|
Name |
Accession |
Description |
Interval |
E-value |
| metH |
PRK09490 |
B12-dependent methionine synthase; Provisional |
19-1261 |
0e+00 |
|
B12-dependent methionine synthase; Provisional
Pssm-ID: 236539 [Multi-domain] Cd Length: 1229 Bit Score: 2152.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 19 RDEINAILQKRIMVLDGGMGTMIQREKLNEEHFRGQEFKDHARPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTF 98
Cdd:PRK09490 8 LAQLRALLAERILVLDGAMGTMIQRYKLEEADYRGERFADWPCDLKGNNDLLVLTQPDVIEAIHRAYLEAGADIIETNTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 99 SSTSIAQADYGLEHLAYRMNMCSAGVARKAAEEVTLQT-GIKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYQ 177
Cdd:PRK09490 88 NATTIAQADYGMESLVYELNFAAARLAREAADEWTAKTpDKPRFVAGVLGPTNRTASISPDVNDPGFRNVTFDELVAAYR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 178 EQAKGLLDGGVDILLIETIFDTANAKAALFALQNLFEEKYAPRPIFISGTIVDKSGRTLSGQTGEGFVISVSHGEPLCIG 257
Cdd:PRK09490 168 EQTRGLIEGGADLILIETIFDTLNAKAAIFAVEEVFEELGVRLPVMISGTITDASGRTLSGQTTEAFWNSLRHAKPLSIG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 258 LNCALGAAEMRPFIEIIGKCTTAYVLCYPNAGLPNTFGDYDETPSMMAKHLKDFAMDGLVNIVGGCCGSTPDHIREIAEA 337
Cdd:PRK09490 248 LNCALGADELRPYVEELSRIADTYVSAHPNAGLPNAFGEYDETPEEMAAQIGEFAESGFLNIVGGCCGTTPEHIAAIAEA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 338 VKNCKPRVPPATafEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALCVAKVQVEMGAQVLDVNM 417
Cdd:PRK09490 328 VAGLPPRKLPEI--PVACRLSGLEPLNIDDDSLFVNVGERTNVTGSAKFARLIKEEDYDEALDVARQQVENGAQIIDINM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 418 DDGMLDGPSAMTRFCNLIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEDDFLEKARKIKKYGAAMVV 497
Cdd:PRK09490 406 DEGMLDSEAAMVRFLNLIASEPDIARVPIMIDSSKWEVIEAGLKCIQGKGIVNSISLKEGEEKFIEHARLVRRYGAAVVV 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 498 MAFDEEGQATETDTKIRVCTRAYHLLVKKLGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATKVIKETLPGARISGGL 577
Cdd:PRK09490 486 MAFDEQGQADTRERKIEICKRAYDILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKQNLPHAKISGGV 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 578 SNLSFSFRGMEAIREAMHGVFLYHAIKSGMDMGIVNAGNLPVYDDIHKELLQLCEDLIWNKDPEATEKLLRYAQT-QGTG 656
Cdd:PRK09490 566 SNVSFSFRGNNPVREAIHAVFLYHAIKAGMDMGIVNAGQLAIYDDIPPELREAVEDVVLNRRPDATERLLEIAEKyRGKG 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 657 GKKVIQTD-EWRNGPVEERLEYALVKGIEKHIIEDTEEARLnqkKYPRPLNIIEGPLMNGMKIVGDLFGAGKMFLPQVIK 735
Cdd:PRK09490 646 GKKAKAEDlEWRSWPVEKRLEHALVKGITEFIEEDTEEARQ---QAARPLEVIEGPLMDGMNVVGDLFGEGKMFLPQVVK 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 736 SARVMKKAVGHLIPFMEKEREetrvlNGTVEEEdpyQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKI 815
Cdd:PRK09490 723 SARVMKQAVAYLEPFIEAKKE-----GGTDRKS---NGKILMATVKGDVHDIGKNIVGVVLQCNNYEVIDLGVMVPAEKI 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 816 LKAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAIRIPLLIGGATTSKTHTAVKIAPRYSAPVIHVLDASKSVVVCSQ 895
Cdd:PRK09490 795 LETAKEENADIIGLSGLITPSLDEMVHVAKEMERQGFTIPLLIGGATTSKAHTAVKIAPNYSGPVVYVTDASRAVGVVSS 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 896 LLDENLKDEYFEEIMEEYEDIRQDHYESLKERRYLPLSQARKSGFQMDWlSEPHPVKPTFIGTQVFEDYDLQKLVDYIDW 975
Cdd:PRK09490 875 LLSDEQRDAYVAETRAEYEKVREQHARKKPRKPLLTLEAARANRFKIDW-EAYTPPKPKFLGVQVFEDYDLAELREYIDW 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 976 KPFFDVWQLRGKYpnrgfPKIFNDKTVGGEARKVYDDAHNMLNTLISQKKLRARGVVGFWPAQSIQDDIHLYAEaavPQA 1055
Cdd:PRK09490 954 TPFFQTWELAGKY-----PAILEDEVVGEEARKLFADAQAMLDKIIAEKWLTARGVIGLFPANSVGDDIEVYTD---ESR 1025
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 1056 AEPIATFYGLRQQAEKDSastEPYYCLSDFIAPLHSGIRDYLGLFAV-ACFGVEELSKAYEDDGDDYSSIMVKALGDRLA 1134
Cdd:PRK09490 1026 TEVLATLHHLRQQTEKRG---RPNYCLADFVAPKESGKADYIGAFAVtAGLGEDELADRFEAAHDDYNAIMVKALADRLA 1102
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 1135 EAFAEELHERVRRELWAYCGSEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLADIEQSTGIRLTESLAMAPASA 1214
Cdd:PRK09490 1103 EAFAEYLHERVRKEFWGYAPDENLSNEELIREKYQGIRPAPGYPACPDHTEKATLFDLLDAEKNTGMKLTESYAMWPGAS 1182
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....*..
gi 169790923 1215 VSGLYFSNLKSKYFAVGKISKDQVEDYALRKNISVAEVEKWLGPILG 1261
Cdd:PRK09490 1183 VSGWYFSHPESKYFAVGKIGRDQVEDYAARKGMSVEEVERWLAPNLG 1229
|
|
| metH |
TIGR02082 |
5-methyltetrahydrofolate--homocysteine methyltransferase; This family represents ... |
26-1230 |
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: 2093.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 26 LQKRIMVLDGGMGTMIQREKLNEEHFRGQeFKDHARPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQ 105
Cdd:TIGR02082 1 LNQRILVLDGAMGTQLQSANLTEADFRGA-FADCHRELKGNNDILNLTKPEVIATIHRAYFEAGADIIETNTFNSTTISQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 106 ADYGLEHLAYRMNMCSAGVARKAAEEVTLQTGIKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYQEQAKGLLD 185
Cdd:TIGR02082 80 ADYDLEDLIYDLNFKGAKLARAVADEFTLTPEKPRFVAGSMGPTNKTATLSPDVERPGFRNVTYDELVDAYTEQAKGLLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 186 GGVDILLIETIFDTANAKAALFALQNLFEEKYAPRPIFISGTIVDKSGRTLSGQTGEGFVISVSHGEPLCIGLNCALGAA 265
Cdd:TIGR02082 160 GGVDLLLIETCFDTLNAKAALFAAETVFEEKGRELPIMISGTIVDTSGRTLSGQTIEAFLTSLEHAGIDMIGLNCALGPD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 266 EMRPFIEIIGKCTTAYVLCYPNAGLPNTFGDYDETPSMMAKHLKDFAMDGLVNIVGGCCGSTPDHIREIAEAVKNCKPRV 345
Cdd:TIGR02082 240 EMRPHLKHLSEHAEAYVSCHPNAGLPNAFGEYDLTPDELAKALADFAAEGGLNIVGGCCGTTPDHIRAIAEAVKNIKPRQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 346 PPAtaFEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALCVAKVQVEMGAQVLDVNMDDGMLDGP 425
Cdd:TIGR02082 320 RPV--LYEPSRLSGLEAITIAQDSNFVNIGERTNVAGSKKFRRLIIAEDYDEALDIAKQQVENGAQILDINVDYGMLDGV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 426 SAMTRFCNLIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEDDFLEKARKIKKYGAAMVVMAFDEEGQ 505
Cdd:TIGR02082 398 AAMKRFLNLLASEPDISTVPLMLDSSEWAVLEAGLKCIQGKCIVNSISLKDGEERFIETAKLIKEYGAAVVVMAFDEEGQ 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 506 ATETDTKIRVCTRAYHLLVKKLGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATKVIKETLPGARISGGLSNLSFSFR 585
Cdd:TIGR02082 478 ARTADRKIEICKRAYNILTEKVGFPPEDIIFDPNILTIATGIEEHRRYAINFIEAIRWIKEELPDAKISGGVSNVSFSFR 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 586 GMEAIREAMHGVFLYHAIKSGMDMGIVNAGNLPVYDDIHKELLQLCEDLIWNKDPEATEKLLRYAQT-QGTGGK--KVIQ 662
Cdd:TIGR02082 558 GNPAAREAMHSVFLYHAIRAGMDMGIVNAGKILPYDDIDPELRQVVEDLILNRRREATEPLLELAQLyEGTTTKssKEAQ 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 663 TDEWRNGPVEERLEYALVKGIEKHIIEDTEEARlnqKKYPRPLNIIEGPLMNGMKIVGDLFGAGKMFLPQVIKSARVMKK 742
Cdd:TIGR02082 638 QAEWRNLPVEERLEYALVKGEREGIEEDLEEAR---KKLTRPLEIIEGPLMDGMKVVGDLFGSGKMFLPQVVKSARVMKK 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 743 AVGHLIPFMEKEReetrvlngtveEEDPYQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDH 822
Cdd:TIGR02082 715 AVAYLEPHMEKEK-----------SEDSSKGKIVLATVKGDVHDIGKNIVGVVLSCNGYEVVDLGVMVPIEKILEAAKDH 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 823 KADIIGLSGLITPSLDEMIFVAKEMERLAIRIPLLIGGATTSKTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDENLK 902
Cdd:TIGR02082 784 NADVIGLSGLITPSLDEMKEVAEEMNRRGITIPLLIGGAATSKTHTAVKIAPIYKGPVVYVLDASRAVTVMDTLMSAKRK 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 903 DEYFEEIMEEYEDIRQDHYESLKERRYLPLSQARKSGFQMDWLSEPHPVKPTFIGTQVFEDYDLQKLVDYIDWKPFFDVW 982
Cdd:TIGR02082 864 DTENGRIKEEYDTAREKHGEQRSKRIAASEQAARKNVFAPDWSDDIEPPAPPFWGTQIVEASDIAELRPYIDWTPFFLQW 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 983 QLRGKYpnrgfPKIFNDKTVGGEARKVYDDAHNMLNTLISQKKLRARGVVGFWPAQSIQDDIHLYAEAAVpqAAEPIATF 1062
Cdd:TIGR02082 944 QLRGKY-----PKILGDEYEGLEAQKLFPDANEMLDKLSAENLLHARGVYGYFPAQSVGDDIEIYTDETV--ETHPIATV 1016
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 1063 YGLRQQAEKDSAStepYYCLSDFIAPLHSGIRDYLGLFAV-ACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEEL 1141
Cdd:TIGR02082 1017 RYLFHFPRQQSGR---YLCLADFIAPKASGIVDYIGAFAVtAGFGAEELADKLEAQHDDYDYIMVKAIADRLAEAFAEYL 1093
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 1142 HERVRRELWAYCGSEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLADIEQsTGIRLTESLAMAPASAVSGLYFS 1221
Cdd:TIGR02082 1094 HRRVRKELWGYAAEEPLSNEDLLKLRYQGIRPAPGYPACPDHTEKATMFELLEPER-IGVRLTESLAMHPEQSVSGLYFA 1172
|
....*....
gi 169790923 1222 NLKSKYFAV 1230
Cdd:TIGR02082 1173 HPEAKYFAV 1181
|
|
| MetH2 |
COG1410 |
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; ... |
37-1230 |
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: 1561.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 37 MGTMIQREKLNEEHFRGQEFKDHARPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYR 116
Cdd:COG1410 1 MGTMIQLLKLRELDADGAMFTDLQLDLKGNNDLLGLTGPNEILEIHRPELEAGADIIETNTGADAAITAADGAAEALLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 117 MNM-CSAGVARKAAEEVTLQTGIKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYQEQAKGLLDGGVDILLIET 195
Cdd:COG1410 81 YNGaAAALALEAAAAAAAAAAAAARAVAGAPGPTGGTASPGPDVPGLGFRNFDFDELVEAYAEAGLGLGGGGADLLLTET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 196 IFDTANAKAALFALQNLFEEKYAPRPIFISGTIVDKSGRTLSGQTGEGFVISVSHGEPLCIGLNCALGAAEMRPFIEIIG 275
Cdd:COG1410 161 IFDTLNAAAAAAAAAAAAEEEGVPIPVMVTGTITDGSGRTLSGQTAEAFLESLGHAAPGSNGLNCALGAEELRPYLEELS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 276 KCTTAYVLCYPNAGLPNTFGDYDETPSMMAKHLKDFAMDGLVNIVGGCCGSTPDHIREIAEAVKNCKPRVPPAtafEGHM 355
Cdd:COG1410 241 RIPPSAVSNAPNAGLPNGFGEYDETPEEMAAALAEFAEEGGVNIVGGCCGTTPEHIRAIAEAVAGLKPRPREK---PPPA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 356 LLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALCVAKVQVEMGAQVLDVNMDDGMLDGPSAMTRFCNLI 435
Cdd:COG1410 318 VLSGLEPVPIGQDSPFVNIGERTNVTGSKKFRELILEGDYDEALEVAREQVEAGAQILDVNVDEPGRDEVAAMVRFLNLL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 436 ASEpdiAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEDDFLEKARKIKKYGAAMVVMAFDEEGQATETDTKIRV 515
Cdd:COG1410 398 ASE---VRVPLMIDSSKPEVIEAGLKCYQGKPIVNSISLEEGEERFEEVAPLAKKYGAAVVVLAIDEEGQADTAERKLEI 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 516 CTRAYHLLVKKLGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATKVIKETLPGARISGGLSNLSFSFRGmeAIREAMH 595
Cdd:COG1410 475 AERIYDLAVEEYGFPPEDIIFDPLVFTVATGIEEHRNYAVETIEAIRLIKEELPGAKTSLGVSNVSFGLPG--NVREALN 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 596 GVFLYHAIKSGMDMGIVNAGNLPVYDDIHKELLQLCEDLIWNKDPEATEKLLRYAQTQgTGGKKVIQTDEWRNGPVEERL 675
Cdd:COG1410 553 SVFLYHAIKAGLDMAIVNPGQLEPYDDIPPELRELAEDVLLNRRPDALERLIELFEGV-KGAKAKKADLEWRELPVEERL 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 676 EYALVKGIEKHIIEDTEEARlnqKKYPRPLNIIEGPLMNGMKIVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEr 755
Cdd:COG1410 632 KHAIVKGIKEGIEEDTEEAL---AEGARPLEIINGPLMPGMNVVGDLFGAGKMFLPQVLKSAEVMKAAVAYLEPFMEKE- 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 756 eetrvlngtvEEEDPYQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGLITP 835
Cdd:COG1410 708 ----------KGESSSKGKIVLATVKGDVHDIGKNIVGVVLENNGYEVIDLGVMVPAEKILEAAKEHKADIIGLSGLMTT 777
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 836 SLDEMIFVAKEMERLAIRIPLLIGGATTSKTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDENLKDEYFEEIMEEYED 915
Cdd:COG1410 778 SLDEMKEVAEEMRRRGLDIPVLIGGAALTRAYTAVKIAPAYDGAVVYAKDASRAVRVADKLLSKERREAFVAEIKAEYEK 857
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 916 IRQDHYEslKERRYLPLSQARKsgfqmDWLSEPHPVKPTFIGTQVFEDYDLQKLVDYIDWKPFFDVWQLRGKYPNrgfpk 995
Cdd:COG1410 858 LRERHAA--RKKKLLSLEEARS-----NVDSDYPPPTPPFLGTRVLKDIPLAELVPYIDWTPFFQQWGLKGKYLD----- 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 996 ifndktvGGEARKVYDDAHNMLNTLISQKKLRARGVVGFWPAQSIQDDIHLYAeaavPQAAEPIATFYGLRQQaekdsas 1075
Cdd:COG1410 926 -------GEEARELFPDAQAMLDRIIEEKWLTARAVYGYFPANSEGDDIEVYD----DESSEELARFHFPRQQ------- 987
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 1076 TEPYYCLSDFIAPLHSGIRDYLGLFAV-ACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEELHERVRRElWAYCG 1154
Cdd:COG1410 988 RGPNLCLADFVAPKESGERDYVGFFAVtAGIGIEELAAELEAAGDDYDAIMLHALADRLAEAFAEYLHERVRKE-WGYAP 1066
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169790923 1155 SEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLADIEQsTGIRLTESLAMAPASAVSGLYFSNLKSKYFAV 1230
Cdd:COG1410 1067 DEALTNEDLIKEKYRGIRPAPGYPACPDHTEKRKLFDLLDAER-IGVTLTESFAMHPEASVSGIYFHHPEAKYFNV 1141
|
|
| Met_synt_B12 |
pfam02965 |
Vitamin B12 dependent methionine synthase, activation domain; |
965-1246 |
7.89e-165 |
|
Vitamin B12 dependent methionine synthase, activation domain;
Pssm-ID: 460767 [Multi-domain] Cd Length: 273 Bit Score: 491.22 E-value: 7.89e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 965 DLQKLVDYIDWKPFFDVWQLRGKYPnrgfpKIFNDKTVGGEARKVYDDAHNMLNTLISQKKLRARGVVGFWPAQSIQDDI 1044
Cdd:pfam02965 1 DLAELVPYIDWTPFFQAWELKGKYP-----AILDDEVVGEEARKLFADAQAMLDRIIEEKWLTARGVVGFFPANSVGDDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 1045 HLYAEaavPQAAEPIATFYGLRQQAEKDSasTEPYYCLSDFIAPLHSGIRDYLGLFAVAC-FGVEELSKAYEDDGDDYSS 1123
Cdd:pfam02965 76 EVYTD---ESRTEVLATFHTLRQQTEKPE--GRPNLCLADFIAPKESGIADYIGAFAVTAgIGIEELAARFEAAHDDYSA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 1124 IMVKALGDRLAEAFAEELHERVRRELWAYCGSEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLADIEQSTGIRL 1203
Cdd:pfam02965 151 IMVKALADRLAEAFAEYLHERVRKELWGYAPDENLSNEDLIKEKYQGIRPAPGYPACPDHTEKFTLFDLLDAEENIGIRL 230
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 169790923 1204 TESLAMAPASAVSGLYFSNLKSKYFAVGKISKDQVEDYALRKN 1246
Cdd:pfam02965 231 TESFAMTPAASVSGLYFAHPESRYFAVGKIGKDQVEDYAKRKG 273
|
|
| MeTr |
cd00740 |
MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent ... |
371-627 |
1.60e-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: 421.42 E-value: 1.60e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 371 FVNIGERCNVAGSRKFAKLIMAGNYEEALCVAKVQVEMGAQVLDVNMDDGMLDGPSAMTRFCNLIASEPdiaKVPLCIDS 450
Cdd:cd00740 1 FLNIGERTNVTGSKKFRELIKAEDYDEALDVARQQVEGGAQILDLNVDYGGLDGVSAMKWLLNLLATEP---TVPLMLDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 451 SNFAVIEAGLKCCQGKCIVNSISLKEGEDDFLEKARKIKKYGAAMVVMAFDEEGQATETDTKIRVCTRAYHLLVKKLGFN 530
Cdd:cd00740 78 TNWEVIEAGLKCCQGKCVVNSINLEDGEERFLKVARLAKEHGAAVVVLAFDEQGQAKTRDKKVEIAERAYEALTEFVGFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 531 PNDIIFDPNILTIGTGMEEHNLYAINFIHATKVIKETLPGARISGGLSNLSFSFrgMEAIREAMHGVFLYHAIKSGMDMG 610
Cdd:cd00740 158 PEDIIFDPLILPIATGIEEHRPYALETIDAIRMIKERLPAVKISLGVSNVSFGF--NPAAREALNSVFLYEAIKAGLDMA 235
|
250
....*....|....*..
gi 169790923 611 IVNAGNLPVYDDIHKEL 627
Cdd:cd00740 236 IVNAGKLAPIEDIPEEL 252
|
|
| B12-binding_2 |
smart01018 |
B12 binding domain; Cobalamin-dependent methionine synthase is a large modular protein that ... |
670-755 |
1.73e-34 |
|
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: 126.82 E-value: 1.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 670 PVEERLEYALVKGIEKHIIEDTEEARlnqKKYPRPLNIIEGPLMNGMKIVGDLFGAGKMFLPQVIKSARVMKKAVGHLIP 749
Cdd:smart01018 2 PLLERLAEAIVDGDEEGVEELVEEAL---AEGVDPLEIINEGLIPGMNVVGDLFEAGEYFLPQVLMSAEAMKAAVAILKP 78
|
....*.
gi 169790923 750 FMEKER 755
Cdd:smart01018 79 LLEKEK 84
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| metH |
PRK09490 |
B12-dependent methionine synthase; Provisional |
19-1261 |
0e+00 |
|
B12-dependent methionine synthase; Provisional
Pssm-ID: 236539 [Multi-domain] Cd Length: 1229 Bit Score: 2152.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 19 RDEINAILQKRIMVLDGGMGTMIQREKLNEEHFRGQEFKDHARPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTF 98
Cdd:PRK09490 8 LAQLRALLAERILVLDGAMGTMIQRYKLEEADYRGERFADWPCDLKGNNDLLVLTQPDVIEAIHRAYLEAGADIIETNTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 99 SSTSIAQADYGLEHLAYRMNMCSAGVARKAAEEVTLQT-GIKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYQ 177
Cdd:PRK09490 88 NATTIAQADYGMESLVYELNFAAARLAREAADEWTAKTpDKPRFVAGVLGPTNRTASISPDVNDPGFRNVTFDELVAAYR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 178 EQAKGLLDGGVDILLIETIFDTANAKAALFALQNLFEEKYAPRPIFISGTIVDKSGRTLSGQTGEGFVISVSHGEPLCIG 257
Cdd:PRK09490 168 EQTRGLIEGGADLILIETIFDTLNAKAAIFAVEEVFEELGVRLPVMISGTITDASGRTLSGQTTEAFWNSLRHAKPLSIG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 258 LNCALGAAEMRPFIEIIGKCTTAYVLCYPNAGLPNTFGDYDETPSMMAKHLKDFAMDGLVNIVGGCCGSTPDHIREIAEA 337
Cdd:PRK09490 248 LNCALGADELRPYVEELSRIADTYVSAHPNAGLPNAFGEYDETPEEMAAQIGEFAESGFLNIVGGCCGTTPEHIAAIAEA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 338 VKNCKPRVPPATafEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALCVAKVQVEMGAQVLDVNM 417
Cdd:PRK09490 328 VAGLPPRKLPEI--PVACRLSGLEPLNIDDDSLFVNVGERTNVTGSAKFARLIKEEDYDEALDVARQQVENGAQIIDINM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 418 DDGMLDGPSAMTRFCNLIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEDDFLEKARKIKKYGAAMVV 497
Cdd:PRK09490 406 DEGMLDSEAAMVRFLNLIASEPDIARVPIMIDSSKWEVIEAGLKCIQGKGIVNSISLKEGEEKFIEHARLVRRYGAAVVV 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 498 MAFDEEGQATETDTKIRVCTRAYHLLVKKLGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATKVIKETLPGARISGGL 577
Cdd:PRK09490 486 MAFDEQGQADTRERKIEICKRAYDILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKQNLPHAKISGGV 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 578 SNLSFSFRGMEAIREAMHGVFLYHAIKSGMDMGIVNAGNLPVYDDIHKELLQLCEDLIWNKDPEATEKLLRYAQT-QGTG 656
Cdd:PRK09490 566 SNVSFSFRGNNPVREAIHAVFLYHAIKAGMDMGIVNAGQLAIYDDIPPELREAVEDVVLNRRPDATERLLEIAEKyRGKG 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 657 GKKVIQTD-EWRNGPVEERLEYALVKGIEKHIIEDTEEARLnqkKYPRPLNIIEGPLMNGMKIVGDLFGAGKMFLPQVIK 735
Cdd:PRK09490 646 GKKAKAEDlEWRSWPVEKRLEHALVKGITEFIEEDTEEARQ---QAARPLEVIEGPLMDGMNVVGDLFGEGKMFLPQVVK 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 736 SARVMKKAVGHLIPFMEKEREetrvlNGTVEEEdpyQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKI 815
Cdd:PRK09490 723 SARVMKQAVAYLEPFIEAKKE-----GGTDRKS---NGKILMATVKGDVHDIGKNIVGVVLQCNNYEVIDLGVMVPAEKI 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 816 LKAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAIRIPLLIGGATTSKTHTAVKIAPRYSAPVIHVLDASKSVVVCSQ 895
Cdd:PRK09490 795 LETAKEENADIIGLSGLITPSLDEMVHVAKEMERQGFTIPLLIGGATTSKAHTAVKIAPNYSGPVVYVTDASRAVGVVSS 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 896 LLDENLKDEYFEEIMEEYEDIRQDHYESLKERRYLPLSQARKSGFQMDWlSEPHPVKPTFIGTQVFEDYDLQKLVDYIDW 975
Cdd:PRK09490 875 LLSDEQRDAYVAETRAEYEKVREQHARKKPRKPLLTLEAARANRFKIDW-EAYTPPKPKFLGVQVFEDYDLAELREYIDW 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 976 KPFFDVWQLRGKYpnrgfPKIFNDKTVGGEARKVYDDAHNMLNTLISQKKLRARGVVGFWPAQSIQDDIHLYAEaavPQA 1055
Cdd:PRK09490 954 TPFFQTWELAGKY-----PAILEDEVVGEEARKLFADAQAMLDKIIAEKWLTARGVIGLFPANSVGDDIEVYTD---ESR 1025
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 1056 AEPIATFYGLRQQAEKDSastEPYYCLSDFIAPLHSGIRDYLGLFAV-ACFGVEELSKAYEDDGDDYSSIMVKALGDRLA 1134
Cdd:PRK09490 1026 TEVLATLHHLRQQTEKRG---RPNYCLADFVAPKESGKADYIGAFAVtAGLGEDELADRFEAAHDDYNAIMVKALADRLA 1102
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 1135 EAFAEELHERVRRELWAYCGSEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLADIEQSTGIRLTESLAMAPASA 1214
Cdd:PRK09490 1103 EAFAEYLHERVRKEFWGYAPDENLSNEELIREKYQGIRPAPGYPACPDHTEKATLFDLLDAEKNTGMKLTESYAMWPGAS 1182
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....*..
gi 169790923 1215 VSGLYFSNLKSKYFAVGKISKDQVEDYALRKNISVAEVEKWLGPILG 1261
Cdd:PRK09490 1183 VSGWYFSHPESKYFAVGKIGRDQVEDYAARKGMSVEEVERWLAPNLG 1229
|
|
| metH |
TIGR02082 |
5-methyltetrahydrofolate--homocysteine methyltransferase; This family represents ... |
26-1230 |
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: 2093.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 26 LQKRIMVLDGGMGTMIQREKLNEEHFRGQeFKDHARPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQ 105
Cdd:TIGR02082 1 LNQRILVLDGAMGTQLQSANLTEADFRGA-FADCHRELKGNNDILNLTKPEVIATIHRAYFEAGADIIETNTFNSTTISQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 106 ADYGLEHLAYRMNMCSAGVARKAAEEVTLQTGIKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYQEQAKGLLD 185
Cdd:TIGR02082 80 ADYDLEDLIYDLNFKGAKLARAVADEFTLTPEKPRFVAGSMGPTNKTATLSPDVERPGFRNVTYDELVDAYTEQAKGLLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 186 GGVDILLIETIFDTANAKAALFALQNLFEEKYAPRPIFISGTIVDKSGRTLSGQTGEGFVISVSHGEPLCIGLNCALGAA 265
Cdd:TIGR02082 160 GGVDLLLIETCFDTLNAKAALFAAETVFEEKGRELPIMISGTIVDTSGRTLSGQTIEAFLTSLEHAGIDMIGLNCALGPD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 266 EMRPFIEIIGKCTTAYVLCYPNAGLPNTFGDYDETPSMMAKHLKDFAMDGLVNIVGGCCGSTPDHIREIAEAVKNCKPRV 345
Cdd:TIGR02082 240 EMRPHLKHLSEHAEAYVSCHPNAGLPNAFGEYDLTPDELAKALADFAAEGGLNIVGGCCGTTPDHIRAIAEAVKNIKPRQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 346 PPAtaFEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALCVAKVQVEMGAQVLDVNMDDGMLDGP 425
Cdd:TIGR02082 320 RPV--LYEPSRLSGLEAITIAQDSNFVNIGERTNVAGSKKFRRLIIAEDYDEALDIAKQQVENGAQILDINVDYGMLDGV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 426 SAMTRFCNLIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEDDFLEKARKIKKYGAAMVVMAFDEEGQ 505
Cdd:TIGR02082 398 AAMKRFLNLLASEPDISTVPLMLDSSEWAVLEAGLKCIQGKCIVNSISLKDGEERFIETAKLIKEYGAAVVVMAFDEEGQ 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 506 ATETDTKIRVCTRAYHLLVKKLGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATKVIKETLPGARISGGLSNLSFSFR 585
Cdd:TIGR02082 478 ARTADRKIEICKRAYNILTEKVGFPPEDIIFDPNILTIATGIEEHRRYAINFIEAIRWIKEELPDAKISGGVSNVSFSFR 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 586 GMEAIREAMHGVFLYHAIKSGMDMGIVNAGNLPVYDDIHKELLQLCEDLIWNKDPEATEKLLRYAQT-QGTGGK--KVIQ 662
Cdd:TIGR02082 558 GNPAAREAMHSVFLYHAIRAGMDMGIVNAGKILPYDDIDPELRQVVEDLILNRRREATEPLLELAQLyEGTTTKssKEAQ 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 663 TDEWRNGPVEERLEYALVKGIEKHIIEDTEEARlnqKKYPRPLNIIEGPLMNGMKIVGDLFGAGKMFLPQVIKSARVMKK 742
Cdd:TIGR02082 638 QAEWRNLPVEERLEYALVKGEREGIEEDLEEAR---KKLTRPLEIIEGPLMDGMKVVGDLFGSGKMFLPQVVKSARVMKK 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 743 AVGHLIPFMEKEReetrvlngtveEEDPYQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDH 822
Cdd:TIGR02082 715 AVAYLEPHMEKEK-----------SEDSSKGKIVLATVKGDVHDIGKNIVGVVLSCNGYEVVDLGVMVPIEKILEAAKDH 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 823 KADIIGLSGLITPSLDEMIFVAKEMERLAIRIPLLIGGATTSKTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDENLK 902
Cdd:TIGR02082 784 NADVIGLSGLITPSLDEMKEVAEEMNRRGITIPLLIGGAATSKTHTAVKIAPIYKGPVVYVLDASRAVTVMDTLMSAKRK 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 903 DEYFEEIMEEYEDIRQDHYESLKERRYLPLSQARKSGFQMDWLSEPHPVKPTFIGTQVFEDYDLQKLVDYIDWKPFFDVW 982
Cdd:TIGR02082 864 DTENGRIKEEYDTAREKHGEQRSKRIAASEQAARKNVFAPDWSDDIEPPAPPFWGTQIVEASDIAELRPYIDWTPFFLQW 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 983 QLRGKYpnrgfPKIFNDKTVGGEARKVYDDAHNMLNTLISQKKLRARGVVGFWPAQSIQDDIHLYAEAAVpqAAEPIATF 1062
Cdd:TIGR02082 944 QLRGKY-----PKILGDEYEGLEAQKLFPDANEMLDKLSAENLLHARGVYGYFPAQSVGDDIEIYTDETV--ETHPIATV 1016
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 1063 YGLRQQAEKDSAStepYYCLSDFIAPLHSGIRDYLGLFAV-ACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEEL 1141
Cdd:TIGR02082 1017 RYLFHFPRQQSGR---YLCLADFIAPKASGIVDYIGAFAVtAGFGAEELADKLEAQHDDYDYIMVKAIADRLAEAFAEYL 1093
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 1142 HERVRRELWAYCGSEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLADIEQsTGIRLTESLAMAPASAVSGLYFS 1221
Cdd:TIGR02082 1094 HRRVRKELWGYAAEEPLSNEDLLKLRYQGIRPAPGYPACPDHTEKATMFELLEPER-IGVRLTESLAMHPEQSVSGLYFA 1172
|
....*....
gi 169790923 1222 NLKSKYFAV 1230
Cdd:TIGR02082 1173 HPEAKYFAV 1181
|
|
| MetH2 |
COG1410 |
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; ... |
37-1230 |
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: 1561.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 37 MGTMIQREKLNEEHFRGQEFKDHARPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYR 116
Cdd:COG1410 1 MGTMIQLLKLRELDADGAMFTDLQLDLKGNNDLLGLTGPNEILEIHRPELEAGADIIETNTGADAAITAADGAAEALLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 117 MNM-CSAGVARKAAEEVTLQTGIKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYQEQAKGLLDGGVDILLIET 195
Cdd:COG1410 81 YNGaAAALALEAAAAAAAAAAAAARAVAGAPGPTGGTASPGPDVPGLGFRNFDFDELVEAYAEAGLGLGGGGADLLLTET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 196 IFDTANAKAALFALQNLFEEKYAPRPIFISGTIVDKSGRTLSGQTGEGFVISVSHGEPLCIGLNCALGAAEMRPFIEIIG 275
Cdd:COG1410 161 IFDTLNAAAAAAAAAAAAEEEGVPIPVMVTGTITDGSGRTLSGQTAEAFLESLGHAAPGSNGLNCALGAEELRPYLEELS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 276 KCTTAYVLCYPNAGLPNTFGDYDETPSMMAKHLKDFAMDGLVNIVGGCCGSTPDHIREIAEAVKNCKPRVPPAtafEGHM 355
Cdd:COG1410 241 RIPPSAVSNAPNAGLPNGFGEYDETPEEMAAALAEFAEEGGVNIVGGCCGTTPEHIRAIAEAVAGLKPRPREK---PPPA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 356 LLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALCVAKVQVEMGAQVLDVNMDDGMLDGPSAMTRFCNLI 435
Cdd:COG1410 318 VLSGLEPVPIGQDSPFVNIGERTNVTGSKKFRELILEGDYDEALEVAREQVEAGAQILDVNVDEPGRDEVAAMVRFLNLL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 436 ASEpdiAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEDDFLEKARKIKKYGAAMVVMAFDEEGQATETDTKIRV 515
Cdd:COG1410 398 ASE---VRVPLMIDSSKPEVIEAGLKCYQGKPIVNSISLEEGEERFEEVAPLAKKYGAAVVVLAIDEEGQADTAERKLEI 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 516 CTRAYHLLVKKLGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATKVIKETLPGARISGGLSNLSFSFRGmeAIREAMH 595
Cdd:COG1410 475 AERIYDLAVEEYGFPPEDIIFDPLVFTVATGIEEHRNYAVETIEAIRLIKEELPGAKTSLGVSNVSFGLPG--NVREALN 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 596 GVFLYHAIKSGMDMGIVNAGNLPVYDDIHKELLQLCEDLIWNKDPEATEKLLRYAQTQgTGGKKVIQTDEWRNGPVEERL 675
Cdd:COG1410 553 SVFLYHAIKAGLDMAIVNPGQLEPYDDIPPELRELAEDVLLNRRPDALERLIELFEGV-KGAKAKKADLEWRELPVEERL 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 676 EYALVKGIEKHIIEDTEEARlnqKKYPRPLNIIEGPLMNGMKIVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEr 755
Cdd:COG1410 632 KHAIVKGIKEGIEEDTEEAL---AEGARPLEIINGPLMPGMNVVGDLFGAGKMFLPQVLKSAEVMKAAVAYLEPFMEKE- 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 756 eetrvlngtvEEEDPYQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGLITP 835
Cdd:COG1410 708 ----------KGESSSKGKIVLATVKGDVHDIGKNIVGVVLENNGYEVIDLGVMVPAEKILEAAKEHKADIIGLSGLMTT 777
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 836 SLDEMIFVAKEMERLAIRIPLLIGGATTSKTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDENLKDEYFEEIMEEYED 915
Cdd:COG1410 778 SLDEMKEVAEEMRRRGLDIPVLIGGAALTRAYTAVKIAPAYDGAVVYAKDASRAVRVADKLLSKERREAFVAEIKAEYEK 857
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 916 IRQDHYEslKERRYLPLSQARKsgfqmDWLSEPHPVKPTFIGTQVFEDYDLQKLVDYIDWKPFFDVWQLRGKYPNrgfpk 995
Cdd:COG1410 858 LRERHAA--RKKKLLSLEEARS-----NVDSDYPPPTPPFLGTRVLKDIPLAELVPYIDWTPFFQQWGLKGKYLD----- 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 996 ifndktvGGEARKVYDDAHNMLNTLISQKKLRARGVVGFWPAQSIQDDIHLYAeaavPQAAEPIATFYGLRQQaekdsas 1075
Cdd:COG1410 926 -------GEEARELFPDAQAMLDRIIEEKWLTARAVYGYFPANSEGDDIEVYD----DESSEELARFHFPRQQ------- 987
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 1076 TEPYYCLSDFIAPLHSGIRDYLGLFAV-ACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEELHERVRRElWAYCG 1154
Cdd:COG1410 988 RGPNLCLADFVAPKESGERDYVGFFAVtAGIGIEELAAELEAAGDDYDAIMLHALADRLAEAFAEYLHERVRKE-WGYAP 1066
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169790923 1155 SEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLADIEQsTGIRLTESLAMAPASAVSGLYFSNLKSKYFAV 1230
Cdd:COG1410 1067 DEALTNEDLIKEKYRGIRPAPGYPACPDHTEKRKLFDLLDAER-IGVTLTESFAMHPEASVSGIYFHHPEAKYFNV 1141
|
|
| MetH1 |
COG0646 |
Methionine synthase I (cobalamin-dependent), methyltransferase domain [Amino acid transport ... |
19-856 |
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: 893.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 19 RDEINAILQKRIMVLDGGMGTMIQREKLNEEHFRGqefkdharpLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTF 98
Cdd:COG0646 3 RAALLELLKERILILDGAMGTMLQAYGLTEGDFRG---------EKGCNELLNLTRPDVIREIHRAYLEAGADIIETNTF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 99 SSTSIAQADYGLEHLAYRMNMCSAGVARKAAEEVTlqtGIKRFVAGALGPTNKTLSvspsverpDYRNITFDELVEAYQE 178
Cdd:COG0646 74 GANRIKLADYGLEDRVYEINRAAARLAREAADEFS---DRPRFVAGSIGPTGKLLS--------PLGNITFDELVEAYRE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 179 QAKGLLDGGVDILLIETIFDTANAKAALFALQNLFEEKYAPRPIFISGTIvDKSGRTLSGQTGEGFVISVSHGEPLCIGL 258
Cdd:COG0646 143 QAEGLIEGGVDLLLIETIFDTLEAKAAIFAAREAFEELGRDLPVMVSGTF-DASGRTLSGQTPEAFATSLEHLGPDAIGL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 259 NCALGAAEMRPFIEIIGKCTTAYVLCYPNAGLPNTFGD---YDETPSMMAKHLKDFAMDGLVNIVGGCCGSTPDHIREIA 335
Cdd:COG0646 222 NCALGPDEMRPHVEELSEVADTPVSAYPNAGLPNLVGGrtvYDETPEEMAEYAEEFAEAGGVNIVGGCCGTTPEHIRAIA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 336 EAVKNCKPRVPPATafEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALCVAKVQVEMGAQVLDV 415
Cdd:COG0646 302 EAVKGLPPRKRPPP--PPALRLSGLEPLTITQDSLFVNVGERTNVTGSKKFARLILEGDYDAALAVARQQVEAGAQVIDV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 416 NMDDGMLDGPSAMTRFCNLIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEDDFLEKARKIKKYGAAM 495
Cdd:COG0646 380 NMDEGMLDGEAAMVEFLNLIASEPDIPRVPDMIDSSKWEVIEAGLKGVQGKGIVNSISLKEGEEKFLELAKLVRRYGAAV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 496 VVMAFDEEGQATETDTKIRVCTRAYHLLVKKLGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATKVIKETLPGARISG 575
Cdd:COG0646 460 VVMAFDEEGQADTAERKVEICARAYDLLTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKLNLPHALVSG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 576 GLSNLSFSFRGMEAIREAMHGVFLYHAIKSGMDMGIVNAGNLPVYDDIHKELLQLCEDLIWNKDPEATEKLLRYAQTQGT 655
Cdd:COG0646 540 GVSNVSFSFRGNNPVREAIHAVFLYHAIAAGMDMGIVNAGQLAIYEEIPEELLLLVEDVVLNRREDATERLLEIAEEVKG 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 656 GGKKVIQTDE-WRNGPVEERLEYALVKGIEKHIIEDTEEARLnqkkYPRPLNIIEGPLMNGMKIVGDLFGAGKMFLPQVI 734
Cdd:COG0646 620 AGKAAEEEAEeERREEEEERLLELLLVGGIEIDEEDDEEAAL----LLAALELIIIELLLGGGMVVGGLGGGGGKLLLVV 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 735 KSARVMKKAVGHLIPFMEKEREETRVLNGtveeedpyQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDK 814
Cdd:COG0646 696 VVKAVVKKKVAVALLKPEEEEKKKGGGKG--------GGVVVGVVVKVVVDDVDIIIVVVVVVVNNGIVVLVVVVIVVVA 767
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 169790923 815 ILKAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAIRIPL 856
Cdd:COG0646 768 LEAAAAAEAAVILLVGGLVLLLLEEEVLAAAEAAAEAAVLLL 809
|
|
| Met_synt_B12 |
pfam02965 |
Vitamin B12 dependent methionine synthase, activation domain; |
965-1246 |
7.89e-165 |
|
Vitamin B12 dependent methionine synthase, activation domain;
Pssm-ID: 460767 [Multi-domain] Cd Length: 273 Bit Score: 491.22 E-value: 7.89e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 965 DLQKLVDYIDWKPFFDVWQLRGKYPnrgfpKIFNDKTVGGEARKVYDDAHNMLNTLISQKKLRARGVVGFWPAQSIQDDI 1044
Cdd:pfam02965 1 DLAELVPYIDWTPFFQAWELKGKYP-----AILDDEVVGEEARKLFADAQAMLDRIIEEKWLTARGVVGFFPANSVGDDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 1045 HLYAEaavPQAAEPIATFYGLRQQAEKDSasTEPYYCLSDFIAPLHSGIRDYLGLFAVAC-FGVEELSKAYEDDGDDYSS 1123
Cdd:pfam02965 76 EVYTD---ESRTEVLATFHTLRQQTEKPE--GRPNLCLADFIAPKESGIADYIGAFAVTAgIGIEELAARFEAAHDDYSA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 1124 IMVKALGDRLAEAFAEELHERVRRELWAYCGSEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLADIEQSTGIRL 1203
Cdd:pfam02965 151 IMVKALADRLAEAFAEYLHERVRKELWGYAPDENLSNEDLIKEKYQGIRPAPGYPACPDHTEKFTLFDLLDAEENIGIRL 230
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 169790923 1204 TESLAMAPASAVSGLYFSNLKSKYFAVGKISKDQVEDYALRKN 1246
Cdd:pfam02965 231 TESFAMTPAASVSGLYFAHPESRYFAVGKIGKDQVEDYAKRKG 273
|
|
| MeTr |
cd00740 |
MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent ... |
371-627 |
1.60e-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: 421.42 E-value: 1.60e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 371 FVNIGERCNVAGSRKFAKLIMAGNYEEALCVAKVQVEMGAQVLDVNMDDGMLDGPSAMTRFCNLIASEPdiaKVPLCIDS 450
Cdd:cd00740 1 FLNIGERTNVTGSKKFRELIKAEDYDEALDVARQQVEGGAQILDLNVDYGGLDGVSAMKWLLNLLATEP---TVPLMLDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 451 SNFAVIEAGLKCCQGKCIVNSISLKEGEDDFLEKARKIKKYGAAMVVMAFDEEGQATETDTKIRVCTRAYHLLVKKLGFN 530
Cdd:cd00740 78 TNWEVIEAGLKCCQGKCVVNSINLEDGEERFLKVARLAKEHGAAVVVLAFDEQGQAKTRDKKVEIAERAYEALTEFVGFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 531 PNDIIFDPNILTIGTGMEEHNLYAINFIHATKVIKETLPGARISGGLSNLSFSFrgMEAIREAMHGVFLYHAIKSGMDMG 610
Cdd:cd00740 158 PEDIIFDPLILPIATGIEEHRPYALETIDAIRMIKERLPAVKISLGVSNVSFGF--NPAAREALNSVFLYEAIKAGLDMA 235
|
250
....*....|....*..
gi 169790923 611 IVNAGNLPVYDDIHKEL 627
Cdd:cd00740 236 IVNAGKLAPIEDIPEEL 252
|
|
| methionine_synthase_B12_BD |
cd02069 |
B12 binding domain of methionine synthase. This domain binds methylcobalamin, which it uses as ... |
671-897 |
6.96e-132 |
|
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: 402.41 E-value: 6.96e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 671 VEERLEYALVKGIEKHIIEDTEEARlnqKKYPRPLNIIEGPLMNGMKIVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPF 750
Cdd:cd02069 1 VEERLKHALVKGIRDGIEEDTEEAR---QQYARPLEIINGPLMDGMKVVGDLFGAGKMFLPQVLKSARVMKAAVAYLEPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 751 MEKEreetrvlngtvEEEDPYQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLS 830
Cdd:cd02069 78 MEKE-----------KGENSSKGKIVLATVKGDVHDIGKNLVGVILSNNGYEVIDLGVMVPIEKILEAAKEHKADIIGLS 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169790923 831 GLITPSLDEMIFVAKEMERLAIRIPLLIGGATTSKTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLL 897
Cdd:cd02069 147 GLLVPSLDEMVEVAEEMNRRGIKIPLLIGGAATSRKHTAVKIAPEYDGPVVYVKDASRALGVANKLL 213
|
|
| S-methyl_trans |
pfam02574 |
Homocysteine S-methyltransferase; This is a family of related homocysteine ... |
31-338 |
1.37e-100 |
|
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: 320.64 E-value: 1.37e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 31 MVLDGGMGTMIQReklneehfRGQEFKDHARplkgNNDILsiTQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQAD-YG 109
Cdd:pfam02574 1 LILDGGMGTELQR--------RGLDLTEPLW----SNELL--TRPEIIREIHRDYLEAGADIIETNTYQASPIKLAEgLE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 110 LEHLAYRMNMCSAGVARKAAEEVtlqtgikrFVAGALGPTNKTLSVSPSverpdyrnITFDELVEAYQEQAKGLLDGGVD 189
Cdd:pfam02574 67 EEEAVYELNRAAVRLAREAADEY--------FVAGSIGPYGATLSDGYG--------LSFDELVDFHREQLEALLDGGVD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 190 ILLIETIFDTANAKAALFALqnlfeEKYAPRPIFISGTIVDKsGRTLSGQTGEGFVISVSHG-EPLCIGLNCALgAAEMR 268
Cdd:pfam02574 131 LLLFETIPDLLEAKAALELL-----AEEPDLPVWISFTIEDG-TRLRSGTTLEAAVAALLHAtGPLAVGVNCAL-PEEML 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169790923 269 PFIEIIGKCTTAYVLCYPNAglpntFGD-YDETPSMMAKHLKDFAMDGlVNIVGGCCGSTPDHIREIAEAV 338
Cdd:pfam02574 204 PLLKELAKDAPTPVSVYPNS-----TGEvYDLTPEEWAEYAEGWLEAG-ANIIGGCCGTTPEHIRAIAEAL 268
|
|
| Pterin_bind |
pfam00809 |
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ... |
375-613 |
9.00e-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: 247.97 E-value: 9.00e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 375 GERCNVAGSRKFAKLIMaGNYEEALCVAKVQVEMGAQVLDVNMDDG-----MLDGPSAMTRFCNLIASEPDIAKVPLCID 449
Cdd:pfam00809 1 MGILNVTPDSFSDGGRF-LDLDKALAHARRMVEEGADIIDIGGESTrpgaeRVDGEEEMERVLPVLAALRDEADVPISVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 450 SSNFAVIEAGLKCcqGKCIVNSISlkeGEDDFLEKARKIKKYGAAMVVMAFD--------EEGQATETDTKIRVCTRAYH 521
Cdd:pfam00809 80 TTKAEVAEAALKA--GADIINDIS---GGDGDPEMAELAAEYGAAVVVMHMDgtpktmqeNEQQYEDVVEEVERFLRARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 522 LLVKKLGFNPNDIIFDPNILTigTGMEEHNLYAINFIHATKVIKetlpGARISGGLSNLSFSFRGME---AIREAMHGVF 598
Cdd:pfam00809 155 AAAEEAGVPPEDIILDPGIGF--GKTEEHNLELLRTLDELRVIL----GVPVLLGVSRKSFIGRGLPlggEERDAGTAAF 228
|
250
....*....|....*
gi 169790923 599 LYHAIKSGMDMGIVN 613
Cdd:pfam00809 229 LALAIAAGADIVRVH 243
|
|
| Pterin_binding |
cd00423 |
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and ... |
371-627 |
9.97e-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: 211.75 E-value: 9.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 371 FVNIGErCNVAGSRKFAkLIMAGNYEEALCVAKVQVEMGAQVLDVNMDDG--------MLDGPSAMTRFCNLIASEPDia 442
Cdd:cd00423 1 TLIMGI-LNVTPDSFSD-GGKFLSLDKALEHARRMVEEGADIIDIGGESTrpgaepvsVEEELERVIPVLRALAGEPD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 443 kVPLCIDSSNFAVIEAGLKCcqGKCIVNSISLKEGEDDFLEKARkikKYGAAMVVMAFDEEGQ--------ATETDTKIR 514
Cdd:cd00423 77 -VPISVDTFNAEVAEAALKA--GADIINDVSGGRGDPEMAPLAA---EYGAPVVLMHMDGTPQtmqnnpyyADVVDEVVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 515 VCTRAYHLLVkKLGFNPNDIIFDPNILTIGTgmEEHNLYAINFIHATKVIketlPGARISGGLSNLSFSFR---GMEAIR 591
Cdd:cd00423 151 FLEERVEAAT-EAGIPPEDIILDPGIGFGKT--EEHNLELLRRLDAFREL----PGLPLLLGVSRKSFLGDllsVGPKDR 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 169790923 592 EAMHGVFLYHAIKSGMDMGIVNAgNLPVYDDIHKEL 627
Cdd:cd00423 224 LAGTAAFLAAAILNGADIVRVHD-VKELRDAIKVAE 258
|
|
| PRK08645 |
PRK08645 |
bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; ... |
15-343 |
5.07e-61 |
|
bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; Reviewed
Pssm-ID: 236321 [Multi-domain] Cd Length: 612 Bit Score: 220.87 E-value: 5.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 15 KKTLRDEinaiLQKRIMVLDGGMGTMIqreklneeHFRGQefkdharPLKGNNDILSITQPDVIYQIHKEYLLAGADIIE 94
Cdd:PRK08645 1 MMKLLER----LKERVLIADGAMGTLL--------YSRGV-------PLDRCFEELNLSHPELILRIHREYIEAGADVIQ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 95 TNTFSSTSIAQADYGLEHLAYRMNMCSAGVARKAAEEvtlqtgiKRFVAGALGPTNKtlsvspsveRPDYRNITFDELVE 174
Cdd:PRK08645 62 TNTFGANRIKLKRYGLEDKVKEINRAAVRLAREAAGD-------DVYVAGTIGPIGG---------RGPLGDISLEEIRR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 175 AYQEQAKGLLDGGVDILLIETIFDTANAKAALFALQNLfeekyAPRPIFISGTiVDKSGRTLSGQTGEGFVISVSHGEPL 254
Cdd:PRK08645 126 EFREQIDALLEEGVDGLLLETFYDLEELLLALEAAREK-----TDLPIIAQVA-FHEDGVTQNGTSLEEALKELVAAGAD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 255 CIGLNCALGAAEMRPFIEIIGKCTTAYVLCYPNAGLPNTFGD---YDETPSMMAKHLKDFAMDGlVNIVGGCCGSTPDHI 331
Cdd:PRK08645 200 VVGLNCGLGPYHMLEALERIPIPENAPLSAYPNAGLPEYVDGryvYSANPEYFAEYALEFVEQG-VRLIGGCCGTTPEHI 278
|
330
....*....|..
gi 169790923 332 REIAEAVKNCKP 343
Cdd:PRK08645 279 RAMARALKGLKP 290
|
|
| MHT1 |
COG2040 |
Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) [Amino acid transport and ... |
26-340 |
3.24e-45 |
|
Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) [Amino acid transport and metabolism];
Pssm-ID: 441643 [Multi-domain] Cd Length: 301 Bit Score: 165.75 E-value: 3.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 26 LQKRIMVLDGGMGTmiqreklnEEHFRGQEFKDH---ARPLkgnndilsITQPDVIYQIHKEYLLAGADIIETNTFSST- 101
Cdd:COG2040 9 LMGRILLLDGGMGT--------ELERRGGDLLDPlwsAFAL--------LEAPELVRAVHRDYFAAGADVITTNSYQASp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 102 -SIAQADYGLEHLAyRMNMCSAGVARKAAEEVTlqTGIKRFVAGALGPTNktlsvspSVERPDYRnITFDELVEAYQEQA 180
Cdd:COG2040 73 dGLAELGYSAEEAE-RLNRRAVALAREARDEYT--PGPPVLVAGSVGPYG-------DEYRPDYG-LSAEEAEAYHRPRI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 181 KGLLDGGVDILLIETIFDTANAKAALFALQNlfeekyAPRPIFISGTiVDKSGRTLSGQT-GEGFVISVSHGEPLCIGLN 259
Cdd:COG2040 142 EALAEAGVDLLAAETIPSLAEAIAIARAAAE------AGKPVWISFT-VEDDGRLRSGEPlAEAIAAVDTDPGPAAVGVN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 260 CAlGAAEMRPFIEIIGKCTTAYVLCYPNAG------LPNTFGDYDETPSMMAKHLKDFAMDGLvNIVGGCCGSTPDHIRE 333
Cdd:COG2040 215 CS-HPEHFEAALEALAAWTGRPIGVYANAGemsdaeLKTWGGLDDGDPEELAEQAAEWVAAGA-RIIGGCCGTGPRHIAA 292
|
....*..
gi 169790923 334 IAEAVKN 340
Cdd:COG2040 293 IARALRA 299
|
|
| corrinoid_protein_B12-BD |
cd02070 |
B12 binding domain of corrinoid proteins. A family of small methanogenic corrinoid proteins ... |
678-892 |
2.96e-43 |
|
B12 binding domain of corrinoid proteins. A family of small methanogenic corrinoid proteins that bind methyl-Co(III) 5-hydroxybenzimidazolylcobamide as a cofactor. They play a role on the methanogenesis from trimethylamine, dimethylamine or monomethylamine, which is initiated by a series of corrinoid-dependent methyltransferases.
Pssm-ID: 239021 [Multi-domain] Cd Length: 201 Bit Score: 156.24 E-value: 2.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 678 ALVKGIEKHIIEDTEEARlnQKKYPrPLNIIEGPLMNGMKIVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREE 757
Cdd:cd02070 4 AIVDGDEEETVELVKKAL--EAGID-PQDIIEEGLAPGMDIVGDKYEEGEIFVPELLMAADAMKAGLDLLKPLLGKSKSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 758 TrvlngtveeedpyQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGLITPSL 837
Cdd:cd02070 81 K-------------KGKVVIGTVEGDIHDIGKNLVATMLEANGFEVIDLGRDVPPEEFVEAVKEHKPDILGLSALMTTTM 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 169790923 838 DEMIFVAKEMER--LAIRIPLLIGGATTSKTHtAVKIAPRYSAPvihvlDASKSVVV 892
Cdd:cd02070 148 GGMKEVIEALKEagLRDKVKVMVGGAPVNQEF-ADEIGADGYAE-----DAAEAVAI 198
|
|
| MtbC1 |
COG5012 |
Methanogenic corrinoid protein MtbC1 [Energy production and conversion]; |
673-861 |
1.71e-42 |
|
Methanogenic corrinoid protein MtbC1 [Energy production and conversion];
Pssm-ID: 444036 [Multi-domain] Cd Length: 219 Bit Score: 155.05 E-value: 1.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 673 ERLEYALVKGIEKHIIEDTEEARLNQKKyprPLNIIEGPLMNGMKIVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFME 752
Cdd:COG5012 12 ESLADAVLEGDEDEALELVAEALAAGMD---PEEIILDGLAPGMREVGELWEEGEIFVPEEHLAAAAMKAGLEILKPLLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 753 KEREetrvlngtveeedpYQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGL 832
Cdd:COG5012 89 EEGG--------------RKGKVVIGTVEGDLHDIGKNIVADMLRAAGFEVIDLGADVPPEEFVEAAKEEKPDIVGLSAL 154
|
170 180 190
....*....|....*....|....*....|.
gi 169790923 833 ITPSLDEMIFVAKEMERLAIR--IPLLIGGA 861
Cdd:COG5012 155 LTTTMPAMKELIEALREAGLRdkVKVIVGGA 185
|
|
| B12-binding |
cd02067 |
B12 binding domain (B12-BD). This domain binds different cobalamid derivates, like B12 ... |
774-892 |
4.21e-41 |
|
B12 binding domain (B12-BD). This domain binds different cobalamid derivates, like B12 (adenosylcobamide) or methylcobalamin or methyl-Co(III) 5-hydroxybenzimidazolylcobamide, it is found in several enzymes, such as glutamate mutase, methionine synthase and methylmalonyl-CoA mutase. Cobalamin undergoes a conformational change on binding the protein; the dimethylbenzimidazole group, which is coordinated to the cobalt in the free cofactor, moves away from the corrin and is replaced by a histidine contributed by the protein. The sequence Asp-X-His-X-X-Gly, which contains this histidine ligand, is conserved in many cobalamin-binding proteins.
Pssm-ID: 239018 [Multi-domain] Cd Length: 119 Bit Score: 146.88 E-value: 4.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 774 TIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAI- 852
Cdd:cd02067 1 KVVIATVGGDGHDIGKNIVARALRDAGFEVIDLGVDVPPEEIVEAAKEEDADAIGLSGLLTTHMTLMKEVIEELKEAGLd 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 169790923 853 RIPLLIGGATTSKTHtavkIAPRYSAPVIHVLDASKSVVV 892
Cdd:cd02067 81 DIPVLVGGAIVTRDF----KFLKEIGVDAYFGPATEAVEV 116
|
|
| PRK07534 |
PRK07534 |
betaine--homocysteine S-methyltransferase; |
68-370 |
4.88e-38 |
|
betaine--homocysteine S-methyltransferase;
Pssm-ID: 236045 [Multi-domain] Cd Length: 336 Bit Score: 146.05 E-value: 4.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 68 DILSITQPDVIYQIHKEYLLAGADIIETNTFSSTS----IAQADYGLEHLayrmNMCSAGVARKAAEEvtlqTGIKRFVA 143
Cdd:PRK07534 37 ELWNEDHPDNITALHQGFVDAGSDIILTNSFGGTAarlkLHDAQDRVHEL----NRAAAEIAREVADK----AGRKVIVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 144 GALGPTNKTLSVSPSverpdyrnITFDELVEAYQEQAKGLLDGGVDILLIETIFDTANAKAALFALqnlfeeKYAPRPIF 223
Cdd:PRK07534 109 GSVGPTGEIMEPMGA--------LTHALAVEAFHEQAEGLKAGGADVLWVETISAPEEIRAAAEAA------KLAGMPWC 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 224 ISGTIvDKSGRTLSGQTGEGF---VISVSHGePLCIGLNCALGAAE-MRPFIEIIGKCTTAYVLCYPNAGLPNTFGD--- 296
Cdd:PRK07534 175 GTMSF-DTAGRTMMGLTPADLadlVEKLGEP-PLAFGANCGVGASDlLRTVLGFTAQGPERPIIAKGNAGIPKYVDGhih 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169790923 297 YDETPSMMAKHLKdFAMDGLVNIVGGCCGSTPDHIREIAEAVKNcKPRVPPATafeghmllsgLEPF--RIGPYTN 370
Cdd:PRK07534 253 YDGTPELMAEYAV-LARDAGARIIGGCCGTMPEHLAAMRAALDA-RPRGPRPS----------LETIveRLGPFSS 316
|
|
| PRK07535 |
PRK07535 |
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase; Validated |
374-616 |
4.18e-36 |
|
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase; Validated
Pssm-ID: 181022 [Multi-domain] Cd Length: 261 Bit Score: 138.06 E-value: 4.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 374 IGERCNvaGSRK-FAKLIMAGNYEEALCVAKVQVEMGAQVLDVNMDDGMLDGPSAMTRFCNLIAsepDIAKVPLCIDSSN 452
Cdd:PRK07535 4 IGERIN--GTRKsIAEAIEAKDAAFIQKLALKQAEAGADYLDVNAGTAVEEEPETMEWLVETVQ---EVVDVPLCIDSPN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 453 FAVIEAGLKCCQGKCIVNSISlkeGEDDFLEKARK-IKKYGAAMVVMAFDEEGQATETDTKIRVCTRayhlLVKKL---G 528
Cdd:PRK07535 79 PAAIEAGLKVAKGPPLINSVS---AEGEKLEVVLPlVKKYNAPVVALTMDDTGIPKDAEDRLAVAKE----LVEKAdeyG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 529 FNPNDIIFDPNILTIGTgMEEHnlyAINFIHATKVIKETLPGARISGGLSNLSFsfrGMEAiREAMHGVFLYHAIKSGMD 608
Cdd:PRK07535 152 IPPEDIYIDPLVLPLSA-AQDA---GPEVLETIRRIKELYPKVHTTCGLSNISF---GLPN-RKLINRAFLVMAMGAGMD 223
|
....*...
gi 169790923 609 MGIVNAGN 616
Cdd:PRK07535 224 SAILDPLD 231
|
|
| B12-binding_2 |
smart01018 |
B12 binding domain; Cobalamin-dependent methionine synthase is a large modular protein that ... |
670-755 |
1.73e-34 |
|
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: 126.82 E-value: 1.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 670 PVEERLEYALVKGIEKHIIEDTEEARlnqKKYPRPLNIIEGPLMNGMKIVGDLFGAGKMFLPQVIKSARVMKKAVGHLIP 749
Cdd:smart01018 2 PLLERLAEAIVDGDEEGVEELVEEAL---AEGVDPLEIINEGLIPGMNVVGDLFEAGEYFLPQVLMSAEAMKAAVAILKP 78
|
....*.
gi 169790923 750 FMEKER 755
Cdd:smart01018 79 LLEKEK 84
|
|
| mmuM |
PRK09485 |
homocysteine methyltransferase; Provisional |
23-340 |
6.38e-34 |
|
homocysteine methyltransferase; Provisional
Pssm-ID: 181899 [Multi-domain] Cd Length: 304 Bit Score: 133.06 E-value: 6.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 23 NAILQKRIMVLDGGMGTMIQReklneehfRGQEFKD---HARPLkgnndilsITQPDVIYQIHKEYLLAGADIIETNTFS 99
Cdd:PRK09485 6 ELLAQGPVLILDGALATELEA--------RGCDLNDslwSAKVL--------LENPELIYQVHLDYFRAGADCAITASYQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 100 STSIAQADYGL-EHLAYRMNMCSAGVARKAAEEVtLQTgiKRFVAGALGPTNKTLSvSPSVERPDYrNITFDELVEAYQE 178
Cdd:PRK09485 70 ATFQGFAARGLsEAEAEELIRRSVELAKEARDEF-WAE--KPLVAGSVGPYGAYLA-DGSEYRGDY-GLSEEELQDFHRP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 179 QAKGLLDGGVDILLIETIFDTANAKAALFALQNLFEEKYAprpiFISGTIVDksGRTLSGQT--GEGFVISVSHGEPLCI 256
Cdd:PRK09485 145 RIEALAEAGADLLACETIPNLDEAEALVELLKEEFPGVPA----WLSFTLRD--GTHISDGTplAEAAALLAASPQVVAV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 257 GLNCAlGAAEMRPFIEIIGKCTTAYVLCYPNAGlpntfGDYD---------ETPSMMAKHLKDFAMDGlVNIVGGCCGST 327
Cdd:PRK09485 219 GVNCT-APELVTAAIAALRAVTDKPLVVYPNSG-----EVYDavtktwhgpADDASLGELAPEWYAAG-ARLIGGCCRTT 291
|
330
....*....|...
gi 169790923 328 PDHIREIAEAVKN 340
Cdd:PRK09485 292 PEDIAALAAALKT 304
|
|
| B12-binding_like |
cd02065 |
B12 binding domain (B12-BD). Most of the members bind different cobalamid derivates, like B12 ... |
774-887 |
9.35e-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: 126.35 E-value: 9.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 774 TIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAIR 853
Cdd:cd02065 1 KVLGATVGGDVHDIGKNIVAIALRDNGFEVIDLGVDVPPEEIVEAAKEEDADVVGLSALSTTHMEAMKLVIEALKELGID 80
|
90 100 110
....*....|....*....|....*....|....
gi 169790923 854 IPLLIGGATTSKTHTAVKIAPRYSAPVIHVLDAS 887
Cdd:cd02065 81 IPVVVGGAHPTADPEEPKVDAVVIGEGEYAGPAL 114
|
|
| pyl_corrinoid |
TIGR02370 |
methyltransferase cognate corrinoid proteins, Methanosarcina family; This model describes a ... |
678-865 |
2.39e-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: 122.22 E-value: 2.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 678 ALVKGIEKHIIEDTEEARLNQKKyprPLNIIEGPLMNGMKIVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKeREE 757
Cdd:TIGR02370 5 AIFEGEEDDVVEGAQKALDAGID---PIELIEKGLMAGMGVVGKLFEDGELFLPHVMMSADAMLAGIKVLTPEMEK-AVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 758 TRVLngtveeedpyqGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGLITPSL 837
Cdd:TIGR02370 81 TEVL-----------GKVVCGVAEGDVHDIGKNIVVTMLRANGFDVIDLGRDVPIDTVVEKVKKEKPLMLTGSALMTTTM 149
|
170 180 190
....*....|....*....|....*....|.
gi 169790923 838 ---DEMIFVAKEmERLAIRIPLLIGGATTSK 865
Cdd:TIGR02370 150 ygqKDINDKLKE-EGYRDSVKFMVGGAPVTQ 179
|
|
| B12-binding |
pfam02310 |
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ... |
773-861 |
6.10e-22 |
|
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several enzymes, such as glutamate mutase, methionine synthase and methylmalonyl-CoA mutase. It contains a conserved DxHxxGx(41)SxVx(26)GG motif, which is important for B12 binding.
Pssm-ID: 426713 [Multi-domain] Cd Length: 121 Bit Score: 92.39 E-value: 6.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 773 GTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAI 852
Cdd:pfam02310 1 GKVVVATVGGDLHPLGLNYVAAALRAAGFEVIILGANVPPEDIVAAARDEKPDVVGLSALMTTTLPGAKELIRLLKGIRP 80
|
....*....
gi 169790923 853 RIPLLIGGA 861
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 ... |
675-747 |
1.11e-19 |
|
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: 84.06 E-value: 1.11e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169790923 675 LEYALVKGIEKHIIEDTEEARLNqkkypRPLNIIEGPLMNGMKIVGDLFGAGKMFLPQVIKSARVMKKAVGHL 747
Cdd:pfam02607 1 LLEALLEGDEEAAEELLEEALEI-----DPEEIIEDLLIPGMDEVGELWEAGEIFVPQEHLAAEAMKAALAVL 68
|
|
| PLN02489 |
PLN02489 |
homocysteine S-methyltransferase |
32-340 |
2.14e-15 |
|
homocysteine S-methyltransferase
Pssm-ID: 215269 Cd Length: 335 Bit Score: 78.90 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 32 VLDGGMGTMIQReklneehfRGQEFKDharPLKgnNDILSITQPDVIYQIHKEYLLAGADIIETNTFSST---------S 102
Cdd:PLN02489 24 VIDGGFATELER--------HGADLND---PLW--SAKCLITSPHLIRKVHLDYLEAGADIIITASYQATiqgfesrglS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 103 IAQADYGLE---HLAY--RMNMCSAGVARKAAEEVTLQTGIKRFVAGALGPTNKTLSvSPSVERPDY-RNITFDELVEAY 176
Cdd:PLN02489 91 REESETLLRksvEIACeaRDIFWDKCQKGSTSRPGRELSYRPILVAASIGSYGAYLA-DGSEYSGDYgPSVTLEKLKDFH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 177 QEQAKGLLDGGVDILLIETIFDTANAKAalfaLQNLFEEKYAPRPIFISGTIVDKsgrtlsgqtgegfvISVSHGEPL-- 254
Cdd:PLN02489 170 RRRLQVLAEAGPDLIAFETIPNKLEAQA----YVELLEEENIKIPAWISFNSKDG--------------VNVVSGDSLle 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 255 CI------------GLNCAlgaaemrP--FIE----IIGKCTTAYVLCYPNAG----------LPNT-FGDYDetpsmMA 305
Cdd:PLN02489 232 CAsiadsckkvvavGINCT-------PprFIHglilSIRKVTSKPIVVYPNSGetydgeakewVESTgVSDED-----FV 299
|
330 340 350
....*....|....*....|....*....|....*
gi 169790923 306 KHLKDFAMDGlVNIVGGCCGSTPDHIREIAEAVKN 340
Cdd:PLN02489 300 SYVNKWRDAG-ASLIGGCCRTTPNTIRAISKALSE 333
|
|
| Sbm |
COG2185 |
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ... |
774-860 |
2.14e-09 |
|
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and metabolism];
Pssm-ID: 441788 [Multi-domain] Cd Length: 134 Bit Score: 57.07 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 774 TIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSglitpSLDE--MIFVAKEMERL- 850
Cdd:COG2185 12 RVLLAKPGLDGHDRGAKVIARALRDAGFEVIYLGLFQTPEEIVRAAIEEDADVIGVS-----SLDGghLELVPELIELLk 86
|
90
....*....|...
gi 169790923 851 ---AIRIPLLIGG 860
Cdd:COG2185 87 eagAGDILVVVGG 99
|
|
| PRK02261 |
PRK02261 |
methylaspartate mutase subunit S; Provisional |
774-832 |
1.44e-08 |
|
methylaspartate mutase subunit S; Provisional
Pssm-ID: 179400 [Multi-domain] Cd Length: 137 Bit Score: 54.57 E-value: 1.44e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 169790923 774 TIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGL 832
Cdd:PRK02261 5 TVVLGVIGADCHAVGNKILDRALTEAGFEVINLGVMTSQEEFIDAAIETDADAILVSSL 63
|
|
| Glm_B12_BD |
cd02072 |
B12 binding domain of glutamate mutase (Glm). Glutamate mutase catalysis the conversion of (S) ... |
774-832 |
1.06e-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: 52.08 E-value: 1.06e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 169790923 774 TIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGL 832
Cdd:cd02072 1 TIVLGVIGSDCHAVGNKILDHAFTEAGFNVVNLGVLSPQEEFIDAAIETDADAILVSSL 59
|
|
| MM_CoA_mut_B12_BD |
cd02071 |
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), ... |
775-860 |
5.22e-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: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790923 775 IVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVM-TPcDKILKAALDHKADIIGLSGLitpSLDEMIFVAKEMERLAIR 853
Cdd:cd02071 2 ILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRqTP-EEIVEAAIQEDVDVIGLSSL---SGGHMTLFPEVIELLREL 77
|
90
....*....|.
gi 169790923 854 ----IPLLIGG 860
Cdd:cd02071 78 gagdILVVGGG 88
|
|
| |
