG3383 154 PPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAK-KNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVII 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 81 NNEKFNREYTEAYTNaslivredyGFEDglftgydaekrkydksswtyeldengfakrdttlqhprcvwnlLKQHVSRYT 160
Cdd:COG3383 233 EEGLVDEDFIAERTE---------GFEE-------------------------------------------LKASVAKYT 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 161 PDVVENICGTPKDAFLKVCEYIAETsahdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQ 240
Cdd:COG3383 261 PERVAEITGVPAEDIREAARLIAEA----KRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQ 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 241 GLTDLGLLSQSLPGYMTLPSEKqtdlqtyltantpkpllegqvnywgnypkffvsmmkaffgDKATAENSWGFDWLPKWd 320
Cdd:COG3383 337 GGRDMGALPNVLPGYRDVTDPE----------------------------------------HRAKVADAWGVPPLPDK- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 321 KGYDVLQYFEMMKEGKVNGYICQGFNPVASFPNKNKVIGCLSKLKFLVTIDPLNTETSNFwqnhgelnevdsskiqTEVF 400
Cdd:COG3383 376 PGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEY----------------ADVV 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 401 rLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIALTDGEILSGIflrLRKMyaeqgGANpdqvlnmtWNYAiphepSSEE 480
Cdd:COG3383 440 -LPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIAEL---ARRL-----GYG--------FDYD-----SPEE 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 481 VAMEsngkaladitdpatgavivkkgqqlssfaqlrddgttscgcwifagswtpegnqmarrdnadpsglgntlgWAWAW 560
Cdd:COG3383 498 VFDE-----------------------------------------------------------------------IARLT 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 561 PLNRRILYNRasadpqgnpwdpkrqLLKWDGTKWtgwdiPDYSAAPPGSgvgpfimqqegmGRLFAldkmaegpfpehyE 640
Cdd:COG3383 507 PDYSGISYER---------------LEALGGVQW-----PCPSEDHPGT------------PRLFT-------------G 541
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 641 PFETPLGTNPLHPNVISNPAARIfkdDAEalgkadkFPYVGTTYRLTEHFH--YWTKHALLNAILQPEQFVEIGESLANK 718
Cdd:COG3383 542 RFPTPDGKARFVPVEYRPPAELP---DEE-------YPLVLTTGRLLDQWHtgTRTRRSPRLNKHAPEPFVEIHPEDAAR 611
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 719 LGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlkangkdiDTIGIPIHWGYEGvakkgfiANTLTPFVGDANTQTPEFKSFL 798
Cdd:COG3383 612 LGIKDGDLVRVSSRRGEVVLRARVTDRVRP--------GTVFMPFHWGEGA-------ANALTNDALDPVSKQPEYKACA 676
|
....*.
gi 535687910 799 VNVEKV 804
Cdd:COG3383 677 VRVEKV 682
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
1-795 |
4.20e-80 |
|
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate dehydrogenase alpha chains found mainly archaea but also in alpha and gamma proteobacteria and a small number of gram positive bacteria. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The enzyme's purpose is to allow growth on formate in some circumstances and, in the case of FdhH in gamma proteobacteria, to pass electrons to hydrogenase (by which process acid is neutralized). This model is well-defined, with only a single fragmentary sequence falling between trusted and noise. The alpha subunit of a version of nitrate reductase is closely related.
Pssm-ID: 130652 [Multi-domain] Cd Length: 671 Bit Score: 270.88 E-value: 4.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 1 MTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLL 80
Cdd:TIGR01591 146 MSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAK-RNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVII 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 81 NNEKFNREYTEAYTNaslivredyGFEDglftgydaekrkydksswtyeldengfakrdttlqhprcvwnlLKQHVSRYT 160
Cdd:TIGR01591 225 EEGLYDKAFIEKRTE---------GFEE-------------------------------------------FREIVKGYT 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 161 PDVVENICGTPKDAFLKvceyIAETSAHDKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQ 240
Cdd:TIGR01591 253 PEYVEDITGVPADLIRE----AARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQ 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 241 GLTDLGLLSQSLPGYMTLPSEkqtdlqtyltantpkpllegqvnywgnypkffvSMMKAFfgdkataENSWGFDWLPKwD 320
Cdd:TIGR01591 329 GACDMGALPDFLPGYQPVSDE---------------------------------EVREKF-------AKAWGVVKLPA-E 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 321 KGYDVLQYFEMMKEGKVNGYICQGFNPVASFPNKNKVIGCLSKLKFLVTIDPLNTETSNFwqnhgelnevdsskiqTEVF 400
Cdd:TIGR01591 368 PGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKY----------------ADVV 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 401 rLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIALTDGEILsgiflrlrKMYAEQGGANpdqvlnmtWNYAIPHEpssee 480
Cdd:TIGR01591 432 -LPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEII--------QELANALGLD--------WNYNHPQE----- 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 481 vamesngkaladitdpatgavIVKKGQQLssfaqlrddgttscgCWIFAGswtpegnqMARRDNADPSGLgntlgwawAW 560
Cdd:TIGR01591 490 ---------------------IMDEIREL---------------TPLFAG--------LTYERLDELGSL--------QW 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 561 PLNrrilynraSADPQGNPwdpkrqLLKWDgtkwtGWDIPDysaappgsgvgpfimqqeGMGRLFALDKMAegpfpehye 640
Cdd:TIGR01591 518 PCN--------DSDASPTS------YLYKD-----KFATPD------------------GKAKFIPLEWVA--------- 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 641 PFETPlgtnplhpnvisnpaarifkddaealgkADKFPYVGTTYRLTEHFHY--WTKHALLNAILQPEQFVEIGESLANK 718
Cdd:TIGR01591 552 PIEEP----------------------------DDEYPLILTTGRVLTHYNVgeMTRRVAGLRRLSPEPYVEINTEDAKK 603
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 535687910 719 LGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlkangkdiDTIGIPIHWGYEGVakkgfiaNTLTPFVGDANTQTPEFK 795
Cdd:TIGR01591 604 LGIKDGDLVKVKSRRGEITLRAKVSDRVNK--------GAIYITMHFWDGAV-------NNLTTDDLDPISGTPEYK 665
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
2-804 |
1.61e-70 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 244.75 E-value: 1.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 2 TNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKIHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLLN 81
Cdd:COG0243 179 TVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRGAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVLIE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 82 NEKFNREYTEAYTNaslivredyGFEDglftgydaekrkydksswtyeldengfakrdttlqhprcvwnlLKQHVSRYTP 161
Cdd:COG0243 259 EGLYDRDFLARHTV---------GFDE-------------------------------------------LAAYVAAYTP 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 162 DVVENICGTPKDAFLKVCEYIAETsahdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSniqg 241
Cdd:COG0243 287 EWAAEITGVPAEDIRELAREFATA----KPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTGEA---- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 242 ltdlgllsqslpgymtlpsekqtdlqtyltantpkpLLEGqvnywgnypkffvsmmkaffgdkataenswgfdwlpkwdk 321
Cdd:COG0243 359 ------------------------------------ILDG---------------------------------------- 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 322 gydvlqyfemmKEGKVNGYICQGFNPVASFPNKNKVIGCLSKLKFLVTIDPLNTETSNFwqnhgelneVDsskiqtevFR 401
Cdd:COG0243 363 -----------KPYPIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARY---------AD--------IV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 402 LPSTCFAEENGSIVNSG-RWLQWHWKGADAPGIALTDGEILSGIFLRLrkmyaeqgGANPdqvlnmtwnyAIPHEPSSEE 480
Cdd:COG0243 415 LPATTWLERDDIVTNSEdRRVHLSRPAVEPPGEARSDWEIFAELAKRL--------GFEE----------AFPWGRTEED 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 481 VamesngkaLADITDPATGAVIvkkgqqlsSFAQLRDDGttscgcwifagswtpegnqmarrdnadpsglgntlgwAWAW 560
Cdd:COG0243 477 Y--------LRELLEATRGRGI--------TFEELREKG-------------------------------------PVQL 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 561 PLnrrilynrasadPQGNPWdpkrqllKWDGtkwtGWDIPDysaappgsgvgpfimqqegmGRL-FALDKMAEGPFPEHY 639
Cdd:COG0243 504 PV------------PPEPAF-------RNDG----PFPTPS--------------------GKAeFYSETLALPPLPRYA 540
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 640 EPFEtplgtnplhpnvisnpaarifkddaEALGKADKFPYVGTTYRLTEHFHYWT-KHALLNAIlQPEQFVEIGESLANK 718
Cdd:COG0243 541 PPYE-------------------------GAEPLDAEYPLRLITGRSRDQWHSTTyNNPRLREI-GPRPVVEINPEDAAA 594
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 719 LGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlkangkdiDTIGIPIHWGYEGVAKKGFIANTLTPFVGDANTQTPEFKSFL 798
Cdd:COG0243 595 LGIKDGDLVRVESDRGEVLARAKVTEGIRP--------GVVFAPHGWWYEPADDKGGNVNVLTPDATDPLSGTPAFKSVP 666
|
....*.
gi 535687910 799 VNVEKV 804
Cdd:COG0243 667 VRVEKA 672
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
1-465 |
9.85e-67 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. Members of the MopB_Formate-Dh-H CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239154 [Multi-domain] Cd Length: 512 Bit Score: 230.56 E-value: 9.85e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 1 MTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKIhNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLL 80
Cdd:cd02753 147 MTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKR-NGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVII 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 81 NNEKFNREYTEAYTNaslivredyGFEDglftgydaekrkydksswtyeldengfakrdttlqhprcvwnlLKQHVSRYT 160
Cdd:cd02753 226 EEGLYDEEFIEERTE---------GFEE-------------------------------------------LKEIVEKYT 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 161 PDVVENICGTPKDAFLKvceyIAETSAHDKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQ 240
Cdd:cd02753 254 PEYAERITGVPAEDIRE----AARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQ 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 241 GLTDLGLLSQSLPGYmtlpsekqtdlqtyltantpkpllegqvnywgnypkffvsmmkaffgdkataenswgfdwlpkwd 320
Cdd:cd02753 330 GACDMGALPNVLPGY----------------------------------------------------------------- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 321 kgydvlqyfemmkegkVNGYICQGFNPVASFPNKNKVIGCLSKLKFLVTIDPLNTETSNFwqnhgelnevdsskiqTEVF 400
Cdd:cd02753 345 ----------------VKALYIMGENPALSDPNTNHVRKALESLEFLVVQDIFLTETAEL----------------ADVV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 535687910 401 rLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIALTDGEILSGIflrLRKMYAEQGGANPDQVLN 465
Cdd:cd02753 393 -LPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQEL---ANRLGYPGFYSHPEEIFD 453
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
7-448 |
2.04e-54 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239155 [Multi-domain] Cd Length: 565 Bit Score: 197.45 E-value: 2.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 7 DIKNANLVVVMGGNAAEAHPVGFRWAMEAK-IHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLLNNEKF 85
Cdd:cd02754 154 DIEHADCFFLIGSNMAECHPILFRRLLDRKkANPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLI 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 86 NREYTEAYTNaslivredyGFEDglftgydaekrkydksswtyeldengfakrdttlqhprcvwnlLKQHVSRYTPDVVE 165
Cdd:cd02754 234 DRDFIDAHTE---------GFEE-------------------------------------------LKAFVADYTPEKVA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 166 NICGTPKDAFLKVCEYIAETsahdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDL 245
Cdd:cd02754 262 EITGVPEADIREAARLFGEA----RKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNAMGGREV 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 246 GLLSQSLPGYMTLPSEKqtdlqtyltantpkpllegqvnywgnypkffvsmmkaffgDKATAENSWGFDWLPKWDK-GYD 324
Cdd:cd02754 338 GGLANLLPGHRSVNNPE----------------------------------------HRAEVAKFWGVPEGTIPPKpGLH 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 325 VLQYFEMMKEGKVNGYICQGFNPVASFPNKNKVIGCLSKLKFLVTIDP-LNTETsnfwqnhGELNEVdsskiqtevfRLP 403
Cdd:cd02754 378 AVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVVVQDAfADTET-------AEYADL----------VLP 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 535687910 404 STCFAEENGSIVNSGRWLQwHWKGA-DAPGIALTDGEILSGIFLRL 448
Cdd:cd02754 441 AASWGEKEGTMTNSERRVS-LLRAAvEPPGEARPDWWILADVARRL 485
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
675-803 |
1.29e-53 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. This CD (MopB_CT_Formate-Dh-Na-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239193 [Multi-domain] Cd Length: 122 Bit Score: 181.27 E-value: 1.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 675 DKFPYVGTTYRLTEHFHYW--TKHALLNAILQPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlkan 752
Cdd:cd02792 1 EEFPLVLTTGRLTEHFHGGnmTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKP---- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 535687910 753 gkdiDTIGIPIHWGYEGVAkKGFIANTLTPFVGDANTQTPEFKSFLVNVEK 803
Cdd:cd02792 77 ----HEVGIPYHWGGMGLV-IGDSANTLTPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
675-803 |
2.83e-40 |
|
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 238282 [Multi-domain] Cd Length: 120 Bit Score: 143.80 E-value: 2.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 675 DKFPYVGTTYRLTEHFHYW--TKHALLNAILQPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRtlkan 752
Cdd:cd00508 1 EEYPLVLTTGRLLEHWHTGtmTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVR----- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 535687910 753 gkdIDTIGIPIHWGYEGvakKGFIANTLTPFVGDANTQTPEFKSFLVNVEK 803
Cdd:cd00508 76 ---PGTVFMPFHWGGEV---SGGAANALTNDALDPVSGQPEFKACAVRIEK 120
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
1-448 |
1.25e-35 |
|
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site.
Pssm-ID: 238218 [Multi-domain] Cd Length: 374 Bit Score: 139.00 E-value: 1.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 1 MTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGvllyll 80
Cdd:cd00368 147 PTNTLADIENADLILLWGSNPAETHPVLAARLRRAK-KRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA------ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 81 nnekfnreyteaytnaslivredygfedglftgydaekrkydksswtyeldengfakrdttlqhprcvwnllkqhvsryt 160
Cdd:cd00368 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 161 pDVVENICGTPKDAFLKVCEYIAETsahdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNAlrghsniq 240
Cdd:cd00368 220 -EWAAEITGVPAETIRALAREFAAA----KRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP-------- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 241 gltdlgllsqslpgymtlpsekqtdlqtyltantpkpllegqvnywgnypkffvsmmkaffgdkataenswgfdwlpkwd 320
Cdd:cd00368 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 321 kgydvlqyfemmkegkvngyicqGFNPVASFPNKNKVIGCLSKLKFLVTIDPLNTETSNFwqnhgelnevdsskiqtEVF 400
Cdd:cd00368 287 -----------------------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAY-----------------ADV 326
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 535687910 401 RLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIALTDGEILSGIFLRL 448
Cdd:cd00368 327 VLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
2-241 |
3.76e-29 |
|
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239166 [Multi-domain] Cd Length: 567 Bit Score: 122.97 E-value: 3.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 2 TNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLLN 81
Cdd:cd02765 151 TNEITDWVNAKTIIIWGSNILETQFQDAEFFLDAR-ENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 82 NEKFNREYTEAYTNASLIVREDYG----FEDGLFTGYDAEKRKYDKSSWTYE-LDENG--FAKR-----DTTLQHPrcVW 149
Cdd:cd02765 230 HNWYDEAFLKSNTSAPFLVREDNGtllrQADVTATPAEDGYVVWDTNSDSPEpVAATNinPALEgeytiNGVKVHT--VL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 150 NLLKQHVSRYTPDVVENICGTPKdaflKVCEYIAETSAHDKtASFLYALGWTQH-SIGAQNIRTMAMIQLLLGNMGMAGG 228
Cdd:cd02765 308 TALREQAASYPPKAAAEICGLEE----AIIETLAEWYATGK-PSGIWGFGGVDRyYHSHVFGRTAAILAALTGNIGRVGG 382
|
250
....*....|....*..
gi 535687910 229 GVNALRG----HSNIQG 241
Cdd:cd02765 383 GVGQIKFmyfmGSNFLG 399
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
7-371 |
1.10e-26 |
|
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239168 [Multi-domain] Cd Length: 574 Bit Score: 115.48 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 7 DIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDP-------RF----------TRTAAVADYYAPIRSGTDI 69
Cdd:cd02767 160 DFEHTDLIFFIGQNPGTNHPRMLHYLREAK-KRGGKIIVINPlrepgleRFanpqnpesmlTGGTKIADEYFQVRIGGDI 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 70 AFLSGVLLYLLNNEK-----FNREYTEAYTNaslivredygfedglftGYDAEKRKYDKSSWtyeldengfakrdttlqh 144
Cdd:cd02767 239 ALLNGMAKHLIERDDepgnvLDHDFIAEHTS-----------------GFEEYVAALRALSW------------------ 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 145 prcvwnllkqhvsrytpDVVENICGTPKDAFLKVceyiAETSAHDKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMG 224
Cdd:cd02767 284 -----------------DEIERASGLSREEIEAF----AAMYAKSERVVFVWGMGITQHAHGVDNVRAIVNLALLRGNIG 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 225 MAGGGVNALRGHSNIQGLTDLGLlsqslpgymtlpsekqtdlqtyltanTPKPLLEgqvnywgnypkFFVSMmkaffgdk 304
Cdd:cd02767 343 RPGAGLMPIRGHSNVQGDRTMGI--------------------------TEKPFPE-----------FLDAL-------- 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 535687910 305 ataENSWGFDwLPKWdKGYDVLQYFEMMKEGKVNGYICQGFNPVASFPNKNKVIGCLSKLKFLVTID 371
Cdd:cd02767 378 ---EEVFGFT-PPRD-PGLDTVEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVA 439
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
7-228 |
2.85e-26 |
|
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Members of the MopB_Thiosulfate-R-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239156 [Multi-domain] Cd Length: 454 Bit Score: 112.78 E-value: 2.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 7 DIKNANLVVVMGGNAAEAHPVGFRWAMEAKIHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLLNNEKFN 86
Cdd:cd02755 153 DFENARYIILFGRNLAEAIIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISENLYD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 87 REYTEAYTNaslivredyGFEdglftgydaekrkydksswtyeldengfakrdttlqhprcvwnLLKQHVSRYTPDVVEN 166
Cdd:cd02755 233 AAFVEKYTN---------GFE-------------------------------------------LLKAHVKPYTPEWAAQ 260
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 535687910 167 ICGTPKDAFLKVCEYIAETSAHDKTASFLYALgWTQHSIGAQniRTMAMIQLLLGNMGMAGG 228
Cdd:cd02755 261 ITDIPADTIRRIAREFAAAAPHAVVDPGWRGT-FYSNSFQTR--RAIAIINALLGNIDKRGG 319
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
7-242 |
6.96e-25 |
|
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239167 [Multi-domain] Cd Length: 501 Bit Score: 109.26 E-value: 6.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 7 DIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLLNNEKFN 86
Cdd:cd02766 154 DMVNADLIVIWGINPAATNIHLMRIIQEAR-KRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 87 REYTEAYTnaslivredYGFEDglftgydaekrkydksswtyeldengfakrdttlqhprcvwnlLKQHVSRYTPDVVEN 166
Cdd:cd02766 233 RDFLARHT---------EGFEE-------------------------------------------LKAHLETYTPEWAAE 260
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 535687910 167 ICGTPKDAFLKVCEYIAETsahdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGL 242
Cdd:cd02766 261 ITGVSAEEIEELARLYGEA----KPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGGAFYSNSGPPVKAL 332
|
|
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
7-377 |
1.63e-23 |
|
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of oxidoreductase alpha subunits most closely related to a group of formate dehydrogenases including the E. coli FdhH protein (TIGR01591). These alpha subunits contain a molybdopterin cofactor and generally associate with two other subunits which contain iron-sulfur clusters and cytochromes. The particular subunits with which this enzyme interacts and the substrate which is reduced is unknown at this time. In Ralstonia, the gene is associated with the cbb operon, but is not essential for CO2 fixation.
Pssm-ID: 273765 [Multi-domain] Cd Length: 743 Bit Score: 106.43 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 7 DIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDP-------RFTRTAA-----------VADYYAPIRSGTD 68
Cdd:TIGR01701 195 DFEHTDCLVFIGSNAGTNHPRMLKYLYAAK-KRGAKIIAINPlrergleRFWIPQIpesmltgggtqISSEYYQVRIGGD 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 69 IAFLSGVLLYLLNNEK------FNREYTEAYTNaslivredygfedglftgydaekrkydksswtyeldenGFAKrdttl 142
Cdd:TIGR01701 274 IALFNGVMKLLIEAEDaqpgslIDHEFIANHTN--------------------------------------GFDE----- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 143 qhprcvwnlLKQHVSRYTPDVVENICGTPKDAFLKVCEYIAETSAhdktASFLYALGWTQHSIGAQNIRTMAMIQLLLGN 222
Cdd:TIGR01701 311 ---------LRRHVLQLNWNDIERSSGLSQEEILEFAKLLANSRR----VVFCWAMGLTQHAHGVDNISQVANLALLRGN 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 223 MGMAGGGVNALRGHSNIQGltdlgllsqslpgymtlpsekqtdlqtyltantpkpllEGQVNYWGNYPKFFvsmmkaffg 302
Cdd:TIGR01701 378 IGKPGAGVCPIRGHSNVQG--------------------------------------DRTMGITEKPEEEF--------- 410
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 535687910 303 dKATAENSWGFDwLPKWdKGYDVLQYFEMMKEGKVNGYICQGFNPVASFPNKNKVIGCLSKLKFLVTIDPLNTET 377
Cdd:TIGR01701 411 -LARLSQIYGFT-PPDW-PGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHVATKLNRS 482
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
686-795 |
6.67e-23 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 93.92 E-value: 6.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 686 LTEHFH--YWTKHALLNAiLQPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlkangkdiDTIGIPI 763
Cdd:cd02775 1 LRDHFHsgTRTRNPWLRE-LAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPP--------GVVFLPH 71
|
90 100 110
....*....|....*....|....*....|..
gi 535687910 764 HWGYEGvaKKGFIANTLTPFVGDANTQTPEFK 795
Cdd:cd02775 72 GWGHRG--GRGGNANVLTPDALDPPSGGPAYK 101
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
3-237 |
2.68e-20 |
|
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239171 [Multi-domain] Cd Length: 617 Bit Score: 95.85 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 3 NHWVDIKNANLVVVMGGNAAEAHPVGFR---WAMEAKiHNGAKLIVIDPRFTRTAAV-ADYYAPIRSGTDIAFLSGVLLY 78
Cdd:cd02770 159 SSLDDLKDSKLVVLFGHNPAETRMGGGGstyYYLQAK-KAGAKFIVIDPRYTDTAVTlADEWIPIRPGTDAALVAAMAYV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 79 LLNNEKFNREYTEAYTnaslivredYGF-EDGLFTGYDAEKRKYDksswtYEL--DENGFAKrdttlqhprcvwnllkqh 155
Cdd:cd02770 238 MITENLHDQAFLDRYC---------VGFdAEHLPEGAPPNESYKD-----YVLgtGYDGTPK------------------ 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 156 vsryTPDVVENICGTPKDAFLKVCEYIAETsahdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGvNALRG 235
Cdd:cd02770 286 ----TPEWASEITGVPAETIRRLAREIATT----KPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGN-TGARP 356
|
..
gi 535687910 236 HS 237
Cdd:cd02770 357 GG 358
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
675-804 |
3.68e-19 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
Pssm-ID: 239192 [Multi-domain] Cd Length: 122 Bit Score: 83.78 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 675 DKFPYVGTTYRLTEHFHYWT---KHALLNAILqPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlka 751
Cdd:cd02791 1 AEYPLWLNTGRVRDQWHTMTrtgRVPRLNAHV-PEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRP--- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 535687910 752 nGkdidTIGIPIHWGYEGVAKKGfiANTLTPFVGDANTQTPEFKSFLVNVEKV 804
Cdd:cd02791 77 -G----EVFVPMHWGDQFGRSGR--VNALTLDATDPVSGQPEFKHCAVRIEKV 122
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
675-803 |
1.07e-18 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239191 [Multi-domain] Cd Length: 116 Bit Score: 82.29 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 675 DKFPYVGTTYRLTEHFHYWT---KHALLNAIlQPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlka 751
Cdd:cd02790 1 EEYPLVLTTGRVLYHYHTGTmtrRAEGLDAI-APEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPE--- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 535687910 752 ngkdiDTIGIPIHWgYEGVakkgfiANTLTPFVGDANTQTPEFKSFLVNVEK 803
Cdd:cd02790 77 -----GVVFMPFHF-AEAA------ANLLTNAALDPVAKIPEFKVCAVRVEK 116
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
7-232 |
1.11e-17 |
|
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239160 [Multi-domain] Cd Length: 477 Bit Score: 86.98 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 7 DIKNANLVVVMGGNAAEAHPVGFRWAMEAKIHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLLNNEKFN 86
Cdd:cd02759 157 DWENPECIVLWGKNPLNSNLDLQGHWLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVIINEGLYD 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 87 REYTEAYTnaslivredYGFEDglftgydaekrkydksswtyeldengfakrdttlqhprcvwnlLKQHVSRYTPDVVEN 166
Cdd:cd02759 237 KDFVENWC---------YGFEE-------------------------------------------LAERVQEYTPEKVAE 264
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 535687910 167 ICGTPKDAFLKVCEYIAETsahdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNA 232
Cdd:cd02759 265 ITGVPAEKIRKAARLYATA----KPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGNLLI 326
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
682-798 |
2.39e-17 |
|
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules.
Pssm-ID: 426328 [Multi-domain] Cd Length: 110 Bit Score: 78.47 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 682 TTYRLTEHFH--YWTKHALLNAILQPEqFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlkangkdiDTI 759
Cdd:pfam01568 4 ITGRVLGQYHsqTRTRRVLRLAKPEPE-VVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRP--------GVV 74
|
90 100 110
....*....|....*....|....*....|....*....
gi 535687910 760 GIPIHWGYEgvaKKGFIANTLTPFVGDANTQTPEFKSFL 798
Cdd:pfam01568 75 FMPFGWWYE---PRGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
7-378 |
1.40e-14 |
|
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239163 [Multi-domain] Cd Length: 539 Bit Score: 77.44 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 7 DIKNANLVVVMGGNAAEAHpvGFRWAM-------EAKIHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGvLLYL 79
Cdd:cd02762 153 DIDRTDYLLILGANPLQSN--GSLRTApdrvlrlKAAKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLAA-MLAV 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 80 LnnekfnreyteaytnaslivredygFEDGLFtgydaekrkydksswtyelDENGFAKRDTTLQHprcvwnlLKQHVSRY 159
Cdd:cd02762 230 L-------------------------LAEGLT-------------------DRRFLAEHCDGLDE-------VRAALAEF 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 160 TPDVVENICGTPKDAFLKVCEYIAetSAhdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGgvnalrghsni 239
Cdd:cd02762 259 TPEAYAPRCGVPAETIRRLAREFA--AA--PSAAVYGRLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGG----------- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 240 qgltdlGLLSQSLpgymtLPSEKQTDLQTYLTANTPKPllegqvnywgnypkffVSMMKAFFGD---KATAEnswgfdwl 316
Cdd:cd02762 324 ------AMFTTPA-----LDLVGQTSGRTIGRGEWRSR----------------VSGLPEIAGElpvNVLAE-------- 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 535687910 317 pkwdkgydvlqyfEMMK--EGKVNGYICQGFNPVASFPNKNKVIGCLSKLKFLVTIDPLNTETS 378
Cdd:cd02762 369 -------------EILTdgPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETT 419
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
7-370 |
1.59e-14 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 77.78 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 7 DIKNANLVVVMGGNAAEAHPVGFRwAMEAKIHNGAKLIVIDP-------RFT-----------RTAAVADYYAPIRSGTD 68
Cdd:PRK09939 205 DFEKCDLVICIGHNPGTNHPRMLT-SLRALVKRGAKMIAINPlqergleRFTapqnpfemltnSETQLASAYYNVRIGGD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 69 IAFLSGVLLYLLNNEkfnrEYTEAYTNASLIvreDYGFEDGLFTGYDAEKRKYDKSSWtyeldengfakRDttlqhprcv 148
Cdd:PRK09939 284 MALLKGMMRLLIERD----DAASAAGRPSLL---DDEFIQTHTVGFDELRRDVLNSEW-----------KD--------- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 149 wnllkqhvsrytpdvVENICGTPKdafLKVCEYIAETSAHDKTAsFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGG 228
Cdd:PRK09939 337 ---------------IERISGLSQ---TQIAELADAYAAAERTI-ICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGA 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 229 GVNALRGHSNIQGLTDLGLlsqslpgymtlpsekqtdlqtyltanTPKPLLEgqvnywgnypkfFVSMMKAFFGdkatae 308
Cdd:PRK09939 398 GICPLRGHSNVQGDRTVGI--------------------------TEKPSAE------------FLARLGERYG------ 433
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 535687910 309 nswgfdWLPKWDKGYDVLQYFEMMKEGKVNGYICQGFNPVASFPNKNKVIGCLSKLKFLVTI 370
Cdd:PRK09939 434 ------FTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHV 489
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
7-228 |
2.51e-14 |
|
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other related proteins. The Salmonella enterica tetrathionate reductase catalyses the reduction of trithionate but not sulfur or thiosulfate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239159 [Multi-domain] Cd Length: 735 Bit Score: 77.00 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 7 DIKNANLVVVMGGNAAEAHPvGFRWA----MEAKIHNGAKLIVIDPRFTRTAAVAD---YYAPIRSGTDIAFLSGVLLYL 79
Cdd:cd02758 208 DFDNAEFALFIGTSPAQAGN-PFKRQarrlAEARTEGNFKYVVVDPVLPNTTSAAGeniRWVPIKPGGDGALAMAMIRWI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 80 LNNEKFNREYTEaytNASLIVredygfedglftgydAEKRKYdkSSWTyeldeNG-----FAKRDTTLQhprcvwnLLKQ 154
Cdd:cd02758 287 IENERYNAEYLS---IPSKEA---------------AKAAGE--PSWT-----NAthlviTVRVKSALQ-------LLKE 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 535687910 155 HVSRYTPDVVENICGTPKDaflKVCEYIAETSAHDKTASFLYAlGWTQHSIGAQNIRTMAMIQLLLGNMGMAGG 228
Cdd:cd02758 335 EAFSYSLEEYAEICGVPEA---KIIELAKEFTSHGRAAAVVHH-GGTMHSNGFYNAYAIRMLNALIGNLNWKGG 404
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
7-235 |
3.62e-14 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 76.61 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 7 DIKNANLVVVMGGNAAEAHPVG---FRWAMEAKIHNGAKLIVIDPRFTRT-AAVADYYAPIRSGTDIAFLSGvLLYLLNN 82
Cdd:PRK14990 228 DIENSKLVVLFGNNPGETRMSGggvTYYLEQARQKSNARMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNG-LAYVMIT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 83 EKFnreyteaytnaslivrEDYGFEDGLFTGydaekrkYDKSSWTYELDENGFAKRDTTLQHPRCVWNllkqhvsryTPD 162
Cdd:PRK14990 307 ENL----------------VDQPFLDKYCVG-------YDEKTLPASAPKNGHYKAYILGEGPDGVAK---------TPE 354
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 535687910 163 VVENICGTPKDAFLKVCEYIAETsahdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRG 235
Cdd:PRK14990 355 WASQITGVPADKIIKLAREIGST----KPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGAREG 423
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
7-228 |
1.93e-13 |
|
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other related proteins. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239158 [Multi-domain] Cd Length: 523 Bit Score: 73.63 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 7 DIKNANLVVVMGGNAAEA-HPVGFRWAMEAKIHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLLNNEKF 85
Cdd:cd02757 159 DYANAKYILFFGADPLESnRQNPHAQRIWGGKMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHVILTEGLW 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 86 NREYTEAYTNASLIVREDYGFEDGLFtgydaekrkydKSSWTYELDEngfakrdttlqhprcvWnlLKQHVSRYTPDVVE 165
Cdd:cd02757 239 DKDFVGDFVDGKNYFKAGETVDEESF-----------KEKSTEGLVK----------------W--WNLELKDYTPEWAA 289
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 535687910 166 NICGTPKDAFLKVCEYIAetSAHDKTASFLYAlGWTQHSIGAQNIRTMAMIQLLLGNMGMAGG 228
Cdd:cd02757 290 KISGIPAETIERVAREFA--TAAPAAAAFTWR-GATMQNRGSYNSMACHALNGLVGSIDSKGG 349
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
3-253 |
6.06e-13 |
|
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. Members of the MopB_DMSOR-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239152 [Multi-domain] Cd Length: 609 Bit Score: 72.26 E-value: 6.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 3 NHWVDI-KNANLVVVMGGNAAE--------AHPVGFRWAMEAKiHNGAKLIVIDPRFTRTAA-VADYYAPIRSGTDIAFL 72
Cdd:cd02751 161 TSWDDIaEHSDLVVLFGANPLKtrqgggggPDHGSYYYLKQAK-DAGVRFICIDPRYTDTAAvLAAEWIPIRPGTDVALM 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 73 SGVLLYLLNNEKFNREYTEAYTnaslivredygfedglfTGYDAEKRkydksswtYELDEN-GFAKrdttlqhprcvwnl 151
Cdd:cd02751 240 LAMAHTLITEDLHDQAFLARYT-----------------VGFDEFKD--------YLLGESdGVPK-------------- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 152 lkqhvsryTPDVVENICGTPKDAFLKVCEYIAetsahDKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVN 231
Cdd:cd02751 281 --------TPEWAAEITGVPAETIRALAREIA-----SKRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFG 347
|
250 260
....*....|....*....|..
gi 535687910 232 ALRGHSNIQGLTDLGLLSQSLP 253
Cdd:cd02751 348 FGYGYSNGGGPPRGGAGGPGLP 369
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
10-235 |
1.40e-12 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. Members of the MopB_Nitrate-R-NarG-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239151 [Multi-domain] Cd Length: 461 Bit Score: 70.81 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 10 NANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLLNNEKFNREY 89
Cdd:cd02750 170 NADYIIMWGSNVPVTRTPDAHFLTEAR-YNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDEDY 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 90 TEAYTNASLIVredygfedglftgydaekrkydksswtyeldengfakrdttlqhprcvwnllkqhvsrYTPDVVENICG 169
Cdd:cd02750 249 LKEYTDLPFLV----------------------------------------------------------YTPAWQEAITG 270
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 535687910 170 TPKDAFLKVCEYIAETsahdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRG 235
Cdd:cd02750 271 VPRETVIRLAREFATN----GRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVG 332
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
7-228 |
4.82e-12 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 69.70 E-value: 4.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 7 DIKNANLVVVMGGNAAEAHPVGF-RWAMEAKIHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLLNNEKF 85
Cdd:PRK15488 193 DLANSKYIINFGHNLYEGINMSDtRGLMTAQMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLY 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 86 NREYTEAYTNaslivredyGFEDglftgydaekrkydksswtyeldengfakrdttlqhprcvwnlLKQHVSRYTPDVVE 165
Cdd:PRK15488 273 DKAFVERYTS---------GFEE-------------------------------------------LAASVKEYTPEWAE 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 535687910 166 NICGTPKDAFLKVCEYIAETSAHdKTASFLYALGWTQHSIgaQNIRTMAMIQLLLGNMGMAGG 228
Cdd:PRK15488 301 AISDVPADDIRRIARELAAAAPH-AIVDFGHRATFTPEEF--DMRRAIFAANVLLGNIERKGG 360
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
7-228 |
1.09e-11 |
|
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239164 [Multi-domain] Cd Length: 679 Bit Score: 68.32 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 7 DIKNANLVVvMGGNAAEAHPVGFRWAMEAKIHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLLNNEKFN 86
Cdd:cd02763 152 DLEHTKYFM-MIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILALAHELLKAGLID 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 87 REYTEAYTNASLIVredygfedglftgydaekrkydksswtyeldengfakrdttlqhprcvwnllkqhvsRYTPDVVEN 166
Cdd:cd02763 231 WEFLKRYTNAAELV---------------------------------------------------------DYTPEWVEK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 167 ICGTPKDAFLKVCEYIAETS-----------------AHDKT----ASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGM 225
Cdd:cd02763 254 ITGIPADTIRRIAKELGVTArdqpielpiawtdvwgrKHEKItgrpVSFHAMRGIAAHSNGFQTIRALFVLMMLLGTIDR 333
|
...
gi 535687910 226 AGG 228
Cdd:cd02763 334 PGG 336
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
697-803 |
2.38e-08 |
|
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Also included in this CD is the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), which has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. The MopB_CT_Thiosulfate-R-like CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239179 [Multi-domain] Cd Length: 123 Bit Score: 53.05 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 697 ALLNAILqPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlkangkdiDTIGIPIHWGYegVAKKGFI 776
Cdd:cd02778 21 PLLHELT-PENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRP--------DTVFMPHGFGH--WAPALSR 89
|
90 100 110
....*....|....*....|....*....|....
gi 535687910 777 A-------NTLTPFVGDANTQTPEFKSFLVNVEK 803
Cdd:cd02778 90 AygggvndNNLLPGSTEPVSGGAGLQEFTVTVRK 123
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
677-772 |
1.73e-07 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins.
Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 51.14 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 677 FPYVGTTYRLTEHFHYWTKHALLNAILqPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlkangkdi 756
Cdd:cd02780 1 YPFILVTFKSNLNSHRSANAPWLKEIK-PENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRP-------- 71
|
90
....*....|....*....
gi 535687910 757 DTIGIPI---HWGYEGVAK 772
Cdd:cd02780 72 GVVAIEHgygHWAYGAVAS 90
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
1-86 |
7.56e-07 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 52.02 E-value: 7.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 1 MTNHWVDIKNANLVVVMGGNAAEAHPVGfrWAME--AKIHNGAKLIVIDPRFTRTAAVAdyYAPIRSGTDIAFLSGVLLY 78
Cdd:pfam00384 99 FNSSIADIENADLILLIGTNPREEAPIL--NARIrkAALKGKAKVIVIGPRLDLTYADE--HLGIKPGTDLALALAGAHV 174
|
90
....*....|..
gi 535687910 79 ----LLNNEKFN 86
Cdd:pfam00384 175 fikeLKKDKDFA 186
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
7-186 |
9.37e-07 |
|
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), and other related proteins. The phenylacetyl-CoA:acceptor oxidoreductase has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239161 [Multi-domain] Cd Length: 760 Bit Score: 52.66 E-value: 9.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 7 DIKNANLVVVMGGNA-AEAHPVGFRWAMEAKIHnGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAF---LSGVLLYLLNN 82
Cdd:cd02760 170 DTPLANYVISFGSNVeASGGPCAVTRHADARVR-GYKRVQVEPHLSVTGACSAEWVPIRPKTDPAFmfaMIHVMVHEQGL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 83 EKFNREYTEAYTNASLIVRedygfEDGLFTgYDAEKRK---YD-KSSWTYELDENGFAK----------------RDTTL 142
Cdd:cd02760 249 GKLDVPFLRDRTSSPYLVG-----PDGLYL-RDAATGKplvWDeRSGRAVPFDTRGAVPavagdfavdgavsvdaDDETA 322
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 535687910 143 QHP----RCVWNLLKQHVSRYTPDVVENICGTPKDAFLKVC-EYIAETS 186
Cdd:cd02760 323 IHQgvegTTAFTMLVEHMRKYTPEWAESICDVPAATIRRIArEFLENAS 371
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
676-747 |
2.49e-06 |
|
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239186 [Multi-domain] Cd Length: 124 Bit Score: 47.36 E-value: 2.49e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 535687910 676 KFPYVGTTY--RLTEHFHYWTKHALLnaILQPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIR 747
Cdd:cd02785 1 KYPLACIQRhsRFRVHSQFSNVPWLL--ELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQ 72
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
677-803 |
6.20e-05 |
|
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239182 [Multi-domain] Cd Length: 130 Bit Score: 43.45 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 677 FPYVGTTYRLTEHFHywTKHALLNAI--LQPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlkangk 754
Cdd:cd02781 3 PLILTTGARSYYYFH--SEHRQLPSLreLHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRP------ 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 535687910 755 diDTIGIPIHWGY--EGVAKKGFI------ANTLT------PFVGDANtqtpeFKSFLVNVEK 803
Cdd:cd02781 75 --GVVRAEHGWWYpeREAGEPALGgvwesnANALTsddwndPVSGSSP-----LRSMLCKIYK 130
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
716-747 |
1.63e-04 |
|
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239178 [Multi-domain] Cd Length: 127 Bit Score: 42.19 E-value: 1.63e-04
10 20 30
....*....|....*....|....*....|..
gi 535687910 716 ANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIR 747
Cdd:cd02777 43 AAARGIKDGDIVRVFNDRGAVLAGARVTDRIM 74
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
716-747 |
2.53e-04 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239194 [Multi-domain] Cd Length: 129 Bit Score: 41.47 E-value: 2.53e-04
10 20 30
....*....|....*....|....*....|..
gi 535687910 716 ANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIR 747
Cdd:cd02793 42 AAARGIADGDIVRVFNDRGACLAGAVVTDGIM 73
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
7-73 |
5.51e-04 |
|
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, subunit B (FmdB/FwdB), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239162 [Multi-domain] Cd Length: 415 Bit Score: 43.09 E-value: 5.51e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 535687910 7 DIKN-ANLVVVMGGNAAEAHPVGFR---WAMEAKIHNGA----KLIVIDPRFTRTAAVADYYAPIRSGTDIAFLS 73
Cdd:cd02761 127 EVKNrADVIVYWGTNPMHAHPRHMSrysVFPRGFFREGGredrTLIVVDPRKSDTAKLADIHLQIDPGSDYELLA 201
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
8-94 |
2.29e-03 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239170 [Multi-domain] Cd Length: 609 Bit Score: 41.48 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 8 IKNANLVVVMGGNA----------AEAHPVgfRWAMEAKIHNGAKLIVIDPRFTRTAAVADY-YAPIRSGTDIAFLSGVL 76
Cdd:cd02769 168 AEHTELVVAFGADPlknaqiawggIPDHQA--YSYLKALKDRGIRFISISPLRDDTAAELGAeWIAIRPGTDVALMLALA 245
|
90
....*....|....*...
gi 535687910 77 LYLLNNEKFNREYTEAYT 94
Cdd:cd02769 246 HTLVTEGLHDKAFLARYT 263
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
1-150 |
2.29e-03 |
|
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 41.31 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 1 MTNHWVDIKNANLVVVMGGNAAEAHPVGF-----------------RWAMEAKIHNGAKLIVIDPRFTRTAAVADYYA-- 61
Cdd:cd02756 214 LNNSYEDARLADTIVLWGNNPYETQTVYFlnhwlpnlrgatvsekqQWFPPGEPVPPGRIIVVDPRRTETVHAAEAAAgk 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 62 ------PIRSGTDIAFLSGVLLYLLNNekfnreYTEAYTNASLIvredygfedglfTGYDAEKRKYdKSSWTYELDENGF 135
Cdd:cd02756 294 drvlhlQVNPGTDTALANAIARYIYES------LDEVLAEAEQI------------TGVPRAQIEK-AADWIAKPKEGGY 354
|
170
....*....|....*
gi 535687910 136 AKRDTTLQHPRCVWN 150
Cdd:cd02756 355 RKRVMFEYEKGIIWG 369
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
718-803 |
6.69e-03 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 37.52 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687910 718 KLGIAQGDTVKVSSNRGYIKAKAVVTKRIrtlkangkdidtigipihwgYEGVAkkgFI-----ANTLTPfvgdANTQ-- 790
Cdd:COG1153 42 KLGIKEGDKVKVTSEYGEVVVKAKESEDL--------------------HPGLV---FIpmgpwANAVVP----PETHst 94
|
90
....*....|....
gi 535687910 791 -TPEFKSFLVNVEK 803
Cdd:COG1153 95 gMPDFKGVPVEVEP 108
|
|
| |
