|
Name |
Accession |
Description |
Interval |
E-value |
| metH |
PRK09490 |
B12-dependent methionine synthase; Provisional |
1-1249 |
0e+00 |
|
B12-dependent methionine synthase; Provisional
Pssm-ID: 236539 [Multi-domain] Cd Length: 1229 Bit Score: 2154.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 1 MKKTLQDEIEAILRKRIMVLDGGMGTMIQRYKLSEENFQGQEFKDHSRPLKGNNDILSITQPDVIYQIHKEYLLAGADII 80
Cdd:PRK09490 3 DMSSRLAQLRALLAERILVLDGAMGTMIQRYKLEEADYRGERFADWPCDLKGNNDLLVLTQPDVIEAIHRAYLEAGADII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 81 ETNTFSSTSIAQADYGLEHLAYRMNKCSADVARKAAEEITLQTGVK-RFVAGSLGPTNKTLSVSPSVERPDYRNITFDEL 159
Cdd:PRK09490 83 ETNTFNATTIAQADYGMESLVYELNFAAARLAREAADEWTAKTPDKpRFVAGVLGPTNRTASISPDVNDPGFRNVTFDEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 160 VEAYQEQAKGLLDGGVDILLIETIFDTANAKAALFALQKLFEENyaSPR-PIFISGTIVDKSGRTLSGQTGEAFVTSVSH 238
Cdd:PRK09490 163 VAAYREQTRGLIEGGADLILIETIFDTLNAKAAIFAVEEVFEEL--GVRlPVMISGTITDASGRTLSGQTTEAFWNSLRH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 239 SDPLCIGLNCALGAAEMRPFIETIGKCTTAYVLCYPNAGLPNTFGDYDETPAMMAMHLKDFAVDGLVNVVGGCCGSTPDH 318
Cdd:PRK09490 241 AKPLSIGLNCALGADELRPYVEELSRIADTYVSAHPNAGLPNAFGEYDETPEEMAAQIGEFAESGFLNIVGGCCGTTPEH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 319 IREIAEAVKNCKPRVPPDSvfEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSKKFAKLIMAGNYEEALSVAKVQVEMGA 398
Cdd:PRK09490 321 IAAIAEAVAGLPPRKLPEI--PVACRLSGLEPLNIDDDSLFVNVGERTNVTGSAKFARLIKEEDYDEALDVARQQVENGA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 399 QVLDINMDDGMLDGPSAMTKFCNFIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEEDFLEKARKIKK 478
Cdd:PRK09490 399 QIIDINMDEGMLDSEAAMVRFLNLIASEPDIARVPIMIDSSKWEVIEAGLKCIQGKGIVNSISLKEGEEKFIEHARLVRR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 479 FGAAVVVMAFDEEGQATETDVKVSVCTRAYHLLVEKVGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPG 558
Cdd:PRK09490 479 YGAAVVVMAFDEQGQADTRERKIEICKRAYDILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKQNLPH 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 559 VRISGGLSNLSFAFRGMDAIREAMHGVFLYHAIKFGMDMGIVNAGSLPVYDDIHKDLLQLCEDLIWNRDAEATEKLLRYA 638
Cdd:PRK09490 559 AKISGGVSNVSFSFRGNNPVREAIHAVFLYHAIKAGMDMGIVNAGQLAIYDDIPPELREAVEDVVLNRRPDATERLLEIA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 639 QT-HGKGGKKVIQTD-EWRNGSIEERLEYALVKGIEKHIVEDTEEARLnreKYPRPLNIIEGPLMNGMKVVGDLFGAGKM 716
Cdd:PRK09490 639 EKyRGKGGKKAKAEDlEWRSWPVEKRLEHALVKGITEFIEEDTEEARQ---QAARPLEVIEGPLMDGMNVVGDLFGEGKM 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 717 FLPQVIKSARVMKKAVGHLIPFMEKEREEarvlngsvEEEDPYQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGV 796
Cdd:PRK09490 716 FLPQVVKSARVMKQAVAYLEPFIEAKKEG--------GTDRKSNGKILMATVKGDVHDIGKNIVGVVLQCNNYEVIDLGV 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 797 MTPCDKILQAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAIKIPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDASK 876
Cdd:PRK09490 788 MVPAEKILETAKEENADIIGLSGLITPSLDEMVHVAKEMERQGFTIPLLIGGATTSKAHTAVKIAPNYSGPVVYVTDASR 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 877 SVVVCSQLLDENLKDDYFEEILEEYEDIRQDHYESLKERKYLPLSQARKHSFHIDWlSEPHPVKPTFIGTQVFEDYNLQK 956
Cdd:PRK09490 868 AVGVVSSLLSDEQRDAYVAETRAEYEKVREQHARKKPRKPLLTLEAARANRFKIDW-EAYTPPKPKFLGVQVFEDYDLAE 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 957 LVDYIDWKPFFDVWQLRGKYpnrgfPKIFNDKAVGEEARKVYEDAQNMLNILISRKKLRARGVVGFWPAQSVQDDIHLYA 1036
Cdd:PRK09490 947 LREYIDWTPFFQTWELAGKY-----PAILEDEVVGEEARKLFADAQAMLDKIIAEKWLTARGVIGLFPANSVGDDIEVYT 1021
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 1037 EgavPQAAEPIATFYGLRQQAEKDSSstdPYHCLSDFVAPLHSGVRDYLGLFAV-ACFGVEELSKAYEDDGDDYSSIMVK 1115
Cdd:PRK09490 1022 D---ESRTEVLATLHHLRQQTEKRGR---PNYCLADFVAPKESGKADYIGAFAVtAGLGEDELADRFEAAHDDYNAIMVK 1095
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 1116 ALGDRLAEAFAEELHERVRRELWAYCGSEQLGVTDLRKLRYEGIRPAPGYPSQPDHTEKLTMWRLANIEQATGIRLTESL 1195
Cdd:PRK09490 1096 ALADRLAEAFAEYLHERVRKEFWGYAPDENLSNEELIREKYQGIRPAPGYPACPDHTEKATLFDLLDAEKNTGMKLTESY 1175
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|....
gi 1958723785 1196 AMAPASAVSGLYFSNVKSKYFAVGKISKDQIEDYALRKNMSVAEVEKWLGPILG 1249
Cdd:PRK09490 1176 AMWPGASVSGWYFSHPESKYFAVGKIGRDQVEDYAARKGMSVEEVERWLAPNLG 1229
|
|
| metH |
TIGR02082 |
5-methyltetrahydrofolate--homocysteine methyltransferase; This family represents ... |
13-1218 |
0e+00 |
|
5-methyltetrahydrofolate--homocysteine methyltransferase; This family represents 5-methyltetrahydrofolate--homocysteine methyltransferase (EC 2.1.1.13), one of at least three different enzymes able to convert homocysteine to methionine by transferring a methyl group on to the sulfur atom. It is also called the vitamin B12(or cobalamine)-dependent methionine synthase. Other methionine synthases include 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase (MetE, EC 2.1.1.14, the cobalamin-independent methionine synthase) and betaine-homocysteine methyltransferase. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273959 [Multi-domain] Cd Length: 1181 Bit Score: 2021.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 13 LRKRIMVLDGGMGTMIQRYKLSEENFQGQeFKDHSRPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQ 92
Cdd:TIGR02082 1 LNQRILVLDGAMGTQLQSANLTEADFRGA-FADCHRELKGNNDILNLTKPEVIATIHRAYFEAGADIIETNTFNSTTISQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 93 ADYGLEHLAYRMNKCSADVARKAAEEITLQTGVKRFVAGSLGPTNKTLSVSPSVERPDYRNITFDELVEAYQEQAKGLLD 172
Cdd:TIGR02082 80 ADYDLEDLIYDLNFKGAKLARAVADEFTLTPEKPRFVAGSMGPTNKTATLSPDVERPGFRNVTYDELVDAYTEQAKGLLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 173 GGVDILLIETIFDTANAKAALFALQKLFEENYAsPRPIFISGTIVDKSGRTLSGQTGEAFVTSVSHSDPLCIGLNCALGA 252
Cdd:TIGR02082 160 GGVDLLLIETCFDTLNAKAALFAAETVFEEKGR-ELPIMISGTIVDTSGRTLSGQTIEAFLTSLEHAGIDMIGLNCALGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 253 AEMRPFIETIGKCTTAYVLCYPNAGLPNTFGDYDETPAMMAMHLKDFAVDGLVNVVGGCCGSTPDHIREIAEAVKNCKPR 332
Cdd:TIGR02082 239 DEMRPHLKHLSEHAEAYVSCHPNAGLPNAFGEYDLTPDELAKALADFAAEGGLNIVGGCCGTTPDHIRAIAEAVKNIKPR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 333 VPPdsVFEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSKKFAKLIMAGNYEEALSVAKVQVEMGAQVLDINMDDGMLDG 412
Cdd:TIGR02082 319 QRP--VLYEPSRLSGLEAITIAQDSNFVNIGERTNVAGSKKFRRLIIAEDYDEALDIAKQQVENGAQILDINVDYGMLDG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 413 PSAMTKFCNFIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEEDFLEKARKIKKFGAAVVVMAFDEEG 492
Cdd:TIGR02082 397 VAAMKRFLNLLASEPDISTVPLMLDSSEWAVLEAGLKCIQGKCIVNSISLKDGEERFIETAKLIKEYGAAVVVMAFDEEG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 493 QATETDVKVSVCTRAYHLLVEKVGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPGVRISGGLSNLSFAF 572
Cdd:TIGR02082 477 QARTADRKIEICKRAYNILTEKVGFPPEDIIFDPNILTIATGIEEHRRYAINFIEAIRWIKEELPDAKISGGVSNVSFSF 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 573 RGMDAIREAMHGVFLYHAIKFGMDMGIVNAGSLPVYDDIHKDLLQLCEDLIWNRDAEATEKLLRYAQTH-GKGGK--KVI 649
Cdd:TIGR02082 557 RGNPAAREAMHSVFLYHAIRAGMDMGIVNAGKILPYDDIDPELRQVVEDLILNRRREATEPLLELAQLYeGTTTKssKEA 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 650 QTDEWRNGSIEERLEYALVKGIEKHIVEDTEEArlnREKYPRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMK 729
Cdd:TIGR02082 637 QQAEWRNLPVEERLEYALVKGEREGIEEDLEEA---RKKLTRPLEIIEGPLMDGMKVVGDLFGSGKMFLPQVVKSARVMK 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 730 KAVGHLIPFMEKEReearvlngsveEEDPYQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILQAALD 809
Cdd:TIGR02082 714 KAVAYLEPHMEKEK-----------SEDSSKGKIVLATVKGDVHDIGKNIVGVVLSCNGYEVVDLGVMVPIEKILEAAKD 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 810 HKADIIGLSGLITPSLDEMIFVAKEMERLAIKIPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDENL 889
Cdd:TIGR02082 783 HNADVIGLSGLITPSLDEMKEVAEEMNRRGITIPLLIGGAATSKTHTAVKIAPIYKGPVVYVLDASRAVTVMDTLMSAKR 862
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 890 KDDYFEEILEEYEDIRQDHYESLKERKYLPLSQARKHSFHIDWLSEPHPVKPTFIGTQVFEDYNLQKLVDYIDWKPFFDV 969
Cdd:TIGR02082 863 KDTENGRIKEEYDTAREKHGEQRSKRIAASEQAARKNVFAPDWSDDIEPPAPPFWGTQIVEASDIAELRPYIDWTPFFLQ 942
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 970 WQLRGKYpnrgfPKIFNDKAVGEEARKVYEDAQNMLNILISRKKLRARGVVGFWPAQSVQDDIHLYAEGAVpqAAEPIAT 1049
Cdd:TIGR02082 943 WQLRGKY-----PKILGDEYEGLEAQKLFPDANEMLDKLSAENLLHARGVYGYFPAQSVGDDIEIYTDETV--ETHPIAT 1015
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 1050 FYGLRQQAEKDSsstDPYHCLSDFVAPLHSGVRDYLGLFAV-ACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEE 1128
Cdd:TIGR02082 1016 VRYLFHFPRQQS---GRYLCLADFIAPKASGIVDYIGAFAVtAGFGAEELADKLEAQHDDYDYIMVKAIADRLAEAFAEY 1092
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 1129 LHERVRRELWAYCGSEQLGVTDLRKLRYEGIRPAPGYPSQPDHTEKLTMWRLANIEQaTGIRLTESLAMAPASAVSGLYF 1208
Cdd:TIGR02082 1093 LHRRVRKELWGYAAEEPLSNEDLLKLRYQGIRPAPGYPACPDHTEKATMFELLEPER-IGVRLTESLAMHPEQSVSGLYF 1171
|
1210
....*....|
gi 1958723785 1209 SNVKSKYFAV 1218
Cdd:TIGR02082 1172 AHPEAKYFAV 1181
|
|
| MetH2 |
COG1410 |
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; ... |
24-1218 |
0e+00 |
|
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; Methionine synthase I, cobalamin-binding domain is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 441020 [Multi-domain] Cd Length: 1141 Bit Score: 1562.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 24 MGTMIQRYKLSEENFQGQEFKDHSRPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYR 103
Cdd:COG1410 1 MGTMIQLLKLRELDADGAMFTDLQLDLKGNNDLLGLTGPNEILEIHRPELEAGADIIETNTGADAAITAADGAAEALLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 104 MNK-CSADVARKAAEEITLQTGVKRFVAGSLGPTNKTLSVSPSVERPDYRNITFDELVEAYQEQAKGLLDGGVDILLIET 182
Cdd:COG1410 81 YNGaAAALALEAAAAAAAAAAAAARAVAGAPGPTGGTASPGPDVPGLGFRNFDFDELVEAYAEAGLGLGGGGADLLLTET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 183 IFDTANAKAALFALQKLFEENyASPRPIFISGTIVDKSGRTLSGQTGEAFVTSVSHSDPLCIGLNCALGAAEMRPFIETI 262
Cdd:COG1410 161 IFDTLNAAAAAAAAAAAAEEE-GVPIPVMVTGTITDGSGRTLSGQTAEAFLESLGHAAPGSNGLNCALGAEELRPYLEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 263 GKCTTAYVLCYPNAGLPNTFGDYDETPAMMAMHLKDFAVDGLVNVVGGCCGSTPDHIREIAEAVKNCKPRVPPDSVFegh 342
Cdd:COG1410 240 SRIPPSAVSNAPNAGLPNGFGEYDETPEEMAAALAEFAEEGGVNIVGGCCGTTPEHIRAIAEAVAGLKPRPREKPPP--- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 343 MLLSGLEPFRIGPYTNFVNIGERCNVAGSKKFAKLIMAGNYEEALSVAKVQVEMGAQVLDINMDDGMLDGPSAMTKFCNF 422
Cdd:COG1410 317 AVLSGLEPVPIGQDSPFVNIGERTNVTGSKKFRELILEGDYDEALEVAREQVEAGAQILDVNVDEPGRDEVAAMVRFLNL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 423 IASEpdiAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEEDFLEKARKIKKFGAAVVVMAFDEEGQATETDVKVS 502
Cdd:COG1410 397 LASE---VRVPLMIDSSKPEVIEAGLKCYQGKPIVNSISLEEGEERFEEVAPLAKKYGAAVVVLAIDEEGQADTAERKLE 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 503 VCTRAYHLLVEKVGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPGVRISGGLSNLSFAFRGmdAIREAM 582
Cdd:COG1410 474 IAERIYDLAVEEYGFPPEDIIFDPLVFTVATGIEEHRNYAVETIEAIRLIKEELPGAKTSLGVSNVSFGLPG--NVREAL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 583 HGVFLYHAIKFGMDMGIVNAGSLPVYDDIHKDLLQLCEDLIWNRDAEATEKLLRYAQTHgKGGKKVIQTDEWRNGSIEER 662
Cdd:COG1410 552 NSVFLYHAIKAGLDMAIVNPGQLEPYDDIPPELRELAEDVLLNRRPDALERLIELFEGV-KGAKAKKADLEWRELPVEER 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 663 LEYALVKGIEKHIVEDTEEARlnrEKYPRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKE 742
Cdd:COG1410 631 LKHAIVKGIKEGIEEDTEEAL---AEGARPLEIINGPLMPGMNVVGDLFGAGKMFLPQVLKSAEVMKAAVAYLEPFMEKE 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 743 reearvlngsvEEEDPYQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGLIT 822
Cdd:COG1410 708 -----------KGESSSKGKIVLATVKGDVHDIGKNIVGVVLENNGYEVIDLGVMVPAEKILEAAKEHKADIIGLSGLMT 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 823 PSLDEMIFVAKEMERLAIKIPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDENLKDDYFEEILEEYE 902
Cdd:COG1410 777 TSLDEMKEVAEEMRRRGLDIPVLIGGAALTRAYTAVKIAPAYDGAVVYAKDASRAVRVADKLLSKERREAFVAEIKAEYE 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 903 DIRQDHYEslKERKYLPLSQARKhsfHIDwlSEPHPVKPTFIGTQVFEDYNLQKLVDYIDWKPFFDVWQLRGKYPNrgfp 982
Cdd:COG1410 857 KLRERHAA--RKKKLLSLEEARS---NVD--SDYPPPTPPFLGTRVLKDIPLAELVPYIDWTPFFQQWGLKGKYLD---- 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 983 kifndkavGEEARKVYEDAQNMLNILISRKKLRARGVVGFWPAQSVQDDIHLYAegavPQAAEPIATFYGLRQQaekdss 1062
Cdd:COG1410 926 --------GEEARELFPDAQAMLDRIIEEKWLTARAVYGYFPANSEGDDIEVYD----DESSEELARFHFPRQQ------ 987
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 1063 sTDPYHCLSDFVAPLHSGVRDYLGLFAV-ACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEELHERVRRElWAYC 1141
Cdd:COG1410 988 -RGPNLCLADFVAPKESGERDYVGFFAVtAGIGIEELAAELEAAGDDYDAIMLHALADRLAEAFAEYLHERVRKE-WGYA 1065
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958723785 1142 GSEQLGVTDLRKLRYEGIRPAPGYPSQPDHTEKLTMWRLANIEQaTGIRLTESLAMAPASAVSGLYFSNVKSKYFAV 1218
Cdd:COG1410 1066 PDEALTNEDLIKEKYRGIRPAPGYPACPDHTEKRKLFDLLDAER-IGVTLTESFAMHPEASVSGIYFHHPEAKYFNV 1141
|
|
| Met_synt_B12 |
pfam02965 |
Vitamin B12 dependent methionine synthase, activation domain; |
954-1234 |
1.48e-163 |
|
Vitamin B12 dependent methionine synthase, activation domain;
Pssm-ID: 460767 [Multi-domain] Cd Length: 273 Bit Score: 487.75 E-value: 1.48e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 954 LQKLVDYIDWKPFFDVWQLRGKYPnrgfpKIFNDKAVGEEARKVYEDAQNMLNILISRKKLRARGVVGFWPAQSVQDDIH 1033
Cdd:pfam02965 2 LAELVPYIDWTPFFQAWELKGKYP-----AILDDEVVGEEARKLFADAQAMLDRIIEEKWLTARGVVGFFPANSVGDDIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 1034 LYAEGAvpqAAEPIATFYGLRQQAEKDSSstDPYHCLSDFVAPLHSGVRDYLGLFAVAC-FGVEELSKAYEDDGDDYSSI 1112
Cdd:pfam02965 77 VYTDES---RTEVLATFHTLRQQTEKPEG--RPNLCLADFIAPKESGIADYIGAFAVTAgIGIEELAARFEAAHDDYSAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 1113 MVKALGDRLAEAFAEELHERVRRELWAYCGSEQLGVTDLRKLRYEGIRPAPGYPSQPDHTEKLTMWRLANIEQATGIRLT 1192
Cdd:pfam02965 152 MVKALADRLAEAFAEYLHERVRKELWGYAPDENLSNEDLIKEKYQGIRPAPGYPACPDHTEKFTLFDLLDAEENIGIRLT 231
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958723785 1193 ESLAMAPASAVSGLYFSNVKSKYFAVGKISKDQIEDYALRKN 1234
Cdd:pfam02965 232 ESFAMTPAASVSGLYFAHPESRYFAVGKIGKDQVEDYAKRKG 273
|
|
| MeTr |
cd00740 |
MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent ... |
359-615 |
6.66e-143 |
|
MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent methyltransferases such as methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) and methionine synthase (MetH). Cobalamin-dependent methyltransferases catalyze the transfer of a methyl group via a methyl- cob(III)amide intermediate. These include MeTr, a functional heterodimer, and the folate binding domain of MetH.
Pssm-ID: 238381 [Multi-domain] Cd Length: 252 Bit Score: 432.59 E-value: 6.66e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 359 FVNIGERCNVAGSKKFAKLIMAGNYEEALSVAKVQVEMGAQVLDINMDDGMLDGPSAMTKFCNFIASEPdiaKVPLCIDS 438
Cdd:cd00740 1 FLNIGERTNVTGSKKFRELIKAEDYDEALDVARQQVEGGAQILDLNVDYGGLDGVSAMKWLLNLLATEP---TVPLMLDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 439 SNFAVIEAGLKCCQGKCIVNSISLKEGEEDFLEKARKIKKFGAAVVVMAFDEEGQATETDVKVSVCTRAYHLLVEKVGFN 518
Cdd:cd00740 78 TNWEVIEAGLKCCQGKCVVNSINLEDGEERFLKVARLAKEHGAAVVVLAFDEQGQAKTRDKKVEIAERAYEALTEFVGFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 519 PNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPGVRISGGLSNLSFAFrgMDAIREAMHGVFLYHAIKFGMDMG 598
Cdd:cd00740 158 PEDIIFDPLILPIATGIEEHRPYALETIDAIRMIKERLPAVKISLGVSNVSFGF--NPAAREALNSVFLYEAIKAGLDMA 235
|
250
....*....|....*..
gi 1958723785 599 IVNAGSLPVYDDIHKDL 615
Cdd:cd00740 236 IVNAGKLAPIEDIPEEL 252
|
|
| B12-binding_2 |
smart01018 |
B12 binding domain; Cobalamin-dependent methionine synthase is a large modular protein that ... |
658-743 |
8.10e-35 |
|
B12 binding domain; Cobalamin-dependent methionine synthase is a large modular protein that catalyses methyl transfer from methyltetrahydrofolate (CH3-H4folate) to homocysteine. During the catalytic cycle, it supports three distinct methyl transfer reactions, each involving the cobalamin (vitamin B12) cofactor and a substrate bound to its own functional unit. The cobalamin cofactor plays an essential role in this reaction, accepting the methyl group from CH3-H4folate to form methylcob(III)alamin, and in turn donating the methyl group to homocysteine to generate methionine and cob(I)alamin. Methionine synthase is a large enzyme composed of four structurally and functionally distinct modules: the first two modules bind homocysteine and CH3-H4folate, the third module binds the cobalamin cofactor and the C-terminal module binds S-adenosylmethionine. The cobalamin-binding module is composed of two structurally distinct domains: a 4-helical bundle cap domain (residues 651-740 in the Escherichia coli enzyme) and an alpha/beta B12-binding domain (residues 741-896). The 4-helical bundle forms a cap over the alpha/beta domain, which acts to shield the methyl ligand of cobalamin from solvent. Furthermore, in the conversion to the active conformation of this enzyme, the 4-helical cap rotates to allow the cobalamin cofactor to bind the activation domain. The alpha/beta domain is a common cobalamin-binding motif, whereas the 4-helical bundle domain with its methyl cap is a distinctive feature of methionine synthases.
Pssm-ID: 198086 [Multi-domain] Cd Length: 84 Bit Score: 127.59 E-value: 8.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 658 SIEERLEYALVKGIEKHIVEDTEEARlnrEKYPRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHLIP 737
Cdd:smart01018 2 PLLERLAEAIVDGDEEGVEELVEEAL---AEGVDPLEIINEGLIPGMNVVGDLFEAGEYFLPQVLMSAEAMKAAVAILKP 78
|
....*.
gi 1958723785 738 FMEKER 743
Cdd:smart01018 79 LLEKEK 84
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| metH |
PRK09490 |
B12-dependent methionine synthase; Provisional |
1-1249 |
0e+00 |
|
B12-dependent methionine synthase; Provisional
Pssm-ID: 236539 [Multi-domain] Cd Length: 1229 Bit Score: 2154.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 1 MKKTLQDEIEAILRKRIMVLDGGMGTMIQRYKLSEENFQGQEFKDHSRPLKGNNDILSITQPDVIYQIHKEYLLAGADII 80
Cdd:PRK09490 3 DMSSRLAQLRALLAERILVLDGAMGTMIQRYKLEEADYRGERFADWPCDLKGNNDLLVLTQPDVIEAIHRAYLEAGADII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 81 ETNTFSSTSIAQADYGLEHLAYRMNKCSADVARKAAEEITLQTGVK-RFVAGSLGPTNKTLSVSPSVERPDYRNITFDEL 159
Cdd:PRK09490 83 ETNTFNATTIAQADYGMESLVYELNFAAARLAREAADEWTAKTPDKpRFVAGVLGPTNRTASISPDVNDPGFRNVTFDEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 160 VEAYQEQAKGLLDGGVDILLIETIFDTANAKAALFALQKLFEENyaSPR-PIFISGTIVDKSGRTLSGQTGEAFVTSVSH 238
Cdd:PRK09490 163 VAAYREQTRGLIEGGADLILIETIFDTLNAKAAIFAVEEVFEEL--GVRlPVMISGTITDASGRTLSGQTTEAFWNSLRH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 239 SDPLCIGLNCALGAAEMRPFIETIGKCTTAYVLCYPNAGLPNTFGDYDETPAMMAMHLKDFAVDGLVNVVGGCCGSTPDH 318
Cdd:PRK09490 241 AKPLSIGLNCALGADELRPYVEELSRIADTYVSAHPNAGLPNAFGEYDETPEEMAAQIGEFAESGFLNIVGGCCGTTPEH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 319 IREIAEAVKNCKPRVPPDSvfEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSKKFAKLIMAGNYEEALSVAKVQVEMGA 398
Cdd:PRK09490 321 IAAIAEAVAGLPPRKLPEI--PVACRLSGLEPLNIDDDSLFVNVGERTNVTGSAKFARLIKEEDYDEALDVARQQVENGA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 399 QVLDINMDDGMLDGPSAMTKFCNFIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEEDFLEKARKIKK 478
Cdd:PRK09490 399 QIIDINMDEGMLDSEAAMVRFLNLIASEPDIARVPIMIDSSKWEVIEAGLKCIQGKGIVNSISLKEGEEKFIEHARLVRR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 479 FGAAVVVMAFDEEGQATETDVKVSVCTRAYHLLVEKVGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPG 558
Cdd:PRK09490 479 YGAAVVVMAFDEQGQADTRERKIEICKRAYDILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKQNLPH 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 559 VRISGGLSNLSFAFRGMDAIREAMHGVFLYHAIKFGMDMGIVNAGSLPVYDDIHKDLLQLCEDLIWNRDAEATEKLLRYA 638
Cdd:PRK09490 559 AKISGGVSNVSFSFRGNNPVREAIHAVFLYHAIKAGMDMGIVNAGQLAIYDDIPPELREAVEDVVLNRRPDATERLLEIA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 639 QT-HGKGGKKVIQTD-EWRNGSIEERLEYALVKGIEKHIVEDTEEARLnreKYPRPLNIIEGPLMNGMKVVGDLFGAGKM 716
Cdd:PRK09490 639 EKyRGKGGKKAKAEDlEWRSWPVEKRLEHALVKGITEFIEEDTEEARQ---QAARPLEVIEGPLMDGMNVVGDLFGEGKM 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 717 FLPQVIKSARVMKKAVGHLIPFMEKEREEarvlngsvEEEDPYQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGV 796
Cdd:PRK09490 716 FLPQVVKSARVMKQAVAYLEPFIEAKKEG--------GTDRKSNGKILMATVKGDVHDIGKNIVGVVLQCNNYEVIDLGV 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 797 MTPCDKILQAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAIKIPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDASK 876
Cdd:PRK09490 788 MVPAEKILETAKEENADIIGLSGLITPSLDEMVHVAKEMERQGFTIPLLIGGATTSKAHTAVKIAPNYSGPVVYVTDASR 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 877 SVVVCSQLLDENLKDDYFEEILEEYEDIRQDHYESLKERKYLPLSQARKHSFHIDWlSEPHPVKPTFIGTQVFEDYNLQK 956
Cdd:PRK09490 868 AVGVVSSLLSDEQRDAYVAETRAEYEKVREQHARKKPRKPLLTLEAARANRFKIDW-EAYTPPKPKFLGVQVFEDYDLAE 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 957 LVDYIDWKPFFDVWQLRGKYpnrgfPKIFNDKAVGEEARKVYEDAQNMLNILISRKKLRARGVVGFWPAQSVQDDIHLYA 1036
Cdd:PRK09490 947 LREYIDWTPFFQTWELAGKY-----PAILEDEVVGEEARKLFADAQAMLDKIIAEKWLTARGVIGLFPANSVGDDIEVYT 1021
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 1037 EgavPQAAEPIATFYGLRQQAEKDSSstdPYHCLSDFVAPLHSGVRDYLGLFAV-ACFGVEELSKAYEDDGDDYSSIMVK 1115
Cdd:PRK09490 1022 D---ESRTEVLATLHHLRQQTEKRGR---PNYCLADFVAPKESGKADYIGAFAVtAGLGEDELADRFEAAHDDYNAIMVK 1095
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 1116 ALGDRLAEAFAEELHERVRRELWAYCGSEQLGVTDLRKLRYEGIRPAPGYPSQPDHTEKLTMWRLANIEQATGIRLTESL 1195
Cdd:PRK09490 1096 ALADRLAEAFAEYLHERVRKEFWGYAPDENLSNEELIREKYQGIRPAPGYPACPDHTEKATLFDLLDAEKNTGMKLTESY 1175
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|....
gi 1958723785 1196 AMAPASAVSGLYFSNVKSKYFAVGKISKDQIEDYALRKNMSVAEVEKWLGPILG 1249
Cdd:PRK09490 1176 AMWPGASVSGWYFSHPESKYFAVGKIGRDQVEDYAARKGMSVEEVERWLAPNLG 1229
|
|
| metH |
TIGR02082 |
5-methyltetrahydrofolate--homocysteine methyltransferase; This family represents ... |
13-1218 |
0e+00 |
|
5-methyltetrahydrofolate--homocysteine methyltransferase; This family represents 5-methyltetrahydrofolate--homocysteine methyltransferase (EC 2.1.1.13), one of at least three different enzymes able to convert homocysteine to methionine by transferring a methyl group on to the sulfur atom. It is also called the vitamin B12(or cobalamine)-dependent methionine synthase. Other methionine synthases include 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase (MetE, EC 2.1.1.14, the cobalamin-independent methionine synthase) and betaine-homocysteine methyltransferase. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273959 [Multi-domain] Cd Length: 1181 Bit Score: 2021.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 13 LRKRIMVLDGGMGTMIQRYKLSEENFQGQeFKDHSRPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQ 92
Cdd:TIGR02082 1 LNQRILVLDGAMGTQLQSANLTEADFRGA-FADCHRELKGNNDILNLTKPEVIATIHRAYFEAGADIIETNTFNSTTISQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 93 ADYGLEHLAYRMNKCSADVARKAAEEITLQTGVKRFVAGSLGPTNKTLSVSPSVERPDYRNITFDELVEAYQEQAKGLLD 172
Cdd:TIGR02082 80 ADYDLEDLIYDLNFKGAKLARAVADEFTLTPEKPRFVAGSMGPTNKTATLSPDVERPGFRNVTYDELVDAYTEQAKGLLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 173 GGVDILLIETIFDTANAKAALFALQKLFEENYAsPRPIFISGTIVDKSGRTLSGQTGEAFVTSVSHSDPLCIGLNCALGA 252
Cdd:TIGR02082 160 GGVDLLLIETCFDTLNAKAALFAAETVFEEKGR-ELPIMISGTIVDTSGRTLSGQTIEAFLTSLEHAGIDMIGLNCALGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 253 AEMRPFIETIGKCTTAYVLCYPNAGLPNTFGDYDETPAMMAMHLKDFAVDGLVNVVGGCCGSTPDHIREIAEAVKNCKPR 332
Cdd:TIGR02082 239 DEMRPHLKHLSEHAEAYVSCHPNAGLPNAFGEYDLTPDELAKALADFAAEGGLNIVGGCCGTTPDHIRAIAEAVKNIKPR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 333 VPPdsVFEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSKKFAKLIMAGNYEEALSVAKVQVEMGAQVLDINMDDGMLDG 412
Cdd:TIGR02082 319 QRP--VLYEPSRLSGLEAITIAQDSNFVNIGERTNVAGSKKFRRLIIAEDYDEALDIAKQQVENGAQILDINVDYGMLDG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 413 PSAMTKFCNFIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEEDFLEKARKIKKFGAAVVVMAFDEEG 492
Cdd:TIGR02082 397 VAAMKRFLNLLASEPDISTVPLMLDSSEWAVLEAGLKCIQGKCIVNSISLKDGEERFIETAKLIKEYGAAVVVMAFDEEG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 493 QATETDVKVSVCTRAYHLLVEKVGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPGVRISGGLSNLSFAF 572
Cdd:TIGR02082 477 QARTADRKIEICKRAYNILTEKVGFPPEDIIFDPNILTIATGIEEHRRYAINFIEAIRWIKEELPDAKISGGVSNVSFSF 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 573 RGMDAIREAMHGVFLYHAIKFGMDMGIVNAGSLPVYDDIHKDLLQLCEDLIWNRDAEATEKLLRYAQTH-GKGGK--KVI 649
Cdd:TIGR02082 557 RGNPAAREAMHSVFLYHAIRAGMDMGIVNAGKILPYDDIDPELRQVVEDLILNRRREATEPLLELAQLYeGTTTKssKEA 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 650 QTDEWRNGSIEERLEYALVKGIEKHIVEDTEEArlnREKYPRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMK 729
Cdd:TIGR02082 637 QQAEWRNLPVEERLEYALVKGEREGIEEDLEEA---RKKLTRPLEIIEGPLMDGMKVVGDLFGSGKMFLPQVVKSARVMK 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 730 KAVGHLIPFMEKEReearvlngsveEEDPYQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILQAALD 809
Cdd:TIGR02082 714 KAVAYLEPHMEKEK-----------SEDSSKGKIVLATVKGDVHDIGKNIVGVVLSCNGYEVVDLGVMVPIEKILEAAKD 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 810 HKADIIGLSGLITPSLDEMIFVAKEMERLAIKIPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDENL 889
Cdd:TIGR02082 783 HNADVIGLSGLITPSLDEMKEVAEEMNRRGITIPLLIGGAATSKTHTAVKIAPIYKGPVVYVLDASRAVTVMDTLMSAKR 862
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 890 KDDYFEEILEEYEDIRQDHYESLKERKYLPLSQARKHSFHIDWLSEPHPVKPTFIGTQVFEDYNLQKLVDYIDWKPFFDV 969
Cdd:TIGR02082 863 KDTENGRIKEEYDTAREKHGEQRSKRIAASEQAARKNVFAPDWSDDIEPPAPPFWGTQIVEASDIAELRPYIDWTPFFLQ 942
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 970 WQLRGKYpnrgfPKIFNDKAVGEEARKVYEDAQNMLNILISRKKLRARGVVGFWPAQSVQDDIHLYAEGAVpqAAEPIAT 1049
Cdd:TIGR02082 943 WQLRGKY-----PKILGDEYEGLEAQKLFPDANEMLDKLSAENLLHARGVYGYFPAQSVGDDIEIYTDETV--ETHPIAT 1015
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 1050 FYGLRQQAEKDSsstDPYHCLSDFVAPLHSGVRDYLGLFAV-ACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEE 1128
Cdd:TIGR02082 1016 VRYLFHFPRQQS---GRYLCLADFIAPKASGIVDYIGAFAVtAGFGAEELADKLEAQHDDYDYIMVKAIADRLAEAFAEY 1092
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 1129 LHERVRRELWAYCGSEQLGVTDLRKLRYEGIRPAPGYPSQPDHTEKLTMWRLANIEQaTGIRLTESLAMAPASAVSGLYF 1208
Cdd:TIGR02082 1093 LHRRVRKELWGYAAEEPLSNEDLLKLRYQGIRPAPGYPACPDHTEKATMFELLEPER-IGVRLTESLAMHPEQSVSGLYF 1171
|
1210
....*....|
gi 1958723785 1209 SNVKSKYFAV 1218
Cdd:TIGR02082 1172 AHPEAKYFAV 1181
|
|
| MetH2 |
COG1410 |
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; ... |
24-1218 |
0e+00 |
|
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; Methionine synthase I, cobalamin-binding domain is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 441020 [Multi-domain] Cd Length: 1141 Bit Score: 1562.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 24 MGTMIQRYKLSEENFQGQEFKDHSRPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYR 103
Cdd:COG1410 1 MGTMIQLLKLRELDADGAMFTDLQLDLKGNNDLLGLTGPNEILEIHRPELEAGADIIETNTGADAAITAADGAAEALLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 104 MNK-CSADVARKAAEEITLQTGVKRFVAGSLGPTNKTLSVSPSVERPDYRNITFDELVEAYQEQAKGLLDGGVDILLIET 182
Cdd:COG1410 81 YNGaAAALALEAAAAAAAAAAAAARAVAGAPGPTGGTASPGPDVPGLGFRNFDFDELVEAYAEAGLGLGGGGADLLLTET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 183 IFDTANAKAALFALQKLFEENyASPRPIFISGTIVDKSGRTLSGQTGEAFVTSVSHSDPLCIGLNCALGAAEMRPFIETI 262
Cdd:COG1410 161 IFDTLNAAAAAAAAAAAAEEE-GVPIPVMVTGTITDGSGRTLSGQTAEAFLESLGHAAPGSNGLNCALGAEELRPYLEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 263 GKCTTAYVLCYPNAGLPNTFGDYDETPAMMAMHLKDFAVDGLVNVVGGCCGSTPDHIREIAEAVKNCKPRVPPDSVFegh 342
Cdd:COG1410 240 SRIPPSAVSNAPNAGLPNGFGEYDETPEEMAAALAEFAEEGGVNIVGGCCGTTPEHIRAIAEAVAGLKPRPREKPPP--- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 343 MLLSGLEPFRIGPYTNFVNIGERCNVAGSKKFAKLIMAGNYEEALSVAKVQVEMGAQVLDINMDDGMLDGPSAMTKFCNF 422
Cdd:COG1410 317 AVLSGLEPVPIGQDSPFVNIGERTNVTGSKKFRELILEGDYDEALEVAREQVEAGAQILDVNVDEPGRDEVAAMVRFLNL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 423 IASEpdiAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEEDFLEKARKIKKFGAAVVVMAFDEEGQATETDVKVS 502
Cdd:COG1410 397 LASE---VRVPLMIDSSKPEVIEAGLKCYQGKPIVNSISLEEGEERFEEVAPLAKKYGAAVVVLAIDEEGQADTAERKLE 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 503 VCTRAYHLLVEKVGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPGVRISGGLSNLSFAFRGmdAIREAM 582
Cdd:COG1410 474 IAERIYDLAVEEYGFPPEDIIFDPLVFTVATGIEEHRNYAVETIEAIRLIKEELPGAKTSLGVSNVSFGLPG--NVREAL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 583 HGVFLYHAIKFGMDMGIVNAGSLPVYDDIHKDLLQLCEDLIWNRDAEATEKLLRYAQTHgKGGKKVIQTDEWRNGSIEER 662
Cdd:COG1410 552 NSVFLYHAIKAGLDMAIVNPGQLEPYDDIPPELRELAEDVLLNRRPDALERLIELFEGV-KGAKAKKADLEWRELPVEER 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 663 LEYALVKGIEKHIVEDTEEARlnrEKYPRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKE 742
Cdd:COG1410 631 LKHAIVKGIKEGIEEDTEEAL---AEGARPLEIINGPLMPGMNVVGDLFGAGKMFLPQVLKSAEVMKAAVAYLEPFMEKE 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 743 reearvlngsvEEEDPYQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGLIT 822
Cdd:COG1410 708 -----------KGESSSKGKIVLATVKGDVHDIGKNIVGVVLENNGYEVIDLGVMVPAEKILEAAKEHKADIIGLSGLMT 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 823 PSLDEMIFVAKEMERLAIKIPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDENLKDDYFEEILEEYE 902
Cdd:COG1410 777 TSLDEMKEVAEEMRRRGLDIPVLIGGAALTRAYTAVKIAPAYDGAVVYAKDASRAVRVADKLLSKERREAFVAEIKAEYE 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 903 DIRQDHYEslKERKYLPLSQARKhsfHIDwlSEPHPVKPTFIGTQVFEDYNLQKLVDYIDWKPFFDVWQLRGKYPNrgfp 982
Cdd:COG1410 857 KLRERHAA--RKKKLLSLEEARS---NVD--SDYPPPTPPFLGTRVLKDIPLAELVPYIDWTPFFQQWGLKGKYLD---- 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 983 kifndkavGEEARKVYEDAQNMLNILISRKKLRARGVVGFWPAQSVQDDIHLYAegavPQAAEPIATFYGLRQQaekdss 1062
Cdd:COG1410 926 --------GEEARELFPDAQAMLDRIIEEKWLTARAVYGYFPANSEGDDIEVYD----DESSEELARFHFPRQQ------ 987
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 1063 sTDPYHCLSDFVAPLHSGVRDYLGLFAV-ACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEELHERVRRElWAYC 1141
Cdd:COG1410 988 -RGPNLCLADFVAPKESGERDYVGFFAVtAGIGIEELAAELEAAGDDYDAIMLHALADRLAEAFAEYLHERVRKE-WGYA 1065
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958723785 1142 GSEQLGVTDLRKLRYEGIRPAPGYPSQPDHTEKLTMWRLANIEQaTGIRLTESLAMAPASAVSGLYFSNVKSKYFAV 1218
Cdd:COG1410 1066 PDEALTNEDLIKEKYRGIRPAPGYPACPDHTEKRKLFDLLDAER-IGVTLTESFAMHPEASVSGIYFHHPEAKYFNV 1141
|
|
| MetH1 |
COG0646 |
Methionine synthase I (cobalamin-dependent), methyltransferase domain [Amino acid transport ... |
7-844 |
0e+00 |
|
Methionine synthase I (cobalamin-dependent), methyltransferase domain [Amino acid transport and metabolism]; Methionine synthase I (cobalamin-dependent), methyltransferase domain is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440411 [Multi-domain] Cd Length: 809 Bit Score: 901.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 7 DEIEAILRKRIMVLDGGMGTMIQRYKLSEENFQGqefkdhsrpLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFS 86
Cdd:COG0646 4 AALLELLKERILILDGAMGTMLQAYGLTEGDFRG---------EKGCNELLNLTRPDVIREIHRAYLEAGADIIETNTFG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 87 STSIAQADYGLEHLAYRMNKCSADVARKAAEEITlqtGVKRFVAGSLGPTNKTLSvspsverpDYRNITFDELVEAYQEQ 166
Cdd:COG0646 75 ANRIKLADYGLEDRVYEINRAAARLAREAADEFS---DRPRFVAGSIGPTGKLLS--------PLGNITFDELVEAYREQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 167 AKGLLDGGVDILLIETIFDTANAKAALFALQKLFEENyASPRPIFISGTIvDKSGRTLSGQTGEAFVTSVSHSDPLCIGL 246
Cdd:COG0646 144 AEGLIEGGVDLLLIETIFDTLEAKAAIFAAREAFEEL-GRDLPVMVSGTF-DASGRTLSGQTPEAFATSLEHLGPDAIGL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 247 NCALGAAEMRPFIETIGKCTTAYVLCYPNAGLPNTFGD---YDETPAMMAMHLKDFAVDGLVNVVGGCCGSTPDHIREIA 323
Cdd:COG0646 222 NCALGPDEMRPHVEELSEVADTPVSAYPNAGLPNLVGGrtvYDETPEEMAEYAEEFAEAGGVNIVGGCCGTTPEHIRAIA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 324 EAVKNCKPRVPPDSvfEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSKKFAKLIMAGNYEEALSVAKVQVEMGAQVLDI 403
Cdd:COG0646 302 EAVKGLPPRKRPPP--PPALRLSGLEPLTITQDSLFVNVGERTNVTGSKKFARLILEGDYDAALAVARQQVEAGAQVIDV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 404 NMDDGMLDGPSAMTKFCNFIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEEDFLEKARKIKKFGAAV 483
Cdd:COG0646 380 NMDEGMLDGEAAMVEFLNLIASEPDIPRVPDMIDSSKWEVIEAGLKGVQGKGIVNSISLKEGEEKFLELAKLVRRYGAAV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 484 VVMAFDEEGQATETDVKVSVCTRAYHLLVEKVGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPGVRISG 563
Cdd:COG0646 460 VVMAFDEEGQADTAERKVEICARAYDLLTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKLNLPHALVSG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 564 GLSNLSFAFRGMDAIREAMHGVFLYHAIKFGMDMGIVNAGSLPVYDDIHKDLLQLCEDLIWNRDAEATEKLLRYAQTHGK 643
Cdd:COG0646 540 GVSNVSFSFRGNNPVREAIHAVFLYHAIAAGMDMGIVNAGQLAIYEEIPEELLLLVEDVVLNRREDATERLLEIAEEVKG 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 644 GGKKVIQTDE-WRNGSIEERLEYALVKGIEKHIVEDTEEARlnREKYPRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVI 722
Cdd:COG0646 620 AGKAAEEEAEeERREEEEERLLELLLVGGIEIDEEDDEEAA--LLLAALELIIIELLLGGGMVVGGLGGGGGKLLLVVVV 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 723 KSARVMKKAVGHLIPFMEKEREEARVLNgsveeedpyqGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDK 802
Cdd:COG0646 698 KAVVKKKVAVALLKPEEEEKKKGGGKGG----------GVVVGVVVKVVVDDVDIIIVVVVVVVNNGIVVLVVVVIVVVA 767
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 1958723785 803 ILQAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAIKIPL 844
Cdd:COG0646 768 LEAAAAAEAAVILLVGGLVLLLLEEEVLAAAEAAAEAAVLLL 809
|
|
| Met_synt_B12 |
pfam02965 |
Vitamin B12 dependent methionine synthase, activation domain; |
954-1234 |
1.48e-163 |
|
Vitamin B12 dependent methionine synthase, activation domain;
Pssm-ID: 460767 [Multi-domain] Cd Length: 273 Bit Score: 487.75 E-value: 1.48e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 954 LQKLVDYIDWKPFFDVWQLRGKYPnrgfpKIFNDKAVGEEARKVYEDAQNMLNILISRKKLRARGVVGFWPAQSVQDDIH 1033
Cdd:pfam02965 2 LAELVPYIDWTPFFQAWELKGKYP-----AILDDEVVGEEARKLFADAQAMLDRIIEEKWLTARGVVGFFPANSVGDDIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 1034 LYAEGAvpqAAEPIATFYGLRQQAEKDSSstDPYHCLSDFVAPLHSGVRDYLGLFAVAC-FGVEELSKAYEDDGDDYSSI 1112
Cdd:pfam02965 77 VYTDES---RTEVLATFHTLRQQTEKPEG--RPNLCLADFIAPKESGIADYIGAFAVTAgIGIEELAARFEAAHDDYSAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 1113 MVKALGDRLAEAFAEELHERVRRELWAYCGSEQLGVTDLRKLRYEGIRPAPGYPSQPDHTEKLTMWRLANIEQATGIRLT 1192
Cdd:pfam02965 152 MVKALADRLAEAFAEYLHERVRKELWGYAPDENLSNEDLIKEKYQGIRPAPGYPACPDHTEKFTLFDLLDAEENIGIRLT 231
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958723785 1193 ESLAMAPASAVSGLYFSNVKSKYFAVGKISKDQIEDYALRKN 1234
Cdd:pfam02965 232 ESFAMTPAASVSGLYFAHPESRYFAVGKIGKDQVEDYAKRKG 273
|
|
| MeTr |
cd00740 |
MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent ... |
359-615 |
6.66e-143 |
|
MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent methyltransferases such as methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) and methionine synthase (MetH). Cobalamin-dependent methyltransferases catalyze the transfer of a methyl group via a methyl- cob(III)amide intermediate. These include MeTr, a functional heterodimer, and the folate binding domain of MetH.
Pssm-ID: 238381 [Multi-domain] Cd Length: 252 Bit Score: 432.59 E-value: 6.66e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 359 FVNIGERCNVAGSKKFAKLIMAGNYEEALSVAKVQVEMGAQVLDINMDDGMLDGPSAMTKFCNFIASEPdiaKVPLCIDS 438
Cdd:cd00740 1 FLNIGERTNVTGSKKFRELIKAEDYDEALDVARQQVEGGAQILDLNVDYGGLDGVSAMKWLLNLLATEP---TVPLMLDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 439 SNFAVIEAGLKCCQGKCIVNSISLKEGEEDFLEKARKIKKFGAAVVVMAFDEEGQATETDVKVSVCTRAYHLLVEKVGFN 518
Cdd:cd00740 78 TNWEVIEAGLKCCQGKCVVNSINLEDGEERFLKVARLAKEHGAAVVVLAFDEQGQAKTRDKKVEIAERAYEALTEFVGFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 519 PNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPGVRISGGLSNLSFAFrgMDAIREAMHGVFLYHAIKFGMDMG 598
Cdd:cd00740 158 PEDIIFDPLILPIATGIEEHRPYALETIDAIRMIKERLPAVKISLGVSNVSFGF--NPAAREALNSVFLYEAIKAGLDMA 235
|
250
....*....|....*..
gi 1958723785 599 IVNAGSLPVYDDIHKDL 615
Cdd:cd00740 236 IVNAGKLAPIEDIPEEL 252
|
|
| methionine_synthase_B12_BD |
cd02069 |
B12 binding domain of methionine synthase. This domain binds methylcobalamin, which it uses as ... |
659-885 |
4.58e-133 |
|
B12 binding domain of methionine synthase. This domain binds methylcobalamin, which it uses as an intermediate methyl carrier from methyltetrahydrofolate (CH3H4folate) to homocysteine (Hcy).
Pssm-ID: 239020 [Multi-domain] Cd Length: 213 Bit Score: 405.11 E-value: 4.58e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 659 IEERLEYALVKGIEKHIVEDTEEARLnreKYPRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPF 738
Cdd:cd02069 1 VEERLKHALVKGIRDGIEEDTEEARQ---QYARPLEIINGPLMDGMKVVGDLFGAGKMFLPQVLKSARVMKAAVAYLEPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 739 MEKEreearvlngsvEEEDPYQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILQAALDHKADIIGLS 818
Cdd:cd02069 78 MEKE-----------KGENSSKGKIVLATVKGDVHDIGKNLVGVILSNNGYEVIDLGVMVPIEKILEAAKEHKADIIGLS 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958723785 819 GLITPSLDEMIFVAKEMERLAIKIPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLL 885
Cdd:cd02069 147 GLLVPSLDEMVEVAEEMNRRGIKIPLLIGGAATSRKHTAVKIAPEYDGPVVYVKDASRALGVANKLL 213
|
|
| S-methyl_trans |
pfam02574 |
Homocysteine S-methyltransferase; This is a family of related homocysteine ... |
18-326 |
3.65e-104 |
|
Homocysteine S-methyltransferase; This is a family of related homocysteine S-methyltransferases enzymes: 5-methyltetrahydrofolate--homocysteine S-methyltransferases also known EC:2.1.1.13; Betaine--homocysteine S-methyltransferase (vitamin B12 dependent), EC:2.1.1.5; and Homocysteine S-methyltransferase, EC:2.1.1.10,.
Pssm-ID: 460598 [Multi-domain] Cd Length: 268 Bit Score: 330.27 E-value: 3.65e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 18 MVLDGGMGTMIQRY--KLSEENfqgqefkdhsrplkGNNDILsiTQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQAD- 94
Cdd:pfam02574 1 LILDGGMGTELQRRglDLTEPL--------------WSNELL--TRPEIIREIHRDYLEAGADIIETNTYQASPIKLAEg 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 95 YGLEHLAYRMNKCSADVARKAAEEitlqtgvkRFVAGSLGPTNKTLSVSPSverpdyrnITFDELVEAYQEQAKGLLDGG 174
Cdd:pfam02574 65 LEEEEAVYELNRAAVRLAREAADE--------YFVAGSIGPYGATLSDGYG--------LSFDELVDFHREQLEALLDGG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 175 VDILLIETIFDTANAKAALFALQKLFEenyaspRPIFISGTIVDKsGRTLSGQTGEAFVTSVSHS-DPLCIGLNCALgAA 253
Cdd:pfam02574 129 VDLLLFETIPDLLEAKAALELLAEEPD------LPVWISFTIEDG-TRLRSGTTLEAAVAALLHAtGPLAVGVNCAL-PE 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958723785 254 EMRPFIETIGKCTTAYVLCYPNAglpntFGD-YDETPAMMAMHLKDFAVDGlVNVVGGCCGSTPDHIREIAEAV 326
Cdd:pfam02574 201 EMLPLLKELAKDAPTPVSVYPNS-----TGEvYDLTPEEWAEYAEGWLEAG-ANIIGGCCGTTPEHIRAIAEAL 268
|
|
| Pterin_bind |
pfam00809 |
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ... |
363-601 |
6.23e-76 |
|
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt a TIM barrel fold. The family includes dihydropteroate synthase EC:2.5.1.15 as well as a group methyltransferase enzymes including methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) that catalyzes a key step in the Wood-Ljungdahl pathway of carbon dioxide fixation. It transfers the N5-methyl group from methyltetrahydrofolate (CH3-H4folate) to a cob(I)amide centre in another protein, the corrinoid iron-sulfur protein. MeTr is a member of a family of proteins that includes methionine synthase and methanogenic enzymes that activate the methyl group of methyltetra-hydromethano(or -sarcino)pterin.
Pssm-ID: 395651 [Multi-domain] Cd Length: 243 Bit Score: 251.44 E-value: 6.23e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 363 GERCNVAGSKKFAKLIMaGNYEEALSVAKVQVEMGAQVLDINMDDG-----MLDGPSAMTKFCNFIASEPDIAKVPLCID 437
Cdd:pfam00809 1 MGILNVTPDSFSDGGRF-LDLDKALAHARRMVEEGADIIDIGGESTrpgaeRVDGEEEMERVLPVLAALRDEADVPISVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 438 SSNFAVIEAGLKCcqGKCIVNSISlkeGEEDFLEKARKIKKFGAAVVVMAFD--------EEGQATETDVKVSVCTRAYH 509
Cdd:pfam00809 80 TTKAEVAEAALKA--GADIINDIS---GGDGDPEMAELAAEYGAAVVVMHMDgtpktmqeNEQQYEDVVEEVERFLRARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 510 LLVEKVGFNPNDIIFDPNILTigTGMEEHNLYAINFIHATRVIKetlpGVRISGGLSNLSFAFRGM---DAIREAMHGVF 586
Cdd:pfam00809 155 AAAEEAGVPPEDIILDPGIGF--GKTEEHNLELLRTLDELRVIL----GVPVLLGVSRKSFIGRGLplgGEERDAGTAAF 228
|
250
....*....|....*
gi 1958723785 587 LYHAIKFGMDMGIVN 601
Cdd:pfam00809 229 LALAIAAGADIVRVH 243
|
|
| Pterin_binding |
cd00423 |
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and ... |
359-612 |
1.91e-64 |
|
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and cobalamin-dependent methyltransferases such as methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) and methionine synthase (MetH). DHPS, a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS. Cobalamin-dependent methyltransferases catalyze the transfer of a methyl group via a methyl- cob(III)amide intermediate. These include MeTr, a functional heterodimer, and the folate binding domain of MetH.
Pssm-ID: 238242 [Multi-domain] Cd Length: 258 Bit Score: 219.45 E-value: 1.91e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 359 FVNIGErCNVAGSKKFAkLIMAGNYEEALSVAKVQVEMGAQVLDINMDDG--------MLDGPSAMTKFCNFIASEPDia 430
Cdd:cd00423 1 TLIMGI-LNVTPDSFSD-GGKFLSLDKALEHARRMVEEGADIIDIGGESTrpgaepvsVEEELERVIPVLRALAGEPD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 431 kVPLCIDSSNFAVIEAGLKCcqGKCIVNSISLKEGEEDFLEKARkikKFGAAVVVMAFDEEGQ--------ATETDVKVS 502
Cdd:cd00423 77 -VPISVDTFNAEVAEAALKA--GADIINDVSGGRGDPEMAPLAA---EYGAPVVLMHMDGTPQtmqnnpyyADVVDEVVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 503 VCTRAYHLLVEkVGFNPNDIIFDPNILTIGTgmEEHNLYAINFIHATRVIketlPGVRISGGLSNLSFAFR---GMDAIR 579
Cdd:cd00423 151 FLEERVEAATE-AGIPPEDIILDPGIGFGKT--EEHNLELLRRLDAFREL----PGLPLLLGVSRKSFLGDllsVGPKDR 223
|
250 260 270
....*....|....*....|....*....|...
gi 1958723785 580 EAMHGVFLYHAIKFGMDMGIVNAgSLPVYDDIH 612
Cdd:cd00423 224 LAGTAAFLAAAILNGADIVRVHD-VKELRDAIK 255
|
|
| PRK08645 |
PRK08645 |
bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; ... |
13-331 |
3.99e-63 |
|
bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; Reviewed
Pssm-ID: 236321 [Multi-domain] Cd Length: 612 Bit Score: 227.04 E-value: 3.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 13 LRKRIMVLDGGMGTMiqrykLSEENFqgqefkdhsrPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQ 92
Cdd:PRK08645 8 LKERVLIADGAMGTL-----LYSRGV----------PLDRCFEELNLSHPELILRIHREYIEAGADVIQTNTFGANRIKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 93 ADYGLEHLAYRMNKCSADVARKAAEEitlqtgvKRFVAGSLGPTNKtlsvspsveRPDYRNITFDELVEAYQEQAKGLLD 172
Cdd:PRK08645 73 KRYGLEDKVKEINRAAVRLAREAAGD-------DVYVAGTIGPIGG---------RGPLGDISLEEIRREFREQIDALLE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 173 GGVDILLIETIFDTANAKAALFALQKLfeenyaSPRPIFISGTiVDKSGRTLSGQTGEAFVTSVSHSDPLCIGLNCALGA 252
Cdd:PRK08645 137 EGVDGLLLETFYDLEELLLALEAAREK------TDLPIIAQVA-FHEDGVTQNGTSLEEALKELVAAGADVVGLNCGLGP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 253 AEMRPFIETIGKCTTAYVLCYPNAGLPNTFGD---YDETPAMMAMHLKDFAVDGlVNVVGGCCGSTPDHIREIAEAVKNC 329
Cdd:PRK08645 210 YHMLEALERIPIPENAPLSAYPNAGLPEYVDGryvYSANPEYFAEYALEFVEQG-VRLIGGCCGTTPEHIRAMARALKGL 288
|
..
gi 1958723785 330 KP 331
Cdd:PRK08645 289 KP 290
|
|
| MHT1 |
COG2040 |
Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) [Amino acid transport and ... |
13-328 |
9.65e-46 |
|
Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) [Amino acid transport and metabolism];
Pssm-ID: 441643 [Multi-domain] Cd Length: 301 Bit Score: 167.29 E-value: 9.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 13 LRKRIMVLDGGMGTmiqryklsEENFQGQEFKDH---SRPLkgnndilsITQPDVIYQIHKEYLLAGADIIETNTFSST- 88
Cdd:COG2040 9 LMGRILLLDGGMGT--------ELERRGGDLLDPlwsAFAL--------LEAPELVRAVHRDYFAAGADVITTNSYQASp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 89 -SIAQADYGLEHLAyRMNKCSADVARKAAEEITlqTGVKRFVAGSLGPTNktlsvspSVERPDYRnITFDELVEAYQEQA 167
Cdd:COG2040 73 dGLAELGYSAEEAE-RLNRRAVALAREARDEYT--PGPPVLVAGSVGPYG-------DEYRPDYG-LSAEEAEAYHRPRI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 168 KGLLDGGVDILLIETIFDTANAKAALFALQklfeenyASPRPIFISGTiVDKSGRTLSGQT-GEAFVTSVSHSDPLCIGL 246
Cdd:COG2040 142 EALAEAGVDLLAAETIPSLAEAIAIARAAA-------EAGKPVWISFT-VEDDGRLRSGEPlAEAIAAVDTDPGPAAVGV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 247 NCAlGAAEMRPFIETIGKCTTAYVLCYPNAG------LPNTFGDYDETPAMMAMHLKDFAVDGLvNVVGGCCGSTPDHIR 320
Cdd:COG2040 214 NCS-HPEHFEAALEALAAWTGRPIGVYANAGemsdaeLKTWGGLDDGDPEELAEQAAEWVAAGA-RIIGGCCGTGPRHIA 291
|
....*...
gi 1958723785 321 EIAEAVKN 328
Cdd:COG2040 292 AIARALRA 299
|
|
| corrinoid_protein_B12-BD |
cd02070 |
B12 binding domain of corrinoid proteins. A family of small methanogenic corrinoid proteins ... |
666-880 |
2.49e-43 |
|
B12 binding domain of corrinoid proteins. A family of small methanogenic corrinoid proteins that bind methyl-Co(III) 5-hydroxybenzimidazolylcobamide as a cofactor. They play a role on the methanogenesis from trimethylamine, dimethylamine or monomethylamine, which is initiated by a series of corrinoid-dependent methyltransferases.
Pssm-ID: 239021 [Multi-domain] Cd Length: 201 Bit Score: 156.63 E-value: 2.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 666 ALVKGIEKHIVEDTEEARlnREKYPrPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREE 745
Cdd:cd02070 4 AIVDGDEEETVELVKKAL--EAGID-PQDIIEEGLAPGMDIVGDKYEEGEIFVPELLMAADAMKAGLDLLKPLLGKSKSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 746 ArvlngsveeedpyQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGLITPSL 825
Cdd:cd02070 81 K-------------KGKVVIGTVEGDIHDIGKNLVATMLEANGFEVIDLGRDVPPEEFVEAVKEHKPDILGLSALMTTTM 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958723785 826 DEMIFVAKEMER--LAIKIPLLIGGATTSRTHtAVKIAPRYSAPvihvlDASKSVVV 880
Cdd:cd02070 148 GGMKEVIEALKEagLRDKVKVMVGGAPVNQEF-ADEIGADGYAE-----DAAEAVAI 198
|
|
| MtbC1 |
COG5012 |
Methanogenic corrinoid protein MtbC1 [Energy production and conversion]; |
661-849 |
1.56e-42 |
|
Methanogenic corrinoid protein MtbC1 [Energy production and conversion];
Pssm-ID: 444036 [Multi-domain] Cd Length: 219 Bit Score: 155.05 E-value: 1.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 661 ERLEYALVKGIEKHIVEDTEEARlnREKYPrPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFME 740
Cdd:COG5012 12 ESLADAVLEGDEDEALELVAEAL--AAGMD-PEEIILDGLAPGMREVGELWEEGEIFVPEEHLAAAAMKAGLEILKPLLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 741 KEREearvlngsveeedpYQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGL 820
Cdd:COG5012 89 EEGG--------------RKGKVVIGTVEGDLHDIGKNIVADMLRAAGFEVIDLGADVPPEEFVEAAKEEKPDIVGLSAL 154
|
170 180 190
....*....|....*....|....*....|.
gi 1958723785 821 ITPSLDEMIFVAKEMERLAI--KIPLLIGGA 849
Cdd:COG5012 155 LTTTMPAMKELIEALREAGLrdKVKVIVGGA 185
|
|
| B12-binding |
cd02067 |
B12 binding domain (B12-BD). This domain binds different cobalamid derivates, like B12 ... |
762-880 |
1.29e-41 |
|
B12 binding domain (B12-BD). This domain binds different cobalamid derivates, like B12 (adenosylcobamide) or methylcobalamin or methyl-Co(III) 5-hydroxybenzimidazolylcobamide, it is found in several enzymes, such as glutamate mutase, methionine synthase and methylmalonyl-CoA mutase. Cobalamin undergoes a conformational change on binding the protein; the dimethylbenzimidazole group, which is coordinated to the cobalt in the free cofactor, moves away from the corrin and is replaced by a histidine contributed by the protein. The sequence Asp-X-His-X-X-Gly, which contains this histidine ligand, is conserved in many cobalamin-binding proteins.
Pssm-ID: 239018 [Multi-domain] Cd Length: 119 Bit Score: 148.42 E-value: 1.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 762 TIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAI- 840
Cdd:cd02067 1 KVVIATVGGDGHDIGKNIVARALRDAGFEVIDLGVDVPPEEIVEAAKEEDADAIGLSGLLTTHMTLMKEVIEELKEAGLd 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1958723785 841 KIPLLIGGATTSRTHtavkIAPRYSAPVIHVLDASKSVVV 880
Cdd:cd02067 81 DIPVLVGGAIVTRDF----KFLKEIGVDAYFGPATEAVEV 116
|
|
| PRK07534 |
PRK07534 |
betaine--homocysteine S-methyltransferase; |
55-338 |
2.30e-39 |
|
betaine--homocysteine S-methyltransferase;
Pssm-ID: 236045 [Multi-domain] Cd Length: 336 Bit Score: 149.90 E-value: 2.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 55 DILSITQPDVIYQIHKEYLLAGADIIETNTFSSTS----IAQADYGLEHLayrmNKCSADVARKAAEEitlqTGVKRFVA 130
Cdd:PRK07534 37 ELWNEDHPDNITALHQGFVDAGSDIILTNSFGGTAarlkLHDAQDRVHEL----NRAAAEIAREVADK----AGRKVIVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 131 GSLGPTNKTLSVSPSverpdyrnITFDELVEAYQEQAKGLLDGGVDILLIETIFDTANAKAALFALQKlfeenyaSPRPI 210
Cdd:PRK07534 109 GSVGPTGEIMEPMGA--------LTHALAVEAFHEQAEGLKAGGADVLWVETISAPEEIRAAAEAAKL-------AGMPW 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 211 FISGTIvDKSGRTLSGQTGEAF---VTSVSHSdPLCIGLNCALGAAE-MRPFIETIGKCTTAYVLCYPNAGLPNTFGD-- 284
Cdd:PRK07534 174 CGTMSF-DTAGRTMMGLTPADLadlVEKLGEP-PLAFGANCGVGASDlLRTVLGFTAQGPERPIIAKGNAGIPKYVDGhi 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958723785 285 -YDETPAMMAMHLKdFAVDGLVNVVGGCCGSTPDHIREIAEAVKNcKPRVPPDSV 338
Cdd:PRK07534 252 hYDGTPELMAEYAV-LARDAGARIIGGCCGTMPEHLAAMRAALDA-RPRGPRPSL 304
|
|
| PRK07535 |
PRK07535 |
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase; Validated |
362-602 |
8.50e-37 |
|
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase; Validated
Pssm-ID: 181022 [Multi-domain] Cd Length: 261 Bit Score: 139.99 E-value: 8.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 362 IGERCNvaGS-KKFAKLIMAGNYEEALSVAKVQVEMGAQVLDINMDDGMLDGPSAMTKFCNFIAsepDIAKVPLCIDSSN 440
Cdd:PRK07535 4 IGERIN--GTrKSIAEAIEAKDAAFIQKLALKQAEAGADYLDVNAGTAVEEEPETMEWLVETVQ---EVVDVPLCIDSPN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 441 FAVIEAGLKCCQGKCIVNSISlkeGEEDFLEKARK-IKKFGAAVVVMAFDEEGQATETDVKVSVCTRayhlLVEKV---G 516
Cdd:PRK07535 79 PAAIEAGLKVAKGPPLINSVS---AEGEKLEVVLPlVKKYNAPVVALTMDDTGIPKDAEDRLAVAKE----LVEKAdeyG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 517 FNPNDIIFDPNILTIGTgMEEHnlyAINFIHATRVIKETLPGVRISGGLSNLSFafrGMDAiREAMHGVFLYHAIKFGMD 596
Cdd:PRK07535 152 IPPEDIYIDPLVLPLSA-AQDA---GPEVLETIRRIKELYPKVHTTCGLSNISF---GLPN-RKLINRAFLVMAMGAGMD 223
|
....*.
gi 1958723785 597 MGIVNA 602
Cdd:PRK07535 224 SAILDP 229
|
|
| mmuM |
PRK09485 |
homocysteine methyltransferase; Provisional |
10-328 |
5.61e-35 |
|
homocysteine methyltransferase; Provisional
Pssm-ID: 181899 [Multi-domain] Cd Length: 304 Bit Score: 136.14 E-value: 5.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 10 EAILRKRIMVLDGGMGTMIQR--YKLseenfqgqefkdhsrplkgNNDILS----ITQPDVIYQIHKEYLLAGADIIETN 83
Cdd:PRK09485 6 ELLAQGPVLILDGALATELEArgCDL-------------------NDSLWSakvlLENPELIYQVHLDYFRAGADCAITA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 84 TFSSTSIAQADYGL-EHLAYRMNKCSADVARKAAEEiTLQTgvKRFVAGSLGPTNKTLSvSPSVERPDYrNITFDELVEA 162
Cdd:PRK09485 67 SYQATFQGFAARGLsEAEAEELIRRSVELAKEARDE-FWAE--KPLVAGSVGPYGAYLA-DGSEYRGDY-GLSEEELQDF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 163 YQEQAKGLLDGGVDILLIETIFDTANAKAALFALQKLFEENYAsprpiFISGTIVDksGRTLSGQT--GEAFVTSVSHSD 240
Cdd:PRK09485 142 HRPRIEALAEAGADLLACETIPNLDEAEALVELLKEEFPGVPA-----WLSFTLRD--GTHISDGTplAEAAALLAASPQ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 241 PLCIGLNCAlGAAEMRPFIETIGKCTTAYVLCYPNAGlpntfGDYD---------ETPAMMAMHLKDFAVDGlVNVVGGC 311
Cdd:PRK09485 215 VVAVGVNCT-APELVTAAIAALRAVTDKPLVVYPNSG-----EVYDavtktwhgpADDASLGELAPEWYAAG-ARLIGGC 287
|
330
....*....|....*..
gi 1958723785 312 CGSTPDHIREIAEAVKN 328
Cdd:PRK09485 288 CRTTPEDIAALAAALKT 304
|
|
| B12-binding_2 |
smart01018 |
B12 binding domain; Cobalamin-dependent methionine synthase is a large modular protein that ... |
658-743 |
8.10e-35 |
|
B12 binding domain; Cobalamin-dependent methionine synthase is a large modular protein that catalyses methyl transfer from methyltetrahydrofolate (CH3-H4folate) to homocysteine. During the catalytic cycle, it supports three distinct methyl transfer reactions, each involving the cobalamin (vitamin B12) cofactor and a substrate bound to its own functional unit. The cobalamin cofactor plays an essential role in this reaction, accepting the methyl group from CH3-H4folate to form methylcob(III)alamin, and in turn donating the methyl group to homocysteine to generate methionine and cob(I)alamin. Methionine synthase is a large enzyme composed of four structurally and functionally distinct modules: the first two modules bind homocysteine and CH3-H4folate, the third module binds the cobalamin cofactor and the C-terminal module binds S-adenosylmethionine. The cobalamin-binding module is composed of two structurally distinct domains: a 4-helical bundle cap domain (residues 651-740 in the Escherichia coli enzyme) and an alpha/beta B12-binding domain (residues 741-896). The 4-helical bundle forms a cap over the alpha/beta domain, which acts to shield the methyl ligand of cobalamin from solvent. Furthermore, in the conversion to the active conformation of this enzyme, the 4-helical cap rotates to allow the cobalamin cofactor to bind the activation domain. The alpha/beta domain is a common cobalamin-binding motif, whereas the 4-helical bundle domain with its methyl cap is a distinctive feature of methionine synthases.
Pssm-ID: 198086 [Multi-domain] Cd Length: 84 Bit Score: 127.59 E-value: 8.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 658 SIEERLEYALVKGIEKHIVEDTEEARlnrEKYPRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHLIP 737
Cdd:smart01018 2 PLLERLAEAIVDGDEEGVEELVEEAL---AEGVDPLEIINEGLIPGMNVVGDLFEAGEYFLPQVLMSAEAMKAAVAILKP 78
|
....*.
gi 1958723785 738 FMEKER 743
Cdd:smart01018 79 LLEKEK 84
|
|
| B12-binding_like |
cd02065 |
B12 binding domain (B12-BD). Most of the members bind different cobalamid derivates, like B12 ... |
762-875 |
5.59e-34 |
|
B12 binding domain (B12-BD). Most of the members bind different cobalamid derivates, like B12 (adenosylcobamide) or methylcobalamin or methyl-Co(III) 5-hydroxybenzimidazolylcobamide. This domain is found in several enzymes, such as glutamate mutase, methionine synthase and methylmalonyl-CoA mutase. Cobalamin undergoes a conformational change on binding the protein; the dimethylbenzimidazole group, which is coordinated to the cobalt in the free cofactor, moves away from the corrin and is replaced by a histidine contributed by the protein. The sequence Asp-X-His-X-X-Gly, which contains this histidine ligand, is conserved in many cobalamin-binding proteins. Not all members of this family contain the conserved binding motif.
Pssm-ID: 239016 [Multi-domain] Cd Length: 125 Bit Score: 127.12 E-value: 5.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 762 TIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAIK 841
Cdd:cd02065 1 KVLGATVGGDVHDIGKNIVAIALRDNGFEVIDLGVDVPPEEIVEAAKEEDADVVGLSALSTTHMEAMKLVIEALKELGID 80
|
90 100 110
....*....|....*....|....*....|....
gi 1958723785 842 IPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDAS 875
Cdd:cd02065 81 IPVVVGGAHPTADPEEPKVDAVVIGEGEYAGPAL 114
|
|
| pyl_corrinoid |
TIGR02370 |
methyltransferase cognate corrinoid proteins, Methanosarcina family; This model describes a ... |
666-852 |
1.90e-30 |
|
methyltransferase cognate corrinoid proteins, Methanosarcina family; This model describes a subfamily of the B12 binding domain (pfam02607, pfam02310) proteins. Members of the seed alignment include corrinoid proteins specific to four different, mutally non-homologous enzymes of the genus Methanosarcina. Three of the four cognate enzymes (trimethylamine, dimethylamine, and monomethylamine methyltransferases) all have the unusual, ribosomally incorporated amino acid pyrrolysine at the active site. All act in systems in which a methyl group is transferred to the corrinoid protein to create methylcobalamin, from which the methyl group is later transferred elsewhere.
Pssm-ID: 131423 [Multi-domain] Cd Length: 197 Bit Score: 119.52 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 666 ALVKGIEKHIVEDTEEARlnrEKYPRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREE 745
Cdd:TIGR02370 5 AIFEGEEDDVVEGAQKAL---DAGIDPIELIEKGLMAGMGVVGKLFEDGELFLPHVMMSADAMLAGIKVLTPEMEKAVET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 746 ARVlngsveeedpyqGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGLITPSL 825
Cdd:TIGR02370 82 EVL------------GKVVCGVAEGDVHDIGKNIVVTMLRANGFDVIDLGRDVPIDTVVEKVKKEKPLMLTGSALMTTTM 149
|
170 180 190
....*....|....*....|....*....|
gi 1958723785 826 ---DEMIFVAKEmERLAIKIPLLIGGATTS 852
Cdd:TIGR02370 150 ygqKDINDKLKE-EGYRDSVKFMVGGAPVT 178
|
|
| B12-binding |
pfam02310 |
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ... |
761-849 |
6.16e-22 |
|
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several enzymes, such as glutamate mutase, methionine synthase and methylmalonyl-CoA mutase. It contains a conserved DxHxxGx(41)SxVx(26)GG motif, which is important for B12 binding.
Pssm-ID: 426713 [Multi-domain] Cd Length: 121 Bit Score: 92.39 E-value: 6.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 761 GTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAI 840
Cdd:pfam02310 1 GKVVVATVGGDLHPLGLNYVAAALRAAGFEVIILGANVPPEDIVAAARDEKPDVVGLSALMTTTLPGAKELIRLLKGIRP 80
|
....*....
gi 1958723785 841 KIPLLIGGA 849
Cdd:pfam02310 81 RVKVVVGGP 89
|
|
| B12-binding_2 |
pfam02607 |
B12 binding domain; This B12 binding domain is found in methionine synthase EC:2.1.1.13, and ... |
663-735 |
8.05e-20 |
|
B12 binding domain; This B12 binding domain is found in methionine synthase EC:2.1.1.13, and other shorter proteins that bind to B12. This domain is always found to the N-terminus of pfam02310. The structure of this domain is known, it is a 4 helix bundle. Many of the conserved residues in this domain are involved in B12 binding, such as those in the MXXVG motif.
Pssm-ID: 460617 [Multi-domain] Cd Length: 68 Bit Score: 84.45 E-value: 8.05e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958723785 663 LEYALVKGIEKHIVEDTEEARLNRekyprPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHL 735
Cdd:pfam02607 1 LLEALLEGDEEAAEELLEEALEID-----PEEIIEDLLIPGMDEVGELWEAGEIFVPQEHLAAEAMKAALAVL 68
|
|
| PLN02489 |
PLN02489 |
homocysteine S-methyltransferase |
19-328 |
3.67e-16 |
|
homocysteine S-methyltransferase
Pssm-ID: 215269 Cd Length: 335 Bit Score: 81.21 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 19 VLDGGMGTMIQRYklseenfqGQEFKDhsrPLKgnNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQADYGL- 97
Cdd:PLN02489 24 VIDGGFATELERH--------GADLND---PLW--SAKCLITSPHLIRKVHLDYLEAGADIIITASYQATIQGFESRGLs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 98 ----EHLAYRmnkcSADVARKA-------------AEEITLQTGVKRFVAGSLGPTNKTLSvSPSVERPDY-RNITFDEL 159
Cdd:PLN02489 91 reesETLLRK----SVEIACEArdifwdkcqkgstSRPGRELSYRPILVAASIGSYGAYLA-DGSEYSGDYgPSVTLEKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 160 VEAYQEQAKGLLDGGVDILLIETIFDTANAKAALFALQklfEENYASPRpiFISGTIVDksGRTLSgqTGEAFVTSVSHS 239
Cdd:PLN02489 166 KDFHRRRLQVLAEAGPDLIAFETIPNKLEAQAYVELLE---EENIKIPA--WISFNSKD--GVNVV--SGDSLLECASIA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 240 DPlC-----IGLNCAlgaaemrP--FIE----TIGKCTTAYVLCYPNAG----------LPNTfgdyDETPAMMAMHLKD 298
Cdd:PLN02489 237 DS-CkkvvaVGINCT-------PprFIHglilSIRKVTSKPIVVYPNSGetydgeakewVEST----GVSDEDFVSYVNK 304
|
330 340 350
....*....|....*....|....*....|
gi 1958723785 299 FAVDGlVNVVGGCCGSTPDHIREIAEAVKN 328
Cdd:PLN02489 305 WRDAG-ASLIGGCCRTTPNTIRAISKALSE 333
|
|
| Sbm |
COG2185 |
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ... |
762-848 |
2.23e-09 |
|
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and metabolism];
Pssm-ID: 441788 [Multi-domain] Cd Length: 134 Bit Score: 56.69 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 762 TIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILQAALDHKADIIGLSglitpSLDE--MIFVAKEMERL- 838
Cdd:COG2185 12 RVLLAKPGLDGHDRGAKVIARALRDAGFEVIYLGLFQTPEEIVRAAIEEDADVIGVS-----SLDGghLELVPELIELLk 86
|
90
....*....|...
gi 1958723785 839 ---AIKIPLLIGG 848
Cdd:COG2185 87 eagAGDILVVVGG 99
|
|
| PRK02261 |
PRK02261 |
methylaspartate mutase subunit S; Provisional |
762-820 |
4.45e-08 |
|
methylaspartate mutase subunit S; Provisional
Pssm-ID: 179400 [Multi-domain] Cd Length: 137 Bit Score: 53.42 E-value: 4.45e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958723785 762 TIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGL 820
Cdd:PRK02261 5 TVVLGVIGADCHAVGNKILDRALTEAGFEVINLGVMTSQEEFIDAAIETDADAILVSSL 63
|
|
| Glm_B12_BD |
cd02072 |
B12 binding domain of glutamate mutase (Glm). Glutamate mutase catalysis the conversion of (S) ... |
762-820 |
2.42e-07 |
|
B12 binding domain of glutamate mutase (Glm). Glutamate mutase catalysis the conversion of (S)-glutamate with (2S,3S)-3-methylaspartate. The rearrangement reaction is initiated by the extraction of a hydrogen from the protein-bound substrate by a 5'-desoxyadenosyl radical, which is generated by the homolytic cleavage of the organometallic bond of the cofactor B12. Glm is a heterotetrameric molecule consisting of two alpha and two epsilon polypeptide chains.
Pssm-ID: 239023 [Multi-domain] Cd Length: 128 Bit Score: 50.93 E-value: 2.42e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958723785 762 TIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGL 820
Cdd:cd02072 1 TIVLGVIGSDCHAVGNKILDHAFTEAGFNVVNLGVLSPQEEFIDAAIETDADAILVSSL 59
|
|
| MM_CoA_mut_B12_BD |
cd02071 |
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), ... |
763-848 |
7.17e-04 |
|
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), which initiates the conversion of succinyl CoA and methylmalonyl CoA by forming an adenosyl radical, which then undergoes a rearrangement exchanging a hydrogen atom with a group attached to a neighboring carbon atom. This family is present in both mammals and bacteria. Bacterial members are heterodimers and involved in the fermentation of pyruvate to propionate. Mammalian members are homodimers and responsible for the conversion of odd-chain fatty acids and branched-chain amino acids via propionyl CoA to succinyl CoA for further degradation.
Pssm-ID: 239022 [Multi-domain] Cd Length: 122 Bit Score: 40.65 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958723785 763 IVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVM-TPcDKILQAALDHKADIIGLSGLitpSLDEMIFVAKEMERL--- 838
Cdd:cd02071 2 ILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRqTP-EEIVEAAIQEDVDVIGLSSL---SGGHMTLFPEVIELLrel 77
|
90
....*....|.
gi 1958723785 839 -AIKIPLLIGG 848
Cdd:cd02071 78 gAGDILVVGGG 88
|
|
| |
