|
Name |
Accession |
Description |
Interval |
E-value |
| formate-DH-alph |
TIGR01553 |
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase ... |
2-1015 |
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: 1484.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 2 QVSRRQFFKICAGGMAGTTAAALGFAPSVALAETRQYKLLRTRETRNTCTYCSVGCGLLMYSLGDGAKNAKASIFHIEGD 81
Cdd:TIGR01553 1 LISRRAFLKLTAGGATLSAFGGLGFDLAPAKAQARALKTVDAKQTTSVCCYCSVSCGLLVYSSSHTGDNKTNRAIHVEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 82 PDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAPGSDKWQQISWEEAFDRIAKLMKEDRDANYIAQNAEGVTVNRWLST 161
Cdd:TIGR01553 81 PDHPINRGSLCPKGASTWDLVNNERRPANPLYRAPGSDQWEEISWDWAIDTIARRVKDTRDATFVTKDAKGQVVNRCDGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 162 GMLCASASSNETGYLTQKFSRALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGF 241
Cdd:TIGR01553 161 ASVGSSAMDNEECWLYQKWLRSLGLFYIEHQARIUHSPTVASLAPSFGRGAMTNNWVDIKNSDLILVMGGNPAENHPIGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 242 RWAMEAKiHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLLNNEKFNREYTEAYTNASLIVREDYGFEDG 321
Cdd:TIGR01553 241 KWAIRAK-KKGAKIIHIDPRFNRTATVADLYAPIRSGSDIAFLNGMIKYILEKELYQKEYVVNYTNASFIVGEGFAFEDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 322 LFTGYDAEKRKYDKSTWTYELDENGFAKRDTTLQHPRCVWNLLKQHVSRYTPDVVENICGTPKDAFLKVCEYIAETSAHD 401
Cdd:TIGR01553 320 LFAGYNKETRKYDKSKWGYEFDENGNPKRDETLKHPRCVFNILKEHYSRYTPEKVSAICGTPKELFLKVYEEYCKTGKPN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 402 KTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLLSQSLPGYMTLPSEKQTDLQTY 481
Cdd:TIGR01553 400 KAMTILYALGWTQHSVGTQNIRAMSINQLLLGNIGVPGGGINALRGHSNVQGSTDHGLLMHILPGYLGTPRASIPTYEQY 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 482 LTANTPKPLLEGQVNYWGNYPKFFVSMMKAFFGDKATAENSWGFDWLPKWDKGYD-VLQYFEMMKEGKVNGYICQGFNPV 560
Cdd:TIGR01553 480 TKKFTPVSKDPQSANYWSNFPKFFASYIKSMWGDAATNENGWAYDYLPKGEDGYDsWLTLFDDMFQGKIKGFFAWGQNPL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 561 ASFPNKNKVIGCLSKLKFLVTIDPLNTETSNFWQNHGelneVDSSKIQTEVFRLPSTCFAEENGSIVNSGRWLQWHWKGA 640
Cdd:TIGR01553 560 NSGPNSNKTREALTKLKWMVVMDPFDNETGSFWRGPG----MDPKEIKTEVFFLPTAVFIEKEGSISNSGRWMQWRYKGP 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 641 DAPGIALTDGEILSGIFLRLRKMYAEQGGANPDQVLNMTWNYAIPHEPSSEEVAMESNGKALADITDPatgAVIVKKGQQ 720
Cdd:TIGR01553 636 DPPGNAIPDGDIIVELAKRVQELYAKEGGKLAEPVTKLKWDYWVPDHPDAHEIAKEINGYALKDFKVG---DVEYKKGQQ 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 721 LSSFAQLRDDGTTSCGCWIFAGSWTPEGNQMARRDNADPSGLGNTLGWAWAWPLNRRILYNRASADPQGNPWDPKRQLLK 800
Cdd:TIGR01553 713 IATFGHLRDDGSTTSGCWLYTGSYTEKGNMAARRDKSDPAGLGLYPGWTWAWPANRRVLYNRASVDLNGKPWDPERALVE 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 801 WDGTKWTgW--DIPDYSA-APPGSGVGPFIMQQEGMGRLFALDKMAEGPFPEHYEPFETPLGTNPLHPNVISNPAARIFK 877
Cdd:TIGR01553 793 WNAAEKK-WvgDIPDYPPtAPPEKGKGAFIMKPEGYGRLFAPGKREDGPLPEHYEPMESPVITNPFHPNVLHNPTALHYK 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 878 DDAEALGKADKFPYVGTTYRLTEHFHYWTKHALLNAILQPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKR 957
Cdd:TIGR01553 872 TDEKAVGDPKRYPFVATTYRLTEHWHTWTRNTPWLLEAEPQMFCEISEELATEKGIQNGDKVILESVRGKIWAKAIVTKR 951
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*...
gi 501574638 958 IRTLKANGKDIDTIGIPIHWGYEGVAKKGFIANTLTPFVGDANTQTPEFKSFLVNVEK 1015
Cdd:TIGR01553 952 IKPLAIQGQQVHMIGIPIHWGWSFLKNGGDATNILTPSVGDPNTGTPETKAFLVNIEK 1009
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
47-874 |
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: 979.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 47 RNTCTYCSVGCGLLMYSLGDgaknakaSIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAPGSDKWQQISW 126
Cdd:cd02752 1 RTICPYCSVGCGLIAYVQNG-------VWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGSGKWEEISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 127 EEAFDRIAKLMKEDRDANYIAQNAEGVTVNRWLSTGMLCASASSNETGYLTQKFSRALGMLAVDNQARVUHGPTVASLAP 206
Cdd:cd02752 74 DEALDEIARKMKDIRDASFVEKNAAGVVVNRPDSIAFLGSAKLSNEECYLIRKFARALGTNNLDHQARIUHSPTVAGLAN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 207 TFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKIHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSG 286
Cdd:cd02752 154 TFGRGAMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEKNGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 287 VLLYLLnnekfnreyteaytnaslivredygfedglftgydaekrkydkstwtyeldengfakrdttlqhprcvwnllkq 366
Cdd:cd02752 234 MINYII-------------------------------------------------------------------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 367 hvsRYTPDVVENICGTPKDAFLKVCEYIAETSAHDKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALR 446
Cdd:cd02752 240 ---RYTPEEVEDICGVPKEDFLKVAEMFAATGRPDKPGTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALR 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 447 GHSNIQGLTDLGLLSQSLPGYMTlpsekqtdlqtyltantpkpllegqvnywgnypkffvsmmkaffgdkataenswgfd 526
Cdd:cd02752 317 GHSNVQGATDLGLLSHNLPGYLG--------------------------------------------------------- 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 527 wlpkwdkgydvlqyfemmkegkvngyicqGFNPVASFPNKNKVIGCLSKLKFLVTIDPLNTETSNFWQNHGelneVDSSK 606
Cdd:cd02752 340 -----------------------------GQNPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKNPG----MDPKS 386
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 607 IQTEVFRLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIALTDGEILSGIFLRLRKMYAEQGGANPDQVLNmtWNYAIPH 686
Cdd:cd02752 387 IQTEVFLLPAACQYEKEGSITNSGRWLQWRYKVVEPPGEAKSDGDILVELAKRLGFLYEKEGGAFPEPITK--WNYGYGD 464
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 687 EPSSEEVAMESNGKALADITDPATGAVIVKKGQQLSSFAQLRDDGTTSCGCWIFAGSWTPEGNqMARRDNADPSGLGNTL 766
Cdd:cd02752 465 EPTPEEIAREINGGALTDGYTGQSPERLKAHGQNVHTFDTLRDDGSTACGCWIYSGSYTEEGR-MARRDTSDPDGLGLYP 543
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 767 GWAWAWPLNRRILYNRASADPQGNPWDPKRQLLKWDGTK-WTGWDIPDYSA-APPGSGVGPFIMQQEGMGRLFALDKmaE 844
Cdd:cd02752 544 GWPWPWPVNRRILYNRASVDMEGKPGYPERPLVEWDGLGwWWKGDVPDGPWpAAKEHGCGPFIMAPEGQARLFVWNF--D 621
|
810 820 830
....*....|....*....|....*....|
gi 501574638 845 GPFPEHYEPFETPLGTNplHPNVISNPAAR 874
Cdd:cd02752 622 GPFPEHYEPLESPRPDL--HSKVAKNPTYK 649
|
|
| formate_DH_Act |
NF041513 |
formate dehydrogenase; Members of this family are the enzyme formate dehydrogenase, of a type ... |
24-1013 |
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: 917.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 24 LGFAPSVALAETRQYKLlRT----RETRNTCTYCSVGCGLLMYslgdgAKNAKasIFHIEGDPDHPVNRGALCPKGAGLV 99
Cdd:NF041513 18 LGRGAAARSARTRALRP-RTatadRVVRSVCPYCAVGCGQKVY-----VKDEK--VVQIEGDPDSPISRGRLCPKGSASL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 100 DFIHSESRLKFPEYRAPGSDKWQQISWEEAFDRIAKLMKEDRDANYIAQNAEGVTVNRWLSTGMLCASASSNETGYLTQK 179
Cdd:NF041513 90 QLVTGPTRVTTVLYRRPYGTEWEELDLDTAMDMIADRVLDTRRETWQDEDDDGRRLRRTMGIASLGGATLDNEENYLIKK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 180 FSRALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVID 259
Cdd:NF041513 170 LFTALGAVQVENQARIUHSSTVPGLGTSFGRGGATTFLQDLANSDCIVIQGSNMAEAHPVGFQWVMEAK-ARGATVIHVD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 260 PRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLLNNEKFNREYTEAYTNASLIVREDY-GFED--GLFTGYDAEKRKYDKS 336
Cdd:NF041513 249 PRFTRTSALADLHVPIRAGSDIAFLGGLINHVLSNELYFREYVLAYTNAATIVSEDFrDTEDldGLFSGFDPETGSYDPA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 337 TWTYELDEN----------------------------------GFAKRDTTLQHPRCVWNLLKQHVSRYTPDVVENICGT 382
Cdd:NF041513 329 SWQYEGVEVaaaagqrdqlydsrggahesargeehgsggapvaGAPRRDETLQDPRCVFQILKRHFARYTPEMVEEICGI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 383 PKDAFLKVCEYIAETSAHDKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLLSQ 462
Cdd:NF041513 409 PRELFLKVADALTANSGRERTTAFCYAVGWTQHTVGVQYIRAASILQLLLGNIGRPGGGIMALRGHASIQGSTDIPTLFN 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 463 SLPGYMTLP-SEKQTDLQTYLTANTPkpllegQVNYWGNYPKFFVSMMKAFFGDKATAENSWGFDWLPKWDKGYDVLQYF 541
Cdd:NF041513 489 LLPGYLPMPhAHKHEDLDSYVEANAS------QKGFWANMRAYTVSLLKAWWGDAATAENDFCFDYLPRLTGDHSTYQTV 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 542 EMMKEGKVNGYICQGFNP-VASFPNKNKVIGcLSKLKFLVTIDPLNTETSNFWQNHGELN--EVDSSKIQTEVFRLPSTC 618
Cdd:NF041513 563 MAMLDGKVKGYFLMGENPaVGSANGRLQRLG-MANLDWLVVRDFSLIESATFWKDGPEIEtgELRTEDIGTEVFFFPAAA 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 619 FAEENGSIVNSGRWLQWHWKGADAPGIALTDGEILSGIFLRLRKMYAEQGGANPDQVLNMTWNYAI--PH-EPSSEEVAM 695
Cdd:NF041513 642 HTEKSGTFTNTQRLLQWRHQAVEPPGDARSDLWFFYHLGRRIREKLAGSTDPRDRPLLDLTWDYPTegPHgEPDAEAVLA 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 696 ESNGKALAditdpatgavivkkGQQLSSFAQLRDDGTTSCGCWIFAGSWTPEGNQMARRDnadPSGLGNTLG--WAWAWP 773
Cdd:NF041513 722 EINGYDLS--------------GRPLSAYTELKDDGSTSCGCWIYCGVYADGVNQAARRK---PGREQDWVAaeWGWAWP 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 774 LNRRILYNRASADPQGNPWDPKRQLLKWDGTK--WTGWDIPDYSAA-------PPG-------SGVGPFIMQQEGMGRLF 837
Cdd:NF041513 785 ANRRILYNRASADPEGRPWSERKKYVWWDAEAgrWTGYDVPDFPVDkppdyrpPPGatgpaalSGDDPFIMQADGKGWLF 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 838 ALDKMAEGPFPEHYEPFETPLGtNPLHPNViSNPAARIFKDDAEALGK------ADKFPYVGTTYRLTEHF-----HYWT 906
Cdd:NF041513 865 APAGLVDGPLPTHYEPQESPVR-NPLYGQQ-RNPARKVYPREDNRYHPsggepgAEVYPYVFTTYRLTEHHtaggmSRWL 942
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 907 KHAllnAILQPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTLKANGKDIDTIGIPIHWGYEGVAkKG 986
Cdd:NF041513 943 PYL---AELQPEMFCEVSPELAAERGLENGGWATIVTARGAIEARVLVTDRMTPLRVQGRTVHQIGLPYHWGPNGLV-TG 1018
|
1050 1060
....*....|....*....|....*..
gi 501574638 987 FIANTLTPFVGDANTQTPEFKSFLVNV 1013
Cdd:NF041513 1019 DAANELLGITLDPNVHIQESKALTCDI 1045
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
43-1016 |
1.13e-153 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 471.29 E-value: 1.13e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 43 TRETRNTCTYCSVGCGLLMYSLGDGaknakasIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAPGsdKWQ 122
Cdd:COG3383 4 MKKVKTVCPYCGVGCGIDLEVKDGK-------IVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGG--EFR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 123 QISWEEAFDRIAKLMKEDRDANyiaqNAEGVtvnrwlstGMLCASASSNETGYLTQKFSRA-LGMLAVDNQARVUHGPTV 201
Cdd:COG3383 75 EVSWDEALDLVAERLREIQAEH----GPDAV--------AFYGSGQLTNEENYLLQKLARGvLGTNNIDNNARLCMASAV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 202 ASLAPTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDI 281
Cdd:COG3383 143 AGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAK-KNGAKLIVVDPRRTETARLADLHLQIKPGTDL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 282 AFLSGVLLYLLNNEKFNREYTEAYTNaslivredyGFEDglftgydaekrkydkstwtyeldengfakrdttlqhprcvw 361
Cdd:COG3383 222 ALLNGLLHVIIEEGLVDEDFIAERTE---------GFEE----------------------------------------- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 362 nlLKQHVSRYTPDVVENICGTPKDAFLKVCEYIAETsahdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGG 441
Cdd:COG3383 252 --LKASVAKYTPERVAEITGVPAEDIREAARLIAEA----KRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 442 VNALRGHSNIQGLTDLGLLSQSLPGYMTLPSEKqtdlqtyltantpkpllegqvnywgnypkffvsmmkaffgDKATAEN 521
Cdd:COG3383 326 PFPLTGQNNVQGGRDMGALPNVLPGYRDVTDPE----------------------------------------HRAKVAD 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 522 SWGFDWLPKWdKGYDVLQYFEMMKEGKVNGYICQGFNPVASFPNKNKVIGCLSKLKFLVTIDPLNTETSNFwqnhgelne 601
Cdd:COG3383 366 AWGVPPLPDK-PGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEY--------- 435
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 602 vdsskiqTEVFrLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIALTDGEILSGIflrLRKMyaeqgGANpdqvlnmtWN 681
Cdd:COG3383 436 -------ADVV-LPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIAEL---ARRL-----GYG--------FD 491
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 682 YAiphepSSEEVAMEsngkaladitdpatgavivkkgqqlssfaqlrddgttscgcwifagswtpegnqmarrdnadpsg 761
Cdd:COG3383 492 YD-----SPEEVFDE----------------------------------------------------------------- 501
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 762 lgntlgWAWAWPLNRRILYNRasadpqgnpwdpkrqLLKWDGTKWtgwdiPDYSAAPPGSgvgpfimqqegmGRLFAldk 841
Cdd:COG3383 502 ------IARLTPDYSGISYER---------------LEALGGVQW-----PCPSEDHPGT------------PRLFT--- 540
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 842 maegpfpehyEPFETPLGTNPLHPNVISNPAARIfkdDAEalgkadkFPYVGTTYRLTEHFH--YWTKHALLNAILQPEQ 919
Cdd:COG3383 541 ----------GRFPTPDGKARFVPVEYRPPAELP---DEE-------YPLVLTTGRLLDQWHtgTRTRRSPRLNKHAPEP 600
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 920 FVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlkangkdiDTIGIPIHWGYEGvakkgfiANTLTPFVGDA 999
Cdd:COG3383 601 FVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRP--------GTVFMPFHWGEGA-------ANALTNDALDP 665
|
970
....*....|....*..
gi 501574638 1000 NTQTPEFKSFLVNVEKV 1016
Cdd:COG3383 666 VSKQPEYKACAVRVEKV 682
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
49-1007 |
3.01e-129 |
|
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: 406.85 E-value: 3.01e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 49 TCTYCSVGCGLLMYslgdgAKNAKasIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRApgSDKWQQISWEE 128
Cdd:TIGR01591 2 VCPYCGVGCSLNLV-----VKDGK--IVRVEPYQGHKANRGHLCVKGYFAWEFINSKDRLTTPLIRE--GDKFREVSWDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 129 AFDRIAKLMKEDRDaNYiaqnaeGVTvnrwlSTGMLCASASSNETGYLTQKFSRA-LGMLAVDNQARVUHGPTVASLAPT 207
Cdd:TIGR01591 73 AISYIAEKLKEIKE-KY------GPD-----SIGFIGSSRGTNEENYLLQKLARAvIGTNNVDNCARVCHGPSVAGLKQT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 208 FGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGV 287
Cdd:TIGR01591 141 VGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAK-RNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 288 LLYLLNNEKFNREYTEAYTNaslivredyGFEDglftgydaekrkydkstwtyeldengfakrdttlqhprcvwnlLKQH 367
Cdd:TIGR01591 220 ANVIIEEGLYDKAFIEKRTE---------GFEE-------------------------------------------FREI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 368 VSRYTPDVVENICGTPKDAFLKvceyIAETSAHDKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:TIGR01591 248 VKGYTPEYVEDITGVPADLIRE----AARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 448 HSNIQGLTDLGLLSQSLPGYMTLPSEkqtdlqtyltantpkpllegqvnywgnypkffvSMMKAFfgdkataENSWGFDW 527
Cdd:TIGR01591 324 QNNVQGACDMGALPDFLPGYQPVSDE---------------------------------EVREKF-------AKAWGVVK 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 528 LPKwDKGYDVLQYFEMMKEGKVNGYICQGFNPVASFPNKNKVIGCLSKLKFLVTIDPLNTETSNFwqnhgelnevdsski 607
Cdd:TIGR01591 364 LPA-EPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKY--------------- 427
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 608 qTEVFrLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIALTDGEILsgiflrlrKMYAEQGGANpdqvlnmtWNYAIPHE 687
Cdd:TIGR01591 428 -ADVV-LPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEII--------QELANALGLD--------WNYNHPQE 489
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 688 psseevamesngkaladitdpatgavIVKKGQQLssfaqlrddgttscgCWIFAGswtpegnqMARRDNADPSGLgntlg 767
Cdd:TIGR01591 490 --------------------------IMDEIREL---------------TPLFAG--------LTYERLDELGSL----- 515
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 768 wawAWPLNrrilynraSADPQGNPwdpkrqLLKWDgtkwtGWDIPDysaappgsgvgpfimqqeGMGRLFALDKMAegpf 847
Cdd:TIGR01591 516 ---QWPCN--------DSDASPTS------YLYKD-----KFATPD------------------GKAKFIPLEWVA---- 551
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 848 pehyePFETPlgtnplhpnvisnpaarifkddaealgkADKFPYVGTTYRLTEHFHY--WTKHALLNAILQPEQFVEIGE 925
Cdd:TIGR01591 552 -----PIEEP----------------------------DDEYPLILTTGRVLTHYNVgeMTRRVAGLRRLSPEPYVEINT 598
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 926 SLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlkangkdiDTIGIPIHWGYEGVakkgfiaNTLTPFVGDANTQTPE 1005
Cdd:TIGR01591 599 EDAKKLGIKDGDLVKVKSRRGEITLRAKVSDRVNK--------GAIYITMHFWDGAV-------NNLTTDDLDPISGTPE 663
|
..
gi 501574638 1006 FK 1007
Cdd:TIGR01591 664 YK 665
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
16-1016 |
1.91e-120 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 383.81 E-value: 1.91e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 16 MAGTTAAALGFAPSVALAETrqykllrTRETRNTCTYCSVGCGLLMYSLGDGAKnakasifHIEGDPDHPVNRGALCPKG 95
Cdd:COG0243 1 MSLRDFKAAGAGAAALEAAG-------TKTVKTTCPGCGVGCGLGVKVEDGRVV-------RVRGDPDHPVNRGRLCAKG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 96 AGLVDFIHSESRLKFPEYR--APGSDKWQQISWEEAFDRIAKLMKEDRDAnyiaQNAEGVtvnrWLSTGMLCASASSNET 173
Cdd:COG0243 67 AALDERLYSPDRLTYPMKRvgPRGSGKFERISWDEALDLIAEKLKAIIDE----YGPEAV----AFYTSGGSAGRLSNEA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 174 GYLTQKFSRALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKIHNGA 253
Cdd:COG0243 139 AYLAQRFARALGTNNLDDNSRLCHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 254 KLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLLNNEKFNREYTEAYTNaslivredyGFEDglftgydaekrky 333
Cdd:COG0243 219 KIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVLIEEGLYDRDFLARHTV---------GFDE------------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 334 dkstwtyeldengfakrdttlqhprcvwnlLKQHVSRYTPDVVENICGTPKDAFLKVCEYIAETsahdKTASFLYALGWT 413
Cdd:COG0243 277 ------------------------------LAAYVAAYTPEWAAEITGVPAEDIRELAREFATA----KPAVILWGMGLQ 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 414 QHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSniqgltdlgllsqslpgymtlpsekqtdlqtyltantpkpLLEG 493
Cdd:COG0243 323 QHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTGEA----------------------------------------ILDG 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 494 qvnywgnypkffvsmmkaffgdkataenswgfdwlpkwdkgydvlqyfemmKEGKVNGYICQGFNPVASFPNKNKVIGCL 573
Cdd:COG0243 363 ---------------------------------------------------KPYPIKALWVYGGNPAVSAPDTNRVREAL 391
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 574 SKLKFLVTIDPLNTETSNFwqnhgelneVDsskiqtevFRLPSTCFAEENGSIVNSG-RWLQWHWKGADAPGIALTDGEI 652
Cdd:COG0243 392 RKLDFVVVIDTFLTETARY---------AD--------IVLPATTWLERDDIVTNSEdRRVHLSRPAVEPPGEARSDWEI 454
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 653 LSGIFLRLrkmyaeqgGANPdqvlnmtwnyAIPHEPSSEEVamesngkaLADITDPATGAVIvkkgqqlsSFAQLRDDGt 732
Cdd:COG0243 455 FAELAKRL--------GFEE----------AFPWGRTEEDY--------LRELLEATRGRGI--------TFEELREKG- 499
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 733 tscgcwifagswtpegnqmarrdnadpsglgntlgwAWAWPLnrrilynrasadPQGNPWdpkrqllKWDGtkwtGWDIP 812
Cdd:COG0243 500 ------------------------------------PVQLPV------------PPEPAF-------RNDG----PFPTP 520
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 813 DysaappgsgvgpfimqqegmGRL-FALDKMAEGPFPEHYEPFEtplgtnplhpnvisnpaarifkddaEALGKADKFPY 891
Cdd:COG0243 521 S--------------------GKAeFYSETLALPPLPRYAPPYE-------------------------GAEPLDAEYPL 555
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 892 VGTTYRLTEHFHYWT-KHALLNAIlQPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlkangkdiDT 970
Cdd:COG0243 556 RLITGRSRDQWHSTTyNNPRLREI-GPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRP--------GV 626
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*.
gi 501574638 971 IGIPIHWGYEGVAKKGFIANTLTPFVGDANTQTPEFKSFLVNVEKV 1016
Cdd:COG0243 627 VFAPHGWWYEPADDKGGNVNVLTPDATDPLSGTPAFKSVPVRVEKA 672
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
49-677 |
6.27e-119 |
|
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: 374.24 E-value: 6.27e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 49 TCTYCSVGCGLLMYSlgdgaKNAKasIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAPGsdKWQQISWEE 128
Cdd:cd02753 3 VCPYCGVGCGLELWV-----KDNK--IVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNG--KFVEASWDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 129 AFDRIAKLMKEDRDAnYIAQnaegvtvnrwlSTGMLCASASSNETGYLTQKFSRA-LGMLAVDNQARVUHGPTVASLAPT 207
Cdd:cd02753 74 ALSLVASRLKEIKDK-YGPD-----------AIAFFGSAKCTNEENYLFQKLARAvGGTNNVDHCARLCHSPTVAGLAET 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 208 FGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKIhNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGV 287
Cdd:cd02753 142 LGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKR-NGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 288 LLYLLNNEKFNREYTEAYTNaslivredyGFEDglftgydaekrkydkstwtyeldengfakrdttlqhprcvwnlLKQH 367
Cdd:cd02753 221 AHVIIEEGLYDEEFIEERTE---------GFEE-------------------------------------------LKEI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 368 VSRYTPDVVENICGTPKDAFLKvceyIAETSAHDKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:cd02753 249 VEKYTPEYAERITGVPAEDIRE----AARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 448 HSNIQGLTDLGLLSQSLPGYmtlpsekqtdlqtyltantpkpllegqvnywgnypkffvsmmkaffgdkataenswgfdw 527
Cdd:cd02753 325 QNNVQGACDMGALPNVLPGY------------------------------------------------------------ 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 528 lpkwdkgydvlqyfemmkegkVNGYICQGFNPVASFPNKNKVIGCLSKLKFLVTIDPLNTETSNFwqnhgelnevdsski 607
Cdd:cd02753 345 ---------------------VKALYIMGENPALSDPNTNHVRKALESLEFLVVQDIFLTETAEL--------------- 388
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 608 qTEVFrLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIALTDGEILSGIflrLRKMYAEQGGANPDQVLN 677
Cdd:cd02753 389 -ADVV-LPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQEL---ANRLGYPGFYSHPEEIFD 453
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
47-660 |
1.94e-88 |
|
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: 294.90 E-value: 1.94e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 47 RNTCTYCSVGCGLLMYSLGDGAKNAKasifhieGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAPGSdKWQQISW 126
Cdd:cd02754 1 KTTCPYCGVGCGVEIGVKDGKVVAVR-------GDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGG-ELVPVSW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 127 EEAFDRIAKLMKEdrdanyiAQNAEGVTVNRWLSTGMLCasassNETGYLTQKFSRA-LGMLAVDNQARVUHGPTVASLA 205
Cdd:cd02754 73 DEALDLIAERFKA-------IQAEYGPDSVAFYGSGQLL-----TEEYYAANKLAKGgLGTNNIDTNSRLCMASAVAGYK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 206 PTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAK-IHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFL 284
Cdd:cd02754 141 RSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDRKkANPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 285 SGVLLYLLNNEKFNREYTEAYTNaslivredyGFEDglftgydaekrkydkstwtyeldengfakrdttlqhprcvwnlL 364
Cdd:cd02754 221 NGLLHVLIEEGLIDRDFIDAHTE---------GFEE-------------------------------------------L 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 365 KQHVSRYTPDVVENICGTPKDAFLKVCEYIAETsahdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNA 444
Cdd:cd02754 249 KAFVADYTPEKVAEITGVPEADIREAARLFGEA----RKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFS 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 445 LRGHSNIQGLTDLGLLSQSLPGYMTLPSEKqtdlqtyltantpkpllegqvnywgnypkffvsmmkaffgDKATAENSWG 524
Cdd:cd02754 325 LTGQPNAMGGREVGGLANLLPGHRSVNNPE----------------------------------------HRAEVAKFWG 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 525 FDWLPKWDK-GYDVLQYFEMMKEGKVNGYICQGFNPVASFPNKNKVIGCLSKLKFLVTIDP-LNTETsnfwqnhGELNEV 602
Cdd:cd02754 365 VPEGTIPPKpGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVVVQDAfADTET-------AEYADL 437
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 501574638 603 dsskiqtevfRLPSTCFAEENGSIVNSGRWLQwHWKGA-DAPGIALTDGEILSGIFLRL 660
Cdd:cd02754 438 ----------VLPAASWGEKEGTMTNSERRVS-LLRAAvEPPGEARPDWWILADVARRL 485
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
47-660 |
8.51e-84 |
|
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: 275.75 E-value: 8.51e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 47 RNTCTYCSVGCGLLMYSlgdgaKNAKasIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAPGSDKWQQISW 126
Cdd:cd00368 1 PSVCPFCGVGCGILVYV-----KDGK--VVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGRGKFVPISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 127 EEAFDRIAKLMKEDRDAnyiaqnaegvtvNRWLSTGMLCASASSNETGYLTQKFSRALGMLAVDNQARVUHGPTVASLaP 206
Cdd:cd00368 74 DEALDEIAEKLKEIREK------------YGPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAAL-K 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 207 TFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSG 286
Cdd:cd00368 141 AFGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAK-KRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 287 vllyllnnekfnreyteaytnaslivredygfedglftgydaekrkydkstwtyeldengfakrdttlqhprcvwnllkq 366
Cdd:cd00368 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 367 hvsrytpDVVENICGTPKDAFLKVCEYIAETsahdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNAlr 446
Cdd:cd00368 220 -------EWAAEITGVPAETIRALAREFAAA----KRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP-- 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 447 ghsniqgltdlgllsqslpgymtlpsekqtdlqtyltantpkpllegqvnywgnypkffvsmmkaffgdkataenswgfd 526
Cdd:cd00368 --------------------------------------------------------------------------------
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 527 wlpkwdkgydvlqyfemmkegkvngyicqGFNPVASFPNKNKVIGCLSKLKFLVTIDPLNTETSNFwqnhgelnevdssk 606
Cdd:cd00368 287 -----------------------------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAY-------------- 323
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 501574638 607 iqtEVFRLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIALTDGEILSGIFLRL 660
Cdd:cd00368 324 ---ADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
887-1015 |
3.45e-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: 3.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 887 DKFPYVGTTYRLTEHFHYW--TKHALLNAILQPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlkan 964
Cdd:cd02792 1 EEFPLVLTTGRLTEHFHGGnmTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKP---- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 501574638 965 gkdiDTIGIPIHWGYEGVAkKGFIANTLTPFVGDANTQTPEFKSFLVNVEK 1015
Cdd:cd02792 77 ----HEVGIPYHWGGMGLV-IGDSANTLTPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
107-583 |
1.59e-49 |
|
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: 185.20 E-value: 1.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 107 RLKFPEYRAPGSDKWQQISWEEAFDRIAKLMKE---DRDANYiaqnaegvtvnrwlSTGMlcasaSSNETGYLTQKFSRA 183
Cdd:cd02767 64 RLTYPMRYDAGSDHYRPISWDEAFAEIAARLRAldpDRAAFY--------------TSGR-----ASNEAAYLYQLFARA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 184 LGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDP--- 260
Cdd:cd02767 125 YGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLEDFEHTDLIFFIGQNPGTNHPRMLHYLREAK-KRGGKIIVINPlre 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 261 ----RF----------TRTAAVADYYAPIRSGTDIAFLSGVLLYLLNNEK-----FNREYTEAYTNaslivredyGFEDg 321
Cdd:cd02767 204 pgleRFanpqnpesmlTGGTKIADEYFQVRIGGDIALLNGMAKHLIERDDepgnvLDHDFIAEHTS---------GFEE- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 322 lftgydaekrkydkstwtyeldengfakrdttlqhprcvwnlLKQHVSRYTPDVVENICGTPKDAFLKVceyiAETSAHD 401
Cdd:cd02767 274 ------------------------------------------YVAALRALSWDEIERASGLSREEIEAF----AAMYAKS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 402 KTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLlsqslpgymtlpsekqtdlqty 481
Cdd:cd02767 308 ERVVFVWGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGI---------------------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 482 ltanTPKPLLEgqvnywgnypkFFVSMmkaffgdkataENSWGFDwLPKWdKGYDVLQYFEMMKEGKVNGYICQGFNPVA 561
Cdd:cd02767 366 ----TEKPFPE-----------FLDAL-----------EEVFGFT-PPRD-PGLDTVEAIEAALEGKVKAFISLGGNFAE 417
|
490 500
....*....|....*....|..
gi 501574638 562 SFPNKNKVIGCLSKLKFLVTID 583
Cdd:cd02767 418 AMPDPAATEEALRRLDLTVHVA 439
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
48-440 |
1.47e-46 |
|
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: 173.64 E-value: 1.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 48 NTCTYCSVGCGLLMYslgdgAKNAKAsiFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAP--GSDKWQQIS 125
Cdd:cd02755 3 SICEMCSSRCGILAR-----VEDGRV--VKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGerGEGKFREAS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 126 WEEAFDRIAKLMKEDRDAnyiaQNAEGVTVNRWLSTGMlcasassnetgYLTQKFSRALGMLAVDNQARVUHGP-TVASL 204
Cdd:cd02755 76 WDEALQYIASKLKEIKEQ----HGPESVLFGGHGGCYS-----------PFFKHFAAAFGSPNIFSHESTCLASkNLAWK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 205 APTFGRGAMTNhwVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKIHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFL 284
Cdd:cd02755 141 LVIDSFGGEVN--PDFENARYIILFGRNLAEAIIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 285 SGVLLYLLNNEKFNREYTEAYTNaslivredyGFEdglftgydaekrkydkstwtyeldengfakrdttlqhprcvwnLL 364
Cdd:cd02755 219 LALIHVLISENLYDAAFVEKYTN---------GFE-------------------------------------------LL 246
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501574638 365 KQHVSRYTPDVVENICGTPKDAFLKVCEYIAETSAHDKTASFLYALgWTQHSIGAQniRTMAMIQLLLGNMGMAGG 440
Cdd:cd02755 247 KAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAPHAVVDPGWRGT-FYSNSFQTR--RAIAIINALLGNIDKRGG 319
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
49-444 |
1.69e-45 |
|
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: 171.33 E-value: 1.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 49 TCTYCSVGCGLLMYslgdgAKNAKasIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRA--PGSDKWQQISW 126
Cdd:cd02759 3 TCPGCHSGCGVLVY-----VKDGK--LVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVgeRGENKWERISW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 127 EEAFDRIAKLMKEDRdANYiaqNAEGVTVnrWLSTGMLCASASSNETGYLTQKFSRALGMLAVDnqarVUHGPT-VASLA 205
Cdd:cd02759 76 DEALDEIAEKLAEIK-AEY---GPESIAT--AVGTGRGTMWQDSLFWIRFVRLFGSPNLFLSGE----SCYWPRdMAHAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 206 PTFGRGAMTNHwvDIKNANLVVVMGGNAAEAHPVGFRWAMEAKIHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLS 285
Cdd:cd02759 146 TTGFGLGYDEP--DWENPECIVLWGKNPLNSNLDLQGHWLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 286 GVLLYLLNNEKFNREYTEAYTnaslivredYGFEDglftgydaekrkydkstwtyeldengfakrdttlqhprcvwnlLK 365
Cdd:cd02759 224 GMLNVIINEGLYDKDFVENWC---------YGFEE-------------------------------------------LA 251
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501574638 366 QHVSRYTPDVVENICGTPKDAFLKVCEYIAETsahdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNA 444
Cdd:cd02759 252 ERVQEYTPEKVAEITGVPAEKIRKAARLYATA----KPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGNLLI 326
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
47-454 |
2.67e-45 |
|
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: 171.28 E-value: 2.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 47 RNTCTY-CSVGCGLLMYSLGDGAKNakasifhIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRA-PGSDKWQQI 124
Cdd:cd02766 1 RSVCPLdCPDTCSLLVTVEDGRIVR-------VEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVgRKGGQWERI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 125 SWEEAFDRIAKLMKEDRDAnyiaQNAEGVTVNRWLSTGMLCASASSNEtgyltqkFSRALGMLAVDNQarVUHGPTVASL 204
Cdd:cd02766 74 SWDEALDTIAAKLKEIKAE----YGPESILPYSYAGTMGLLQRAARGR-------FFHALGASELRGT--ICSGAGIEAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 205 APTFGRgAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFL 284
Cdd:cd02766 141 KYDFGA-SLGNDPEDMVNADLIVIWGINPAATNIHLMRIIQEAR-KRGAKVVVIDPYRTATAARADLHIQIRPGTDGALA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 285 SGVLLYLLNNEKFNREYTEAYTnaslivredYGFEDglftgydaekrkydkstwtyeldengfakrdttlqhprcvwnlL 364
Cdd:cd02766 219 LGVAKVLFREGLYDRDFLARHT---------EGFEE-------------------------------------------L 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 365 KQHVSRYTPDVVENICGTPKDAFLKVCEYIAETsahdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNA 444
Cdd:cd02766 247 KAHLETYTPEWAAEITGVSAEEIEELARLYGEA----KPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGGAFY 322
|
410
....*....|
gi 501574638 445 LRGHSNIQGL 454
Cdd:cd02766 323 SNSGPPVKAL 332
|
|
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
107-589 |
1.73e-43 |
|
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: 169.99 E-value: 1.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 107 RLKFPEYRAPGSDKWQQISWEEAFDRIAKLMKE---DRDANYiaqnaegvtvnrwlSTGMlcasaSSNETGYLTQKFSRA 183
Cdd:TIGR01701 99 RLTYPLSLRPGSDHYTPISWDDAYQEIAAKLNSldpKQVAFY--------------TSGR-----TSNEAAYLYQLFARS 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 184 LGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDP--- 260
Cdd:TIGR01701 160 LGSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAK-KRGAKIIAINPlre 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 261 ----RFTRTAA-----------VADYYAPIRSGTDIAFLSGVLLYLLNNEK------FNREYTEAYTNaslivredygfe 319
Cdd:TIGR01701 239 rgleRFWIPQIpesmltgggtqISSEYYQVRIGGDIALFNGVMKLLIEAEDaqpgslIDHEFIANHTN------------ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 320 dglftgydaekrkydkstwtyeldenGFAKrdttlqhprcvwnlLKQHVSRYTPDVVENICGTPKDAFLKVCEYIAETSA 399
Cdd:TIGR01701 307 --------------------------GFDE--------------LRRHVLQLNWNDIERSSGLSQEEILEFAKLLANSRR 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 400 hdktASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGltdlgllsqslpgymtlpsekqtdlq 479
Cdd:TIGR01701 347 ----VVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQG-------------------------- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 480 tyltantpkpllEGQVNYWGNYPKFFvsmmkaffgdKATAENSWGFDwLPKWdKGYDVLQYFEMMKEGKVNGYICQGFNP 559
Cdd:TIGR01701 397 ------------DRTMGITEKPEEEF----------LARLSQIYGFT-PPDW-PGDTTVAMIEAILTGKVRAFICLGGNF 452
|
490 500 510
....*....|....*....|....*....|
gi 501574638 560 VASFPNKNKVIGCLSKLKFLVTIDPLNTET 589
Cdd:TIGR01701 453 LEAMPDTAAIERALRQLDLRVHVATKLNRS 482
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
887-1015 |
4.58e-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: 4.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 887 DKFPYVGTTYRLTEHFHYW--TKHALLNAILQPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRtlkan 964
Cdd:cd00508 1 EEYPLVLTTGRLLEHWHTGtmTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVR----- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 501574638 965 gkdIDTIGIPIHWGYEGvakKGFIANTLTPFVGDANTQTPEFKSFLVNVEK 1015
Cdd:cd00508 76 ---PGTVFMPFHWGGEV---SGGAANALTNDALDPVSGQPEFKACAVRIEK 120
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
51-453 |
6.42e-40 |
|
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: 156.49 E-value: 6.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 51 TYCSVGCG---LLMYSLGDGaknakaSIFHIEGD--PDHPVNRGalCPKGAGLVDFIHSESRLKFPEYRAP--GSDKWQQ 123
Cdd:cd02765 2 TACPPNCGgrcPLKCHVRDG------KIVKVEPNewPDKTYKRG--CTRGLSHLQRVYSPDRLKYPMKRVGerGEGKFER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 124 ISWEEAFDRIAKLMKEDRDaNYIAQNAEGVTVNRWLSTGMLCASASSNETGYLTQKF----SRALGMlavdnqarvuhgp 199
Cdd:cd02765 74 ITWDEALDTIADKLTEAKR-EYGGKSILWMSSSGDGAILSYLRLALLGGGLQDALTYgidtGVGQGF------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 200 tvaSLAPTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTAAVADYYAPIRSGT 279
Cdd:cd02765 140 ---NRVTGGGFMPPTNEITDWVNAKTIIIWGSNILETQFQDAEFFLDAR-ENGAKIVVIDPVYSTTAAKADQWVPIRPGT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 280 DIAFLSGVLLYLLNNEKFNREYTEAYTNASLIVREDYG----FEDGLFTGYDAEKRKYDKSTWTYE-LDENG--FAKR-- 350
Cdd:cd02765 216 DPALALGMINYILEHNWYDEAFLKSNTSAPFLVREDNGtllrQADVTATPAEDGYVVWDTNSDSPEpVAATNinPALEge 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 351 ---DTTLQHPrcVWNLLKQHVSRYTPDVVENICGTPKdaflKVCEYIAETSAHDKtASFLYALGWTQH-SIGAQNIRTMA 426
Cdd:cd02765 296 ytiNGVKVHT--VLTALREQAASYPPKAAAEICGLEE----AIIETLAEWYATGK-PSGIWGFGGVDRyYHSHVFGRTAA 368
|
410 420 430
....*....|....*....|....*....|.
gi 501574638 427 MIQLLLGNMGMAGGGVNALRG----HSNIQG 453
Cdd:cd02765 369 ILAALTGNIGRVGGGVGQIKFmyfmGSNFLG 399
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
49-590 |
3.74e-35 |
|
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: 141.77 E-value: 3.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 49 TCTYCSVGCGLLMYSlgDGAKNAKasifhIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAPGSdkWQQISWEE 128
Cdd:cd02762 3 ACILCEANCGLVVTV--EDGRVAS-----IRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRRRGGS--FEEIDWDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 129 AFDRIAKLMKEDRDANyiAQNAEGVtvnrWLSTGMLCASASSNETGYLTqkfsRALGMLAVDNQARVUHGPTVASLAPTF 208
Cdd:cd02762 74 AFDEIAERLRAIRARH--GGDAVGV----YGGNPQAHTHAGGAYSPALL----KALGTSNYFSAATADQKPGHFWSGLMF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 209 GRGaMTNHWVDIKNANLVVVMGGNAAEAHpvGFRWAM-------EAKIHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDI 281
Cdd:cd02762 144 GHP-GLHPVPDIDRTDYLLILGANPLQSN--GSLRTApdrvlrlKAAKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 282 AFLSGvLLYLLnnekfnreyteaytnaslivredygFEDGLFtgydaekrkydkstwtyelDENGFAKRDTTLQHprcvw 361
Cdd:cd02762 221 WLLAA-MLAVL-------------------------LAEGLT-------------------DRRFLAEHCDGLDE----- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 362 nlLKQHVSRYTPDVVENICGTPKDAFLKVCEYIAetSAhdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGg 441
Cdd:cd02762 251 --VRAALAEFTPEAYAPRCGVPAETIRRLAREFA--AA--PSAAVYGRLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGG- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 442 vnalrghsniqgltdlGLLSQSLpgymtLPSEKQTDLQTYLTANTPKPllegqvnywgnypkffVSMMKAFFGD---KAT 518
Cdd:cd02762 324 ----------------AMFTTPA-----LDLVGQTSGRTIGRGEWRSR----------------VSGLPEIAGElpvNVL 366
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501574638 519 AEnswgfdwlpkwdkgydvlqyfEMMK--EGKVNGYICQGFNPVASFPNKNKVIGCLSKLKFLVTIDPLNTETS 590
Cdd:cd02762 367 AE---------------------EILTdgPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETT 419
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
49-440 |
1.17e-31 |
|
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: 131.02 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 49 TCTYCSVGCGLLMYslgdgAKNAKASifHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRA------PGSDKWQ 122
Cdd:cd02757 5 TCQGCTAWCGLQAY-----VEDGRVT--KVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTnprkgrDVDPKFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 123 QISWEEAFD----RIAKLMKEDRDANYIaqnaegVTVNRWlstgmlcasasSNETGYLTQKFSRALGMLAVDNQARVUhg 198
Cdd:cd02757 78 PISWDEALDtiadKIRALRKENEPHKIM------LHRGRY-----------GHNNSILYGRFTKMIGSPNNISHSSVC-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 199 ptvaSLAPTFGRGAMTNHW----VDIKNANLVVVMGGNAAEA-HPVGFRWAMEAKIHNGAKLIVIDPRFTRTAAVADYYA 273
Cdd:cd02757 139 ----AESEKFGRYYTEGGWdynsYDYANAKYILFFGADPLESnRQNPHAQRIWGGKMDQAKVVVVDPRLSNTAAKADEWL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 274 PIRSGTDIAFLSGVLLYLLNNEKFNREYTEAYTNASLIVREDYGFEDGLFtgydaekrkydKSTWTYELDEngfakrdtt 353
Cdd:cd02757 215 PIKPGEDGALALAIAHVILTEGLWDKDFVGDFVDGKNYFKAGETVDEESF-----------KEKSTEGLVK--------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 354 lqhprcvWnlLKQHVSRYTPDVVENICGTPKDAFLKVCEYIAetSAHDKTASFLYAlGWTQHSIGAQNIRTMAMIQLLLG 433
Cdd:cd02757 275 -------W--WNLELKDYTPEWAAKISGIPAETIERVAREFA--TAAPAAAAFTWR-GATMQNRGSYNSMACHALNGLVG 342
|
....*..
gi 501574638 434 NMGMAGG 440
Cdd:cd02757 343 SIDSKGG 349
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
79-449 |
7.84e-31 |
|
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: 129.36 E-value: 7.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 79 EGDPDHPVNRGalCPKGAGLVDFIHSESRLKFPEYRAP--GSDKWQQISWEEAFDRIAKLMKEDRDaNYiaqNAEGVTVN 156
Cdd:cd02770 33 DDDPGFHQIRA--CLRGRSQRKRVYNPDRLKYPMKRVGkrGEGKFVRISWDEALDTIASELKRIIE-KY---GNEAIYVN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 157 rwlstgmlCASASSNETGYLTQKFSRALGMLA--VDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLVVVMGGNAA 234
Cdd:cd02770 107 --------YGTGTYGGVPAGRGAIARLLNLTGgyLNYYGTYSWAQITTATPYTYGAAASGSSLDDLKDSKLVVLFGHNPA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 235 EAHPVGFR---WAMEAKiHNGAKLIVIDPRFTRTAAV-ADYYAPIRSGTDIAFLSGVLLYLLNNEKFNREYTEAYTnasl 310
Cdd:cd02770 179 ETRMGGGGstyYYLQAK-KAGAKFIVIDPRYTDTAVTlADEWIPIRPGTDAALVAAMAYVMITENLHDQAFLDRYC---- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 311 ivredYGF-EDGLFTGYDAEKRKYDkstwtYEL--DENGFAKrdttlqhprcvwnllkqhvsryTPDVVENICGTPKDAF 387
Cdd:cd02770 254 -----VGFdAEHLPEGAPPNESYKD-----YVLgtGYDGTPK----------------------TPEWASEITGVPAETI 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501574638 388 LKVCEYIAETsahdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGvNALRGHS 449
Cdd:cd02770 302 RRLAREIATT----KPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGN-TGARPGG 358
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
102-582 |
7.59e-29 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 124.39 E-value: 7.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 102 IHSESRLKFPEYRAPGSDKWQQISWEEAFDRIAKLMKEDRDANYIAQNAEGVTvnrwlstgmlcasasSNETGYLTQKFS 181
Cdd:PRK09939 103 LEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRT---------------SNEAAFLYQLFA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 182 RALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRwAMEAKIHNGAKLIVIDP- 260
Cdd:PRK09939 168 REYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLT-SLRALVKRGAKMIAINPl 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 261 ------RFT-----------RTAAVADYYAPIRSGTDIAFLSGVLLYLLNNEkfnrEYTEAYTNASLIvreDYGFEDGLF 323
Cdd:PRK09939 247 qergleRFTapqnpfemltnSETQLASAYYNVRIGGDMALLKGMMRLLIERD----DAASAAGRPSLL---DDEFIQTHT 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 324 TGYDAEKRKYDKSTWtyeldengfakRDttlqhprcvwnllkqhvsrytpdvVENICGTPKdafLKVCEYIAETSAHDKT 403
Cdd:PRK09939 320 VGFDELRRDVLNSEW-----------KD------------------------IERISGLSQ---TQIAELADAYAAAERT 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 404 AsFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLlsqslpgymtlpsekqtdlqtylt 483
Cdd:PRK09939 362 I-ICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGI------------------------ 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 484 anTPKPLLEgqvnywgnypkfFVSMMKAFFGdkataenswgfdWLPKWDKGYDVLQYFEMMKEGKVNGYICQGFNPVASF 563
Cdd:PRK09939 417 --TEKPSAE------------FLARLGERYG------------FTPPHAPGHAAIASMQAICTGQARALICMGGNFALAM 470
|
490
....*....|....*....
gi 501574638 564 PNKNKVIGCLSKLKFLVTI 582
Cdd:PRK09939 471 PDREASAVPLTQLDLAVHV 489
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
2-447 |
3.62e-28 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 122.06 E-value: 3.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 2 QVSRRQFFKICA-GGMA-GTTAAALGFAPSVALAETRQYKLLRTRETRNTCTY-CSVGCGLLMYSLgDGAknakasIFHI 78
Cdd:PRK14990 13 EVSRRGLVKTTAiGGLAmASSALTLPFSRIAHAVDSAIPTKSDEKVIWSACTVnCGSRCPLRMHVV-DGE------IKYV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 79 EGDPDHPVNRGAL-----CPKGAGLVDFIHSESRLKFPEYR--APGSDKWQQISWEEAFDRIA----KLMKEDRDA---- 143
Cdd:PRK14990 86 ETDNTGDDNYDGLhqvraCLRGRSMRRRVYNPDRLKYPMKRvgARGEGKFERISWEEAYDIIAtnmqRLIKEYGNEsiyl 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 144 NYIAQNAEGVTVNRWLSTGMLCASASSNETGYLTQKFSRALGMLAvdnqarvuhgptvASLAPTFGRGAMTNHWVDIKNA 223
Cdd:PRK14990 166 NYGTGTLGGTMTRSWPPGNTLVARLMNCCGGYLNHYGDYSSAQIA-------------EGLNYTYGGWADGNSPSDIENS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 224 NLVVVMGGNAAEAHPVG---FRWAMEAKIHNGAKLIVIDPRFTRT-AAVADYYAPIRSGTDIAFLSGvLLYLLNNEKFnr 299
Cdd:PRK14990 233 KLVVLFGNNPGETRMSGggvTYYLEQARQKSNARMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNG-LAYVMITENL-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 300 eyteaytnaslivrEDYGFEDGLFTGydaekrkYDKSTWTYELDENGFAKRDTTLQHPRCVWNllkqhvsryTPDVVENI 379
Cdd:PRK14990 310 --------------VDQPFLDKYCVG-------YDEKTLPASAPKNGHYKAYILGEGPDGVAK---------TPEWASQI 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501574638 380 CGTPKDAFLKVCEYIAETsahdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:PRK14990 360 TGVPADKIIKLAREIGST----KPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGAREG 423
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
49-440 |
6.58e-28 |
|
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: 120.71 E-value: 6.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 49 TCTYCSVGCGLLMYsLGDGaknakaSIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAP--GSDKWQQISW 126
Cdd:cd02763 3 TCYMCACRCGIRVH-LRDG------KVRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKGprGSGQFEEIEW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 127 EEAFDRIAKLMKEDRdanyiAQNAEGVTvnrwLSTGmlcasasSNETGYLTQKFSRALGMLAVDNQARVUHGPTVASLAP 206
Cdd:cd02763 76 EEAFSIATKRLKAAR-----ATDPKKFA----FFTG-------RDQMQALTGWFAGQFGTPNYAAHGGFCSVNMAAGGLY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 207 TFGRGAMTNHWVDIKNANLvVVMGGNAAEAHPVGFRWAMEAKIHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSG 286
Cdd:cd02763 140 SIGGSFWEFGGPDLEHTKY-FMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 287 VLLYLLNNEKFNREYTEAYTNASLIVredygfedglftgydaekrkydkstwtyeldengfakrdttlqhprcvwnllkq 366
Cdd:cd02763 219 LAHELLKAGLIDWEFLKRYTNAAELV------------------------------------------------------ 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 367 hvsRYTPDVVENICGTPKDAFLKVCEYIAETS-----------------AHDKT----ASFLYALGWTQHSIGAQNIRTM 425
Cdd:cd02763 245 ---DYTPEWVEKITGIPADTIRRIAKELGVTArdqpielpiawtdvwgrKHEKItgrpVSFHAMRGIAAHSNGFQTIRAL 321
|
410
....*....|....*
gi 501574638 426 AMIQLLLGNMGMAGG 440
Cdd:cd02763 322 FVLMMLLGTIDRPGG 336
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
1-440 |
1.35e-26 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 117.08 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 1 MQVSRRQFFKicaGGMAGTTAAALGFAPSVALAETRQYKLL-RTRETRNTCTYCSVGCGLLMYSLGDgaKNakasIFhIE 79
Cdd:PRK15488 1 MSLSRRDFLK---GAGAGCAACALGSLLPGALAANEIAQLKgKTKLTPSICEMCSTRCPIEARVVNG--KN----VF-IQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 80 GDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAP--GSDKWQQISWEEAFDRIAKLMkedrdaNYIAQN--AEGVTV 155
Cdd:PRK15488 71 GNPKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRVGerGEGKWQEISWDEAYQEIAAKL------NAIKQQhgPESVAF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 156 nrwlstgmlcaSASSNETGYLTQKFSRALGMLAVDNQARVUHGPTVASLAPTFGrGAMTNhwvDIKNANLVVVMGGNAAE 235
Cdd:PRK15488 145 -----------SSKSGSLSSHLFHLATAFGSPNTFTHASTCPAGYAIAAKVMFG-GKLKR---DLANSKYIINFGHNLYE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 236 AHPVGF-RWAMEAKIHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLLNNEKFNREYTEAYTNaslivre 314
Cdd:PRK15488 210 GINMSDtRGLMTAQMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTS------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 315 dyGFEDglftgydaekrkydkstwtyeldengfakrdttlqhprcvwnlLKQHVSRYTPDVVENICGTPKDAFLKVCEYI 394
Cdd:PRK15488 283 --GFEE-------------------------------------------LAASVKEYTPEWAEAISDVPADDIRRIAREL 317
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 501574638 395 AETSAHdKTASFLYALGWTQHSIgaQNIRTMAMIQLLLGNMGMAGG 440
Cdd:PRK15488 318 AAAAPH-AIVDFGHRATFTPEEF--DMRRAIFAANVLLGNIERKGG 360
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
1-567 |
9.63e-26 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 114.61 E-value: 9.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 1 MQVSRRQFFKICAggmAGTTAAALGFA-PSVALAETRQyKLLRTRETRNTCTYCSVGCGLLMyslgdGAKNAKasIFHIE 79
Cdd:PRK13532 1 MKLSRRDFMKANA---AAAAAAAAGLSlPAVANAVVGS-AQTAIKWDKAPCRFCGTGCGVLV-----GTKDGR--VVATQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 80 GDPDHPVNRGALCPKGAGLVDFIHSESRLKFP-------EYRAPGsdKWQQISWEEAFDRIAKLMKEdrdanyiAQNAEG 152
Cdd:PRK13532 70 GDPDAPVNRGLNCIKGYFLSKIMYGKDRLTQPllrmkdgKYDKEG--EFTPVSWDQAFDVMAEKFKK-------ALKEKG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 153 VTvnrwlSTGMLcasASSNET---GYLTQKFSRAlGMLA--VDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLVV 227
Cdd:PRK13532 141 PT-----AVGMF---GSGQWTiweGYAASKLMKA-GFRSnnIDPNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 228 VMGGNAAEAHPVgfRWA--MEAKI-HNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLLNNEKFNREYTEA 304
Cdd:PRK13532 212 LWGSNMAEMHPI--LWSrvTDRRLsNPDVKVAVLSTFEHRSFELADNGIIFTPQTDLAILNYIANYIIQNNAVNWDFVNK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 305 YTNASLIVrEDYGF----EDGLFTgyDAEKRKYDKSTWTYELDEngFAKrdttlqhprcvwnllkqHVSRYTPDVVENIC 380
Cdd:PRK13532 290 HTNFRKGA-TDIGYglrpTHPLEK--AAKNPGTAGKSEPISFEE--FKK-----------------FVAPYTLEKTAKMS 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 381 GTPKDAFLKVCEYIAETSAhdKTASFlYALGWTQHSIG--AQNIrtMAMIQLLLGNMGMAGGGVNALRGHSNIQGLT-DL 457
Cdd:PRK13532 348 GVPKEQLEQLAKLYADPNR--KVVSF-WTMGFNQHTRGvwANNL--VYNIHLLTGKISTPGNGPFSLTGQPSACGTArEV 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 458 GLLSQSLPGYMTLPSEKQtdlqtyltantpkpllegqvnywgnypkffvsmmkaffgdKATAENSWGfdwLPKW---DK- 533
Cdd:PRK13532 423 GTFSHRLPADMVVTNPKH----------------------------------------REIAEKIWK---LPEGtipPKp 459
|
570 580 590
....*....|....*....|....*....|....
gi 501574638 534 GYDVLQYFEMMKEGKVNGYICQGFNPVASFPNKN 567
Cdd:PRK13532 460 GYHAVAQDRMLKDGKLNAYWVMCNNNMQAGPNIN 493
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
49-440 |
2.44e-24 |
|
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: 109.74 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 49 TCTYCSVGCGLLmyslgdgAK--NAKASIFHIEGDPDHPVN---------------------------RGALCPKGAGLV 99
Cdd:cd02758 3 SCLGCWTQCGIR-------VRvdKETGKVLRIAGNPYHPLNtapslpyntplkeslylslvgenglkaRATACARGNAGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 100 DFIHSESRLKFPEYRA--PGSDKWQQISWEEAFDRIA---KLMKE----------DRDANYIAQNAE-GVTVNrwlstgM 163
Cdd:cd02758 76 QYLYDPYRVLQPLKRVgpRGSGKWKPISWEQLIEEVVeggDLFGEghveglkairDLDTPIDPDHPDlGPKAN------Q 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 164 LCASASSNETG-YLTQKFSR-ALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHW-VDIKNANLVVVMGGNAAEAHPvG 240
Cdd:cd02758 150 LLYTFGRDEGRtPFIKRFANqAFGTVNFGGHGSYCGLSYRAGNGALMNDLDGYPHVkPDFDNAEFALFIGTSPAQAGN-P 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 241 FRWA----MEAKIHNGAKLIVIDPRFTRTAAVAD---YYAPIRSGTDIAFLSGVLLYLLNNEKFNREYTEaytNASLIVR 313
Cdd:cd02758 229 FKRQarrlAEARTEGNFKYVVVDPVLPNTTSAAGeniRWVPIKPGGDGALAMAMIRWIIENERYNAEYLS---IPSKEAA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 314 EDYGFEdgLFTGydaekrkydkSTWTYELdengfAKRDTTLQhprcvwnLLKQHVSRYTPDVVENICGTPKDaflKVCEY 393
Cdd:cd02758 306 KAAGEP--SWTN----------ATHLVIT-----VRVKSALQ-------LLKEEAFSYSLEEYAEICGVPEA---KIIEL 358
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 501574638 394 IAETSAHDKTASFLYAlGWTQHSIGAQNIRTMAMIQLLLGNMGMAGG 440
Cdd:cd02758 359 AKEFTSHGRAAAVVHH-GGTMHSNGFYNAYAIRMLNALIGNLNWKGG 404
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
898-1007 |
5.84e-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: 94.31 E-value: 5.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 898 LTEHFH--YWTKHALLNAiLQPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlkangkdiDTIGIPI 975
Cdd:cd02775 1 LRDHFHsgTRTRNPWLRE-LAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPP--------GVVFLPH 71
|
90 100 110
....*....|....*....|....*....|..
gi 501574638 976 HWGYEGvaKKGFIANTLTPFVGDANTQTPEFK 1007
Cdd:cd02775 72 GWGHRG--GRGGNANVLTPDALDPPSGGPAYK 101
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
92-465 |
4.29e-22 |
|
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: 101.92 E-value: 4.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 92 CPKGAGLVDFIHSESRLKFPEYR------------APGSDKWQQISWEEAFDRIAKLMKEDRDAnYiaqNAEGVTVNR-- 157
Cdd:cd02751 32 CPRGRSVRDRVYSPDRIKYPMKRvgwlgngpgsreLRGEGEFVRISWDEALDLVASELKRIREK-Y---GNEAIFGGSyg 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 158 WLSTGMLCASASSnetgyltqkFSRALGMlavdnqarvuHGPTVASLAP---------------TFGRGAMTNHWVDI-K 221
Cdd:cd02751 108 WASAGRLHHAQSL---------LHRFLNL----------IGGYLGSYGTystgaaqvilphvvgSDEVYEQGTSWDDIaE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 222 NANLVVVMGGNAAE--------AHPVGFRWAMEAKiHNGAKLIVIDPRFTRTAAV-ADYYAPIRSGTDIAFLSGVLLYLL 292
Cdd:cd02751 169 HSDLVVLFGANPLKtrqgggggPDHGSYYYLKQAK-DAGVRFICIDPRYTDTAAVlAAEWIPIRPGTDVALMLAMAHTLI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 293 NNEKFNREYTEAYTnaslivredygfedglfTGYDAEKRkydkstwtYELDEN-GFAKrdttlqhprcvwnllkqhvsry 371
Cdd:cd02751 248 TEDLHDQAFLARYT-----------------VGFDEFKD--------YLLGESdGVPK---------------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 372 TPDVVENICGTPKDAFLKVCEYIAetsahDKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNI 451
Cdd:cd02751 281 TPEWAAEITGVPAETIRALAREIA-----SKRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNG 355
|
410
....*....|....
gi 501574638 452 QGLTDLGLLSQSLP 465
Cdd:cd02751 356 GGPPRGGAGGPGLP 369
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
107-654 |
8.35e-22 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 98.24 E-value: 8.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 107 RLKFPEYRApGSDKWQQISWEEAFDRIAKLMKEDRDANyiaqNAEGVTVNRWlstgmlCASASSNETGYLTQKFSRALGM 186
Cdd:pfam00384 1 RLKYPMVRR-GDGKFVRVSWDEALDLIAKKLKRIIKKY----GPDAIAINGG------SGGLTDVESLYALKKLLNRLGS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 187 LAV---DNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGfrWAME--AKIHNGAKLIVIDPR 261
Cdd:pfam00384 70 KNGnteDHNGDLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPIL--NARIrkAALKGKAKVIVIGPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 262 FTRTAAVAdyYAPIRSGTDIAFLSGVLLYLLnnekfnreyteaytnaslivredygfedglftgydaEKRKYDKStwtye 341
Cdd:pfam00384 148 LDLTYADE--HLGIKPGTDLALALAGAHVFI------------------------------------KELKKDKD----- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 342 ldengFAKRdttlqhprcvwnllkqhvsrytpdvvenicgtpkdaflkvceyiaetsahdktASFLYALGWTQHSIGAQN 421
Cdd:pfam00384 185 -----FAPK-----------------------------------------------------PIIIVGAGVLQRQDGEAI 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 422 IRTMAMIQLLLGNMGMAGGGVNALR---GHSNIQGLTDLGLlsqslpgymtlpsekqtdlqtyltantpkpllegqvnyw 498
Cdd:pfam00384 207 FRAIANLADLTGNIGRPGGGWNGLNilqGAASPVGALDLGL--------------------------------------- 247
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 499 gnypkffvsmmkaffgdkataenswgfdwlpkwDKGYDVLQYFEMMKEGKVNGYICQGFNPVASFPNKNKVIGCLSKLKF 578
Cdd:pfam00384 248 ---------------------------------VPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDL 294
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501574638 579 LVTIDplntetsNFWQNHGELNevdsSKIqtevfRLPSTCFAEENGSIVNSGRWLQwHWKGA-DAPGIALTDGEILS 654
Cdd:pfam00384 295 FVVYD-------GHHGDKTAKY----ADV-----ILPAAAYTEKNGTYVNTEGRVQ-STKQAvPPPGEAREDWKILR 354
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
82-447 |
1.35e-20 |
|
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: 96.23 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 82 PDH-PvnRGalCPKGAGLVDFIHSESRLKFPEYRAP--GSDKWQQISWEEAFDRIAKLMKeDRDANYIAQNAEGVTvnRW 158
Cdd:cd02750 44 PDYnP--RG--CQRGASFSWYLYSPDRVKYPLKRVGarGEGKWKRISWDEALELIADAII-DTIKKYGPDRVIGFS--PI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 159 LSTGMLCASASSnetgyltqKFSRALGMLAVDNQARVUHGPTVASLapTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHP 238
Cdd:cd02750 117 PAMSMVSYAAGS--------RFASLIGGVSLSFYDWYGDLPPGSPQ--TWGEQTDVPESADWYNADYIIMWGSNVPVTRT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 239 VGFRWAMEAKiHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLLNNEKFNREYTEAYTNASLIVredygf 318
Cdd:cd02750 187 PDAHFLTEAR-YNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYTDLPFLV------ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 319 edglftgydaekrkydkstwtyeldengfakrdttlqhprcvwnllkqhvsrYTPDVVENICGTPKDAFLKVCEYIAETs 398
Cdd:cd02750 260 ----------------------------------------------------YTPAWQEAITGVPRETVIRLAREFATN- 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 501574638 399 ahdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:cd02750 287 ---GRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVG 332
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
887-1016 |
5.93e-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: 5.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 887 DKFPYVGTTYRLTEHFHYWT---KHALLNAILqPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlka 963
Cdd:cd02791 1 AEYPLWLNTGRVRDQWHTMTrtgRVPRLNAHV-PEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRP--- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 501574638 964 nGkdidTIGIPIHWGYEGVAKKGfiANTLTPFVGDANTQTPEFKSFLVNVEKV 1016
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 ... |
887-1015 |
1.38e-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: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 887 DKFPYVGTTYRLTEHFHYWT---KHALLNAIlQPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlka 963
Cdd:cd02790 1 EEYPLVLTTGRVLYHYHTGTmtrRAEGLDAI-APEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPE--- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 501574638 964 ngkdiDTIGIPIHWgYEGVakkgfiANTLTPFVGDANTQTPEFKSFLVNVEK 1015
Cdd:cd02790 77 -----GVVFMPFHF-AEAA------ANLLTNAALDPVAKIPEFKVCAVRVEK 116
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
43-104 |
3.36e-18 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 79.22 E-value: 3.36e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501574638 43 TRETRNTCTYCSVGCGLLMYSlgdgaKNAKasIFHIEGDPDHPVNRGALCPKGAGLVDFIHS 104
Cdd:smart00926 1 EKWVPTVCPLCGVGCGLLVEV-----KDGR--VVRVRGDPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
43-104 |
2.84e-17 |
|
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface.
Pssm-ID: 428168 [Multi-domain] Cd Length: 55 Bit Score: 76.56 E-value: 2.84e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501574638 43 TRETRNTCTYCSVGCGLLMYSlgdgaKNAKasIFHIEGDPDHPVNRGALCPKGAGLVDFIHS 104
Cdd:pfam04879 1 MKVVKTICPYCGVGCGLEVHV-----KDGK--IVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
894-1010 |
3.03e-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: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 894 TTYRLTEHFH--YWTKHALLNAILQPEqFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlkangkdiDTI 971
Cdd:pfam01568 4 ITGRVLGQYHsqTRTRRVLRLAKPEPE-VVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRP--------GVV 74
|
90 100 110
....*....|....*....|....*....|....*....
gi 501574638 972 GIPIHWGYEgvaKKGFIANTLTPFVGDANTQTPEFKSFL 1010
Cdd:pfam01568 75 FMPFGWWYE---PRGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
50-288 |
4.08e-16 |
|
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone oxidoreductase (NADH-Q-OR)/respiratory complex I/NADH dehydrogenase-1 (NDH-1). The NADH-Q-OR is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The atomic structure of complex I is not known and the mechanisms of electron transfer and proton pumping are not established. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Escherichia coli, this subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The nad11 gene is nuclear-encoded in animals, plants, and fungi, but is still encoded in the mitochondrial genome of some protists. The Nad11/NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain family belongs to the molybdopterin_binding (MopB) superfamily of proteins. Bacterial type II NADH-quinone oxidoreductases and NQR-type sodium-motive NADH-quinone oxidoreductases are not homologs of this domain family.
Pssm-ID: 239169 [Multi-domain] Cd Length: 386 Bit Score: 81.56 E-value: 4.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 50 CTYCSVGCGLLMyslgdGAKNAKasIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRapGSDKWQQISWEEA 129
Cdd:cd02768 4 DVHDALGSNIRV-----DVRGGE--VMRILPRENEAINEEWISDKGRFGYDGLNSRQRLTQPLIK--KGGKLVPVSWEEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 130 FDRIAKLMKEdrdanyIAQNAEGVTVNrwlstgmlcaSASSNETGYLTQKFSRALGMLAVDNQARvuhGPTVASLAPTFG 209
Cdd:cd02768 75 LKTVAEGLKA------VKGDKIGGIAG----------PRADLESLFLLKKLLNKLGSNNIDHRLR---QSDLPADNRLRG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 210 RGAMTNHWVDIKNANLVVVMGGNAAEAHPVgfrwaMEAKI-----HNGAKLIVIDPRFTRTAAVADYYApIRSGTDIAFL 284
Cdd:cd02768 136 NYLFNTSIAEIEEADAVLLIGSNLRKEAPL-----LNARLrkavkKKGAKIAVIGPKDTDLIADLTYPV-SPLGASLATL 209
|
....
gi 501574638 285 SGVL 288
Cdd:cd02768 210 LDIA 213
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
50-398 |
9.22e-15 |
|
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: 78.86 E-value: 9.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 50 CTYCSVGCGLLMYSLGDGAknakasIFHIEGDPD----HPVnRGALCPKGAGLVDFIHSESRLKFPEYRA---------P 116
Cdd:cd02760 4 CYNCVAGPDFMAVKVVDGV------ATEIEPNFAaediHPA-RGRVCVKAYGLVQKTYNPNRVLQPMKRTnpkkgrnedP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 117 GsdkWQQISWEEAFDRIAKLMKEDRDANYIaqNAEGV-----TVNRWLSTGMLCASASSNETGYLTQKFSRALGMLAVDN 191
Cdd:cd02760 77 G---FVPISWDEALDLVAAKLRRVREKGLL--DEKGLprlaaTFGHGGTPAMYMGTFPAFLAAWGPIDFSFGSGQGVKCV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 192 QARVUHGptvaslaptfgrGAMTNHWV---DIKNANLVVVMGGNA-AEAHPVGFRWAMEAKIHnGAKLIVIDPRFTRTAA 267
Cdd:cd02760 152 HSEHLYG------------EFWHRAFTvaaDTPLANYVISFGSNVeASGGPCAVTRHADARVR-GYKRVQVEPHLSVTGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 268 VADYYAPIRSGTDIAF---LSGVLLYLLNNEKFNREYTEAYTNASLIVRedygfEDGLFTgYDAEKRK---YD-KSTWTY 340
Cdd:cd02760 219 CSAEWVPIRPKTDPAFmfaMIHVMVHEQGLGKLDVPFLRDRTSSPYLVG-----PDGLYL-RDAATGKplvWDeRSGRAV 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501574638 341 ELDENGFAK----------------RDTTLQHP----RCVWNLLKQHVSRYTPDVVENICGTPKDAFLKVC-EYIAETS 398
Cdd:cd02760 293 PFDTRGAVPavagdfavdgavsvdaDDETAIHQgvegTTAFTMLVEHMRKYTPEWAESICDVPAATIRRIArEFLENAS 371
|
|
| MopB_NDH-1_NuoG2-N7 |
cd02771 |
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of ... |
49-239 |
1.94e-14 |
|
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239172 [Multi-domain] Cd Length: 472 Bit Score: 77.04 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 49 TCTYCSVGCGLLMyslgdGAKNAKasIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRapGSDKWQQISWEE 128
Cdd:cd02771 3 ICHHCSVGCNISL-----GERYGE--LRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIR--RGGTLVPVSWNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 129 AFDRIAKLMKEDRDAnyiaqnAEGVTVNRwlstgmlcasaSSNETGYLTQKFSR-ALGMLAVDNQARvuhgPTVASLAPT 207
Cdd:cd02771 74 ALDVAAARLKEAKDK------VGGIGSPR-----------ASNESNYALQKLVGaVLGTNNVDHRAR----RLIAEILRN 132
|
170 180 190
....*....|....*....|....*....|..
gi 501574638 208 FGRGAMTNHwvDIKNANLVVVMGGNAAEAHPV 239
Cdd:cd02771 133 GPIYIPSLR--DIESADAVLVLGEDLTQTAPR 162
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
49-362 |
3.24e-12 |
|
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: 70.59 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 49 TCTYCSVGCGLLMY---------------SLG----------DGAKNAKASI----------FHIEGDPDH--PVNRGAL 91
Cdd:cd02756 16 TCHFCIVGCGYHVYvwpvgeeggpspgqnAIGydlvdqvpplNLQWYPKTMHyvvvtqdgreVYIVIVPDKecPVNSGNY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 92 CPKGAGLVDFIHS------ESRLKFPEYRApgSDKWQQISWEEAFDRIAKLMKEDRDANYIAQN----------AEGVTV 155
Cdd:cd02756 96 STRGGTNAERIWSpdnrvgETRLTTPLVRR--GGQLQPTTWDDAIDLVARVIKGILDKDGNDDAvfasrfdhggGGGGFE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 156 NRWlSTGMLCASAssnetgyLTQKFSRalgmlaVDNqaRVUHGPTVASLAPTfGRGAMTNHWVDIKNANLVVVMGGNAAE 235
Cdd:cd02756 174 NNW-GVGKFFFMA-------LQTPFVR------IHN--RPAYNSEVHATREM-GVGELNNSYEDARLADTIVLWGNNPYE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 236 AHPVGF-----------------RWAMEAKIHNGAKLIVIDPRFTRTAAVADYYA--------PIRSGTDIAFLSGVLLY 290
Cdd:cd02756 237 TQTVYFlnhwlpnlrgatvsekqQWFPPGEPVPPGRIIVVDPRRTETVHAAEAAAgkdrvlhlQVNPGTDTALANAIARY 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501574638 291 LLNNekfnreYTEAYTNASLIvredygfedglfTGYDAEKRKYdKSTWTYELDENGFAKRDTTLQHPRCVWN 362
Cdd:cd02756 317 IYES------LDEVLAEAEQI------------TGVPRAQIEK-AADWIAKPKEGGYRKRVMFEYEKGIIWG 369
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
5-288 |
5.48e-11 |
|
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs.
Pssm-ID: 239165 [Multi-domain] Cd Length: 524 Bit Score: 66.36 E-value: 5.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 5 RRQFFKICAGGMAGTTAAALG-----FAPSVALAETRQykLLRTRETRNTCTYCSVGCGLLMySLGDGAKnakasiFHIE 79
Cdd:cd02764 1 RRGFLKLMGASLAMASAAACRypvekIVPYVIWPENIV--PGETVYYATSLVPAGEGQGVLV-KTVDGRP------IKIE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 80 GDPDHPVNRGALCPKGAGLVDFIHSESRLKFPeYRAPGSDKWQQISWEEAFDRIAKLMKEDRDANYIAqnaegvtvnrwL 159
Cdd:cd02764 72 GNPDHPASLGGTSARAQASVLSLYDPDRAQGP-LRRGIDGAYVASDWADFDAKVAEQLKAVKDGGKLA-----------V 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 160 STGMLCASASSNETGYLTQKFSRALGMLAVDNQArvuhGPTVASLAPTFGRGAMTNHwvDIKNANLVVVMGGNAAEAHPV 239
Cdd:cd02764 140 LSGNVNSPTTEALIGDFLKKYPGAKHVVYDPLSA----EDVNEAWQASFGKDVVPGY--DFDKAEVIVSIDADFLGSWIS 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 501574638 240 GFRWA---MEAKIH----NGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVL 288
Cdd:cd02764 214 AIRHRhdfAAKRRLgaeePMSRLVAAESVYTLTGANADVRLAIRPSQEKAFALGLA 269
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
104-260 |
1.26e-09 |
|
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239173 [Multi-domain] Cd Length: 414 Bit Score: 61.60 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 104 SESRLKFPEYRAPGsdKWQQISWEEAFDRIAKLMKEDRDANYIAQnaegvtvnrwlsTGMLCASASSNETGYLTQKFSRA 183
Cdd:cd02772 51 SEDRLTKPMIKKDG--QWQEVDWETALEYVAEGLSAIIKKHGADQ------------IGALASPHSTLEELYLLQKLARG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501574638 184 LGMLAVDNQARVUHGPTVASLAPTFGrgaMTNHWVDIKNANLVVVMGGNAAEAHP-VGFRWAMEAKihNGAKLIVIDP 260
Cdd:cd02772 117 LGSDNIDHRLRQSDFRDDAKASGAPW---LGMPIAEISELDRVLVIGSNLRKEHPlLAQRLRQAVK--KGAKLSAINP 189
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
41-279 |
1.57e-09 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 61.39 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 41 LRTRETrnTCTYCSVGCGLLMyslgdGAKNAKasIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAPGsdK 120
Cdd:COG1034 215 LKKTPS--ICPHCSVGCNIRV-----DVRGGK--VYRVLPRENEAVNEEWLCDKGRFGYDGLNSPDRLTRPLVRKDG--E 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 121 WQQISWEEAFDRIAKLMKEDRDanyiAQNAEGVTvnrwlstgMLCAsassnetgyltqkfsralgmlavdnqarvuhGPT 200
Cdd:COG1034 284 LVEASWEEALAAAAEGLKALKK----AENSVGAA--------LLGA-------------------------------LPD 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 201 VASLAPTFGRGAmtnhwvdiknANLVVVMGGNAAEAHPVgfrwAMEAKIHNGAKLIVIDPRFTRTAAVADYYAPI----- 275
Cdd:COG1034 321 AAAILEAAEAGK----------LKALVLLGADPYDLDPA----AALAALAKADFVVVLDHFGSATAERADVVLPAaafae 386
|
....
gi 501574638 276 RSGT 279
Cdd:COG1034 387 KSGT 390
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
79-306 |
1.24e-08 |
|
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: 58.81 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 79 EGDPDhPvnrgalCPKGAGLVDFIHSESRLKFPEYR-------------APGSDKWQQISWEEAFDRIAKLMKEDRDAnY 145
Cdd:cd02769 25 EEDPD-P------SPLLDGVPDAVYSPTRIKYPMVRrgwlekgpgsdrsLRGKEEFVRVSWDEALDLVAAELKRVRKT-Y 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 146 IAQNAEGVTVNrWLSTGMLCASASS-----NETG-YLTQKFSRALGMLAVDNqarvuhgPTVasLAPTFGRGAMTNHWVD 219
Cdd:cd02769 97 GNEAIFGGSYG-WSSAGRFHHAQSLlhrflNLAGgYVGSVGDYSTGAAQVIL-------PHV--VGSMEVYTEQQTSWPV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 220 I-KNANLVVVMGGNA----------AEAHPVgfRWAMEAKIHNGAKLIVIDPRFTRTAAVADY-YAPIRSGTDIAFLSGV 287
Cdd:cd02769 167 IaEHTELVVAFGADPlknaqiawggIPDHQA--YSYLKALKDRGIRFISISPLRDDTAAELGAeWIAIRPGTDVALMLAL 244
|
250
....*....|....*....
gi 501574638 288 LLYLLNNEKFNREYTEAYT 306
Cdd:cd02769 245 AHTLVTEGLHDKAFLARYT 263
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
49-285 |
1.74e-08 |
|
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: 58.11 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 49 TCTYCSVGCGLLMYSLGDGAKNAKASIfhiegdpdhpvnrgalCPKG-AGLVDFIHSesrlkfpeYRAPGSDKwQQISWE 127
Cdd:cd02761 3 VCPFCGLLCDDIEVEVEDNKITKVRNA----------------CRIGaAKFARYERR--------ITTPRIDG-KPVSLE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 128 EAFDRIAKLMKEDRdanyiaqnaegvtvnRWLSTGMLCASASSNETGYLTQKFSRALgmlaVDNQARVUHGPTVASLAPt 207
Cdd:cd02761 58 EAIEKAAEILKEAK---------------RPLFYGLGTTVCEAQRAGIELAEKLGAI----IDHAASVCHGPNLLALQD- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 208 fgRGAMTNHWVDIKN-ANLVVVMGGNAAEAHPVGFR---WAMEAKIHNGA----KLIVIDPRFTRTAAVADYYAPIRSGT 279
Cdd:cd02761 118 --SGWPTTTLGEVKNrADVIVYWGTNPMHAHPRHMSrysVFPRGFFREGGredrTLIVVDPRKSDTAKLADIHLQIDPGS 195
|
....*.
gi 501574638 280 DIAFLS 285
Cdd:cd02761 196 DYELLA 201
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
909-1015 |
2.53e-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: 53.43 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 909 ALLNAILqPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlkangkdiDTIGIPIHWGYegVAKKGFI 988
Cdd:cd02778 21 PLLHELT-PENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRP--------DTVFMPHGFGH--WAPALSR 89
|
90 100 110
....*....|....*....|....*....|....
gi 501574638 989 A-------NTLTPFVGDANTQTPEFKSFLVNVEK 1015
Cdd:cd02778 90 AygggvndNNLLPGSTEPVSGGAGLQEFTVTVRK 123
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
889-984 |
1.72e-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: 51.53 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 889 FPYVGTTYRLTEHFHYWTKHALLNAILqPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlkangkdi 968
Cdd:cd02780 1 YPFILVTFKSNLNSHRSANAPWLKEIK-PENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRP-------- 71
|
90
....*....|....*....
gi 501574638 969 DTIGIPI---HWGYEGVAK 984
Cdd:cd02780 72 GVVAIEHgygHWAYGAVAS 90
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
888-959 |
2.16e-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: 47.75 E-value: 2.16e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501574638 888 KFPYVGTTY--RLTEHFHYWTKHALLnaILQPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIR 959
Cdd:cd02785 1 KYPLACIQRhsRFRVHSQFSNVPWLL--ELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQ 72
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
889-1015 |
6.91e-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: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 889 FPYVGTTYRLTEHFHywTKHALLNAI--LQPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTlkangk 966
Cdd:cd02781 3 PLILTTGARSYYYFH--SEHRQLPSLreLHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRP------ 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501574638 967 diDTIGIPIHWGY--EGVAKKGFI------ANTLT------PFVGDANtqtpeFKSFLVNVEK 1015
Cdd:cd02781 75 --GVVRAEHGWWYpeREAGEPALGgvwesnANALTsddwndPVSGSSP-----LRSMLCKIYK 130
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
928-959 |
2.04e-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: 2.04e-04
10 20 30
....*....|....*....|....*....|..
gi 501574638 928 ANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIR 959
Cdd:cd02777 43 AAARGIKDGDIVRVFNDRGAVLAGARVTDRIM 74
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
928-959 |
3.26e-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: 3.26e-04
10 20 30
....*....|....*....|....*....|..
gi 501574638 928 ANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIR 959
Cdd:cd02793 42 AAARGIADGDIVRVFNDRGACLAGAVVTDGIM 73
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
930-1015 |
8.60e-03 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 37.52 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501574638 930 KLGIAQGDTVKVSSNRGYIKAKAVVTKRIrtlkangkdidtigipihwgYEGVAkkgFI-----ANTLTPfvgdANTQ-- 1002
Cdd:COG1153 42 KLGIKEGDKVKVTSEYGEVVVKAKESEDL--------------------HPGLV---FIpmgpwANAVVP----PETHst 94
|
90
....*....|....
gi 501574638 1003 -TPEFKSFLVNVEK 1015
Cdd:COG1153 95 gMPDFKGVPVEVEP 108
|
|
| |
