|
Name |
Accession |
Description |
Interval |
E-value |
| metH |
PRK09490 |
B12-dependent methionine synthase; Provisional |
13-1259 |
0e+00 |
|
B12-dependent methionine synthase; Provisional
Pssm-ID: 236539 [Multi-domain] Cd Length: 1229 Bit Score: 2182.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 13 ASSLRLELTELLQQRILVLDGGMGTMIQQRHLEEEEFRGQEFKDHPKSLKGNNDILSITQPDVIYSIHKEYLEAGADIIE 92
Cdd:PRK09490 4 MSSRLAQLRALLAERILVLDGAMGTMIQRYKLEEADYRGERFADWPCDLKGNNDLLVLTQPDVIEAIHRAYLEAGADIIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 93 TNTFSSTSIAQADYGMEDLAYRLNKASAEVARRAADDVSAQTGCK-RFVAGALGPTNKTLSVSPSVERPDYRNITFDELV 171
Cdd:PRK09490 84 TNTFNATTIAQADYGMESLVYELNFAAARLAREAADEWTAKTPDKpRFVAGVLGPTNRTASISPDVNDPGFRNVTFDELV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 172 EAYAEQVKGLLDGGADVLLVETIFDTANAKAALFAIDRLFEESYEARPVLISGTIVDKSGRTLSGQTGEAFVISVSHAQP 251
Cdd:PRK09490 164 AAYREQTRGLIEGGADLILIETIFDTLNAKAAIFAVEEVFEELGVRLPVMISGTITDASGRTLSGQTTEAFWNSLRHAKP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 252 LCIGLNCALGASEMRPFIEAIGKSTSAFVICYPNAGLPNTFGGYDETPDVTAAHLKEFAVDGLVNIVGGCCGTTPDHIRA 331
Cdd:PRK09490 244 LSIGLNCALGADELRPYVEELSRIADTYVSAHPNAGLPNAFGEYDETPEEMAAQIGEFAESGFLNIVGGCCGTTPEHIAA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 332 IAESVRHVKPRVPPTdvYSDYMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQVL 411
Cdd:PRK09490 324 IAEAVAGLPPRKLPE--IPVACRLSGLEPLNIDDDSLFVNVGERTNVTGSAKFARLIKEEDYDEALDVARQQVENGAQII 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 412 DINMDEGMLDGAAAMSRFCNLIASEPDICKVPLCIDSSNFSVIEAGLKCCQGKCIVNSISLKEGEQDFLRRARQVRRYGA 491
Cdd:PRK09490 402 DINMDEGMLDSEAAMVRFLNLIASEPDIARVPIMIDSSKWEVIEAGLKCIQGKGIVNSISLKEGEEKFIEHARLVRRYGA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 492 AVVVMAFDEDGQATETDQKVQICSRAYHLLIDQAGFNPNDIIFDPNILTIGTGMEEHSMYAINFIRATRIIKESLPGARV 571
Cdd:PRK09490 482 AVVVMAFDEQGQADTRERKIEICKRAYDILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKQNLPHAKI 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 572 SGGLSNLSFSFRGMEAIREAMHGAFLYHAIKDGMDMGIVNAGNLPVYDDIDKELLLLCENIIWNRDPDATEKLLLYAQ-- 649
Cdd:PRK09490 562 SGGVSNVSFSFRGNNPVREAIHAVFLYHAIKAGMDMGIVNAGQLAIYDDIPPELREAVEDVVLNRRPDATERLLEIAEky 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 650 NNAKGGKKVVQTDEWRTGSVEERLEYALVKGIEKYVVEDTEEARAQterYPRPLHVIEGPLMNGMKTVGDLFGAGKMFLP 729
Cdd:PRK09490 642 RGKGGKKAKAEDLEWRSWPVEKRLEHALVKGITEFIEEDTEEARQQ---AARPLEVIEGPLMDGMNVVGDLFGEGKMFLP 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 730 QVIKSARVMKKAVGHLIPFMEKEREEMMATSGcveevdpyQGTVLLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMIP 809
Cdd:PRK09490 719 QVVKSARVMKQAVAYLEPFIEAKKEGGTDRKS--------NGKILMATVKGDVHDIGKNIVGVVLQCNNYEVIDLGVMVP 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 810 CDRILREAIHNKADIIGLSGLITPSLDEMIHVAKEMERLGLKIPLLIGGATTSKTHTAVKIAPRYSSPVVHVLDASRSVV 889
Cdd:PRK09490 791 AEKILETAKEENADIIGLSGLITPSLDEMVHVAKEMERQGFTIPLLIGGATTSKAHTAVKIAPNYSGPVVYVTDASRAVG 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 890 VCSQLLDEGVRDDYFEEVQEEYEDIRQDHYDSLKDRRFLSLSRAREKGLHIDWfAQPKPVRPQFLGTHVFDTYDLRKLVD 969
Cdd:PRK09490 871 VVSSLLSDEQRDAYVAETRAEYEKVREQHARKKPRKPLLTLEAARANRFKIDW-EAYTPPKPKFLGVQVFEDYDLAELRE 949
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 970 FIDWKPFFDVWQLRGKypnrgYPKIFKDKTVGEGARRVHDDALKLLNRLIDSRGLQARGIVGFWAAQSDGDDIHLYTDDv 1049
Cdd:PRK09490 950 YIDWTPFFQTWELAGK-----YPAILEDEVVGEEARKLFADAQAMLDKIIAEKWLTARGVIGLFPANSVGDDIEVYTDE- 1023
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 1050 tsPNTTPVATSHGLRQQAEKdsaSSEPYLCVSDFVAPRSSGVQDYVGLFAVSV-FGAEELSQKFKKQGDDYRSIMVKALA 1128
Cdd:PRK09490 1024 --SRTEVLATLHHLRQQTEK---RGRPNYCLADFVAPKESGKADYIGAFAVTAgLGEDELADRFEAAHDDYNAIMVKALA 1098
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 1129 DRLAEAFAEELHVRVRRDLWGYSSEEDLPASDLHKLRYEGIRPAAGYPSQPDHSEKLTMWKLADIQEKTGISLTESLAMS 1208
Cdd:PRK09490 1099 DRLAEAFAEYLHERVRKEFWGYAPDENLSNEELIREKYQGIRPAPGYPACPDHTEKATLFDLLDAEKNTGMKLTESYAMW 1178
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|.
gi 37620202 1209 PAASVSGLYFSNPKSTYFAVGKITKEQVEDYALRKQMEVCEVERWLGPILG 1259
Cdd:PRK09490 1179 PGASVSGWYFSHPESKYFAVGKIGRDQVEDYAARKGMSVEEVERWLAPNLG 1229
|
|
| metH |
TIGR02082 |
5-methyltetrahydrofolate--homocysteine methyltransferase; This family represents ... |
24-1228 |
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: 1883.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 24 LQQRILVLDGGMGTMIQQRHLEEEEFRGQeFKDHPKSLKGNNDILSITQPDVIYSIHKEYLEAGADIIETNTFSSTSIAQ 103
Cdd:TIGR02082 1 LNQRILVLDGAMGTQLQSANLTEADFRGA-FADCHRELKGNNDILNLTKPEVIATIHRAYFEAGADIIETNTFNSTTISQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 104 ADYGMEDLAYRLNKASAEVARRAADDVSAQTGCKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYAEQVKGLLD 183
Cdd:TIGR02082 80 ADYDLEDLIYDLNFKGAKLARAVADEFTLTPEKPRFVAGSMGPTNKTATLSPDVERPGFRNVTYDELVDAYTEQAKGLLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 184 GGADVLLVETIFDTANAKAALFAIDRLFEESYEARPVLISGTIVDKSGRTLSGQTGEAFVISVSHAQPLCIGLNCALGAS 263
Cdd:TIGR02082 160 GGVDLLLIETCFDTLNAKAALFAAETVFEEKGRELPIMISGTIVDTSGRTLSGQTIEAFLTSLEHAGIDMIGLNCALGPD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 264 EMRPFIEAIGKSTSAFVICYPNAGLPNTFGGYDETPDVTAAHLKEFAVDGLVNIVGGCCGTTPDHIRAIAESVRHVKPRV 343
Cdd:TIGR02082 240 EMRPHLKHLSEHAEAYVSCHPNAGLPNAFGEYDLTPDELAKALADFAAEGGLNIVGGCCGTTPDHIRAIAEAVKNIKPRQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 344 PPtdVYSDYMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQVLDINMDEGMLDGA 423
Cdd:TIGR02082 320 RP--VLYEPSRLSGLEAITIAQDSNFVNIGERTNVAGSKKFRRLIIAEDYDEALDIAKQQVENGAQILDINVDYGMLDGV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 424 AAMSRFCNLIASEPDICKVPLCIDSSNFSVIEAGLKCCQGKCIVNSISLKEGEQDFLRRARQVRRYGAAVVVMAFDEDGQ 503
Cdd:TIGR02082 398 AAMKRFLNLLASEPDISTVPLMLDSSEWAVLEAGLKCIQGKCIVNSISLKDGEERFIETAKLIKEYGAAVVVMAFDEEGQ 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 504 ATETDQKVQICSRAYHLLIDQAGFNPNDIIFDPNILTIGTGMEEHSMYAINFIRATRIIKESLPGARVSGGLSNLSFSFR 583
Cdd:TIGR02082 478 ARTADRKIEICKRAYNILTEKVGFPPEDIIFDPNILTIATGIEEHRRYAINFIEAIRWIKEELPDAKISGGVSNVSFSFR 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 584 GMEAIREAMHGAFLYHAIKDGMDMGIVNAGNLPVYDDIDKELLLLCENIIWNRDPDATEKLLLYAQN-NAKGGK--KVVQ 660
Cdd:TIGR02082 558 GNPAAREAMHSVFLYHAIRAGMDMGIVNAGKILPYDDIDPELRQVVEDLILNRRREATEPLLELAQLyEGTTTKssKEAQ 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 661 TDEWRTGSVEERLEYALVKGIEKYVVEDTEEARAQterYPRPLHVIEGPLMNGMKTVGDLFGAGKMFLPQVIKSARVMKK 740
Cdd:TIGR02082 638 QAEWRNLPVEERLEYALVKGEREGIEEDLEEARKK---LTRPLEIIEGPLMDGMKVVGDLFGSGKMFLPQVVKSARVMKK 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 741 AVGHLIPFMEKEREEmmatsgcveevDPYQGTVLLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMIPCDRILREAIHN 820
Cdd:TIGR02082 715 AVAYLEPHMEKEKSE-----------DSSKGKIVLATVKGDVHDIGKNIVGVVLSCNGYEVVDLGVMVPIEKILEAAKDH 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 821 KADIIGLSGLITPSLDEMIHVAKEMERLGLKIPLLIGGATTSKTHTAVKIAPRYSSPVVHVLDASRSVVVCSQLLDEGVR 900
Cdd:TIGR02082 784 NADVIGLSGLITPSLDEMKEVAEEMNRRGITIPLLIGGAATSKTHTAVKIAPIYKGPVVYVLDASRAVTVMDTLMSAKRK 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 901 DDYFEEVQEEYEDIRQDHYDSLKDRRFLSLSRAREKGLHIDWFAQPKPVRPQFLGTHVFDTYDLRKLVDFIDWKPFFDVW 980
Cdd:TIGR02082 864 DTENGRIKEEYDTAREKHGEQRSKRIAASEQAARKNVFAPDWSDDIEPPAPPFWGTQIVEASDIAELRPYIDWTPFFLQW 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 981 QLRGKypnrgYPKIFKDKTVGEGARRVHDDALKLLNRLIDSRGLQARGIVGFWAAQSDGDDIHLYTDDVTSPNttPVATS 1060
Cdd:TIGR02082 944 QLRGK-----YPKILGDEYEGLEAQKLFPDANEMLDKLSAENLLHARGVYGYFPAQSVGDDIEIYTDETVETH--PIATV 1016
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 1061 HGLRQQAEKDSASsepYLCVSDFVAPRSSGVQDYVGLFAVSV-FGAEELSQKFKKQGDDYRSIMVKALADRLAEAFAEEL 1139
Cdd:TIGR02082 1017 RYLFHFPRQQSGR---YLCLADFIAPKASGIVDYIGAFAVTAgFGAEELADKLEAQHDDYDYIMVKAIADRLAEAFAEYL 1093
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 1140 HVRVRRDLWGYSSEEDLPASDLHKLRYEGIRPAAGYPSQPDHSEKLTMWKLADIqEKTGISLTESLAMSPAASVSGLYFS 1219
Cdd:TIGR02082 1094 HRRVRKELWGYAAEEPLSNEDLLKLRYQGIRPAPGYPACPDHTEKATMFELLEP-ERIGVRLTESLAMHPEQSVSGLYFA 1172
|
....*....
gi 37620202 1220 NPKSTYFAV 1228
Cdd:TIGR02082 1173 HPEAKYFAV 1181
|
|
| MetH2 |
COG1410 |
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; ... |
35-1228 |
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: 1580.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 35 MGTMIQQRHLEEEEFRGQEFKDHPKSLKGNNDILSITQPDVIYSIHKEYLEAGADIIETNTFSSTSIAQADYGMEDLAYR 114
Cdd:COG1410 1 MGTMIQLLKLRELDADGAMFTDLQLDLKGNNDLLGLTGPNEILEIHRPELEAGADIIETNTGADAAITAADGAAEALLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 115 LNKASAEVARRAADDVSAQTGCK-RFVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYAEQVKGLLDGGADVLLVET 193
Cdd:COG1410 81 YNGAAAALALEAAAAAAAAAAAAaRAVAGAPGPTGGTASPGPDVPGLGFRNFDFDELVEAYAEAGLGLGGGGADLLLTET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 194 IFDTANAKAALFAIDRLFEESYEARPVLISGTIVDKSGRTLSGQTGEAFVISVSHAQPLCIGLNCALGASEMRPFIEAIG 273
Cdd:COG1410 161 IFDTLNAAAAAAAAAAAAEEEGVPIPVMVTGTITDGSGRTLSGQTAEAFLESLGHAAPGSNGLNCALGAEELRPYLEELS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 274 KSTSAFVICYPNAGLPNTFGGYDETPDVTAAHLKEFAVDGLVNIVGGCCGTTPDHIRAIAESVRHVKPRVPPTDVysdYM 353
Cdd:COG1410 241 RIPPSAVSNAPNAGLPNGFGEYDETPEEMAAALAEFAEEGGVNIVGGCCGTTPEHIRAIAEAVAGLKPRPREKPP---PA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 354 LLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQVLDINMDEGMLDGAAAMSRFCNLI 433
Cdd:COG1410 318 VLSGLEPVPIGQDSPFVNIGERTNVTGSKKFRELILEGDYDEALEVAREQVEAGAQILDVNVDEPGRDEVAAMVRFLNLL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 434 ASEpdiCKVPLCIDSSNFSVIEAGLKCCQGKCIVNSISLKEGEQDFLRRARQVRRYGAAVVVMAFDEDGQATETDQKVQI 513
Cdd:COG1410 398 ASE---VRVPLMIDSSKPEVIEAGLKCYQGKPIVNSISLEEGEERFEEVAPLAKKYGAAVVVLAIDEEGQADTAERKLEI 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 514 CSRAYHLLIDQAGFNPNDIIFDPNILTIGTGMEEHSMYAINFIRATRIIKESLPGARVSGGLSNLSFSFRGmeAIREAMH 593
Cdd:COG1410 475 AERIYDLAVEEYGFPPEDIIFDPLVFTVATGIEEHRNYAVETIEAIRLIKEELPGAKTSLGVSNVSFGLPG--NVREALN 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 594 GAFLYHAIKDGMDMGIVNAGNLPVYDDIDKELLLLCENIIWNRDPDATEKLLLYAQnNAKGGKKVVQTDEWRTGSVEERL 673
Cdd:COG1410 553 SVFLYHAIKAGLDMAIVNPGQLEPYDDIPPELRELAEDVLLNRRPDALERLIELFE-GVKGAKAKKADLEWRELPVEERL 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 674 EYALVKGIEKYVVEDTEEARAQterYPRPLHVIEGPLMNGMKTVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEr 753
Cdd:COG1410 632 KHAIVKGIKEGIEEDTEEALAE---GARPLEIINGPLMPGMNVVGDLFGAGKMFLPQVLKSAEVMKAAVAYLEPFMEKE- 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 754 eemmatsgcvEEVDPYQGTVLLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMIPCDRILREAIHNKADIIGLSGLITP 833
Cdd:COG1410 708 ----------KGESSSKGKIVLATVKGDVHDIGKNIVGVVLENNGYEVIDLGVMVPAEKILEAAKEHKADIIGLSGLMTT 777
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 834 SLDEMIHVAKEMERLGLKIPLLIGGATTSKTHTAVKIAPRYSSPVVHVLDASRSVVVCSQLLDEGVRDDYFEEVQEEYED 913
Cdd:COG1410 778 SLDEMKEVAEEMRRRGLDIPVLIGGAALTRAYTAVKIAPAYDGAVVYAKDASRAVRVADKLLSKERREAFVAEIKAEYEK 857
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 914 IRQDHYDslKDRRFLSLSRAREKglhIDwfAQPKPVRPQFLGTHVFDTYDLRKLVDFIDWKPFFDVWQLRGKYPNrgypk 993
Cdd:COG1410 858 LRERHAA--RKKKLLSLEEARSN---VD--SDYPPPTPPFLGTRVLKDIPLAELVPYIDWTPFFQQWGLKGKYLD----- 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 994 ifkdktvGEGARRVHDDALKLLNRLIDSRGLQARGIVGFWAAQSDGDDIHLYTDDvtspNTTPVATSHGLRQQaekdsas 1073
Cdd:COG1410 926 -------GEEARELFPDAQAMLDRIIEEKWLTARAVYGYFPANSEGDDIEVYDDE----SSEELARFHFPRQQ------- 987
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 1074 SEPYLCVSDFVAPRSSGVQDYVGLFAVSV-FGAEELSQKFKKQGDDYRSIMVKALADRLAEAFAEELHVRVRRDlWGYSS 1152
Cdd:COG1410 988 RGPNLCLADFVAPKESGERDYVGFFAVTAgIGIEELAAELEAAGDDYDAIMLHALADRLAEAFAEYLHERVRKE-WGYAP 1066
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37620202 1153 EEDLPASDLHKLRYEGIRPAAGYPSQPDHSEKLTMWKLADIqEKTGISLTESLAMSPAASVSGLYFSNPKSTYFAV 1228
Cdd:COG1410 1067 DEALTNEDLIKEKYRGIRPAPGYPACPDHTEKRKLFDLLDA-ERIGVTLTESFAMHPEASVSGIYFHHPEAKYFNV 1141
|
|
| Met_synt_B12 |
pfam02965 |
Vitamin B12 dependent methionine synthase, activation domain; |
963-1243 |
6.80e-162 |
|
Vitamin B12 dependent methionine synthase, activation domain;
Pssm-ID: 460767 [Multi-domain] Cd Length: 273 Bit Score: 483.51 E-value: 6.80e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 963 DLRKLVDFIDWKPFFDVWQLRGKYPnrgypKIFKDKTVGEGARRVHDDALKLLNRLIDSRGLQARGIVGFWAAQSDGDDI 1042
Cdd:pfam02965 1 DLAELVPYIDWTPFFQAWELKGKYP-----AILDDEVVGEEARKLFADAQAMLDRIIEEKWLTARGVVGFFPANSVGDDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 1043 HLYTDDVTspnTTPVATSHGLRQQAEKDSasSEPYLCVSDFVAPRSSGVQDYVGLFAVSV-FGAEELSQKFKKQGDDYRS 1121
Cdd:pfam02965 76 EVYTDESR---TEVLATFHTLRQQTEKPE--GRPNLCLADFIAPKESGIADYIGAFAVTAgIGIEELAARFEAAHDDYSA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 1122 IMVKALADRLAEAFAEELHVRVRRDLWGYSSEEDLPASDLHKLRYEGIRPAAGYPSQPDHSEKLTMWKLADIQEKTGISL 1201
Cdd:pfam02965 151 IMVKALADRLAEAFAEYLHERVRKELWGYAPDENLSNEDLIKEKYQGIRPAPGYPACPDHTEKFTLFDLLDAEENIGIRL 230
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 37620202 1202 TESLAMSPAASVSGLYFSNPKSTYFAVGKITKEQVEDYALRK 1243
Cdd:pfam02965 231 TESFAMTPAASVSGLYFAHPESRYFAVGKIGKDQVEDYAKRK 272
|
|
| MeTr |
cd00740 |
MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent ... |
369-625 |
4.29e-135 |
|
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: 412.17 E-value: 4.29e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 369 FVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQVLDINMDEGMLDGAAAMSRFCNLIASEPdicKVPLCIDS 448
Cdd:cd00740 1 FLNIGERTNVTGSKKFRELIKAEDYDEALDVARQQVEGGAQILDLNVDYGGLDGVSAMKWLLNLLATEP---TVPLMLDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 449 SNFSVIEAGLKCCQGKCIVNSISLKEGEQDFLRRARQVRRYGAAVVVMAFDEDGQATETDQKVQICSRAYHLLIDQAGFN 528
Cdd:cd00740 78 TNWEVIEAGLKCCQGKCVVNSINLEDGEERFLKVARLAKEHGAAVVVLAFDEQGQAKTRDKKVEIAERAYEALTEFVGFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 529 PNDIIFDPNILTIGTGMEEHSMYAINFIRATRIIKESLPGARVSGGLSNLSFSFrgMEAIREAMHGAFLYHAIKDGMDMG 608
Cdd:cd00740 158 PEDIIFDPLILPIATGIEEHRPYALETIDAIRMIKERLPAVKISLGVSNVSFGF--NPAAREALNSVFLYEAIKAGLDMA 235
|
250
....*....|....*..
gi 37620202 609 IVNAGNLPVYDDIDKEL 625
Cdd:cd00740 236 IVNAGKLAPIEDIPEEL 252
|
|
| B12-binding_2 |
smart01018 |
B12 binding domain; Cobalamin-dependent methionine synthase is a large modular protein that ... |
668-753 |
2.31e-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: 2.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 668 SVEERLEYALVKGIEKYVVEDTEEARAQterYPRPLHVIEGPLMNGMKTVGDLFGAGKMFLPQVIKSARVMKKAVGHLIP 747
Cdd:smart01018 2 PLLERLAEAIVDGDEEGVEELVEEALAE---GVDPLEIINEGLIPGMNVVGDLFEAGEYFLPQVLMSAEAMKAAVAILKP 78
|
....*.
gi 37620202 748 FMEKER 753
Cdd:smart01018 79 LLEKEK 84
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| metH |
PRK09490 |
B12-dependent methionine synthase; Provisional |
13-1259 |
0e+00 |
|
B12-dependent methionine synthase; Provisional
Pssm-ID: 236539 [Multi-domain] Cd Length: 1229 Bit Score: 2182.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 13 ASSLRLELTELLQQRILVLDGGMGTMIQQRHLEEEEFRGQEFKDHPKSLKGNNDILSITQPDVIYSIHKEYLEAGADIIE 92
Cdd:PRK09490 4 MSSRLAQLRALLAERILVLDGAMGTMIQRYKLEEADYRGERFADWPCDLKGNNDLLVLTQPDVIEAIHRAYLEAGADIIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 93 TNTFSSTSIAQADYGMEDLAYRLNKASAEVARRAADDVSAQTGCK-RFVAGALGPTNKTLSVSPSVERPDYRNITFDELV 171
Cdd:PRK09490 84 TNTFNATTIAQADYGMESLVYELNFAAARLAREAADEWTAKTPDKpRFVAGVLGPTNRTASISPDVNDPGFRNVTFDELV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 172 EAYAEQVKGLLDGGADVLLVETIFDTANAKAALFAIDRLFEESYEARPVLISGTIVDKSGRTLSGQTGEAFVISVSHAQP 251
Cdd:PRK09490 164 AAYREQTRGLIEGGADLILIETIFDTLNAKAAIFAVEEVFEELGVRLPVMISGTITDASGRTLSGQTTEAFWNSLRHAKP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 252 LCIGLNCALGASEMRPFIEAIGKSTSAFVICYPNAGLPNTFGGYDETPDVTAAHLKEFAVDGLVNIVGGCCGTTPDHIRA 331
Cdd:PRK09490 244 LSIGLNCALGADELRPYVEELSRIADTYVSAHPNAGLPNAFGEYDETPEEMAAQIGEFAESGFLNIVGGCCGTTPEHIAA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 332 IAESVRHVKPRVPPTdvYSDYMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQVL 411
Cdd:PRK09490 324 IAEAVAGLPPRKLPE--IPVACRLSGLEPLNIDDDSLFVNVGERTNVTGSAKFARLIKEEDYDEALDVARQQVENGAQII 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 412 DINMDEGMLDGAAAMSRFCNLIASEPDICKVPLCIDSSNFSVIEAGLKCCQGKCIVNSISLKEGEQDFLRRARQVRRYGA 491
Cdd:PRK09490 402 DINMDEGMLDSEAAMVRFLNLIASEPDIARVPIMIDSSKWEVIEAGLKCIQGKGIVNSISLKEGEEKFIEHARLVRRYGA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 492 AVVVMAFDEDGQATETDQKVQICSRAYHLLIDQAGFNPNDIIFDPNILTIGTGMEEHSMYAINFIRATRIIKESLPGARV 571
Cdd:PRK09490 482 AVVVMAFDEQGQADTRERKIEICKRAYDILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKQNLPHAKI 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 572 SGGLSNLSFSFRGMEAIREAMHGAFLYHAIKDGMDMGIVNAGNLPVYDDIDKELLLLCENIIWNRDPDATEKLLLYAQ-- 649
Cdd:PRK09490 562 SGGVSNVSFSFRGNNPVREAIHAVFLYHAIKAGMDMGIVNAGQLAIYDDIPPELREAVEDVVLNRRPDATERLLEIAEky 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 650 NNAKGGKKVVQTDEWRTGSVEERLEYALVKGIEKYVVEDTEEARAQterYPRPLHVIEGPLMNGMKTVGDLFGAGKMFLP 729
Cdd:PRK09490 642 RGKGGKKAKAEDLEWRSWPVEKRLEHALVKGITEFIEEDTEEARQQ---AARPLEVIEGPLMDGMNVVGDLFGEGKMFLP 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 730 QVIKSARVMKKAVGHLIPFMEKEREEMMATSGcveevdpyQGTVLLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMIP 809
Cdd:PRK09490 719 QVVKSARVMKQAVAYLEPFIEAKKEGGTDRKS--------NGKILMATVKGDVHDIGKNIVGVVLQCNNYEVIDLGVMVP 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 810 CDRILREAIHNKADIIGLSGLITPSLDEMIHVAKEMERLGLKIPLLIGGATTSKTHTAVKIAPRYSSPVVHVLDASRSVV 889
Cdd:PRK09490 791 AEKILETAKEENADIIGLSGLITPSLDEMVHVAKEMERQGFTIPLLIGGATTSKAHTAVKIAPNYSGPVVYVTDASRAVG 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 890 VCSQLLDEGVRDDYFEEVQEEYEDIRQDHYDSLKDRRFLSLSRAREKGLHIDWfAQPKPVRPQFLGTHVFDTYDLRKLVD 969
Cdd:PRK09490 871 VVSSLLSDEQRDAYVAETRAEYEKVREQHARKKPRKPLLTLEAARANRFKIDW-EAYTPPKPKFLGVQVFEDYDLAELRE 949
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 970 FIDWKPFFDVWQLRGKypnrgYPKIFKDKTVGEGARRVHDDALKLLNRLIDSRGLQARGIVGFWAAQSDGDDIHLYTDDv 1049
Cdd:PRK09490 950 YIDWTPFFQTWELAGK-----YPAILEDEVVGEEARKLFADAQAMLDKIIAEKWLTARGVIGLFPANSVGDDIEVYTDE- 1023
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 1050 tsPNTTPVATSHGLRQQAEKdsaSSEPYLCVSDFVAPRSSGVQDYVGLFAVSV-FGAEELSQKFKKQGDDYRSIMVKALA 1128
Cdd:PRK09490 1024 --SRTEVLATLHHLRQQTEK---RGRPNYCLADFVAPKESGKADYIGAFAVTAgLGEDELADRFEAAHDDYNAIMVKALA 1098
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 1129 DRLAEAFAEELHVRVRRDLWGYSSEEDLPASDLHKLRYEGIRPAAGYPSQPDHSEKLTMWKLADIQEKTGISLTESLAMS 1208
Cdd:PRK09490 1099 DRLAEAFAEYLHERVRKEFWGYAPDENLSNEELIREKYQGIRPAPGYPACPDHTEKATLFDLLDAEKNTGMKLTESYAMW 1178
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|.
gi 37620202 1209 PAASVSGLYFSNPKSTYFAVGKITKEQVEDYALRKQMEVCEVERWLGPILG 1259
Cdd:PRK09490 1179 PGASVSGWYFSHPESKYFAVGKIGRDQVEDYAARKGMSVEEVERWLAPNLG 1229
|
|
| metH |
TIGR02082 |
5-methyltetrahydrofolate--homocysteine methyltransferase; This family represents ... |
24-1228 |
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: 1883.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 24 LQQRILVLDGGMGTMIQQRHLEEEEFRGQeFKDHPKSLKGNNDILSITQPDVIYSIHKEYLEAGADIIETNTFSSTSIAQ 103
Cdd:TIGR02082 1 LNQRILVLDGAMGTQLQSANLTEADFRGA-FADCHRELKGNNDILNLTKPEVIATIHRAYFEAGADIIETNTFNSTTISQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 104 ADYGMEDLAYRLNKASAEVARRAADDVSAQTGCKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYAEQVKGLLD 183
Cdd:TIGR02082 80 ADYDLEDLIYDLNFKGAKLARAVADEFTLTPEKPRFVAGSMGPTNKTATLSPDVERPGFRNVTYDELVDAYTEQAKGLLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 184 GGADVLLVETIFDTANAKAALFAIDRLFEESYEARPVLISGTIVDKSGRTLSGQTGEAFVISVSHAQPLCIGLNCALGAS 263
Cdd:TIGR02082 160 GGVDLLLIETCFDTLNAKAALFAAETVFEEKGRELPIMISGTIVDTSGRTLSGQTIEAFLTSLEHAGIDMIGLNCALGPD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 264 EMRPFIEAIGKSTSAFVICYPNAGLPNTFGGYDETPDVTAAHLKEFAVDGLVNIVGGCCGTTPDHIRAIAESVRHVKPRV 343
Cdd:TIGR02082 240 EMRPHLKHLSEHAEAYVSCHPNAGLPNAFGEYDLTPDELAKALADFAAEGGLNIVGGCCGTTPDHIRAIAEAVKNIKPRQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 344 PPtdVYSDYMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQVLDINMDEGMLDGA 423
Cdd:TIGR02082 320 RP--VLYEPSRLSGLEAITIAQDSNFVNIGERTNVAGSKKFRRLIIAEDYDEALDIAKQQVENGAQILDINVDYGMLDGV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 424 AAMSRFCNLIASEPDICKVPLCIDSSNFSVIEAGLKCCQGKCIVNSISLKEGEQDFLRRARQVRRYGAAVVVMAFDEDGQ 503
Cdd:TIGR02082 398 AAMKRFLNLLASEPDISTVPLMLDSSEWAVLEAGLKCIQGKCIVNSISLKDGEERFIETAKLIKEYGAAVVVMAFDEEGQ 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 504 ATETDQKVQICSRAYHLLIDQAGFNPNDIIFDPNILTIGTGMEEHSMYAINFIRATRIIKESLPGARVSGGLSNLSFSFR 583
Cdd:TIGR02082 478 ARTADRKIEICKRAYNILTEKVGFPPEDIIFDPNILTIATGIEEHRRYAINFIEAIRWIKEELPDAKISGGVSNVSFSFR 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 584 GMEAIREAMHGAFLYHAIKDGMDMGIVNAGNLPVYDDIDKELLLLCENIIWNRDPDATEKLLLYAQN-NAKGGK--KVVQ 660
Cdd:TIGR02082 558 GNPAAREAMHSVFLYHAIRAGMDMGIVNAGKILPYDDIDPELRQVVEDLILNRRREATEPLLELAQLyEGTTTKssKEAQ 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 661 TDEWRTGSVEERLEYALVKGIEKYVVEDTEEARAQterYPRPLHVIEGPLMNGMKTVGDLFGAGKMFLPQVIKSARVMKK 740
Cdd:TIGR02082 638 QAEWRNLPVEERLEYALVKGEREGIEEDLEEARKK---LTRPLEIIEGPLMDGMKVVGDLFGSGKMFLPQVVKSARVMKK 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 741 AVGHLIPFMEKEREEmmatsgcveevDPYQGTVLLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMIPCDRILREAIHN 820
Cdd:TIGR02082 715 AVAYLEPHMEKEKSE-----------DSSKGKIVLATVKGDVHDIGKNIVGVVLSCNGYEVVDLGVMVPIEKILEAAKDH 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 821 KADIIGLSGLITPSLDEMIHVAKEMERLGLKIPLLIGGATTSKTHTAVKIAPRYSSPVVHVLDASRSVVVCSQLLDEGVR 900
Cdd:TIGR02082 784 NADVIGLSGLITPSLDEMKEVAEEMNRRGITIPLLIGGAATSKTHTAVKIAPIYKGPVVYVLDASRAVTVMDTLMSAKRK 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 901 DDYFEEVQEEYEDIRQDHYDSLKDRRFLSLSRAREKGLHIDWFAQPKPVRPQFLGTHVFDTYDLRKLVDFIDWKPFFDVW 980
Cdd:TIGR02082 864 DTENGRIKEEYDTAREKHGEQRSKRIAASEQAARKNVFAPDWSDDIEPPAPPFWGTQIVEASDIAELRPYIDWTPFFLQW 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 981 QLRGKypnrgYPKIFKDKTVGEGARRVHDDALKLLNRLIDSRGLQARGIVGFWAAQSDGDDIHLYTDDVTSPNttPVATS 1060
Cdd:TIGR02082 944 QLRGK-----YPKILGDEYEGLEAQKLFPDANEMLDKLSAENLLHARGVYGYFPAQSVGDDIEIYTDETVETH--PIATV 1016
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 1061 HGLRQQAEKDSASsepYLCVSDFVAPRSSGVQDYVGLFAVSV-FGAEELSQKFKKQGDDYRSIMVKALADRLAEAFAEEL 1139
Cdd:TIGR02082 1017 RYLFHFPRQQSGR---YLCLADFIAPKASGIVDYIGAFAVTAgFGAEELADKLEAQHDDYDYIMVKAIADRLAEAFAEYL 1093
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 1140 HVRVRRDLWGYSSEEDLPASDLHKLRYEGIRPAAGYPSQPDHSEKLTMWKLADIqEKTGISLTESLAMSPAASVSGLYFS 1219
Cdd:TIGR02082 1094 HRRVRKELWGYAAEEPLSNEDLLKLRYQGIRPAPGYPACPDHTEKATMFELLEP-ERIGVRLTESLAMHPEQSVSGLYFA 1172
|
....*....
gi 37620202 1220 NPKSTYFAV 1228
Cdd:TIGR02082 1173 HPEAKYFAV 1181
|
|
| MetH2 |
COG1410 |
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; ... |
35-1228 |
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: 1580.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 35 MGTMIQQRHLEEEEFRGQEFKDHPKSLKGNNDILSITQPDVIYSIHKEYLEAGADIIETNTFSSTSIAQADYGMEDLAYR 114
Cdd:COG1410 1 MGTMIQLLKLRELDADGAMFTDLQLDLKGNNDLLGLTGPNEILEIHRPELEAGADIIETNTGADAAITAADGAAEALLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 115 LNKASAEVARRAADDVSAQTGCK-RFVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYAEQVKGLLDGGADVLLVET 193
Cdd:COG1410 81 YNGAAAALALEAAAAAAAAAAAAaRAVAGAPGPTGGTASPGPDVPGLGFRNFDFDELVEAYAEAGLGLGGGGADLLLTET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 194 IFDTANAKAALFAIDRLFEESYEARPVLISGTIVDKSGRTLSGQTGEAFVISVSHAQPLCIGLNCALGASEMRPFIEAIG 273
Cdd:COG1410 161 IFDTLNAAAAAAAAAAAAEEEGVPIPVMVTGTITDGSGRTLSGQTAEAFLESLGHAAPGSNGLNCALGAEELRPYLEELS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 274 KSTSAFVICYPNAGLPNTFGGYDETPDVTAAHLKEFAVDGLVNIVGGCCGTTPDHIRAIAESVRHVKPRVPPTDVysdYM 353
Cdd:COG1410 241 RIPPSAVSNAPNAGLPNGFGEYDETPEEMAAALAEFAEEGGVNIVGGCCGTTPEHIRAIAEAVAGLKPRPREKPP---PA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 354 LLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQVLDINMDEGMLDGAAAMSRFCNLI 433
Cdd:COG1410 318 VLSGLEPVPIGQDSPFVNIGERTNVTGSKKFRELILEGDYDEALEVAREQVEAGAQILDVNVDEPGRDEVAAMVRFLNLL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 434 ASEpdiCKVPLCIDSSNFSVIEAGLKCCQGKCIVNSISLKEGEQDFLRRARQVRRYGAAVVVMAFDEDGQATETDQKVQI 513
Cdd:COG1410 398 ASE---VRVPLMIDSSKPEVIEAGLKCYQGKPIVNSISLEEGEERFEEVAPLAKKYGAAVVVLAIDEEGQADTAERKLEI 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 514 CSRAYHLLIDQAGFNPNDIIFDPNILTIGTGMEEHSMYAINFIRATRIIKESLPGARVSGGLSNLSFSFRGmeAIREAMH 593
Cdd:COG1410 475 AERIYDLAVEEYGFPPEDIIFDPLVFTVATGIEEHRNYAVETIEAIRLIKEELPGAKTSLGVSNVSFGLPG--NVREALN 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 594 GAFLYHAIKDGMDMGIVNAGNLPVYDDIDKELLLLCENIIWNRDPDATEKLLLYAQnNAKGGKKVVQTDEWRTGSVEERL 673
Cdd:COG1410 553 SVFLYHAIKAGLDMAIVNPGQLEPYDDIPPELRELAEDVLLNRRPDALERLIELFE-GVKGAKAKKADLEWRELPVEERL 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 674 EYALVKGIEKYVVEDTEEARAQterYPRPLHVIEGPLMNGMKTVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEr 753
Cdd:COG1410 632 KHAIVKGIKEGIEEDTEEALAE---GARPLEIINGPLMPGMNVVGDLFGAGKMFLPQVLKSAEVMKAAVAYLEPFMEKE- 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 754 eemmatsgcvEEVDPYQGTVLLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMIPCDRILREAIHNKADIIGLSGLITP 833
Cdd:COG1410 708 ----------KGESSSKGKIVLATVKGDVHDIGKNIVGVVLENNGYEVIDLGVMVPAEKILEAAKEHKADIIGLSGLMTT 777
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 834 SLDEMIHVAKEMERLGLKIPLLIGGATTSKTHTAVKIAPRYSSPVVHVLDASRSVVVCSQLLDEGVRDDYFEEVQEEYED 913
Cdd:COG1410 778 SLDEMKEVAEEMRRRGLDIPVLIGGAALTRAYTAVKIAPAYDGAVVYAKDASRAVRVADKLLSKERREAFVAEIKAEYEK 857
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 914 IRQDHYDslKDRRFLSLSRAREKglhIDwfAQPKPVRPQFLGTHVFDTYDLRKLVDFIDWKPFFDVWQLRGKYPNrgypk 993
Cdd:COG1410 858 LRERHAA--RKKKLLSLEEARSN---VD--SDYPPPTPPFLGTRVLKDIPLAELVPYIDWTPFFQQWGLKGKYLD----- 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 994 ifkdktvGEGARRVHDDALKLLNRLIDSRGLQARGIVGFWAAQSDGDDIHLYTDDvtspNTTPVATSHGLRQQaekdsas 1073
Cdd:COG1410 926 -------GEEARELFPDAQAMLDRIIEEKWLTARAVYGYFPANSEGDDIEVYDDE----SSEELARFHFPRQQ------- 987
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 1074 SEPYLCVSDFVAPRSSGVQDYVGLFAVSV-FGAEELSQKFKKQGDDYRSIMVKALADRLAEAFAEELHVRVRRDlWGYSS 1152
Cdd:COG1410 988 RGPNLCLADFVAPKESGERDYVGFFAVTAgIGIEELAAELEAAGDDYDAIMLHALADRLAEAFAEYLHERVRKE-WGYAP 1066
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37620202 1153 EEDLPASDLHKLRYEGIRPAAGYPSQPDHSEKLTMWKLADIqEKTGISLTESLAMSPAASVSGLYFSNPKSTYFAV 1228
Cdd:COG1410 1067 DEALTNEDLIKEKYRGIRPAPGYPACPDHTEKRKLFDLLDA-ERIGVTLTESFAMHPEASVSGIYFHHPEAKYFNV 1141
|
|
| MetH1 |
COG0646 |
Methionine synthase I (cobalamin-dependent), methyltransferase domain [Amino acid transport ... |
19-854 |
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: 936.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 19 ELTELLQQRILVLDGGMGTMIQQRHLEEEEFRGqefkdhpksLKGNNDILSITQPDVIYSIHKEYLEAGADIIETNTFSS 98
Cdd:COG0646 5 ALLELLKERILILDGAMGTMLQAYGLTEGDFRG---------EKGCNELLNLTRPDVIREIHRAYLEAGADIIETNTFGA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 99 TSIAQADYGMEDLAYRLNKASAEVARRAADDVSAQtgcKRFVAGALGPTNKTLSvspsverpDYRNITFDELVEAYAEQV 178
Cdd:COG0646 76 NRIKLADYGLEDRVYEINRAAARLAREAADEFSDR---PRFVAGSIGPTGKLLS--------PLGNITFDELVEAYREQA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 179 KGLLDGGADVLLVETIFDTANAKAALFAIDRLFEESYEARPVLISGTIvDKSGRTLSGQTGEAFVISVSHAQPLCIGLNC 258
Cdd:COG0646 145 EGLIEGGVDLLLIETIFDTLEAKAAIFAAREAFEELGRDLPVMVSGTF-DASGRTLSGQTPEAFATSLEHLGPDAIGLNC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 259 ALGASEMRPFIEAIGKSTSAFVICYPNAGLPNTFGG---YDETPDVTAAHLKEFAVDGLVNIVGGCCGTTPDHIRAIAES 335
Cdd:COG0646 224 ALGPDEMRPHVEELSEVADTPVSAYPNAGLPNLVGGrtvYDETPEEMAEYAEEFAEAGGVNIVGGCCGTTPEHIRAIAEA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 336 VRHVKPRVPPTDvySDYMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQVLDINM 415
Cdd:COG0646 304 VKGLPPRKRPPP--PPALRLSGLEPLTITQDSLFVNVGERTNVTGSKKFARLILEGDYDAALAVARQQVEAGAQVIDVNM 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 416 DEGMLDGAAAMSRFCNLIASEPDICKVPLCIDSSNFSVIEAGLKCCQGKCIVNSISLKEGEQDFLRRARQVRRYGAAVVV 495
Cdd:COG0646 382 DEGMLDGEAAMVEFLNLIASEPDIPRVPDMIDSSKWEVIEAGLKGVQGKGIVNSISLKEGEEKFLELAKLVRRYGAAVVV 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 496 MAFDEDGQATETDQKVQICSRAYHLLIDQAGFNPNDIIFDPNILTIGTGMEEHSMYAINFIRATRIIKESLPGARVSGGL 575
Cdd:COG0646 462 MAFDEEGQADTAERKVEICARAYDLLTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKLNLPHALVSGGV 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 576 SNLSFSFRGMEAIREAMHGAFLYHAIKDGMDMGIVNAGNLPVYDDIDKELLLLCENIIWNRDPDATEKLLLYAQNNAKGG 655
Cdd:COG0646 542 SNVSFSFRGNNPVREAIHAVFLYHAIAAGMDMGIVNAGQLAIYEEIPEELLLLVEDVVLNRREDATERLLEIAEEVKGAG 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 656 KKVVQTDEWRT-GSVEERLEYALVKGIEKYVVEDTEEARAQTEryprPLHVIEGPLMNGMKTVGDLFGAGKMFLPQVIKS 734
Cdd:COG0646 622 KAAEEEAEEERrEEEEERLLELLLVGGIEIDEEDDEEAALLLA----ALELIIIELLLGGGMVVGGLGGGGGKLLLVVVV 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 735 ARVMKKAVGHLIPFMEKEREEMMATSGcveevdpyQGTVLLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMIPCDRIL 814
Cdd:COG0646 698 KAVVKKKVAVALLKPEEEEKKKGGGKG--------GGVVVGVVVKVVVDDVDIIIVVVVVVVNNGIVVLVVVVIVVVALE 769
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 37620202 815 REAIHNKADIIGLSGLITPSLDEMIHVAKEMERLGLKIPL 854
Cdd:COG0646 770 AAAAAEAAVILLVGGLVLLLLEEEVLAAAEAAAEAAVLLL 809
|
|
| Met_synt_B12 |
pfam02965 |
Vitamin B12 dependent methionine synthase, activation domain; |
963-1243 |
6.80e-162 |
|
Vitamin B12 dependent methionine synthase, activation domain;
Pssm-ID: 460767 [Multi-domain] Cd Length: 273 Bit Score: 483.51 E-value: 6.80e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 963 DLRKLVDFIDWKPFFDVWQLRGKYPnrgypKIFKDKTVGEGARRVHDDALKLLNRLIDSRGLQARGIVGFWAAQSDGDDI 1042
Cdd:pfam02965 1 DLAELVPYIDWTPFFQAWELKGKYP-----AILDDEVVGEEARKLFADAQAMLDRIIEEKWLTARGVVGFFPANSVGDDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 1043 HLYTDDVTspnTTPVATSHGLRQQAEKDSasSEPYLCVSDFVAPRSSGVQDYVGLFAVSV-FGAEELSQKFKKQGDDYRS 1121
Cdd:pfam02965 76 EVYTDESR---TEVLATFHTLRQQTEKPE--GRPNLCLADFIAPKESGIADYIGAFAVTAgIGIEELAARFEAAHDDYSA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 1122 IMVKALADRLAEAFAEELHVRVRRDLWGYSSEEDLPASDLHKLRYEGIRPAAGYPSQPDHSEKLTMWKLADIQEKTGISL 1201
Cdd:pfam02965 151 IMVKALADRLAEAFAEYLHERVRKELWGYAPDENLSNEDLIKEKYQGIRPAPGYPACPDHTEKFTLFDLLDAEENIGIRL 230
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 37620202 1202 TESLAMSPAASVSGLYFSNPKSTYFAVGKITKEQVEDYALRK 1243
Cdd:pfam02965 231 TESFAMTPAASVSGLYFAHPESRYFAVGKIGKDQVEDYAKRK 272
|
|
| MeTr |
cd00740 |
MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent ... |
369-625 |
4.29e-135 |
|
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: 412.17 E-value: 4.29e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 369 FVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQVLDINMDEGMLDGAAAMSRFCNLIASEPdicKVPLCIDS 448
Cdd:cd00740 1 FLNIGERTNVTGSKKFRELIKAEDYDEALDVARQQVEGGAQILDLNVDYGGLDGVSAMKWLLNLLATEP---TVPLMLDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 449 SNFSVIEAGLKCCQGKCIVNSISLKEGEQDFLRRARQVRRYGAAVVVMAFDEDGQATETDQKVQICSRAYHLLIDQAGFN 528
Cdd:cd00740 78 TNWEVIEAGLKCCQGKCVVNSINLEDGEERFLKVARLAKEHGAAVVVLAFDEQGQAKTRDKKVEIAERAYEALTEFVGFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 529 PNDIIFDPNILTIGTGMEEHSMYAINFIRATRIIKESLPGARVSGGLSNLSFSFrgMEAIREAMHGAFLYHAIKDGMDMG 608
Cdd:cd00740 158 PEDIIFDPLILPIATGIEEHRPYALETIDAIRMIKERLPAVKISLGVSNVSFGF--NPAAREALNSVFLYEAIKAGLDMA 235
|
250
....*....|....*..
gi 37620202 609 IVNAGNLPVYDDIDKEL 625
Cdd:cd00740 236 IVNAGKLAPIEDIPEEL 252
|
|
| methionine_synthase_B12_BD |
cd02069 |
B12 binding domain of methionine synthase. This domain binds methylcobalamin, which it uses as ... |
669-895 |
7.95e-130 |
|
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: 396.64 E-value: 7.95e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 669 VEERLEYALVKGIEKYVVEDTEEARAQterYPRPLHVIEGPLMNGMKTVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPF 748
Cdd:cd02069 1 VEERLKHALVKGIRDGIEEDTEEARQQ---YARPLEIINGPLMDGMKVVGDLFGAGKMFLPQVLKSARVMKAAVAYLEPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 749 MEKEREEmmatsgcveevDPYQGTVLLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMIPCDRILREAIHNKADIIGLS 828
Cdd:cd02069 78 MEKEKGE-----------NSSKGKIVLATVKGDVHDIGKNLVGVILSNNGYEVIDLGVMVPIEKILEAAKEHKADIIGLS 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37620202 829 GLITPSLDEMIHVAKEMERLGLKIPLLIGGATTSKTHTAVKIAPRYSSPVVHVLDASRSVVVCSQLL 895
Cdd:cd02069 147 GLLVPSLDEMVEVAEEMNRRGIKIPLLIGGAATSRKHTAVKIAPEYDGPVVYVKDASRALGVANKLL 213
|
|
| S-methyl_trans |
pfam02574 |
Homocysteine S-methyltransferase; This is a family of related homocysteine ... |
29-336 |
3.57e-106 |
|
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: 335.66 E-value: 3.57e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 29 LVLDGGMGTMIQQRHLE-EEEFRgqefkdhpkslkgNNDILsiTQPDVIYSIHKEYLEAGADIIETNTFSSTSIAQAD-Y 106
Cdd:pfam02574 1 LILDGGMGTELQRRGLDlTEPLW-------------SNELL--TRPEIIREIHRDYLEAGADIIETNTYQASPIKLAEgL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 107 GMEDLAYRLNKASAEVARRAADDVsaqtgckrFVAGALGPTNKTLSVSPSverpdyrnITFDELVEAYAEQVKGLLDGGA 186
Cdd:pfam02574 66 EEEEAVYELNRAAVRLAREAADEY--------FVAGSIGPYGATLSDGYG--------LSFDELVDFHREQLEALLDGGV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 187 DVLLVETIFDTANAKAALfaidRLFEESYEArPVLISGTIVDKsGRTLSGQTGEAFVISVSHA-QPLCIGLNCALgASEM 265
Cdd:pfam02574 130 DLLLFETIPDLLEAKAAL----ELLAEEPDL-PVWISFTIEDG-TRLRSGTTLEAAVAALLHAtGPLAVGVNCAL-PEEM 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37620202 266 RPFIEAIGKSTSAFVICYPNAglpntFGG-YDETPDVTAAHLKEFAVDGlVNIVGGCCGTTPDHIRAIAESV 336
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 ... |
373-611 |
7.15e-72 |
|
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: 239.88 E-value: 7.15e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 373 GERCNVAGSRKFAKLIMaGNYEEALSIAKAQVEMGAQVLDINMDEG-----MLDGAAAMSRFCNLIASEPDICKVPLCID 447
Cdd:pfam00809 1 MGILNVTPDSFSDGGRF-LDLDKALAHARRMVEEGADIIDIGGESTrpgaeRVDGEEEMERVLPVLAALRDEADVPISVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 448 SSNFSVIEAGLKCcqGKCIVNSISlkeGEQDFLRRARQVRRYGAAVVVMAFDED--------GQATETDQKVQICSRAYH 519
Cdd:pfam00809 80 TTKAEVAEAALKA--GADIINDIS---GGDGDPEMAELAAEYGAAVVVMHMDGTpktmqeneQQYEDVVEEVERFLRARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 520 LLIDQAGFNPNDIIFDPNILTigTGMEEHSMYAINFIRATRIIKeslpGARVSGGLSNLSFSFRGME---AIREAMHGAF 596
Cdd:pfam00809 155 AAAEEAGVPPEDIILDPGIGF--GKTEEHNLELLRTLDELRVIL----GVPVLLGVSRKSFIGRGLPlggEERDAGTAAF 228
|
250
....*....|....*
gi 37620202 597 LYHAIKDGMDMGIVN 611
Cdd:pfam00809 229 LALAIAAGADIVRVH 243
|
|
| PRK08645 |
PRK08645 |
bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; ... |
22-341 |
3.91e-66 |
|
bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; Reviewed
Pssm-ID: 236321 [Multi-domain] Cd Length: 612 Bit Score: 235.89 E-value: 3.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 22 ELLQQRILVLDGGMGTMIQQRHLeeeeFRGQEFkdhpkslkgnnDILSITQPDVIYSIHKEYLEAGADIIETNTFSSTSI 101
Cdd:PRK08645 6 ERLKERVLIADGAMGTLLYSRGV----PLDRCF-----------EELNLSHPELILRIHREYIEAGADVIQTNTFGANRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 102 AQADYGMEDLAYRLNKASAEVARRAADDvsaqtgcKRFVAGALGPTNKtlsvspsveRPDYRNITFDELVEAYAEQVKGL 181
Cdd:PRK08645 71 KLKRYGLEDKVKEINRAAVRLAREAAGD-------DVYVAGTIGPIGG---------RGPLGDISLEEIRREFREQIDAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 182 LDGGADVLLVETIFDTANAKAALFAIDRLfeesYEArPVLISGTiVDKSGRTLSGQTGEAFVISVSHAQPLCIGLNCALG 261
Cdd:PRK08645 135 LEEGVDGLLLETFYDLEELLLALEAAREK----TDL-PIIAQVA-FHEDGVTQNGTSLEEALKELVAAGADVVGLNCGLG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 262 ASEMRPFIEAIGKSTSAFVICYPNAGLPNTFGG---YDETPDVTAAHLKEFAVDGlVNIVGGCCGTTPDHIRAIAESVRH 338
Cdd:PRK08645 209 PYHMLEALERIPIPENAPLSAYPNAGLPEYVDGryvYSANPEYFAEYALEFVEQG-VRLIGGCCGTTPEHIRAMARALKG 287
|
...
gi 37620202 339 VKP 341
Cdd:PRK08645 288 LKP 290
|
|
| Pterin_binding |
cd00423 |
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and ... |
369-625 |
1.61e-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: 214.06 E-value: 1.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 369 FVNIGErCNVAGSRKFAkLIMAGNYEEALSIAKAQVEMGAQVLDINMDEG--------MLDGAAAMSRFCNLIASEPDic 440
Cdd:cd00423 1 TLIMGI-LNVTPDSFSD-GGKFLSLDKALEHARRMVEEGADIIDIGGESTrpgaepvsVEEELERVIPVLRALAGEPD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 441 kVPLCIDSSNFSVIEAGLKCcqGKCIVNSISLKEGEqdfLRRARQVRRYGAAVVVMAFDEDGQ--------ATETDQKVQ 512
Cdd:cd00423 77 -VPISVDTFNAEVAEAALKA--GADIINDVSGGRGD---PEMAPLAAEYGAPVVLMHMDGTPQtmqnnpyyADVVDEVVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 513 ICSRAYHLLIDqAGFNPNDIIFDPNILTIGTgmEEHSMYAINFIRATRiikeSLPGARVSGGLSNLSFSFR---GMEAIR 589
Cdd:cd00423 151 FLEERVEAATE-AGIPPEDIILDPGIGFGKT--EEHNLELLRRLDAFR----ELPGLPLLLGVSRKSFLGDllsVGPKDR 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 37620202 590 EAMHGAFLYHAIKDGMDMGIVNAgNLPVYDDIDKEL 625
Cdd:cd00423 224 LAGTAAFLAAAILNGADIVRVHD-VKELRDAIKVAE 258
|
|
| MHT1 |
COG2040 |
Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) [Amino acid transport and ... |
23-337 |
1.75e-53 |
|
Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) [Amino acid transport and metabolism];
Pssm-ID: 441643 [Multi-domain] Cd Length: 301 Bit Score: 189.64 E-value: 1.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 23 LLQQRILVLDGGMGTmiqqrhleEEEFRGQEFKDHPKSLKgnndILsITQPDVIYSIHKEYLEAGADIIETNTFSST--S 100
Cdd:COG2040 8 LLMGRILLLDGGMGT--------ELERRGGDLLDPLWSAF----AL-LEAPELVRAVHRDYFAAGADVITTNSYQASpdG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 101 IAQADYGMEDLAyRLNKASAEVARRAADDvsAQTGCKRFVAGALGPTNktlsvspSVERPDYRnITFDELVEAYAEQVKG 180
Cdd:COG2040 75 LAELGYSAEEAE-RLNRRAVALAREARDE--YTPGPPVLVAGSVGPYG-------DEYRPDYG-LSAEEAEAYHRPRIEA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 181 LLDGGADVLLVETIFDTANAKAALfaidRLFEESyeARPVLISGTiVDKSGRTLSGQT-GEAFVISVSHAQPLCIGLNCA 259
Cdd:COG2040 144 LAEAGVDLLAAETIPSLAEAIAIA----RAAAEA--GKPVWISFT-VEDDGRLRSGEPlAEAIAAVDTDPGPAAVGVNCS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 260 lGASEMRPFIEAIGKSTSAFVICYPNAG------LPNTFGGYDETPDVTAAHLKEFAVDGLvNIVGGCCGTTPDHIRAIA 333
Cdd:COG2040 217 -HPEHFEAALEALAAWTGRPIGVYANAGemsdaeLKTWGGLDDGDPEELAEQAAEWVAAGA-RIIGGCCGTGPRHIAAIA 294
|
....
gi 37620202 334 ESVR 337
Cdd:COG2040 295 RALR 298
|
|
| PRK07534 |
PRK07534 |
betaine--homocysteine S-methyltransferase; |
20-346 |
1.17e-47 |
|
betaine--homocysteine S-methyltransferase;
Pssm-ID: 236045 [Multi-domain] Cd Length: 336 Bit Score: 173.78 E-value: 1.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 20 LTELLQQR-ILVLDGGMGTMIQQRHLEEeefrgqefKDHPkslkgnnDILSITQPDVIYSIHKEYLEAGADIIETNTFSS 98
Cdd:PRK07534 5 LSDLLAERgVLLADGATGTNLFNMGLES--------GEAP-------ELWNEDHPDNITALHQGFVDAGSDIILTNSFGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 99 TSIAQADYGMEDLAYRLNKASAEVARRAADdvsaQTGCKRFVAGALGPTNKTLSVSPSverpdyrnITFDELVEAYAEQV 178
Cdd:PRK07534 70 TAARLKLHDAQDRVHELNRAAAEIAREVAD----KAGRKVIVAGSVGPTGEIMEPMGA--------LTHALAVEAFHEQA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 179 KGLLDGGADVLLVETIFDTANAKAALFAIDRLfeesyeARPVLISGTIvDKSGRTLSGQTGEAF---VISVSHAqPLCIG 255
Cdd:PRK07534 138 EGLKAGGADVLWVETISAPEEIRAAAEAAKLA------GMPWCGTMSF-DTAGRTMMGLTPADLadlVEKLGEP-PLAFG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 256 LNCALGASE-MRPFIEAIGKSTSAFVICYPNAGLPNTFGG---YDETPDVTAAHLKeFAVDGLVNIVGGCCGTTPDHIRA 331
Cdd:PRK07534 210 ANCGVGASDlLRTVLGFTAQGPERPIIAKGNAGIPKYVDGhihYDGTPELMAEYAV-LARDAGARIIGGCCGTMPEHLAA 288
|
330
....*....|....*
gi 37620202 332 IAESVRHVKPRVPPT 346
Cdd:PRK07534 289 MRAALDARPRGPRPS 303
|
|
| mmuM |
PRK09485 |
homocysteine methyltransferase; Provisional |
20-337 |
1.00e-44 |
|
homocysteine methyltransferase; Provisional
Pssm-ID: 181899 [Multi-domain] Cd Length: 304 Bit Score: 164.26 E-value: 1.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 20 LTELL-QQRILVLDGGMGTmiqqrhleEEEFRGQEFKDHPKSLKgnndILsITQPDVIYSIHKEYLEAGADIIETNTFSS 98
Cdd:PRK09485 4 FKELLaQGPVLILDGALAT--------ELEARGCDLNDSLWSAK----VL-LENPELIYQVHLDYFRAGADCAITASYQA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 99 TSIAQADYGM-EDLAYRLNKASAEVARRAADDVSAQtgcKRFVAGALGPTNKTLSvSPSVERPDYrNITFDELVEAYAEQ 177
Cdd:PRK09485 71 TFQGFAARGLsEAEAEELIRRSVELAKEARDEFWAE---KPLVAGSVGPYGAYLA-DGSEYRGDY-GLSEEELQDFHRPR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 178 VKGLLDGGADVLLVETIFDTANAKAALfaidRLFEESYEARPVLISGTIVDksGRTLSGQT--GEAFVISVSHAQPLCIG 255
Cdd:PRK09485 146 IEALAEAGADLLACETIPNLDEAEALV----ELLKEEFPGVPAWLSFTLRD--GTHISDGTplAEAAALLAASPQVVAVG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 256 LNCAlGASEMRPFIEAIGKSTSAFVICYPNAGlpntfGGYDE-----TPDVTAAHLKEFAVDGL---VNIVGGCCGTTPD 327
Cdd:PRK09485 220 VNCT-APELVTAAIAALRAVTDKPLVVYPNSG-----EVYDAvtktwHGPADDASLGELAPEWYaagARLIGGCCRTTPE 293
|
330
....*....|
gi 37620202 328 HIRAIAESVR 337
Cdd:PRK09485 294 DIAALAAALK 303
|
|
| MtbC1 |
COG5012 |
Methanogenic corrinoid protein MtbC1 [Energy production and conversion]; |
671-859 |
3.01e-42 |
|
Methanogenic corrinoid protein MtbC1 [Energy production and conversion];
Pssm-ID: 444036 [Multi-domain] Cd Length: 219 Bit Score: 154.28 E-value: 3.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 671 ERLEYALVKGIEKYVVEDTEEARAqtERYPrPLHVIEGPLMNGMKTVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFME 750
Cdd:COG5012 12 ESLADAVLEGDEDEALELVAEALA--AGMD-PEEIILDGLAPGMREVGELWEEGEIFVPEEHLAAAAMKAGLEILKPLLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 751 KEREemmatsgcveevdpYQGTVLLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMIPCDRILREAIHNKADIIGLSGL 830
Cdd:COG5012 89 EEGG--------------RKGKVVIGTVEGDLHDIGKNIVADMLRAAGFEVIDLGADVPPEEFVEAAKEEKPDIVGLSAL 154
|
170 180 190
....*....|....*....|....*....|.
gi 37620202 831 ITPSLDEMIHVAKEMERLGL--KIPLLIGGA 859
Cdd:COG5012 155 LTTTMPAMKELIEALREAGLrdKVKVIVGGA 185
|
|
| corrinoid_protein_B12-BD |
cd02070 |
B12 binding domain of corrinoid proteins. A family of small methanogenic corrinoid proteins ... |
676-863 |
3.75e-42 |
|
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: 153.16 E-value: 3.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 676 ALVKGIEKYVVEDTEEAraqTERYPRPLHVIEGPLMNGMKTVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREE 755
Cdd:cd02070 4 AIVDGDEEETVELVKKA---LEAGIDPQDIIEEGLAPGMDIVGDKYEEGEIFVPELLMAADAMKAGLDLLKPLLGKSKSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 756 MmatsgcveevdpyQGTVLLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMIPCDRILREAIHNKADIIGLSGLITPSL 835
Cdd:cd02070 81 K-------------KGKVVIGTVEGDIHDIGKNLVATMLEANGFEVIDLGRDVPPEEFVEAVKEHKPDILGLSALMTTTM 147
|
170 180 190
....*....|....*....|....*....|
gi 37620202 836 DEMIHVAKEMERLGL--KIPLLIGGATTSK 863
Cdd:cd02070 148 GGMKEVIEALKEAGLrdKVKVMVGGAPVNQ 177
|
|
| B12-binding |
cd02067 |
B12 binding domain (B12-BD). This domain binds different cobalamid derivates, like B12 ... |
772-890 |
3.10e-40 |
|
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: 144.57 E-value: 3.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 772 TVLLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMIPCDRILREAIHNKADIIGLSGLITPSLDEMIHVAKEMERLGL- 850
Cdd:cd02067 1 KVVIATVGGDGHDIGKNIVARALRDAGFEVIDLGVDVPPEEIVEAAKEEDADAIGLSGLLTTHMTLMKEVIEELKEAGLd 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 37620202 851 KIPLLIGGATTSKTHtavkIAPRYSSPVVHVLDASRSVVV 890
Cdd:cd02067 81 DIPVLVGGAIVTRDF----KFLKEIGVDAYFGPATEAVEV 116
|
|
| PRK07535 |
PRK07535 |
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase; Validated |
372-638 |
3.69e-36 |
|
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase; Validated
Pssm-ID: 181022 [Multi-domain] Cd Length: 261 Bit Score: 138.06 E-value: 3.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 372 IGERCNvaGSRK-FAKLIMAGNYEEALSIAKAQVEMGAQVLDINMDEGMLDGAAAMSRFCNLIASEPDickVPLCIDSSN 450
Cdd:PRK07535 4 IGERIN--GTRKsIAEAIEAKDAAFIQKLALKQAEAGADYLDVNAGTAVEEEPETMEWLVETVQEVVD---VPLCIDSPN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 451 FSVIEAGLKCCQGKCIVNSISlkeGEQDFLRRARQ-VRRYGAAVVVMAFDEDGQATETDQKVQIcsrAYHLL--IDQAGF 527
Cdd:PRK07535 79 PAAIEAGLKVAKGPPLINSVS---AEGEKLEVVLPlVKKYNAPVVALTMDDTGIPKDAEDRLAV---AKELVekADEYGI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 528 NPNDIIFDPNILTIGTgMEEHsmyAINFIRATRIIKESLPGARVSGGLSNLSFsfrGMEAiREAMHGAFLYHAIKDGMDM 607
Cdd:PRK07535 153 PPEDIYIDPLVLPLSA-AQDA---GPEVLETIRRIKELYPKVHTTCGLSNISF---GLPN-RKLINRAFLVMAMGAGMDS 224
|
250 260 270
....*....|....*....|....*....|...
gi 37620202 608 GIVNAgnlpvyddIDKELL--LLCENIIWNRDP 638
Cdd:PRK07535 225 AILDP--------LDRDLMgaIAAAEALLGQDP 249
|
|
| B12-binding_2 |
smart01018 |
B12 binding domain; Cobalamin-dependent methionine synthase is a large modular protein that ... |
668-753 |
2.31e-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: 2.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 668 SVEERLEYALVKGIEKYVVEDTEEARAQterYPRPLHVIEGPLMNGMKTVGDLFGAGKMFLPQVIKSARVMKKAVGHLIP 747
Cdd:smart01018 2 PLLERLAEAIVDGDEEGVEELVEEALAE---GVDPLEIINEGLIPGMNVVGDLFEAGEYFLPQVLMSAEAMKAAVAILKP 78
|
....*.
gi 37620202 748 FMEKER 753
Cdd:smart01018 79 LLEKEK 84
|
|
| B12-binding_like |
cd02065 |
B12 binding domain (B12-BD). Most of the members bind different cobalamid derivates, like B12 ... |
772-885 |
5.84e-33 |
|
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: 124.04 E-value: 5.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 772 TVLLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMIPCDRILREAIHNKADIIGLSGLITPSLDEMIHVAKEMERLGLK 851
Cdd:cd02065 1 KVLGATVGGDVHDIGKNIVAIALRDNGFEVIDLGVDVPPEEIVEAAKEEDADVVGLSALSTTHMEAMKLVIEALKELGID 80
|
90 100 110
....*....|....*....|....*....|....
gi 37620202 852 IPLLIGGATTSKTHTAVKIAPRYSSPVVHVLDAS 885
Cdd:cd02065 81 IPVVVGGAHPTADPEEPKVDAVVIGEGEYAGPAL 114
|
|
| pyl_corrinoid |
TIGR02370 |
methyltransferase cognate corrinoid proteins, Methanosarcina family; This model describes a ... |
676-863 |
6.90e-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: 117.98 E-value: 6.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 676 ALVKGIEKYVVEDTEEARAQTERyprPLHVIEGPLMNGMKTVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREE 755
Cdd:TIGR02370 5 AIFEGEEDDVVEGAQKALDAGID---PIELIEKGLMAGMGVVGKLFEDGELFLPHVMMSADAMLAGIKVLTPEMEKAVET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 756 MMatsgcveevdpyQGTVLLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMIPCDRILREAIHNKADIIGLSGLITPSL 835
Cdd:TIGR02370 82 EV------------LGKVVCGVAEGDVHDIGKNIVVTMLRANGFDVIDLGRDVPIDTVVEKVKKEKPLMLTGSALMTTTM 149
|
170 180 190
....*....|....*....|....*....|
gi 37620202 836 DEMIHVAKEMERLGLK--IPLLIGGATTSK 863
Cdd:TIGR02370 150 YGQKDINDKLKEEGYRdsVKFMVGGAPVTQ 179
|
|
| PLN02489 |
PLN02489 |
homocysteine S-methyltransferase |
20-337 |
1.25e-22 |
|
homocysteine S-methyltransferase
Pssm-ID: 215269 Cd Length: 335 Bit Score: 100.86 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 20 LTELLQQR--ILVLDGGMGTmiqqrhleEEEFRGQEFKDHPKSLKgnndiLSITQPDVIYSIHKEYLEAGADIIETNTFS 97
Cdd:PLN02489 12 LEDLLRQAggCAVIDGGFAT--------ELERHGADLNDPLWSAK-----CLITSPHLIRKVHLDYLEAGADIIITASYQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 98 STSIAQADYGM-----EDLayrLNKaSAEVARRAADDVsaqtgCKRFVAGALGPTNKTLSVSP----------------- 155
Cdd:PLN02489 79 ATIQGFESRGLsreesETL---LRK-SVEIACEARDIF-----WDKCQKGSTSRPGRELSYRPilvaasigsygayladg 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 156 SVERPDY-RNITFDELVEAYAEQVKGLLDGGADVLLVETIFDTANAKAALfaidRLFEESYEARPVLISGTIVDksGRTL 234
Cdd:PLN02489 150 SEYSGDYgPSVTLEKLKDFHRRRLQVLAEAGPDLIAFETIPNKLEAQAYV----ELLEEENIKIPAWISFNSKD--GVNV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 235 SgqTGEAFVISVSHA----QPLCIGLNCAlgasemrP--FIEA----IGKSTSAFVICYPNAG----------LPNTfgg 294
Cdd:PLN02489 224 V--SGDSLLECASIAdsckKVVAVGINCT-------PprFIHGlilsIRKVTSKPIVVYPNSGetydgeakewVEST--- 291
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 37620202 295 yDETPDVTAAHLKEFAVDGlVNIVGGCCGTTPDHIRAIAESVR 337
Cdd:PLN02489 292 -GVSDEDFVSYVNKWRDAG-ASLIGGCCRTTPNTIRAISKALS 332
|
|
| B12-binding |
pfam02310 |
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ... |
771-859 |
2.07e-21 |
|
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: 90.85 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 771 GTVLLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMIPCDRILREAIHNKADIIGLSGLITPSLDEMIHVAKEMERLGL 850
Cdd:pfam02310 1 GKVVVATVGGDLHPLGLNYVAAALRAAGFEVIILGANVPPEDIVAAARDEKPDVVGLSALMTTTLPGAKELIRLLKGIRP 80
|
....*....
gi 37620202 851 KIPLLIGGA 859
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 ... |
673-745 |
5.14e-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: 5.14e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37620202 673 LEYALVKGIEKYVVEDTEEARAqteryPRPLHVIEGPLMNGMKTVGDLFGAGKMFLPQVIKSARVMKKAVGHL 745
Cdd:pfam02607 1 LLEALLEGDEEAAEELLEEALE-----IDPEEIIEDLLIPGMDEVGELWEAGEIFVPQEHLAAEAMKAALAVL 68
|
|
| Sbm |
COG2185 |
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ... |
772-858 |
7.92e-08 |
|
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and metabolism];
Pssm-ID: 441788 [Multi-domain] Cd Length: 134 Bit Score: 52.45 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 772 TVLLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMIPCDRILREAIHNKADIIGLSglitpSLDE-----MIHVAKEME 846
Cdd:COG2185 12 RVLLAKPGLDGHDRGAKVIARALRDAGFEVIYLGLFQTPEEIVRAAIEEDADVIGVS-----SLDGghlelVPELIELLK 86
|
90
....*....|...
gi 37620202 847 RLGLK-IPLLIGG 858
Cdd:COG2185 87 EAGAGdILVVVGG 99
|
|
| PRK02261 |
PRK02261 |
methylaspartate mutase subunit S; Provisional |
772-830 |
1.43e-04 |
|
methylaspartate mutase subunit S; Provisional
Pssm-ID: 179400 [Multi-domain] Cd Length: 137 Bit Score: 43.01 E-value: 1.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 37620202 772 TVLLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMIPCDRILREAIHNKADIIGLSGL 830
Cdd:PRK02261 5 TVVLGVIGADCHAVGNKILDRALTEAGFEVINLGVMTSQEEFIDAAIETDADAILVSSL 63
|
|
| Glm_B12_BD |
cd02072 |
B12 binding domain of glutamate mutase (Glm). Glutamate mutase catalysis the conversion of (S) ... |
772-830 |
1.31e-03 |
|
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: 40.14 E-value: 1.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 37620202 772 TVLLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMIPCDRILREAIHNKADIIGLSGL 830
Cdd:cd02072 1 TIVLGVIGSDCHAVGNKILDHAFTEAGFNVVNLGVLSPQEEFIDAAIETDADAILVSSL 59
|
|
| MM_CoA_mut_B12_BD |
cd02071 |
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), ... |
773-858 |
4.55e-03 |
|
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: 38.34 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37620202 773 VLLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMIPCDRILREAIHNKADIIGLSGLITPSLDEMIHVAKEMERLGL-K 851
Cdd:cd02071 2 ILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRQTPEEIVEAAIQEDVDVIGLSSLSGGHMTLFPEVIELLRELGAgD 81
|
....*..
gi 37620202 852 IPLLIGG 858
Cdd:cd02071 82 ILVVGGG 88
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