|
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: 2140.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 1 MKKTLQDEIEAILRKRIMVLDGGMGTMIQRYKLSEEHFQGQEFKDHSRPLKGNNDILSITQPDIIYQIHKEYLLAGADII 80
Cdd:PRK09490 3 DMSSRLAQLRALLAERILVLDGAMGTMIQRYKLEEADYRGERFADWPCDLKGNNDLLVLTQPDVIEAIHRAYLEAGADII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 81 ETNTFSSTSIAQADYGLEHLAYRMNKCSADVARKAAEEITLQTGVK-RFVAGALGPTNKTLSVSPSVERPDYRNITFDEL 159
Cdd:PRK09490 83 ETNTFNATTIAQADYGMESLVYELNFAAARLAREAADEWTAKTPDKpRFVAGVLGPTNRTASISPDVNDPGFRNVTFDEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 160 VDAYQEQAKGLLDGRVDILLIETIFDTANAKAALFAIQNLFEENyAPPRPIFISGTIVDKSGRTLSGQTGEAFVTSVSHS 239
Cdd:PRK09490 163 VAAYREQTRGLIEGGADLILIETIFDTLNAKAAIFAVEEVFEEL-GVRLPVMISGTITDASGRTLSGQTTEAFWNSLRHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 240 DPLCIGLNCSLGAAEMRPFIETIGKCTTAYVLCYPNAGLPNTFGDYDETPSTMATHLKDFAVDGLVNIVGGCCGSTPDHI 319
Cdd:PRK09490 242 KPLSIGLNCALGADELRPYVEELSRIADTYVSAHPNAGLPNAFGEYDETPEEMAAQIGEFAESGFLNIVGGCCGTTPEHI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 320 REIAEAVKKCKPRVPPASvfEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQ 399
Cdd:PRK09490 322 AAIAEAVAGLPPRKLPEI--PVACRLSGLEPLNIDDDSLFVNVGERTNVTGSAKFARLIKEEDYDEALDVARQQVENGAQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 400 VLDINMDDGMLDGPSAMTRFCNSIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEGDFLEKARKIKKF 479
Cdd:PRK09490 400 IIDINMDEGMLDSEAAMVRFLNLIASEPDIARVPIMIDSSKWEVIEAGLKCIQGKGIVNSISLKEGEEKFIEHARLVRRY 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 480 GAAVVVMAFDEEGQATETDVKVNVCTRAYHLLVDKVGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPGV 559
Cdd:PRK09490 480 GAAVVVMAFDEQGQADTRERKIEICKRAYDILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKQNLPHA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 560 RISGGLSNLSFSFRGMEAIREAMHGVFLYHAIKFGMDMGIVNAGNLPVYDAIHKDLLQLCEDLIWNKDSEATEKLLRYAQ 639
Cdd:PRK09490 560 KISGGVSNVSFSFRGNNPVREAIHAVFLYHAIKAGMDMGIVNAGQLAIYDDIPPELREAVEDVVLNRRPDATERLLEIAE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 640 T-HGTGGKKVIQTD-EWRNGSIEERLEYALVKGIEKHIVEDTEEARLngeKYPRPLNIIEGPLMNGMKVVGDLFGAGKMF 717
Cdd:PRK09490 640 KyRGKGGKKAKAEDlEWRSWPVEKRLEHALVKGITEFIEEDTEEARQ---QAARPLEVIEGPLMDGMNVVGDLFGEGKMF 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 718 LPQVIKSARVMKKAVGHLIPFMEKEREEarlingsvEEEDPYQGTIVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVM 797
Cdd:PRK09490 717 LPQVVKSARVMKQAVAYLEPFIEAKKEG--------GTDRKSNGKILMATVKGDVHDIGKNIVGVVLQCNNYEVIDLGVM 788
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 798 TPCDKILQAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAIKIPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDASKS 877
Cdd:PRK09490 789 VPAEKILETAKEENADIIGLSGLITPSLDEMVHVAKEMERQGFTIPLLIGGATTSKAHTAVKIAPNYSGPVVYVTDASRA 868
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 878 VVVCSQLLDENLRDDYFEEILEEYEDIRQDHYESLKERKYVPLSQARKHGFHIDWlSEPHPVKPTFIGTQVFEDYNLQKL 957
Cdd:PRK09490 869 VGVVSSLLSDEQRDAYVAETRAEYEKVREQHARKKPRKPLLTLEAARANRFKIDW-EAYTPPKPKFLGVQVFEDYDLAEL 947
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 958 VDYIDWKPFFDVWQLRGKYpnrgfPKIFNDKAVGEEARKVYNDAQNMLNILISQKKLQARGVVGFWPAQSVQDDIHLYAE 1037
Cdd:PRK09490 948 REYIDWTPFFQTWELAGKY-----PAILEDEVVGEEARKLFADAQAMLDKIIAEKWLTARGVIGLFPANSVGDDIEVYTD 1022
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 1038 gvvPQAAEPIATFYGLRQQAEKDSSstdPYHCLSDFIAPLHSGVCDYLGLFAV-ACFGVEELSKTYEDDGDDYSSIMVKA 1116
Cdd:PRK09490 1023 ---ESRTEVLATLHHLRQQTEKRGR---PNYCLADFVAPKESGKADYIGAFAVtAGLGEDELADRFEAAHDDYNAIMVKA 1096
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 1117 LGDRLAEAFAEELHERVRRELWAYSRSEQLGVPDLRRLRYEGIRPAPGYPSQPDHTEKLTMWRLASIEQATGIRLTESLA 1196
Cdd:PRK09490 1097 LADRLAEAFAEYLHERVRKEFWGYAPDENLSNEELIREKYQGIRPAPGYPACPDHTEKATLFDLLDAEKNTGMKLTESYA 1176
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|...
gi 124487479 1197 MAPASAVSGLYFSNVKAKYFAVGKISKDQTEDYALRKNMPVAEVEKWLGPILG 1249
Cdd:PRK09490 1177 MWPGASVSGWYFSHPESKYFAVGKIGRDQVEDYAARKGMSVEEVERWLAPNLG 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: 2005.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 13 LRKRIMVLDGGMGTMIQRYKLSEEHFQGQeFKDHSRPLKGNNDILSITQPDIIYQIHKEYLLAGADIIETNTFSSTSIAQ 92
Cdd:TIGR02082 1 LNQRILVLDGAMGTQLQSANLTEADFRGA-FADCHRELKGNNDILNLTKPEVIATIHRAYFEAGADIIETNTFNSTTISQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 93 ADYGLEHLAYRMNKCSADVARKAAEEITLQTGVKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVDAYQEQAKGLLD 172
Cdd:TIGR02082 80 ADYDLEDLIYDLNFKGAKLARAVADEFTLTPEKPRFVAGSMGPTNKTATLSPDVERPGFRNVTYDELVDAYTEQAKGLLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 173 GRVDILLIETIFDTANAKAALFAIQNLFEENYAPpRPIFISGTIVDKSGRTLSGQTGEAFVTSVSHSDPLCIGLNCSLGA 252
Cdd:TIGR02082 160 GGVDLLLIETCFDTLNAKAALFAAETVFEEKGRE-LPIMISGTIVDTSGRTLSGQTIEAFLTSLEHAGIDMIGLNCALGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 253 AEMRPFIETIGKCTTAYVLCYPNAGLPNTFGDYDETPSTMATHLKDFAVDGLVNIVGGCCGSTPDHIREIAEAVKKCKPR 332
Cdd:TIGR02082 239 DEMRPHLKHLSEHAEAYVSCHPNAGLPNAFGEYDLTPDELAKALADFAAEGGLNIVGGCCGTTPDHIRAIAEAVKNIKPR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 333 VPPasVFEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQVLDINMDDGMLDG 412
Cdd:TIGR02082 319 QRP--VLYEPSRLSGLEAITIAQDSNFVNIGERTNVAGSKKFRRLIIAEDYDEALDIAKQQVENGAQILDINVDYGMLDG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 413 PSAMTRFCNSIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEGDFLEKARKIKKFGAAVVVMAFDEEG 492
Cdd:TIGR02082 397 VAAMKRFLNLLASEPDISTVPLMLDSSEWAVLEAGLKCIQGKCIVNSISLKDGEERFIETAKLIKEYGAAVVVMAFDEEG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 493 QATETDVKVNVCTRAYHLLVDKVGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPGVRISGGLSNLSFSF 572
Cdd:TIGR02082 477 QARTADRKIEICKRAYNILTEKVGFPPEDIIFDPNILTIATGIEEHRRYAINFIEAIRWIKEELPDAKISGGVSNVSFSF 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 573 RGMEAIREAMHGVFLYHAIKFGMDMGIVNAGNLPVYDAIHKDLLQLCEDLIWNKDSEATEKLLRYAQTH-GTGGK--KVI 649
Cdd:TIGR02082 557 RGNPAAREAMHSVFLYHAIRAGMDMGIVNAGKILPYDDIDPELRQVVEDLILNRRREATEPLLELAQLYeGTTTKssKEA 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 650 QTDEWRNGSIEERLEYALVKGIEKHIVEDTEEARlngEKYPRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMK 729
Cdd:TIGR02082 637 QQAEWRNLPVEERLEYALVKGEREGIEEDLEEAR---KKLTRPLEIIEGPLMDGMKVVGDLFGSGKMFLPQVVKSARVMK 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 730 KAVGHLIPFMEKEReearlingsveEEDPYQGTIVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVMTPCDKILQAALD 809
Cdd:TIGR02082 714 KAVAYLEPHMEKEK-----------SEDSSKGKIVLATVKGDVHDIGKNIVGVVLSCNGYEVVDLGVMVPIEKILEAAKD 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 810 HKADIIGLSGLITPSLDEMIFVAKEMERLAIKIPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDENL 889
Cdd:TIGR02082 783 HNADVIGLSGLITPSLDEMKEVAEEMNRRGITIPLLIGGAATSKTHTAVKIAPIYKGPVVYVLDASRAVTVMDTLMSAKR 862
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 890 RDDYFEEILEEYEDIRQDHYESLKERKYVPLSQARKHGFHIDWLSEPHPVKPTFIGTQVFEDYNLQKLVDYIDWKPFFDV 969
Cdd:TIGR02082 863 KDTENGRIKEEYDTAREKHGEQRSKRIAASEQAARKNVFAPDWSDDIEPPAPPFWGTQIVEASDIAELRPYIDWTPFFLQ 942
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 970 WQLRGKYpnrgfPKIFNDKAVGEEARKVYNDAQNMLNILISQKKLQARGVVGFWPAQSVQDDIHLYAEGVVpqAAEPIAT 1049
Cdd:TIGR02082 943 WQLRGKY-----PKILGDEYEGLEAQKLFPDANEMLDKLSAENLLHARGVYGYFPAQSVGDDIEIYTDETV--ETHPIAT 1015
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 1050 FYGLRQQAEKDSsstDPYHCLSDFIAPLHSGVCDYLGLFAV-ACFGVEELSKTYEDDGDDYSSIMVKALGDRLAEAFAEE 1128
Cdd:TIGR02082 1016 VRYLFHFPRQQS---GRYLCLADFIAPKASGIVDYIGAFAVtAGFGAEELADKLEAQHDDYDYIMVKAIADRLAEAFAEY 1092
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 1129 LHERVRRELWAYSRSEQLGVPDLRRLRYEGIRPAPGYPSQPDHTEKLTMWRLASIEQaTGIRLTESLAMAPASAVSGLYF 1208
Cdd:TIGR02082 1093 LHRRVRKELWGYAAEEPLSNEDLLKLRYQGIRPAPGYPACPDHTEKATMFELLEPER-IGVRLTESLAMHPEQSVSGLYF 1171
|
1210
....*....|
gi 124487479 1209 SNVKAKYFAV 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: 1553.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 24 MGTMIQRYKLSEEHFQGQEFKDHSRPLKGNNDILSITQPDIIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYR 103
Cdd:COG1410 1 MGTMIQLLKLRELDADGAMFTDLQLDLKGNNDLLGLTGPNEILEIHRPELEAGADIIETNTGADAAITAADGAAEALLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 104 MNK-CSADVARKAAEEITLQTGVKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVDAYQEQAKGLLDGRVDILLIET 182
Cdd:COG1410 81 YNGaAAALALEAAAAAAAAAAAAARAVAGAPGPTGGTASPGPDVPGLGFRNFDFDELVEAYAEAGLGLGGGGADLLLTET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 183 IFDTANAKAALFAIQNLFEENYAPPrPIFISGTIVDKSGRTLSGQTGEAFVTSVSHSDPLCIGLNCSLGAAEMRPFIETI 262
Cdd:COG1410 161 IFDTLNAAAAAAAAAAAAEEEGVPI-PVMVTGTITDGSGRTLSGQTAEAFLESLGHAAPGSNGLNCALGAEELRPYLEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 263 GKCTTAYVLCYPNAGLPNTFGDYDETPSTMATHLKDFAVDGLVNIVGGCCGSTPDHIREIAEAVKKCKPRVPPASVFegh 342
Cdd:COG1410 240 SRIPPSAVSNAPNAGLPNGFGEYDETPEEMAAALAEFAEEGGVNIVGGCCGTTPEHIRAIAEAVAGLKPRPREKPPP--- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 343 MLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQVLDINMDDGMLDGPSAMTRFCNS 422
Cdd:COG1410 317 AVLSGLEPVPIGQDSPFVNIGERTNVTGSKKFRELILEGDYDEALEVAREQVEAGAQILDVNVDEPGRDEVAAMVRFLNL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 423 IASEpdiAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEGDFLEKARKIKKFGAAVVVMAFDEEGQATETDVKVN 502
Cdd:COG1410 397 LASE---VRVPLMIDSSKPEVIEAGLKCYQGKPIVNSISLEEGEERFEEVAPLAKKYGAAVVVLAIDEEGQADTAERKLE 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 503 VCTRAYHLLVDKVGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPGVRISGGLSNLSFSFRGmeAIREAM 582
Cdd:COG1410 474 IAERIYDLAVEEYGFPPEDIIFDPLVFTVATGIEEHRNYAVETIEAIRLIKEELPGAKTSLGVSNVSFGLPG--NVREAL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 583 HGVFLYHAIKFGMDMGIVNAGNLPVYDAIHKDLLQLCEDLIWNKDSEATEKLLRYAQTHgTGGKKVIQTDEWRNGSIEER 662
Cdd:COG1410 552 NSVFLYHAIKAGLDMAIVNPGQLEPYDDIPPELRELAEDVLLNRRPDALERLIELFEGV-KGAKAKKADLEWRELPVEER 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 663 LEYALVKGIEKHIVEDTEEARlngEKYPRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKE 742
Cdd:COG1410 631 LKHAIVKGIKEGIEEDTEEAL---AEGARPLEIINGPLMPGMNVVGDLFGAGKMFLPQVLKSAEVMKAAVAYLEPFMEKE 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 743 reearlingsvEEEDPYQGTIVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGLIT 822
Cdd:COG1410 708 -----------KGESSSKGKIVLATVKGDVHDIGKNIVGVVLENNGYEVIDLGVMVPAEKILEAAKEHKADIIGLSGLMT 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 823 PSLDEMIFVAKEMERLAIKIPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDENLRDDYFEEILEEYE 902
Cdd:COG1410 777 TSLDEMKEVAEEMRRRGLDIPVLIGGAALTRAYTAVKIAPAYDGAVVYAKDASRAVRVADKLLSKERREAFVAEIKAEYE 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 903 DIRQDHYEslKERKYVPLSQARKhgfHIDwlSEPHPVKPTFIGTQVFEDYNLQKLVDYIDWKPFFDVWQLRGKYPNrgfp 982
Cdd:COG1410 857 KLRERHAA--RKKKLLSLEEARS---NVD--SDYPPPTPPFLGTRVLKDIPLAELVPYIDWTPFFQQWGLKGKYLD---- 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 983 kifndkavGEEARKVYNDAQNMLNILISQKKLQARGVVGFWPAQSVQDDIHLYAegvvPQAAEPIATFYGLRQQaekdss 1062
Cdd:COG1410 926 --------GEEARELFPDAQAMLDRIIEEKWLTARAVYGYFPANSEGDDIEVYD----DESSEELARFHFPRQQ------ 987
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 1063 sTDPYHCLSDFIAPLHSGVCDYLGLFAV-ACFGVEELSKTYEDDGDDYSSIMVKALGDRLAEAFAEELHERVRRElWAYS 1141
Cdd:COG1410 988 -RGPNLCLADFVAPKESGERDYVGFFAVtAGIGIEELAAELEAAGDDYDAIMLHALADRLAEAFAEYLHERVRKE-WGYA 1065
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124487479 1142 RSEQLGVPDLRRLRYEGIRPAPGYPSQPDHTEKLTMWRLASIEQaTGIRLTESLAMAPASAVSGLYFSNVKAKYFAV 1218
Cdd:COG1410 1066 PDEALTNEDLIKEKYRGIRPAPGYPACPDHTEKRKLFDLLDAER-IGVTLTESFAMHPEASVSGIYFHHPEAKYFNV 1141
|
|
| Met_synt_B12 |
pfam02965 |
Vitamin B12 dependent methionine synthase, activation domain; |
954-1234 |
2.38e-161 |
|
Vitamin B12 dependent methionine synthase, activation domain;
Pssm-ID: 460767 [Multi-domain] Cd Length: 273 Bit Score: 481.97 E-value: 2.38e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 954 LQKLVDYIDWKPFFDVWQLRGKYPnrgfpKIFNDKAVGEEARKVYNDAQNMLNILISQKKLQARGVVGFWPAQSVQDDIH 1033
Cdd:pfam02965 2 LAELVPYIDWTPFFQAWELKGKYP-----AILDDEVVGEEARKLFADAQAMLDRIIEEKWLTARGVVGFFPANSVGDDIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 1034 LYAEGvvpQAAEPIATFYGLRQQAEKDSSstDPYHCLSDFIAPLHSGVCDYLGLFAVAC-FGVEELSKTYEDDGDDYSSI 1112
Cdd:pfam02965 77 VYTDE---SRTEVLATFHTLRQQTEKPEG--RPNLCLADFIAPKESGIADYIGAFAVTAgIGIEELAARFEAAHDDYSAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 1113 MVKALGDRLAEAFAEELHERVRRELWAYSRSEQLGVPDLRRLRYEGIRPAPGYPSQPDHTEKLTMWRLASIEQATGIRLT 1192
Cdd:pfam02965 152 MVKALADRLAEAFAEYLHERVRKELWGYAPDENLSNEDLIKEKYQGIRPAPGYPACPDHTEKFTLFDLLDAEENIGIRLT 231
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 124487479 1193 ESLAMAPASAVSGLYFSNVKAKYFAVGKISKDQTEDYALRKN 1234
Cdd:pfam02965 232 ESFAMTPAASVSGLYFAHPESRYFAVGKIGKDQVEDYAKRKG 273
|
|
| MeTr |
cd00740 |
MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent ... |
359-615 |
9.59e-138 |
|
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: 419.10 E-value: 9.59e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 359 FVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQVLDINMDDGMLDGPSAMTRFCNSIASEPdiaKVPLCIDS 438
Cdd:cd00740 1 FLNIGERTNVTGSKKFRELIKAEDYDEALDVARQQVEGGAQILDLNVDYGGLDGVSAMKWLLNLLATEP---TVPLMLDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 439 SNFAVIEAGLKCCQGKCIVNSISLKEGEGDFLEKARKIKKFGAAVVVMAFDEEGQATETDVKVNVCTRAYHLLVDKVGFN 518
Cdd:cd00740 78 TNWEVIEAGLKCCQGKCVVNSINLEDGEERFLKVARLAKEHGAAVVVLAFDEQGQAKTRDKKVEIAERAYEALTEFVGFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 519 PNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPGVRISGGLSNLSFSFrgMEAIREAMHGVFLYHAIKFGMDMG 598
Cdd:cd00740 158 PEDIIFDPLILPIATGIEEHRPYALETIDAIRMIKERLPAVKISLGVSNVSFGF--NPAAREALNSVFLYEAIKAGLDMA 235
|
250
....*....|....*..
gi 124487479 599 IVNAGNLPVYDAIHKDL 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 |
2.76e-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: 129.13 E-value: 2.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 658 SIEERLEYALVKGIEKHIVEDTEEARLNGEkypRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHLIP 737
Cdd:smart01018 2 PLLERLAEAIVDGDEEGVEELVEEALAEGV---DPLEIINEGLIPGMNVVGDLFEAGEYFLPQVLMSAEAMKAAVAILKP 78
|
....*.
gi 124487479 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: 2140.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 1 MKKTLQDEIEAILRKRIMVLDGGMGTMIQRYKLSEEHFQGQEFKDHSRPLKGNNDILSITQPDIIYQIHKEYLLAGADII 80
Cdd:PRK09490 3 DMSSRLAQLRALLAERILVLDGAMGTMIQRYKLEEADYRGERFADWPCDLKGNNDLLVLTQPDVIEAIHRAYLEAGADII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 81 ETNTFSSTSIAQADYGLEHLAYRMNKCSADVARKAAEEITLQTGVK-RFVAGALGPTNKTLSVSPSVERPDYRNITFDEL 159
Cdd:PRK09490 83 ETNTFNATTIAQADYGMESLVYELNFAAARLAREAADEWTAKTPDKpRFVAGVLGPTNRTASISPDVNDPGFRNVTFDEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 160 VDAYQEQAKGLLDGRVDILLIETIFDTANAKAALFAIQNLFEENyAPPRPIFISGTIVDKSGRTLSGQTGEAFVTSVSHS 239
Cdd:PRK09490 163 VAAYREQTRGLIEGGADLILIETIFDTLNAKAAIFAVEEVFEEL-GVRLPVMISGTITDASGRTLSGQTTEAFWNSLRHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 240 DPLCIGLNCSLGAAEMRPFIETIGKCTTAYVLCYPNAGLPNTFGDYDETPSTMATHLKDFAVDGLVNIVGGCCGSTPDHI 319
Cdd:PRK09490 242 KPLSIGLNCALGADELRPYVEELSRIADTYVSAHPNAGLPNAFGEYDETPEEMAAQIGEFAESGFLNIVGGCCGTTPEHI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 320 REIAEAVKKCKPRVPPASvfEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQ 399
Cdd:PRK09490 322 AAIAEAVAGLPPRKLPEI--PVACRLSGLEPLNIDDDSLFVNVGERTNVTGSAKFARLIKEEDYDEALDVARQQVENGAQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 400 VLDINMDDGMLDGPSAMTRFCNSIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEGDFLEKARKIKKF 479
Cdd:PRK09490 400 IIDINMDEGMLDSEAAMVRFLNLIASEPDIARVPIMIDSSKWEVIEAGLKCIQGKGIVNSISLKEGEEKFIEHARLVRRY 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 480 GAAVVVMAFDEEGQATETDVKVNVCTRAYHLLVDKVGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPGV 559
Cdd:PRK09490 480 GAAVVVMAFDEQGQADTRERKIEICKRAYDILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKQNLPHA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 560 RISGGLSNLSFSFRGMEAIREAMHGVFLYHAIKFGMDMGIVNAGNLPVYDAIHKDLLQLCEDLIWNKDSEATEKLLRYAQ 639
Cdd:PRK09490 560 KISGGVSNVSFSFRGNNPVREAIHAVFLYHAIKAGMDMGIVNAGQLAIYDDIPPELREAVEDVVLNRRPDATERLLEIAE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 640 T-HGTGGKKVIQTD-EWRNGSIEERLEYALVKGIEKHIVEDTEEARLngeKYPRPLNIIEGPLMNGMKVVGDLFGAGKMF 717
Cdd:PRK09490 640 KyRGKGGKKAKAEDlEWRSWPVEKRLEHALVKGITEFIEEDTEEARQ---QAARPLEVIEGPLMDGMNVVGDLFGEGKMF 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 718 LPQVIKSARVMKKAVGHLIPFMEKEREEarlingsvEEEDPYQGTIVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVM 797
Cdd:PRK09490 717 LPQVVKSARVMKQAVAYLEPFIEAKKEG--------GTDRKSNGKILMATVKGDVHDIGKNIVGVVLQCNNYEVIDLGVM 788
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 798 TPCDKILQAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAIKIPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDASKS 877
Cdd:PRK09490 789 VPAEKILETAKEENADIIGLSGLITPSLDEMVHVAKEMERQGFTIPLLIGGATTSKAHTAVKIAPNYSGPVVYVTDASRA 868
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 878 VVVCSQLLDENLRDDYFEEILEEYEDIRQDHYESLKERKYVPLSQARKHGFHIDWlSEPHPVKPTFIGTQVFEDYNLQKL 957
Cdd:PRK09490 869 VGVVSSLLSDEQRDAYVAETRAEYEKVREQHARKKPRKPLLTLEAARANRFKIDW-EAYTPPKPKFLGVQVFEDYDLAEL 947
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 958 VDYIDWKPFFDVWQLRGKYpnrgfPKIFNDKAVGEEARKVYNDAQNMLNILISQKKLQARGVVGFWPAQSVQDDIHLYAE 1037
Cdd:PRK09490 948 REYIDWTPFFQTWELAGKY-----PAILEDEVVGEEARKLFADAQAMLDKIIAEKWLTARGVIGLFPANSVGDDIEVYTD 1022
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 1038 gvvPQAAEPIATFYGLRQQAEKDSSstdPYHCLSDFIAPLHSGVCDYLGLFAV-ACFGVEELSKTYEDDGDDYSSIMVKA 1116
Cdd:PRK09490 1023 ---ESRTEVLATLHHLRQQTEKRGR---PNYCLADFVAPKESGKADYIGAFAVtAGLGEDELADRFEAAHDDYNAIMVKA 1096
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 1117 LGDRLAEAFAEELHERVRRELWAYSRSEQLGVPDLRRLRYEGIRPAPGYPSQPDHTEKLTMWRLASIEQATGIRLTESLA 1196
Cdd:PRK09490 1097 LADRLAEAFAEYLHERVRKEFWGYAPDENLSNEELIREKYQGIRPAPGYPACPDHTEKATLFDLLDAEKNTGMKLTESYA 1176
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|...
gi 124487479 1197 MAPASAVSGLYFSNVKAKYFAVGKISKDQTEDYALRKNMPVAEVEKWLGPILG 1249
Cdd:PRK09490 1177 MWPGASVSGWYFSHPESKYFAVGKIGRDQVEDYAARKGMSVEEVERWLAPNLG 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: 2005.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 13 LRKRIMVLDGGMGTMIQRYKLSEEHFQGQeFKDHSRPLKGNNDILSITQPDIIYQIHKEYLLAGADIIETNTFSSTSIAQ 92
Cdd:TIGR02082 1 LNQRILVLDGAMGTQLQSANLTEADFRGA-FADCHRELKGNNDILNLTKPEVIATIHRAYFEAGADIIETNTFNSTTISQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 93 ADYGLEHLAYRMNKCSADVARKAAEEITLQTGVKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVDAYQEQAKGLLD 172
Cdd:TIGR02082 80 ADYDLEDLIYDLNFKGAKLARAVADEFTLTPEKPRFVAGSMGPTNKTATLSPDVERPGFRNVTYDELVDAYTEQAKGLLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 173 GRVDILLIETIFDTANAKAALFAIQNLFEENYAPpRPIFISGTIVDKSGRTLSGQTGEAFVTSVSHSDPLCIGLNCSLGA 252
Cdd:TIGR02082 160 GGVDLLLIETCFDTLNAKAALFAAETVFEEKGRE-LPIMISGTIVDTSGRTLSGQTIEAFLTSLEHAGIDMIGLNCALGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 253 AEMRPFIETIGKCTTAYVLCYPNAGLPNTFGDYDETPSTMATHLKDFAVDGLVNIVGGCCGSTPDHIREIAEAVKKCKPR 332
Cdd:TIGR02082 239 DEMRPHLKHLSEHAEAYVSCHPNAGLPNAFGEYDLTPDELAKALADFAAEGGLNIVGGCCGTTPDHIRAIAEAVKNIKPR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 333 VPPasVFEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQVLDINMDDGMLDG 412
Cdd:TIGR02082 319 QRP--VLYEPSRLSGLEAITIAQDSNFVNIGERTNVAGSKKFRRLIIAEDYDEALDIAKQQVENGAQILDINVDYGMLDG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 413 PSAMTRFCNSIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEGDFLEKARKIKKFGAAVVVMAFDEEG 492
Cdd:TIGR02082 397 VAAMKRFLNLLASEPDISTVPLMLDSSEWAVLEAGLKCIQGKCIVNSISLKDGEERFIETAKLIKEYGAAVVVMAFDEEG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 493 QATETDVKVNVCTRAYHLLVDKVGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPGVRISGGLSNLSFSF 572
Cdd:TIGR02082 477 QARTADRKIEICKRAYNILTEKVGFPPEDIIFDPNILTIATGIEEHRRYAINFIEAIRWIKEELPDAKISGGVSNVSFSF 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 573 RGMEAIREAMHGVFLYHAIKFGMDMGIVNAGNLPVYDAIHKDLLQLCEDLIWNKDSEATEKLLRYAQTH-GTGGK--KVI 649
Cdd:TIGR02082 557 RGNPAAREAMHSVFLYHAIRAGMDMGIVNAGKILPYDDIDPELRQVVEDLILNRRREATEPLLELAQLYeGTTTKssKEA 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 650 QTDEWRNGSIEERLEYALVKGIEKHIVEDTEEARlngEKYPRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMK 729
Cdd:TIGR02082 637 QQAEWRNLPVEERLEYALVKGEREGIEEDLEEAR---KKLTRPLEIIEGPLMDGMKVVGDLFGSGKMFLPQVVKSARVMK 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 730 KAVGHLIPFMEKEReearlingsveEEDPYQGTIVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVMTPCDKILQAALD 809
Cdd:TIGR02082 714 KAVAYLEPHMEKEK-----------SEDSSKGKIVLATVKGDVHDIGKNIVGVVLSCNGYEVVDLGVMVPIEKILEAAKD 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 810 HKADIIGLSGLITPSLDEMIFVAKEMERLAIKIPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDENL 889
Cdd:TIGR02082 783 HNADVIGLSGLITPSLDEMKEVAEEMNRRGITIPLLIGGAATSKTHTAVKIAPIYKGPVVYVLDASRAVTVMDTLMSAKR 862
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 890 RDDYFEEILEEYEDIRQDHYESLKERKYVPLSQARKHGFHIDWLSEPHPVKPTFIGTQVFEDYNLQKLVDYIDWKPFFDV 969
Cdd:TIGR02082 863 KDTENGRIKEEYDTAREKHGEQRSKRIAASEQAARKNVFAPDWSDDIEPPAPPFWGTQIVEASDIAELRPYIDWTPFFLQ 942
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 970 WQLRGKYpnrgfPKIFNDKAVGEEARKVYNDAQNMLNILISQKKLQARGVVGFWPAQSVQDDIHLYAEGVVpqAAEPIAT 1049
Cdd:TIGR02082 943 WQLRGKY-----PKILGDEYEGLEAQKLFPDANEMLDKLSAENLLHARGVYGYFPAQSVGDDIEIYTDETV--ETHPIAT 1015
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 1050 FYGLRQQAEKDSsstDPYHCLSDFIAPLHSGVCDYLGLFAV-ACFGVEELSKTYEDDGDDYSSIMVKALGDRLAEAFAEE 1128
Cdd:TIGR02082 1016 VRYLFHFPRQQS---GRYLCLADFIAPKASGIVDYIGAFAVtAGFGAEELADKLEAQHDDYDYIMVKAIADRLAEAFAEY 1092
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 1129 LHERVRRELWAYSRSEQLGVPDLRRLRYEGIRPAPGYPSQPDHTEKLTMWRLASIEQaTGIRLTESLAMAPASAVSGLYF 1208
Cdd:TIGR02082 1093 LHRRVRKELWGYAAEEPLSNEDLLKLRYQGIRPAPGYPACPDHTEKATMFELLEPER-IGVRLTESLAMHPEQSVSGLYF 1171
|
1210
....*....|
gi 124487479 1209 SNVKAKYFAV 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: 1553.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 24 MGTMIQRYKLSEEHFQGQEFKDHSRPLKGNNDILSITQPDIIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYR 103
Cdd:COG1410 1 MGTMIQLLKLRELDADGAMFTDLQLDLKGNNDLLGLTGPNEILEIHRPELEAGADIIETNTGADAAITAADGAAEALLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 104 MNK-CSADVARKAAEEITLQTGVKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVDAYQEQAKGLLDGRVDILLIET 182
Cdd:COG1410 81 YNGaAAALALEAAAAAAAAAAAAARAVAGAPGPTGGTASPGPDVPGLGFRNFDFDELVEAYAEAGLGLGGGGADLLLTET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 183 IFDTANAKAALFAIQNLFEENYAPPrPIFISGTIVDKSGRTLSGQTGEAFVTSVSHSDPLCIGLNCSLGAAEMRPFIETI 262
Cdd:COG1410 161 IFDTLNAAAAAAAAAAAAEEEGVPI-PVMVTGTITDGSGRTLSGQTAEAFLESLGHAAPGSNGLNCALGAEELRPYLEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 263 GKCTTAYVLCYPNAGLPNTFGDYDETPSTMATHLKDFAVDGLVNIVGGCCGSTPDHIREIAEAVKKCKPRVPPASVFegh 342
Cdd:COG1410 240 SRIPPSAVSNAPNAGLPNGFGEYDETPEEMAAALAEFAEEGGVNIVGGCCGTTPEHIRAIAEAVAGLKPRPREKPPP--- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 343 MLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQVLDINMDDGMLDGPSAMTRFCNS 422
Cdd:COG1410 317 AVLSGLEPVPIGQDSPFVNIGERTNVTGSKKFRELILEGDYDEALEVAREQVEAGAQILDVNVDEPGRDEVAAMVRFLNL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 423 IASEpdiAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEGDFLEKARKIKKFGAAVVVMAFDEEGQATETDVKVN 502
Cdd:COG1410 397 LASE---VRVPLMIDSSKPEVIEAGLKCYQGKPIVNSISLEEGEERFEEVAPLAKKYGAAVVVLAIDEEGQADTAERKLE 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 503 VCTRAYHLLVDKVGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPGVRISGGLSNLSFSFRGmeAIREAM 582
Cdd:COG1410 474 IAERIYDLAVEEYGFPPEDIIFDPLVFTVATGIEEHRNYAVETIEAIRLIKEELPGAKTSLGVSNVSFGLPG--NVREAL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 583 HGVFLYHAIKFGMDMGIVNAGNLPVYDAIHKDLLQLCEDLIWNKDSEATEKLLRYAQTHgTGGKKVIQTDEWRNGSIEER 662
Cdd:COG1410 552 NSVFLYHAIKAGLDMAIVNPGQLEPYDDIPPELRELAEDVLLNRRPDALERLIELFEGV-KGAKAKKADLEWRELPVEER 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 663 LEYALVKGIEKHIVEDTEEARlngEKYPRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKE 742
Cdd:COG1410 631 LKHAIVKGIKEGIEEDTEEAL---AEGARPLEIINGPLMPGMNVVGDLFGAGKMFLPQVLKSAEVMKAAVAYLEPFMEKE 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 743 reearlingsvEEEDPYQGTIVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGLIT 822
Cdd:COG1410 708 -----------KGESSSKGKIVLATVKGDVHDIGKNIVGVVLENNGYEVIDLGVMVPAEKILEAAKEHKADIIGLSGLMT 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 823 PSLDEMIFVAKEMERLAIKIPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDENLRDDYFEEILEEYE 902
Cdd:COG1410 777 TSLDEMKEVAEEMRRRGLDIPVLIGGAALTRAYTAVKIAPAYDGAVVYAKDASRAVRVADKLLSKERREAFVAEIKAEYE 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 903 DIRQDHYEslKERKYVPLSQARKhgfHIDwlSEPHPVKPTFIGTQVFEDYNLQKLVDYIDWKPFFDVWQLRGKYPNrgfp 982
Cdd:COG1410 857 KLRERHAA--RKKKLLSLEEARS---NVD--SDYPPPTPPFLGTRVLKDIPLAELVPYIDWTPFFQQWGLKGKYLD---- 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 983 kifndkavGEEARKVYNDAQNMLNILISQKKLQARGVVGFWPAQSVQDDIHLYAegvvPQAAEPIATFYGLRQQaekdss 1062
Cdd:COG1410 926 --------GEEARELFPDAQAMLDRIIEEKWLTARAVYGYFPANSEGDDIEVYD----DESSEELARFHFPRQQ------ 987
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 1063 sTDPYHCLSDFIAPLHSGVCDYLGLFAV-ACFGVEELSKTYEDDGDDYSSIMVKALGDRLAEAFAEELHERVRRElWAYS 1141
Cdd:COG1410 988 -RGPNLCLADFVAPKESGERDYVGFFAVtAGIGIEELAAELEAAGDDYDAIMLHALADRLAEAFAEYLHERVRKE-WGYA 1065
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124487479 1142 RSEQLGVPDLRRLRYEGIRPAPGYPSQPDHTEKLTMWRLASIEQaTGIRLTESLAMAPASAVSGLYFSNVKAKYFAV 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: 894.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 7 DEIEAILRKRIMVLDGGMGTMIQRYKLSEEHFQGqefkdhsrpLKGNNDILSITQPDIIYQIHKEYLLAGADIIETNTFS 86
Cdd:COG0646 4 AALLELLKERILILDGAMGTMLQAYGLTEGDFRG---------EKGCNELLNLTRPDVIREIHRAYLEAGADIIETNTFG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 87 STSIAQADYGLEHLAYRMNKCSADVARKAAEEITlqtGVKRFVAGALGPTNKTLSvspsverpDYRNITFDELVDAYQEQ 166
Cdd:COG0646 75 ANRIKLADYGLEDRVYEINRAAARLAREAADEFS---DRPRFVAGSIGPTGKLLS--------PLGNITFDELVEAYREQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 167 AKGLLDGRVDILLIETIFDTANAKAALFAIQNLFEENyAPPRPIFISGTIvDKSGRTLSGQTGEAFVTSVSHSDPLCIGL 246
Cdd:COG0646 144 AEGLIEGGVDLLLIETIFDTLEAKAAIFAAREAFEEL-GRDLPVMVSGTF-DASGRTLSGQTPEAFATSLEHLGPDAIGL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 247 NCSLGAAEMRPFIETIGKCTTAYVLCYPNAGLPNTFGD---YDETPSTMATHLKDFAVDGLVNIVGGCCGSTPDHIREIA 323
Cdd:COG0646 222 NCALGPDEMRPHVEELSEVADTPVSAYPNAGLPNLVGGrtvYDETPEEMAEYAEEFAEAGGVNIVGGCCGTTPEHIRAIA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 324 EAVKKCKPRVPPASvfEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQVLDI 403
Cdd:COG0646 302 EAVKGLPPRKRPPP--PPALRLSGLEPLTITQDSLFVNVGERTNVTGSKKFARLILEGDYDAALAVARQQVEAGAQVIDV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 404 NMDDGMLDGPSAMTRFCNSIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEGDFLEKARKIKKFGAAV 483
Cdd:COG0646 380 NMDEGMLDGEAAMVEFLNLIASEPDIPRVPDMIDSSKWEVIEAGLKGVQGKGIVNSISLKEGEEKFLELAKLVRRYGAAV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 484 VVMAFDEEGQATETDVKVNVCTRAYHLLVDKVGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPGVRISG 563
Cdd:COG0646 460 VVMAFDEEGQADTAERKVEICARAYDLLTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKLNLPHALVSG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 564 GLSNLSFSFRGMEAIREAMHGVFLYHAIKFGMDMGIVNAGNLPVYDAIHKDLLQLCEDLIWNKDSEATEKLLRYAQT-HG 642
Cdd:COG0646 540 GVSNVSFSFRGNNPVREAIHAVFLYHAIAAGMDMGIVNAGQLAIYEEIPEELLLLVEDVVLNRREDATERLLEIAEEvKG 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 643 TGGKKVIQTDEWRNGSIEERLEYALVKGIEKHIVEDTEEARLngEKYPRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVI 722
Cdd:COG0646 620 AGKAAEEEAEEERREEEEERLLELLLVGGIEIDEEDDEEAAL--LLAALELIIIELLLGGGMVVGGLGGGGGKLLLVVVV 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 723 KSARVMKKAVGHLIPFMEKEREEARLINgsveeedpyqGTIVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVMTPCDK 802
Cdd:COG0646 698 KAVVKKKVAVALLKPEEEEKKKGGGKGG----------GVVVGVVVKVVVDDVDIIIVVVVVVVNNGIVVLVVVVIVVVA 767
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 124487479 803 ILQAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAIKIPL 844
Cdd:COG0646 768 LEAAAAAEAAVILLVGGLVLLLLEEEVLAAAEAAAEAAVLLL 809
|
|
| Met_synt_B12 |
pfam02965 |
Vitamin B12 dependent methionine synthase, activation domain; |
954-1234 |
2.38e-161 |
|
Vitamin B12 dependent methionine synthase, activation domain;
Pssm-ID: 460767 [Multi-domain] Cd Length: 273 Bit Score: 481.97 E-value: 2.38e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 954 LQKLVDYIDWKPFFDVWQLRGKYPnrgfpKIFNDKAVGEEARKVYNDAQNMLNILISQKKLQARGVVGFWPAQSVQDDIH 1033
Cdd:pfam02965 2 LAELVPYIDWTPFFQAWELKGKYP-----AILDDEVVGEEARKLFADAQAMLDRIIEEKWLTARGVVGFFPANSVGDDIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 1034 LYAEGvvpQAAEPIATFYGLRQQAEKDSSstDPYHCLSDFIAPLHSGVCDYLGLFAVAC-FGVEELSKTYEDDGDDYSSI 1112
Cdd:pfam02965 77 VYTDE---SRTEVLATFHTLRQQTEKPEG--RPNLCLADFIAPKESGIADYIGAFAVTAgIGIEELAARFEAAHDDYSAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 1113 MVKALGDRLAEAFAEELHERVRRELWAYSRSEQLGVPDLRRLRYEGIRPAPGYPSQPDHTEKLTMWRLASIEQATGIRLT 1192
Cdd:pfam02965 152 MVKALADRLAEAFAEYLHERVRKELWGYAPDENLSNEDLIKEKYQGIRPAPGYPACPDHTEKFTLFDLLDAEENIGIRLT 231
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 124487479 1193 ESLAMAPASAVSGLYFSNVKAKYFAVGKISKDQTEDYALRKN 1234
Cdd:pfam02965 232 ESFAMTPAASVSGLYFAHPESRYFAVGKIGKDQVEDYAKRKG 273
|
|
| MeTr |
cd00740 |
MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent ... |
359-615 |
9.59e-138 |
|
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: 419.10 E-value: 9.59e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 359 FVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQVLDINMDDGMLDGPSAMTRFCNSIASEPdiaKVPLCIDS 438
Cdd:cd00740 1 FLNIGERTNVTGSKKFRELIKAEDYDEALDVARQQVEGGAQILDLNVDYGGLDGVSAMKWLLNLLATEP---TVPLMLDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 439 SNFAVIEAGLKCCQGKCIVNSISLKEGEGDFLEKARKIKKFGAAVVVMAFDEEGQATETDVKVNVCTRAYHLLVDKVGFN 518
Cdd:cd00740 78 TNWEVIEAGLKCCQGKCVVNSINLEDGEERFLKVARLAKEHGAAVVVLAFDEQGQAKTRDKKVEIAERAYEALTEFVGFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 519 PNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPGVRISGGLSNLSFSFrgMEAIREAMHGVFLYHAIKFGMDMG 598
Cdd:cd00740 158 PEDIIFDPLILPIATGIEEHRPYALETIDAIRMIKERLPAVKISLGVSNVSFGF--NPAAREALNSVFLYEAIKAGLDMA 235
|
250
....*....|....*..
gi 124487479 599 IVNAGNLPVYDAIHKDL 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 |
1.11e-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: 406.65 E-value: 1.11e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 659 IEERLEYALVKGIEKHIVEDTEEARLngeKYPRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPF 738
Cdd:cd02069 1 VEERLKHALVKGIRDGIEEDTEEARQ---QYARPLEIINGPLMDGMKVVGDLFGAGKMFLPQVLKSARVMKAAVAYLEPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 739 MEKEreearlingsvEEEDPYQGTIVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVMTPCDKILQAALDHKADIIGLS 818
Cdd:cd02069 78 MEKE-----------KGENSSKGKIVLATVKGDVHDIGKNLVGVILSNNGYEVIDLGVMVPIEKILEAAKEHKADIIGLS 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124487479 819 GLITPSLDEMIFVAKEMERLAIKIPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLL 885
Cdd:cd02069 147 GLLVPSLDEMVEVAEEMNRRGIKIPLLIGGAATSRKHTAVKIAPEYDGPVVYVKDASRALGVANKLL 213
|
|
| S-methyl_trans |
pfam02574 |
Homocysteine S-methyltransferase; This is a family of related homocysteine ... |
18-326 |
7.94e-103 |
|
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: 326.42 E-value: 7.94e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 18 MVLDGGMGTMIQRYKLseehfqgqefkDHSRPLkGNNDILsiTQPDIIYQIHKEYLLAGADIIETNTFSSTSIAQAD-YG 96
Cdd:pfam02574 1 LILDGGMGTELQRRGL-----------DLTEPL-WSNELL--TRPEIIREIHRDYLEAGADIIETNTYQASPIKLAEgLE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 97 LEHLAYRMNKCSADVARKAAEEitlqtgvkRFVAGALGPTNKTLSVSPSverpdyrnITFDELVDAYQEQAKGLLDGRVD 176
Cdd:pfam02574 67 EEEAVYELNRAAVRLAREAADE--------YFVAGSIGPYGATLSDGYG--------LSFDELVDFHREQLEALLDGGVD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 177 ILLIETIFDTANAKAALFAIQNLfeenyaPPRPIFISGTIVDKsGRTLSGQTGEAFVTSVSHS-DPLCIGLNCSLgAAEM 255
Cdd:pfam02574 131 LLLFETIPDLLEAKAALELLAEE------PDLPVWISFTIEDG-TRLRSGTTLEAAVAALLHAtGPLAVGVNCAL-PEEM 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124487479 256 RPFIETIGKCTTAYVLCYPNAglpntFGD-YDETPSTMATHLKDFAVDGlVNIVGGCCGSTPDHIREIAEAV 326
Cdd:pfam02574 203 LPLLKELAKDAPTPVSVYPNS-----TGEvYDLTPEEWAEYAEGWLEAG-ANIIGGCCGTTPEHIRAIAEAL 268
|
|
| Pterin_bind |
pfam00809 |
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ... |
363-601 |
1.93e-75 |
|
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: 249.90 E-value: 1.93e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 363 GERCNVAGSRKFAKLIMaGNYEEALSIAKAQVEMGAQVLDINMDDG-----MLDGPSAMTRFCNSIASEPDIAKVPLCID 437
Cdd:pfam00809 1 MGILNVTPDSFSDGGRF-LDLDKALAHARRMVEEGADIIDIGGESTrpgaeRVDGEEEMERVLPVLAALRDEADVPISVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 438 SSNFAVIEAGLKCcqGKCIVNSISLKEGegdFLEKARKIKKFGAAVVVMAFD--------EEGQATETDVKVNVCTRAYH 509
Cdd:pfam00809 80 TTKAEVAEAALKA--GADIINDISGGDG---DPEMAELAAEYGAAVVVMHMDgtpktmqeNEQQYEDVVEEVERFLRARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 510 LLVDKVGFNPNDIIFDPNILTigTGMEEHNLYAINFIHATRVIKetlpGVRISGGLSNLSFSFRGME---AIREAMHGVF 586
Cdd:pfam00809 155 AAAEEAGVPPEDIILDPGIGF--GKTEEHNLELLRTLDELRVIL----GVPVLLGVSRKSFIGRGLPlggEERDAGTAAF 228
|
250
....*....|....*
gi 124487479 587 LYHAIKFGMDMGIVN 601
Cdd:pfam00809 229 LALAIAAGADIVRVH 243
|
|
| Pterin_binding |
cd00423 |
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and ... |
359-612 |
1.11e-62 |
|
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: 214.44 E-value: 1.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 359 FVNIGErCNVAGSRKFAkLIMAGNYEEALSIAKAQVEMGAQVLDINMDDG--------MLDGPSAMTRFCNSIASEPDia 430
Cdd:cd00423 1 TLIMGI-LNVTPDSFSD-GGKFLSLDKALEHARRMVEEGADIIDIGGESTrpgaepvsVEEELERVIPVLRALAGEPD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 431 kVPLCIDSSNFAVIEAGLKCcqGKCIVNSISLKEGEGDFLEKARkikKFGAAVVVMAFDEEGQ--------ATETDVKVN 502
Cdd:cd00423 77 -VPISVDTFNAEVAEAALKA--GADIINDVSGGRGDPEMAPLAA---EYGAPVVLMHMDGTPQtmqnnpyyADVVDEVVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 503 VCTRAYHLLVDkVGFNPNDIIFDPNILTIGTgmEEHNLYAINFIHATRVIketlPGVRISGGLSNLSFSFR---GMEAIR 579
Cdd:cd00423 151 FLEERVEAATE-AGIPPEDIILDPGIGFGKT--EEHNLELLRRLDAFREL----PGLPLLLGVSRKSFLGDllsVGPKDR 223
|
250 260 270
....*....|....*....|....*....|...
gi 124487479 580 EAMHGVFLYHAIKFGMDMGIVNAgNLPVYDAIH 612
Cdd:cd00423 224 LAGTAAFLAAAILNGADIVRVHD-VKELRDAIK 255
|
|
| PRK08645 |
PRK08645 |
bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; ... |
13-331 |
6.45e-61 |
|
bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; Reviewed
Pssm-ID: 236321 [Multi-domain] Cd Length: 612 Bit Score: 220.49 E-value: 6.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 13 LRKRIMVLDGGMGTMIqryklseehfqgqefkdHSR--PLKGNNDILSITQPDIIYQIHKEYLLAGADIIETNTFSSTSI 90
Cdd:PRK08645 8 LKERVLIADGAMGTLL-----------------YSRgvPLDRCFEELNLSHPELILRIHREYIEAGADVIQTNTFGANRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 91 AQADYGLEHLAYRMNKCSADVARKAAEEitlqtgvKRFVAGALGPTNKtlsvspsveRPDYRNITFDELVDAYQEQAKGL 170
Cdd:PRK08645 71 KLKRYGLEDKVKEINRAAVRLAREAAGD-------DVYVAGTIGPIGG---------RGPLGDISLEEIRREFREQIDAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 171 LDGRVDILLIETIFDTANAKAALFAIQNLFeenyapPRPIFISGTiVDKSGRTLSGQTGEAFVTSVSHSDPLCIGLNCSL 250
Cdd:PRK08645 135 LEEGVDGLLLETFYDLEELLLALEAAREKT------DLPIIAQVA-FHEDGVTQNGTSLEEALKELVAAGADVVGLNCGL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 251 GAAEMRPFIETIGKCTTAYVLCYPNAGLPNTFGD---YDETPSTMATHLKDFAVDGlVNIVGGCCGSTPDHIREIAEAVK 327
Cdd:PRK08645 208 GPYHMLEALERIPIPENAPLSAYPNAGLPEYVDGryvYSANPEYFAEYALEFVEQG-VRLIGGCCGTTPEHIRAMARALK 286
|
....
gi 124487479 328 KCKP 331
Cdd:PRK08645 287 GLKP 290
|
|
| MHT1 |
COG2040 |
Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) [Amino acid transport and ... |
13-327 |
4.14e-45 |
|
Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) [Amino acid transport and metabolism];
Pssm-ID: 441643 [Multi-domain] Cd Length: 301 Bit Score: 165.37 E-value: 4.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 13 LRKRIMVLDGGMGTMIQR--YKLSEEHFQgqefkdhSRPLkgnndilsITQPDIIYQIHKEYLLAGADIIETNTFSST-- 88
Cdd:COG2040 9 LMGRILLLDGGMGTELERrgGDLLDPLWS-------AFAL--------LEAPELVRAVHRDYFAAGADVITTNSYQASpd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 89 SIAQADYGLEHLAyRMNKCSADVARKAAEEITlqTGVKRFVAGALGPTNktlsvspSVERPDYRnITFDELVDAYQEQAK 168
Cdd:COG2040 74 GLAELGYSAEEAE-RLNRRAVALAREARDEYT--PGPPVLVAGSVGPYG-------DEYRPDYG-LSAEEAEAYHRPRIE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 169 GLLDGRVDILLIETIFDTANAKAALFAIQNLfeenyapPRPIFISGTiVDKSGRTLSGQT-GEAFVTSVSHSDPLCIGLN 247
Cdd:COG2040 143 ALAEAGVDLLAAETIPSLAEAIAIARAAAEA-------GKPVWISFT-VEDDGRLRSGEPlAEAIAAVDTDPGPAAVGVN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 248 CSlGAAEMRPFIETIGKCTTAYVLCYPNAG------LPNTFGDYDETPSTMATHLKDFAVDGLvNIVGGCCGSTPDHIRE 321
Cdd:COG2040 215 CS-HPEHFEAALEALAAWTGRPIGVYANAGemsdaeLKTWGGLDDGDPEELAEQAAEWVAAGA-RIIGGCCGTGPRHIAA 292
|
....*.
gi 124487479 322 IAEAVK 327
Cdd:COG2040 293 IARALR 298
|
|
| corrinoid_protein_B12-BD |
cd02070 |
B12 binding domain of corrinoid proteins. A family of small methanogenic corrinoid proteins ... |
666-880 |
4.68e-44 |
|
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: 158.55 E-value: 4.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 666 ALVKGIEKHIVEDTEEARLNGEKyprPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREE 745
Cdd:cd02070 4 AIVDGDEEETVELVKKALEAGID---PQDIIEEGLAPGMDIVGDKYEEGEIFVPELLMAADAMKAGLDLLKPLLGKSKSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 746 ArlingsveeedpyQGTIVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGLITPSL 825
Cdd:cd02070 81 K-------------KGKVVIGTVEGDIHDIGKNLVATMLEANGFEVIDLGRDVPPEEFVEAVKEHKPDILGLSALMTTTM 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 124487479 826 DEMIFVAKEMER--LAIKIPLLIGGATTSRTHtAVKIAPRYSAPvihvlDASKSVVV 880
Cdd:cd02070 148 GGMKEVIEALKEagLRDKVKVMVGGAPVNQEF-ADEIGADGYAE-----DAAEAVAI 198
|
|
| MtbC1 |
COG5012 |
Methanogenic corrinoid protein MtbC1 [Energy production and conversion]; |
661-849 |
1.31e-43 |
|
Methanogenic corrinoid protein MtbC1 [Energy production and conversion];
Pssm-ID: 444036 [Multi-domain] Cd Length: 219 Bit Score: 158.13 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 661 ERLEYALVKGIEKHIVEDTEEARLNGEKyprPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFME 740
Cdd:COG5012 12 ESLADAVLEGDEDEALELVAEALAAGMD---PEEIILDGLAPGMREVGELWEEGEIFVPEEHLAAAAMKAGLEILKPLLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 741 KEREearlingsveeedpYQGTIVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGL 820
Cdd:COG5012 89 EEGG--------------RKGKVVIGTVEGDLHDIGKNIVADMLRAAGFEVIDLGADVPPEEFVEAAKEEKPDIVGLSAL 154
|
170 180 190
....*....|....*....|....*....|.
gi 124487479 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 |
7.56e-42 |
|
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: 149.19 E-value: 7.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 762 TIVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAI- 840
Cdd:cd02067 1 KVVIATVGGDGHDIGKNIVARALRDAGFEVIDLGVDVPPEEIVEAAKEEDADAIGLSGLLTTHMTLMKEVIEELKEAGLd 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 124487479 841 KIPLLIGGATTSRTHtavkIAPRYSAPVIHVLDASKSVVV 880
Cdd:cd02067 81 DIPVLVGGAIVTRDF----KFLKEIGVDAYFGPATEAVEV 116
|
|
| PRK07535 |
PRK07535 |
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase; Validated |
362-612 |
1.02e-37 |
|
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase; Validated
Pssm-ID: 181022 [Multi-domain] Cd Length: 261 Bit Score: 142.68 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 362 IGERCNvaGSRK-FAKLIMAGNYEEALSIAKAQVEMGAQVLDINMDDGMLDGPSAMTRFCNSIAsepDIAKVPLCIDSSN 440
Cdd:PRK07535 4 IGERIN--GTRKsIAEAIEAKDAAFIQKLALKQAEAGADYLDVNAGTAVEEEPETMEWLVETVQ---EVVDVPLCIDSPN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 441 FAVIEAGLKCCQGKCIVNSISlkeGEGDFLEKARK-IKKFGAAVVVMAFDEEGQATETDVKVNVctrAYHLL--VDKVGF 517
Cdd:PRK07535 79 PAAIEAGLKVAKGPPLINSVS---AEGEKLEVVLPlVKKYNAPVVALTMDDTGIPKDAEDRLAV---AKELVekADEYGI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 518 NPNDIIFDPNILTIGTgMEEHnlyAINFIHATRVIKETLPGVRISGGLSNLSFsfrGMEAiREAMHGVFLYHAIKFGMDM 597
Cdd:PRK07535 153 PPEDIYIDPLVLPLSA-AQDA---GPEVLETIRRIKELYPKVHTTCGLSNISF---GLPN-RKLINRAFLVMAMGAGMDS 224
|
250
....*....|....*
gi 124487479 598 GIVNAGNLPVYDAIH 612
Cdd:PRK07535 225 AILDPLDRDLMGAIA 239
|
|
| PRK07534 |
PRK07534 |
betaine--homocysteine S-methyltransferase; |
55-338 |
6.89e-36 |
|
betaine--homocysteine S-methyltransferase;
Pssm-ID: 236045 [Multi-domain] Cd Length: 336 Bit Score: 139.50 E-value: 6.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 55 DILSITQPDIIYQIHKEYLLAGADIIETNTFSSTS----IAQADYGLEHLayrmNKCSADVARKAAEEitlqTGVKRFVA 130
Cdd:PRK07534 37 ELWNEDHPDNITALHQGFVDAGSDIILTNSFGGTAarlkLHDAQDRVHEL----NRAAAEIAREVADK----AGRKVIVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 131 GALGPTNKTLSVSPSverpdyrnITFDELVDAYQEQAKGLLDGRVDILLIETIFDTANAKAALFAIQnlfeenyAPPRPI 210
Cdd:PRK07534 109 GSVGPTGEIMEPMGA--------LTHALAVEAFHEQAEGLKAGGADVLWVETISAPEEIRAAAEAAK-------LAGMPW 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 211 FISGTIvDKSGRTLSGQTGEAF---VTSVSHSdPLCIGLNCSLGAAE-MRPFIETIGKCTTAYVLCYPNAGLPNTFGD-- 284
Cdd:PRK07534 174 CGTMSF-DTAGRTMMGLTPADLadlVEKLGEP-PLAFGANCGVGASDlLRTVLGFTAQGPERPIIAKGNAGIPKYVDGhi 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 124487479 285 -YDETPSTMATHLKdFAVDGLVNIVGGCCGSTPDHIREIAEAVKKcKPRVPPASV 338
Cdd:PRK07534 252 hYDGTPELMAEYAV-LARDAGARIIGGCCGTMPEHLAAMRAALDA-RPRGPRPSL 304
|
|
| B12-binding_2 |
smart01018 |
B12 binding domain; Cobalamin-dependent methionine synthase is a large modular protein that ... |
658-743 |
2.76e-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: 129.13 E-value: 2.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 658 SIEERLEYALVKGIEKHIVEDTEEARLNGEkypRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHLIP 737
Cdd:smart01018 2 PLLERLAEAIVDGDEEGVEELVEEALAEGV---DPLEIINEGLIPGMNVVGDLFEAGEYFLPQVLMSAEAMKAAVAILKP 78
|
....*.
gi 124487479 738 FMEKER 743
Cdd:smart01018 79 LLEKEK 84
|
|
| mmuM |
PRK09485 |
homocysteine methyltransferase; Provisional |
10-328 |
1.05e-34 |
|
homocysteine methyltransferase; Provisional
Pssm-ID: 181899 [Multi-domain] Cd Length: 304 Bit Score: 135.37 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 10 EAILRKRIMVLDGGMGTMIQR--YKLseehfqgqefkdhsrplkgNNDILS----ITQPDIIYQIHKEYLLAGADIIETN 83
Cdd:PRK09485 6 ELLAQGPVLILDGALATELEArgCDL-------------------NDSLWSakvlLENPELIYQVHLDYFRAGADCAITA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 84 TFSSTSIAQADYGL-EHLAYRMNKCSADVARKAAEEiTLQTgvKRFVAGALGPTNKTLSvSPSVERPDYrNITFDELVDA 162
Cdd:PRK09485 67 SYQATFQGFAARGLsEAEAEELIRRSVELAKEARDE-FWAE--KPLVAGSVGPYGAYLA-DGSEYRGDY-GLSEEELQDF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 163 YQEQAKGLLDGRVDILLIETIFDTANAKAALFAIQNLFEENYApprpiFISGTIVDksGRTLSGQT--GEAFVTSVSHSD 240
Cdd:PRK09485 142 HRPRIEALAEAGADLLACETIPNLDEAEALVELLKEEFPGVPA-----WLSFTLRD--GTHISDGTplAEAAALLAASPQ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 241 PLCIGLNCSlGAAEMRPFIETIGKCTTAYVLCYPNAGlpntfGDYD---------ETPSTMATHLKDFAVDGlVNIVGGC 311
Cdd:PRK09485 215 VVAVGVNCT-APELVTAAIAALRAVTDKPLVVYPNSG-----EVYDavtktwhgpADDASLGELAPEWYAAG-ARLIGGC 287
|
330
....*....|....*..
gi 124487479 312 CGSTPDHIREIAEAVKK 328
Cdd:PRK09485 288 CRTTPEDIAALAAALKT 304
|
|
| B12-binding_like |
cd02065 |
B12 binding domain (B12-BD). Most of the members bind different cobalamid derivates, like B12 ... |
762-875 |
3.28e-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: 127.50 E-value: 3.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 762 TIVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAIK 841
Cdd:cd02065 1 KVLGATVGGDVHDIGKNIVAIALRDNGFEVIDLGVDVPPEEIVEAAKEEDADVVGLSALSTTHMEAMKLVIEALKELGID 80
|
90 100 110
....*....|....*....|....*....|....
gi 124487479 842 IPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDAS 875
Cdd:cd02065 81 IPVVVGGAHPTADPEEPKVDAVVIGEGEYAGPAL 114
|
|
| pyl_corrinoid |
TIGR02370 |
methyltransferase cognate corrinoid proteins, Methanosarcina family; This model describes a ... |
666-852 |
5.11e-31 |
|
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: 121.06 E-value: 5.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 666 ALVKGIEKHIVEDTEEARLNGEKyprPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREE 745
Cdd:TIGR02370 5 AIFEGEEDDVVEGAQKALDAGID---PIELIEKGLMAGMGVVGKLFEDGELFLPHVMMSADAMLAGIKVLTPEMEKAVET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 746 ARLingsveeedpyqGTIVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGLITPSL 825
Cdd:TIGR02370 82 EVL------------GKVVCGVAEGDVHDIGKNIVVTMLRANGFDVIDLGRDVPIDTVVEKVKKEKPLMLTGSALMTTTM 149
|
170 180 190
....*....|....*....|....*....|
gi 124487479 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 |
5.93e-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: 5.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 761 GTIVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAI 840
Cdd:pfam02310 1 GKVVVATVGGDLHPLGLNYVAAALRAAGFEVIILGANVPPEDIVAAARDEKPDVVGLSALMTTTLPGAKELIRLLKGIRP 80
|
....*....
gi 124487479 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 |
5.35e-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: 84.83 E-value: 5.35e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124487479 663 LEYALVKGIEKHIVEDTEEARLNgekypRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHL 735
Cdd:pfam02607 1 LLEALLEGDEEAAEELLEEALEI-----DPEEIIEDLLIPGMDEVGELWEAGEIFVPQEHLAAEAMKAALAVL 68
|
|
| PLN02489 |
PLN02489 |
homocysteine S-methyltransferase |
19-328 |
3.32e-14 |
|
homocysteine S-methyltransferase
Pssm-ID: 215269 Cd Length: 335 Bit Score: 75.43 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 19 VLDGGMGTMIQRYklseehfqGQEFKDhsrPLKgnNDILSITQPDIIYQIHKEYLLAGADIIETNTFSSTSIAQADYGL- 97
Cdd:PLN02489 24 VIDGGFATELERH--------GADLND---PLW--SAKCLITSPHLIRKVHLDYLEAGADIIITASYQATIQGFESRGLs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 98 ----EHLAYRmnkcSADVARKAAEEITLQTGVKRFVAGALGPTNKTLSVSPSV------------ERPDY-RNITFDELV 160
Cdd:PLN02489 91 reesETLLRK----SVEIACEARDIFWDKCQKGSTSRPGRELSYRPILVAASIgsygayladgseYSGDYgPSVTLEKLK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 161 DAYQEQAKGLLDGRVDILLIETIFDTANAKAAlfaIQNLFEENYAppRPIFISGTIVDksGRTLSgqTGEAFVTSVSHSD 240
Cdd:PLN02489 167 DFHRRRLQVLAEAGPDLIAFETIPNKLEAQAY---VELLEEENIK--IPAWISFNSKD--GVNVV--SGDSLLECASIAD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 241 PlC-----IGLNCSlgaaemrP--FIE----TIGKCTTAYVLCYPNAG----------LPNTfgdyDETPSTMATHLKDF 299
Cdd:PLN02489 238 S-CkkvvaVGINCT-------PprFIHglilSIRKVTSKPIVVYPNSGetydgeakewVEST----GVSDEDFVSYVNKW 305
|
330 340
....*....|....*....|....*....
gi 124487479 300 AVDGlVNIVGGCCGSTPDHIREIAEAVKK 328
Cdd:PLN02489 306 RDAG-ASLIGGCCRTTPNTIRAISKALSE 333
|
|
| Sbm |
COG2185 |
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ... |
762-848 |
7.26e-10 |
|
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and metabolism];
Pssm-ID: 441788 [Multi-domain] Cd Length: 134 Bit Score: 58.23 E-value: 7.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 762 TIVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVMTPCDKILQAALDHKADIIGLSglitpSLDE--MIFVAKEMERL- 838
Cdd:COG2185 12 RVLLAKPGLDGHDRGAKVIARALRDAGFEVIYLGLFQTPEEIVRAAIEEDADVIGVS-----SLDGghLELVPELIELLk 86
|
90
....*....|...
gi 124487479 839 ---AIKIPLLIGG 848
Cdd:COG2185 87 eagAGDILVVVGG 99
|
|
| PRK02261 |
PRK02261 |
methylaspartate mutase subunit S; Provisional |
762-820 |
6.74e-08 |
|
methylaspartate mutase subunit S; Provisional
Pssm-ID: 179400 [Multi-domain] Cd Length: 137 Bit Score: 52.64 E-value: 6.74e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 124487479 762 TIVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGL 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 |
1.48e-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: 51.70 E-value: 1.48e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 124487479 762 TIVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGL 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 |
1.20e-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: 42.96 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487479 763 IVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVM-TPcDKILQAALDHKADIIGLSGLitpSLDEMIFVAKEMERL--- 838
Cdd:cd02071 2 ILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRqTP-EEIVEAAIQEDVDVIGLSSL---SGGHMTLFPEVIELLrel 77
|
90
....*....|.
gi 124487479 839 -AIKIPLLIGG 848
Cdd:cd02071 78 gAGDILVVGGG 88
|
|
| |
