|
Name |
Accession |
Description |
Interval |
E-value |
| metH |
PRK09490 |
B12-dependent methionine synthase; Provisional |
1-1223 |
0e+00 |
|
B12-dependent methionine synthase; Provisional
Pssm-ID: 236539 [Multi-domain] Cd Length: 1229 Bit Score: 2694.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 1 MSNKVEQLHQQLRERILVLDGGMGTMIQGYRLSEQDFRGERFADWPCDLKGNNDLLVLSKPEVIREIHDAYFAAGADIIE 80
Cdd:PRK09490 4 MSSRLAQLRALLAERILVLDGAMGTMIQRYKLEEADYRGERFADWPCDLKGNNDLLVLTQPDVIEAIHRAYLEAGADIIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 81 TNTFNSTTIAMADYQMESLSAEINFAAAKLARASADAWTARTPEKPRYVAGVLGPTNRTASISPDVNDPAFRNITFDQLV 160
Cdd:PRK09490 84 TNTFNATTIAQADYGMESLVYELNFAAARLAREAADEWTAKTPDKPRFVAGVLGPTNRTASISPDVNDPGFRNVTFDELV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 161 AAYRESTKALVEGGSDLILIETVFDTLNAKAAIFAVKEEFEALGVELPIMISGTITDASGRTLSGQTTEAFYNSLRHADA 240
Cdd:PRK09490 164 AAYREQTRGLIEGGADLILIETIFDTLNAKAAIFAVEEVFEELGVRLPVMISGTITDASGRTLSGQTTEAFWNSLRHAKP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 241 LTFGLNCALGPDELRQYVQELSRIAECYVTAHPNAGLPNAFGEYDLDADTMAAQIREWAQAGFLNIVGGCCGTTPEHIAA 320
Cdd:PRK09490 244 LSIGLNCALGADELRPYVEELSRIADTYVSAHPNAGLPNAFGEYDETPEEMAAQIGEFAESGFLNIVGGCCGTTPEHIAA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 321 MSRAVEGLPPRQLPELPVACRLSGLEPLNIGDDSLFVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVESGAQIIDI 400
Cdd:PRK09490 324 IAEAVAGLPPRKLPEIPVACRLSGLEPLNIDDDSLFVNVGERTNVTGSAKFARLIKEEDYDEALDVARQQVENGAQIIDI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 401 NMDEGMLDAEAAMVRFLNLIAGEPDIARVPIMIDSSKWEVIEKGLKCIQGKGIVNSISMKEGVEPFIHHAKLVRRYGAAM 480
Cdd:PRK09490 404 NMDEGMLDSEAAMVRFLNLIASEPDIARVPIMIDSSKWEVIEAGLKCIQGKGIVNSISLKEGEEKFIEHARLVRRYGAAV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 481 VVMAFDEVGQADTRERKIEICRRAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISG 560
Cdd:PRK09490 484 VVMAFDEQGQADTRERKIEICKRAYDILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKQNLPHAKISG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 561 GVSNVSFSFRGNDPVREAIHAVFLYYAIRNGMDMGIVNAGQLAIYDDLPGELRDAVEDVILNRRDDSTERLLELAEKYRG 640
Cdd:PRK09490 564 GVSNVSFSFRGNNPVREAIHAVFLYHAIKAGMDMGIVNAGQLAIYDDIPPELREAVEDVVLNRRPDATERLLEIAEKYRG 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 641 sKADDSANAQQAEWRSWDVKKRLEYSLVKGITEFIEQDTEEARQQAERPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVK 720
Cdd:PRK09490 644 -KGGKKAKAEDLEWRSWPVEKRLEHALVKGITEFIEEDTEEARQQAARPLEVIEGPLMDGMNVVGDLFGEGKMFLPQVVK 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 721 SARVMKQAVAYLEPYIEASKEQG---SSNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPAEKILRTAREEN 797
Cdd:PRK09490 723 SARVMKQAVAYLEPFIEAKKEGGtdrKSNGKILMATVKGDVHDIGKNIVGVVLQCNNYEVIDLGVMVPAEKILETAKEEN 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 798 ADLIGLSGLITPSLDEMVNVAKEMERQGFTIPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVSALLSATQRD 877
Cdd:PRK09490 803 ADIIGLSGLITPSLDEMVHVAKEMERQGFTIPLLIGGATTSKAHTAVKIAPNYSGPVVYVTDASRAVGVVSSLLSDEQRD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 878 DFVARTRKEYETVRIQHGRKKPRTPPVTLQAARENDLAFDWESYTPPVAHRLGVQEVEA-SIETLRNYIDWTPFFMTWSL 956
Cdd:PRK09490 883 AYVAETRAEYEKVREQHARKKPRKPLLTLEAARANRFKIDWEAYTPPKPKFLGVQVFEDyDLAELREYIDWTPFFQTWEL 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 957 AGKYPRILEDEVVGEEAQRLFKDANDLLDKLSAEKTLNPRGVVGLFPANRVGDDVEIYRDEIRTHVLTVSHHLRQQTEKV 1036
Cdd:PRK09490 963 AGKYPAILEDEVVGEEARKLFADAQAMLDKIIAEKWLTARGVIGLFPANSVGDDIEVYTDESRTEVLATLHHLRQQTEKR 1042
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 1037 GFANYCLADFVAPKLSGKADYIGAFAVTGGLEEDALAEAYEAQHDDYNKIMVKAIADRLAEAFAEYLHEKVRKVYWGYAA 1116
Cdd:PRK09490 1043 GRPNYCLADFVAPKESGKADYIGAFAVTAGLGEDELADRFEAAHDDYNAIMVKALADRLAEAFAEYLHERVRKEFWGYAP 1122
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 1117 NENLSNEELIRENYQGIRPAPGYPACPEHTEKATIWELLDVEAHTGMKLTESFAMWPGASVSGWYFSHPDSKYFAVAQIQ 1196
Cdd:PRK09490 1123 DENLSNEELIREKYQGIRPAPGYPACPDHTEKATLFDLLDAEKNTGMKLTESYAMWPGASVSGWYFSHPESKYFAVGKIG 1202
|
1210 1220
....*....|....*....|....*..
gi 578218282 1197 RDQVEDYALRKGMTAAEVERWLAPNLG 1223
Cdd:PRK09490 1203 RDQVEDYAARKGMSVEEVERWLAPNLG 1229
|
|
| metH |
TIGR02082 |
5-methyltetrahydrofolate--homocysteine methyltransferase; This family represents ... |
12-1192 |
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: 2028.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 12 LRERILVLDGGMGTMIQGYRLSEQDFRGErFADWPCDLKGNNDLLVLSKPEVIREIHDAYFAAGADIIETNTFNSTTIAM 91
Cdd:TIGR02082 1 LNQRILVLDGAMGTQLQSANLTEADFRGA-FADCHRELKGNNDILNLTKPEVIATIHRAYFEAGADIIETNTFNSTTISQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 92 ADYQMESLSAEINFAAAKLARASADAWTaRTPEKPRYVAGVLGPTNRTASISPDVNDPAFRNITFDQLVAAYRESTKALV 171
Cdd:TIGR02082 80 ADYDLEDLIYDLNFKGAKLARAVADEFT-LTPEKPRFVAGSMGPTNKTATLSPDVERPGFRNVTYDELVDAYTEQAKGLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 172 EGGSDLILIETVFDTLNAKAAIFAVKEEFEALGVELPIMISGTITDASGRTLSGQTTEAFYNSLRHADALTFGLNCALGP 251
Cdd:TIGR02082 159 DGGVDLLLIETCFDTLNAKAALFAAETVFEEKGRELPIMISGTIVDTSGRTLSGQTIEAFLTSLEHAGIDMIGLNCALGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 252 DELRQYVQELSRIAECYVTAHPNAGLPNAFGEYDLDADTMAAQIREWAQAGFLNIVGGCCGTTPEHIAAMSRAVEGLPPR 331
Cdd:TIGR02082 239 DEMRPHLKHLSEHAEAYVSCHPNAGLPNAFGEYDLTPDELAKALADFAAEGGLNIVGGCCGTTPDHIRAIAEAVKNIKPR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 332 QLPELPVACRLSGLEPLNIGDDSLFVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVESGAQIIDINMDEGMLDAEA 411
Cdd:TIGR02082 319 QRPVLYEPSRLSGLEAITIAQDSNFVNIGERTNVAGSKKFRRLIIAEDYDEALDIAKQQVENGAQILDINVDYGMLDGVA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 412 AMVRFLNLIAGEPDIARVPIMIDSSKWEVIEKGLKCIQGKGIVNSISMKEGVEPFIHHAKLVRRYGAAMVVMAFDEVGQA 491
Cdd:TIGR02082 399 AMKRFLNLLASEPDISTVPLMLDSSEWAVLEAGLKCIQGKCIVNSISLKDGEERFIETAKLIKEYGAAVVVMAFDEEGQA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 492 DTRERKIEICRRAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISGGVSNVSFSFRG 571
Cdd:TIGR02082 479 RTADRKIEICKRAYNILTEKVGFPPEDIIFDPNILTIATGIEEHRRYAINFIEAIRWIKEELPDAKISGGVSNVSFSFRG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 572 NDPVREAIHAVFLYYAIRNGMDMGIVNAGQLAIYDDLPGELRDAVEDVILNRRDDSTERLLELAEKYRGSKADDSANAQQ 651
Cdd:TIGR02082 559 NPAAREAMHSVFLYHAIRAGMDMGIVNAGKILPYDDIDPELRQVVEDLILNRRREATEPLLELAQLYEGTTTKSSKEAQQ 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 652 AEWRSWDVKKRLEYSLVKGITEFIEQDTEEARQQAERPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAY 731
Cdd:TIGR02082 639 AEWRNLPVEERLEYALVKGEREGIEEDLEEARKKLTRPLEIIEGPLMDGMKVVGDLFGSGKMFLPQVVKSARVMKKAVAY 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 732 LEPYIEASKEQGSSNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPAEKILRTAREENADLIGLSGLITPSL 811
Cdd:TIGR02082 719 LEPHMEKEKSEDSSKGKIVLATVKGDVHDIGKNIVGVVLSCNGYEVVDLGVMVPIEKILEAAKDHNADVIGLSGLITPSL 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 812 DEMVNVAKEMERQGFTIPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVSALLSATQRDDFVARTRKEYETVR 891
Cdd:TIGR02082 799 DEMKEVAEEMNRRGITIPLLIGGAATSKTHTAVKIAPIYKGPVVYVLDASRAVTVMDTLMSAKRKDTENGRIKEEYDTAR 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 892 IQHGRKKPRTPPVTLQAARENDLAFDW-ESYTPPVAHRLGVQEVEAS-IETLRNYIDWTPFFMTWSLAGKYPRILEDEVV 969
Cdd:TIGR02082 879 EKHGEQRSKRIAASEQAARKNVFAPDWsDDIEPPAPPFWGTQIVEASdIAELRPYIDWTPFFLQWQLRGKYPKILGDEYE 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 970 GEEAQRLFKDANDLLDKLSAEKTLNPRGVVGLFPANRVGDDVEIYRDEIR-THVLTVS----HHLRQQTEKvgfaNYCLA 1044
Cdd:TIGR02082 959 GLEAQKLFPDANEMLDKLSAENLLHARGVYGYFPAQSVGDDIEIYTDETVeTHPIATVrylfHFPRQQSGR----YLCLA 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 1045 DFVAPKLSGKADYIGAFAVTGGLEEDALAEAYEAQHDDYNKIMVKAIADRLAEAFAEYLHEKVRKVYWGYAANENLSNEE 1124
Cdd:TIGR02082 1035 DFIAPKASGIVDYIGAFAVTAGFGAEELADKLEAQHDDYDYIMVKAIADRLAEAFAEYLHRRVRKELWGYAAEEPLSNED 1114
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578218282 1125 LIRENYQGIRPAPGYPACPEHTEKATIWELLDVEaHTGMKLTESFAMWPGASVSGWYFSHPDSKYFAV 1192
Cdd:TIGR02082 1115 LLKLRYQGIRPAPGYPACPDHTEKATMFELLEPE-RIGVRLTESLAMHPEQSVSGLYFAHPEAKYFAV 1181
|
|
| MetH2 |
COG1410 |
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; ... |
23-1192 |
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: 1772.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 23 MGTMIQGYRLSEQDFRGERFADWPCDLKGNNDLLVLSKPEVIREIHDAYFAAGADIIETNTFNSTTIAMADYQMESLSAE 102
Cdd:COG1410 1 MGTMIQLLKLRELDADGAMFTDLQLDLKGNNDLLGLTGPNEILEIHRPELEAGADIIETNTGADAAITAADGAAEALLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 103 INFAAAKLARASADAWTARTPEKPRYVAGVLGPTNRTASISPDVNDPAFRNITFDQLVAAYRESTKALVEGGSDLILIET 182
Cdd:COG1410 81 YNGAAAALALEAAAAAAAAAAAAARAVAGAPGPTGGTASPGPDVPGLGFRNFDFDELVEAYAEAGLGLGGGGADLLLTET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 183 VFDTLNAKAAIFAVKEEFEALGVELPIMISGTITDASGRTLSGQTTEAFYNSLRHADALTFGLNCALGPDELRQYVQELS 262
Cdd:COG1410 161 IFDTLNAAAAAAAAAAAAEEEGVPIPVMVTGTITDGSGRTLSGQTAEAFLESLGHAAPGSNGLNCALGAEELRPYLEELS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 263 RIAECYVTAHPNAGLPNAFGEYDLDADTMAAQIREWAQAGFLNIVGGCCGTTPEHIAAMSRAVEGLPPRQlPELPVACRL 342
Cdd:COG1410 241 RIPPSAVSNAPNAGLPNGFGEYDETPEEMAAALAEFAEEGGVNIVGGCCGTTPEHIRAIAEAVAGLKPRP-REKPPPAVL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 343 SGLEPLNIGDDSLFVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVESGAQIIDINMDEGMLDAEAAMVRFLNLIAG 422
Cdd:COG1410 320 SGLEPVPIGQDSPFVNIGERTNVTGSKKFRELILEGDYDEALEVAREQVEAGAQILDVNVDEPGRDEVAAMVRFLNLLAS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 423 EpdiARVPIMIDSSKWEVIEKGLKCIQGKGIVNSISMKEGVEPFIHHAKLVRRYGAAMVVMAFDEVGQADTRERKIEICR 502
Cdd:COG1410 400 E---VRVPLMIDSSKPEVIEAGLKCYQGKPIVNSISLEEGEERFEEVAPLAKKYGAAVVVLAIDEEGQADTAERKLEIAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 503 RAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISGGVSNVSFSFRGNdpVREAIHAV 582
Cdd:COG1410 477 RIYDLAVEEYGFPPEDIIFDPLVFTVATGIEEHRNYAVETIEAIRLIKEELPGAKTSLGVSNVSFGLPGN--VREALNSV 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 583 FLYYAIRNGMDMGIVNAGQLAIYDDLPGELRDAVEDVILNRRDDSTERLLELAEKYRGSKADdsanAQQAEWRSWDVKKR 662
Cdd:COG1410 555 FLYHAIKAGLDMAIVNPGQLEPYDDIPPELRELAEDVLLNRRPDALERLIELFEGVKGAKAK----KADLEWRELPVEER 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 663 LEYSLVKGITEFIEQDTEEARQQAERPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPYIEASKEQ 742
Cdd:COG1410 631 LKHAIVKGIKEGIEEDTEEALAEGARPLEIINGPLMPGMNVVGDLFGAGKMFLPQVLKSAEVMKAAVAYLEPFMEKEKGE 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 743 GSSNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPAEKILRTAREENADLIGLSGLITPSLDEMVNVAKEME 822
Cdd:COG1410 711 SSSKGKIVLATVKGDVHDIGKNIVGVVLENNGYEVIDLGVMVPAEKILEAAKEHKADIIGLSGLMTTSLDEMKEVAEEMR 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 823 RQGFTIPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVSALLSATQRDDFVARTRKEYETVRIQHGRKKprTP 902
Cdd:COG1410 791 RRGLDIPVLIGGAALTRAYTAVKIAPAYDGAVVYAKDASRAVRVADKLLSKERREAFVAEIKAEYEKLRERHAARK--KK 868
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 903 PVTLQAARENDLAfdweSYTPPVAHRLGVQEVEA-SIETLRNYIDWTPFFMTWSLAGKYpriLEdevvGEEAQRLFKDAN 981
Cdd:COG1410 869 LLSLEEARSNVDS----DYPPPTPPFLGTRVLKDiPLAELVPYIDWTPFFQQWGLKGKY---LD----GEEARELFPDAQ 937
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 982 DLLDKLSAEKTLNPRGVVGLFPANRVGDDVEIYRDEiRTHVLTVSHHLRQQTEkvgfANYCLADFVAPKLSGKADYIGAF 1061
Cdd:COG1410 938 AMLDRIIEEKWLTARAVYGYFPANSEGDDIEVYDDE-SSEELARFHFPRQQRG----PNLCLADFVAPKESGERDYVGFF 1012
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 1062 AVTGGLEEDALAEAYEAQHDDYNKIMVKAIADRLAEAFAEYLHEKVRKVyWGYAANENLSNEELIRENYQGIRPAPGYPA 1141
Cdd:COG1410 1013 AVTAGIGIEELAAELEAAGDDYDAIMLHALADRLAEAFAEYLHERVRKE-WGYAPDEALTNEDLIKEKYRGIRPAPGYPA 1091
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|.
gi 578218282 1142 CPEHTEKATIWELLDVEaHTGMKLTESFAMWPGASVSGWYFSHPDSKYFAV 1192
Cdd:COG1410 1092 CPDHTEKRKLFDLLDAE-RIGVTLTESFAMHPEASVSGIYFHHPEAKYFNV 1141
|
|
| Met_synt_B12 |
pfam02965 |
Vitamin B12 dependent methionine synthase, activation domain; |
937-1208 |
0e+00 |
|
Vitamin B12 dependent methionine synthase, activation domain;
Pssm-ID: 460767 [Multi-domain] Cd Length: 273 Bit Score: 552.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 937 SIETLRNYIDWTPFFMTWSLAGKYPRILEDEVVGEEAQRLFKDANDLLDKLSAEKTLNPRGVVGLFPANRVGDDVEIYRD 1016
Cdd:pfam02965 1 DLAELVPYIDWTPFFQAWELKGKYPAILDDEVVGEEARKLFADAQAMLDRIIEEKWLTARGVVGFFPANSVGDDIEVYTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 1017 EIRTHVLTVSHHLRQQTEK-VGFANYCLADFVAPKLSGKADYIGAFAVTGGLEEDALAEAYEAQHDDYNKIMVKAIADRL 1095
Cdd:pfam02965 81 ESRTEVLATFHTLRQQTEKpEGRPNLCLADFIAPKESGIADYIGAFAVTAGIGIEELAARFEAAHDDYSAIMVKALADRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 1096 AEAFAEYLHEKVRKVYWGYAANENLSNEELIRENYQGIRPAPGYPACPEHTEKATIWELLDVEAHTGMKLTESFAMWPGA 1175
Cdd:pfam02965 161 AEAFAEYLHERVRKELWGYAPDENLSNEDLIKEKYQGIRPAPGYPACPDHTEKFTLFDLLDAEENIGIRLTESFAMTPAA 240
|
250 260 270
....*....|....*....|....*....|...
gi 578218282 1176 SVSGWYFSHPDSKYFAVAQIQRDQVEDYALRKG 1208
Cdd:pfam02965 241 SVSGLYFAHPESRYFAVGKIGKDQVEDYAKRKG 273
|
|
| MeTr |
cd00740 |
MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent ... |
356-612 |
2.78e-137 |
|
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: 417.56 E-value: 2.78e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 356 FVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVESGAQIIDINMDEGMLDAEAAMVRFLNLIAGEPdiaRVPIMIDS 435
Cdd:cd00740 1 FLNIGERTNVTGSKKFRELIKAEDYDEALDVARQQVEGGAQILDLNVDYGGLDGVSAMKWLLNLLATEP---TVPLMLDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 436 SKWEVIEKGLKCIQGKGIVNSISMKEGVEPFIHHAKLVRRYGAAMVVMAFDEVGQADTRERKIEICRRAYKILTEEVGFP 515
Cdd:cd00740 78 TNWEVIEAGLKCCQGKCVVNSINLEDGEERFLKVARLAKEHGAAVVVLAFDEQGQAKTRDKKVEIAERAYEALTEFVGFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 516 PEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISGGVSNVSFSFrgNDPVREAIHAVFLYYAIRNGMDMG 595
Cdd:cd00740 158 PEDIIFDPLILPIATGIEEHRPYALETIDAIRMIKERLPAVKISLGVSNVSFGF--NPAAREALNSVFLYEAIKAGLDMA 235
|
250
....*....|....*..
gi 578218282 596 IVNAGQLAIYDDLPGEL 612
Cdd:cd00740 236 IVNAGKLAPIEDIPEEL 252
|
|
| B12-binding_2 |
smart01018 |
B12 binding domain; Cobalamin-dependent methionine synthase is a large modular protein that ... |
657-740 |
8.74e-35 |
|
B12 binding domain; Cobalamin-dependent methionine synthase is a large modular protein that catalyses methyl transfer from methyltetrahydrofolate (CH3-H4folate) to homocysteine. During the catalytic cycle, it supports three distinct methyl transfer reactions, each involving the cobalamin (vitamin B12) cofactor and a substrate bound to its own functional unit. The cobalamin cofactor plays an essential role in this reaction, accepting the methyl group from CH3-H4folate to form methylcob(III)alamin, and in turn donating the methyl group to homocysteine to generate methionine and cob(I)alamin. Methionine synthase is a large enzyme composed of four structurally and functionally distinct modules: the first two modules bind homocysteine and CH3-H4folate, the third module binds the cobalamin cofactor and the C-terminal module binds S-adenosylmethionine. The cobalamin-binding module is composed of two structurally distinct domains: a 4-helical bundle cap domain (residues 651-740 in the Escherichia coli enzyme) and an alpha/beta B12-binding domain (residues 741-896). The 4-helical bundle forms a cap over the alpha/beta domain, which acts to shield the methyl ligand of cobalamin from solvent. Furthermore, in the conversion to the active conformation of this enzyme, the 4-helical cap rotates to allow the cobalamin cofactor to bind the activation domain. The alpha/beta domain is a common cobalamin-binding motif, whereas the 4-helical bundle domain with its methyl cap is a distinctive feature of methionine synthases.
Pssm-ID: 198086 [Multi-domain] Cd Length: 84 Bit Score: 127.59 E-value: 8.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 657 WDVKKRLEYSLVKGITEFIEQDTEEARQQAERPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPYI 736
Cdd:smart01018 1 MPLLERLAEAIVDGDEEGVEELVEEALAEGVDPLEIINEGLIPGMNVVGDLFEAGEYFLPQVLMSAEAMKAAVAILKPLL 80
|
....
gi 578218282 737 EASK 740
Cdd:smart01018 81 EKEK 84
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| metH |
PRK09490 |
B12-dependent methionine synthase; Provisional |
1-1223 |
0e+00 |
|
B12-dependent methionine synthase; Provisional
Pssm-ID: 236539 [Multi-domain] Cd Length: 1229 Bit Score: 2694.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 1 MSNKVEQLHQQLRERILVLDGGMGTMIQGYRLSEQDFRGERFADWPCDLKGNNDLLVLSKPEVIREIHDAYFAAGADIIE 80
Cdd:PRK09490 4 MSSRLAQLRALLAERILVLDGAMGTMIQRYKLEEADYRGERFADWPCDLKGNNDLLVLTQPDVIEAIHRAYLEAGADIIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 81 TNTFNSTTIAMADYQMESLSAEINFAAAKLARASADAWTARTPEKPRYVAGVLGPTNRTASISPDVNDPAFRNITFDQLV 160
Cdd:PRK09490 84 TNTFNATTIAQADYGMESLVYELNFAAARLAREAADEWTAKTPDKPRFVAGVLGPTNRTASISPDVNDPGFRNVTFDELV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 161 AAYRESTKALVEGGSDLILIETVFDTLNAKAAIFAVKEEFEALGVELPIMISGTITDASGRTLSGQTTEAFYNSLRHADA 240
Cdd:PRK09490 164 AAYREQTRGLIEGGADLILIETIFDTLNAKAAIFAVEEVFEELGVRLPVMISGTITDASGRTLSGQTTEAFWNSLRHAKP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 241 LTFGLNCALGPDELRQYVQELSRIAECYVTAHPNAGLPNAFGEYDLDADTMAAQIREWAQAGFLNIVGGCCGTTPEHIAA 320
Cdd:PRK09490 244 LSIGLNCALGADELRPYVEELSRIADTYVSAHPNAGLPNAFGEYDETPEEMAAQIGEFAESGFLNIVGGCCGTTPEHIAA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 321 MSRAVEGLPPRQLPELPVACRLSGLEPLNIGDDSLFVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVESGAQIIDI 400
Cdd:PRK09490 324 IAEAVAGLPPRKLPEIPVACRLSGLEPLNIDDDSLFVNVGERTNVTGSAKFARLIKEEDYDEALDVARQQVENGAQIIDI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 401 NMDEGMLDAEAAMVRFLNLIAGEPDIARVPIMIDSSKWEVIEKGLKCIQGKGIVNSISMKEGVEPFIHHAKLVRRYGAAM 480
Cdd:PRK09490 404 NMDEGMLDSEAAMVRFLNLIASEPDIARVPIMIDSSKWEVIEAGLKCIQGKGIVNSISLKEGEEKFIEHARLVRRYGAAV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 481 VVMAFDEVGQADTRERKIEICRRAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISG 560
Cdd:PRK09490 484 VVMAFDEQGQADTRERKIEICKRAYDILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKQNLPHAKISG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 561 GVSNVSFSFRGNDPVREAIHAVFLYYAIRNGMDMGIVNAGQLAIYDDLPGELRDAVEDVILNRRDDSTERLLELAEKYRG 640
Cdd:PRK09490 564 GVSNVSFSFRGNNPVREAIHAVFLYHAIKAGMDMGIVNAGQLAIYDDIPPELREAVEDVVLNRRPDATERLLEIAEKYRG 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 641 sKADDSANAQQAEWRSWDVKKRLEYSLVKGITEFIEQDTEEARQQAERPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVK 720
Cdd:PRK09490 644 -KGGKKAKAEDLEWRSWPVEKRLEHALVKGITEFIEEDTEEARQQAARPLEVIEGPLMDGMNVVGDLFGEGKMFLPQVVK 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 721 SARVMKQAVAYLEPYIEASKEQG---SSNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPAEKILRTAREEN 797
Cdd:PRK09490 723 SARVMKQAVAYLEPFIEAKKEGGtdrKSNGKILMATVKGDVHDIGKNIVGVVLQCNNYEVIDLGVMVPAEKILETAKEEN 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 798 ADLIGLSGLITPSLDEMVNVAKEMERQGFTIPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVSALLSATQRD 877
Cdd:PRK09490 803 ADIIGLSGLITPSLDEMVHVAKEMERQGFTIPLLIGGATTSKAHTAVKIAPNYSGPVVYVTDASRAVGVVSSLLSDEQRD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 878 DFVARTRKEYETVRIQHGRKKPRTPPVTLQAARENDLAFDWESYTPPVAHRLGVQEVEA-SIETLRNYIDWTPFFMTWSL 956
Cdd:PRK09490 883 AYVAETRAEYEKVREQHARKKPRKPLLTLEAARANRFKIDWEAYTPPKPKFLGVQVFEDyDLAELREYIDWTPFFQTWEL 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 957 AGKYPRILEDEVVGEEAQRLFKDANDLLDKLSAEKTLNPRGVVGLFPANRVGDDVEIYRDEIRTHVLTVSHHLRQQTEKV 1036
Cdd:PRK09490 963 AGKYPAILEDEVVGEEARKLFADAQAMLDKIIAEKWLTARGVIGLFPANSVGDDIEVYTDESRTEVLATLHHLRQQTEKR 1042
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 1037 GFANYCLADFVAPKLSGKADYIGAFAVTGGLEEDALAEAYEAQHDDYNKIMVKAIADRLAEAFAEYLHEKVRKVYWGYAA 1116
Cdd:PRK09490 1043 GRPNYCLADFVAPKESGKADYIGAFAVTAGLGEDELADRFEAAHDDYNAIMVKALADRLAEAFAEYLHERVRKEFWGYAP 1122
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 1117 NENLSNEELIRENYQGIRPAPGYPACPEHTEKATIWELLDVEAHTGMKLTESFAMWPGASVSGWYFSHPDSKYFAVAQIQ 1196
Cdd:PRK09490 1123 DENLSNEELIREKYQGIRPAPGYPACPDHTEKATLFDLLDAEKNTGMKLTESYAMWPGASVSGWYFSHPESKYFAVGKIG 1202
|
1210 1220
....*....|....*....|....*..
gi 578218282 1197 RDQVEDYALRKGMTAAEVERWLAPNLG 1223
Cdd:PRK09490 1203 RDQVEDYAARKGMSVEEVERWLAPNLG 1229
|
|
| metH |
TIGR02082 |
5-methyltetrahydrofolate--homocysteine methyltransferase; This family represents ... |
12-1192 |
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: 2028.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 12 LRERILVLDGGMGTMIQGYRLSEQDFRGErFADWPCDLKGNNDLLVLSKPEVIREIHDAYFAAGADIIETNTFNSTTIAM 91
Cdd:TIGR02082 1 LNQRILVLDGAMGTQLQSANLTEADFRGA-FADCHRELKGNNDILNLTKPEVIATIHRAYFEAGADIIETNTFNSTTISQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 92 ADYQMESLSAEINFAAAKLARASADAWTaRTPEKPRYVAGVLGPTNRTASISPDVNDPAFRNITFDQLVAAYRESTKALV 171
Cdd:TIGR02082 80 ADYDLEDLIYDLNFKGAKLARAVADEFT-LTPEKPRFVAGSMGPTNKTATLSPDVERPGFRNVTYDELVDAYTEQAKGLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 172 EGGSDLILIETVFDTLNAKAAIFAVKEEFEALGVELPIMISGTITDASGRTLSGQTTEAFYNSLRHADALTFGLNCALGP 251
Cdd:TIGR02082 159 DGGVDLLLIETCFDTLNAKAALFAAETVFEEKGRELPIMISGTIVDTSGRTLSGQTIEAFLTSLEHAGIDMIGLNCALGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 252 DELRQYVQELSRIAECYVTAHPNAGLPNAFGEYDLDADTMAAQIREWAQAGFLNIVGGCCGTTPEHIAAMSRAVEGLPPR 331
Cdd:TIGR02082 239 DEMRPHLKHLSEHAEAYVSCHPNAGLPNAFGEYDLTPDELAKALADFAAEGGLNIVGGCCGTTPDHIRAIAEAVKNIKPR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 332 QLPELPVACRLSGLEPLNIGDDSLFVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVESGAQIIDINMDEGMLDAEA 411
Cdd:TIGR02082 319 QRPVLYEPSRLSGLEAITIAQDSNFVNIGERTNVAGSKKFRRLIIAEDYDEALDIAKQQVENGAQILDINVDYGMLDGVA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 412 AMVRFLNLIAGEPDIARVPIMIDSSKWEVIEKGLKCIQGKGIVNSISMKEGVEPFIHHAKLVRRYGAAMVVMAFDEVGQA 491
Cdd:TIGR02082 399 AMKRFLNLLASEPDISTVPLMLDSSEWAVLEAGLKCIQGKCIVNSISLKDGEERFIETAKLIKEYGAAVVVMAFDEEGQA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 492 DTRERKIEICRRAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISGGVSNVSFSFRG 571
Cdd:TIGR02082 479 RTADRKIEICKRAYNILTEKVGFPPEDIIFDPNILTIATGIEEHRRYAINFIEAIRWIKEELPDAKISGGVSNVSFSFRG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 572 NDPVREAIHAVFLYYAIRNGMDMGIVNAGQLAIYDDLPGELRDAVEDVILNRRDDSTERLLELAEKYRGSKADDSANAQQ 651
Cdd:TIGR02082 559 NPAAREAMHSVFLYHAIRAGMDMGIVNAGKILPYDDIDPELRQVVEDLILNRRREATEPLLELAQLYEGTTTKSSKEAQQ 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 652 AEWRSWDVKKRLEYSLVKGITEFIEQDTEEARQQAERPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAY 731
Cdd:TIGR02082 639 AEWRNLPVEERLEYALVKGEREGIEEDLEEARKKLTRPLEIIEGPLMDGMKVVGDLFGSGKMFLPQVVKSARVMKKAVAY 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 732 LEPYIEASKEQGSSNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPAEKILRTAREENADLIGLSGLITPSL 811
Cdd:TIGR02082 719 LEPHMEKEKSEDSSKGKIVLATVKGDVHDIGKNIVGVVLSCNGYEVVDLGVMVPIEKILEAAKDHNADVIGLSGLITPSL 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 812 DEMVNVAKEMERQGFTIPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVSALLSATQRDDFVARTRKEYETVR 891
Cdd:TIGR02082 799 DEMKEVAEEMNRRGITIPLLIGGAATSKTHTAVKIAPIYKGPVVYVLDASRAVTVMDTLMSAKRKDTENGRIKEEYDTAR 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 892 IQHGRKKPRTPPVTLQAARENDLAFDW-ESYTPPVAHRLGVQEVEAS-IETLRNYIDWTPFFMTWSLAGKYPRILEDEVV 969
Cdd:TIGR02082 879 EKHGEQRSKRIAASEQAARKNVFAPDWsDDIEPPAPPFWGTQIVEASdIAELRPYIDWTPFFLQWQLRGKYPKILGDEYE 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 970 GEEAQRLFKDANDLLDKLSAEKTLNPRGVVGLFPANRVGDDVEIYRDEIR-THVLTVS----HHLRQQTEKvgfaNYCLA 1044
Cdd:TIGR02082 959 GLEAQKLFPDANEMLDKLSAENLLHARGVYGYFPAQSVGDDIEIYTDETVeTHPIATVrylfHFPRQQSGR----YLCLA 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 1045 DFVAPKLSGKADYIGAFAVTGGLEEDALAEAYEAQHDDYNKIMVKAIADRLAEAFAEYLHEKVRKVYWGYAANENLSNEE 1124
Cdd:TIGR02082 1035 DFIAPKASGIVDYIGAFAVTAGFGAEELADKLEAQHDDYDYIMVKAIADRLAEAFAEYLHRRVRKELWGYAAEEPLSNED 1114
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578218282 1125 LIRENYQGIRPAPGYPACPEHTEKATIWELLDVEaHTGMKLTESFAMWPGASVSGWYFSHPDSKYFAV 1192
Cdd:TIGR02082 1115 LLKLRYQGIRPAPGYPACPDHTEKATMFELLEPE-RIGVRLTESLAMHPEQSVSGLYFAHPEAKYFAV 1181
|
|
| MetH2 |
COG1410 |
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; ... |
23-1192 |
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: 1772.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 23 MGTMIQGYRLSEQDFRGERFADWPCDLKGNNDLLVLSKPEVIREIHDAYFAAGADIIETNTFNSTTIAMADYQMESLSAE 102
Cdd:COG1410 1 MGTMIQLLKLRELDADGAMFTDLQLDLKGNNDLLGLTGPNEILEIHRPELEAGADIIETNTGADAAITAADGAAEALLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 103 INFAAAKLARASADAWTARTPEKPRYVAGVLGPTNRTASISPDVNDPAFRNITFDQLVAAYRESTKALVEGGSDLILIET 182
Cdd:COG1410 81 YNGAAAALALEAAAAAAAAAAAAARAVAGAPGPTGGTASPGPDVPGLGFRNFDFDELVEAYAEAGLGLGGGGADLLLTET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 183 VFDTLNAKAAIFAVKEEFEALGVELPIMISGTITDASGRTLSGQTTEAFYNSLRHADALTFGLNCALGPDELRQYVQELS 262
Cdd:COG1410 161 IFDTLNAAAAAAAAAAAAEEEGVPIPVMVTGTITDGSGRTLSGQTAEAFLESLGHAAPGSNGLNCALGAEELRPYLEELS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 263 RIAECYVTAHPNAGLPNAFGEYDLDADTMAAQIREWAQAGFLNIVGGCCGTTPEHIAAMSRAVEGLPPRQlPELPVACRL 342
Cdd:COG1410 241 RIPPSAVSNAPNAGLPNGFGEYDETPEEMAAALAEFAEEGGVNIVGGCCGTTPEHIRAIAEAVAGLKPRP-REKPPPAVL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 343 SGLEPLNIGDDSLFVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVESGAQIIDINMDEGMLDAEAAMVRFLNLIAG 422
Cdd:COG1410 320 SGLEPVPIGQDSPFVNIGERTNVTGSKKFRELILEGDYDEALEVAREQVEAGAQILDVNVDEPGRDEVAAMVRFLNLLAS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 423 EpdiARVPIMIDSSKWEVIEKGLKCIQGKGIVNSISMKEGVEPFIHHAKLVRRYGAAMVVMAFDEVGQADTRERKIEICR 502
Cdd:COG1410 400 E---VRVPLMIDSSKPEVIEAGLKCYQGKPIVNSISLEEGEERFEEVAPLAKKYGAAVVVLAIDEEGQADTAERKLEIAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 503 RAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISGGVSNVSFSFRGNdpVREAIHAV 582
Cdd:COG1410 477 RIYDLAVEEYGFPPEDIIFDPLVFTVATGIEEHRNYAVETIEAIRLIKEELPGAKTSLGVSNVSFGLPGN--VREALNSV 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 583 FLYYAIRNGMDMGIVNAGQLAIYDDLPGELRDAVEDVILNRRDDSTERLLELAEKYRGSKADdsanAQQAEWRSWDVKKR 662
Cdd:COG1410 555 FLYHAIKAGLDMAIVNPGQLEPYDDIPPELRELAEDVLLNRRPDALERLIELFEGVKGAKAK----KADLEWRELPVEER 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 663 LEYSLVKGITEFIEQDTEEARQQAERPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPYIEASKEQ 742
Cdd:COG1410 631 LKHAIVKGIKEGIEEDTEEALAEGARPLEIINGPLMPGMNVVGDLFGAGKMFLPQVLKSAEVMKAAVAYLEPFMEKEKGE 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 743 GSSNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPAEKILRTAREENADLIGLSGLITPSLDEMVNVAKEME 822
Cdd:COG1410 711 SSSKGKIVLATVKGDVHDIGKNIVGVVLENNGYEVIDLGVMVPAEKILEAAKEHKADIIGLSGLMTTSLDEMKEVAEEMR 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 823 RQGFTIPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVSALLSATQRDDFVARTRKEYETVRIQHGRKKprTP 902
Cdd:COG1410 791 RRGLDIPVLIGGAALTRAYTAVKIAPAYDGAVVYAKDASRAVRVADKLLSKERREAFVAEIKAEYEKLRERHAARK--KK 868
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 903 PVTLQAARENDLAfdweSYTPPVAHRLGVQEVEA-SIETLRNYIDWTPFFMTWSLAGKYpriLEdevvGEEAQRLFKDAN 981
Cdd:COG1410 869 LLSLEEARSNVDS----DYPPPTPPFLGTRVLKDiPLAELVPYIDWTPFFQQWGLKGKY---LD----GEEARELFPDAQ 937
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 982 DLLDKLSAEKTLNPRGVVGLFPANRVGDDVEIYRDEiRTHVLTVSHHLRQQTEkvgfANYCLADFVAPKLSGKADYIGAF 1061
Cdd:COG1410 938 AMLDRIIEEKWLTARAVYGYFPANSEGDDIEVYDDE-SSEELARFHFPRQQRG----PNLCLADFVAPKESGERDYVGFF 1012
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 1062 AVTGGLEEDALAEAYEAQHDDYNKIMVKAIADRLAEAFAEYLHEKVRKVyWGYAANENLSNEELIRENYQGIRPAPGYPA 1141
Cdd:COG1410 1013 AVTAGIGIEELAAELEAAGDDYDAIMLHALADRLAEAFAEYLHERVRKE-WGYAPDEALTNEDLIKEKYRGIRPAPGYPA 1091
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|.
gi 578218282 1142 CPEHTEKATIWELLDVEaHTGMKLTESFAMWPGASVSGWYFSHPDSKYFAV 1192
Cdd:COG1410 1092 CPDHTEKRKLFDLLDAE-RIGVTLTESFAMHPEASVSGIYFHHPEAKYFNV 1141
|
|
| MetH1 |
COG0646 |
Methionine synthase I (cobalamin-dependent), methyltransferase domain [Amino acid transport ... |
6-830 |
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: 1008.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 6 EQLHQQLRERILVLDGGMGTMIQGYRLSEQDFRGErfadwpcdlKGNNDLLVLSKPEVIREIHDAYFAAGADIIETNTFN 85
Cdd:COG0646 4 AALLELLKERILILDGAMGTMLQAYGLTEGDFRGE---------KGCNELLNLTRPDVIREIHRAYLEAGADIIETNTFG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 86 STTIAMADYQMESLSAEINFAAAKLARASADAWTartpEKPRYVAGVLGPTNRTASispdvndpAFRNITFDQLVAAYRE 165
Cdd:COG0646 75 ANRIKLADYGLEDRVYEINRAAARLAREAADEFS----DRPRFVAGSIGPTGKLLS--------PLGNITFDELVEAYRE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 166 STKALVEGGSDLILIETVFDTLNAKAAIFAVKEEFEALGVELPIMISGTItDASGRTLSGQTTEAFYNSLRHADALTFGL 245
Cdd:COG0646 143 QAEGLIEGGVDLLLIETIFDTLEAKAAIFAAREAFEELGRDLPVMVSGTF-DASGRTLSGQTPEAFATSLEHLGPDAIGL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 246 NCALGPDELRQYVQELSRIAECYVTAHPNAGLPNAFGE---YDLDADTMAAQIREWAQAGFLNIVGGCCGTTPEHIAAMS 322
Cdd:COG0646 222 NCALGPDEMRPHVEELSEVADTPVSAYPNAGLPNLVGGrtvYDETPEEMAEYAEEFAEAGGVNIVGGCCGTTPEHIRAIA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 323 RAVEGLPPRQLPELPVACRLSGLEPLNIGDDSLFVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVESGAQIIDINM 402
Cdd:COG0646 302 EAVKGLPPRKRPPPPPALRLSGLEPLTITQDSLFVNVGERTNVTGSKKFARLILEGDYDAALAVARQQVEAGAQVIDVNM 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 403 DEGMLDAEAAMVRFLNLIAGEPDIARVPIMIDSSKWEVIEKGLKCIQGKGIVNSISMKEGVEPFIHHAKLVRRYGAAMVV 482
Cdd:COG0646 382 DEGMLDGEAAMVEFLNLIASEPDIPRVPDMIDSSKWEVIEAGLKGVQGKGIVNSISLKEGEEKFLELAKLVRRYGAAVVV 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 483 MAFDEVGQADTRERKIEICRRAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISGGV 562
Cdd:COG0646 462 MAFDEEGQADTAERKVEICARAYDLLTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKLNLPHALVSGGV 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 563 SNVSFSFRGNDPVREAIHAVFLYYAIRNGMDMGIVNAGQLAIYDDLPGELRDAVEDVILNRRDDSTERLLELAEKYRGSK 642
Cdd:COG0646 542 SNVSFSFRGNNPVREAIHAVFLYHAIAAGMDMGIVNAGQLAIYEEIPEELLLLVEDVVLNRREDATERLLEIAEEVKGAG 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 643 ADDSAnAQQAEWRSWDVKKRLEYSLVKGITEFIEQDTEEARQQAERPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSA 722
Cdd:COG0646 622 KAAEE-EAEEERREEEEERLLELLLVGGIEIDEEDDEEAALLLAALELIIIELLLGGGMVVGGLGGGGGKLLLVVVVKAV 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 723 RVMKQAVAYLEPYIEASKE-QGSSNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPAEKILRTAREENADLI 801
Cdd:COG0646 701 VKKKVAVALLKPEEEEKKKgGGKGGGVVVGVVVKVVVDDVDIIIVVVVVVVNNGIVVLVVVVIVVVALEAAAAAEAAVIL 780
|
810 820
....*....|....*....|....*....
gi 578218282 802 GLSGLITPSLDEMVNVAKEMERQGFTIPL 830
Cdd:COG0646 781 LVGGLVLLLLEEEVLAAAEAAAEAAVLLL 809
|
|
| Met_synt_B12 |
pfam02965 |
Vitamin B12 dependent methionine synthase, activation domain; |
937-1208 |
0e+00 |
|
Vitamin B12 dependent methionine synthase, activation domain;
Pssm-ID: 460767 [Multi-domain] Cd Length: 273 Bit Score: 552.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 937 SIETLRNYIDWTPFFMTWSLAGKYPRILEDEVVGEEAQRLFKDANDLLDKLSAEKTLNPRGVVGLFPANRVGDDVEIYRD 1016
Cdd:pfam02965 1 DLAELVPYIDWTPFFQAWELKGKYPAILDDEVVGEEARKLFADAQAMLDRIIEEKWLTARGVVGFFPANSVGDDIEVYTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 1017 EIRTHVLTVSHHLRQQTEK-VGFANYCLADFVAPKLSGKADYIGAFAVTGGLEEDALAEAYEAQHDDYNKIMVKAIADRL 1095
Cdd:pfam02965 81 ESRTEVLATFHTLRQQTEKpEGRPNLCLADFIAPKESGIADYIGAFAVTAGIGIEELAARFEAAHDDYSAIMVKALADRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 1096 AEAFAEYLHEKVRKVYWGYAANENLSNEELIRENYQGIRPAPGYPACPEHTEKATIWELLDVEAHTGMKLTESFAMWPGA 1175
Cdd:pfam02965 161 AEAFAEYLHERVRKELWGYAPDENLSNEDLIKEKYQGIRPAPGYPACPDHTEKFTLFDLLDAEENIGIRLTESFAMTPAA 240
|
250 260 270
....*....|....*....|....*....|...
gi 578218282 1176 SVSGWYFSHPDSKYFAVAQIQRDQVEDYALRKG 1208
Cdd:pfam02965 241 SVSGLYFAHPESRYFAVGKIGKDQVEDYAKRKG 273
|
|
| MeTr |
cd00740 |
MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent ... |
356-612 |
2.78e-137 |
|
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: 417.56 E-value: 2.78e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 356 FVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVESGAQIIDINMDEGMLDAEAAMVRFLNLIAGEPdiaRVPIMIDS 435
Cdd:cd00740 1 FLNIGERTNVTGSKKFRELIKAEDYDEALDVARQQVEGGAQILDLNVDYGGLDGVSAMKWLLNLLATEP---TVPLMLDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 436 SKWEVIEKGLKCIQGKGIVNSISMKEGVEPFIHHAKLVRRYGAAMVVMAFDEVGQADTRERKIEICRRAYKILTEEVGFP 515
Cdd:cd00740 78 TNWEVIEAGLKCCQGKCVVNSINLEDGEERFLKVARLAKEHGAAVVVLAFDEQGQAKTRDKKVEIAERAYEALTEFVGFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 516 PEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISGGVSNVSFSFrgNDPVREAIHAVFLYYAIRNGMDMG 595
Cdd:cd00740 158 PEDIIFDPLILPIATGIEEHRPYALETIDAIRMIKERLPAVKISLGVSNVSFGF--NPAAREALNSVFLYEAIKAGLDMA 235
|
250
....*....|....*..
gi 578218282 596 IVNAGQLAIYDDLPGEL 612
Cdd:cd00740 236 IVNAGKLAPIEDIPEEL 252
|
|
| methionine_synthase_B12_BD |
cd02069 |
B12 binding domain of methionine synthase. This domain binds methylcobalamin, which it uses as ... |
659-871 |
2.11e-135 |
|
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: 410.89 E-value: 2.11e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 659 VKKRLEYSLVKGITEFIEQDTEEARQQAERPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPYIEA 738
Cdd:cd02069 1 VEERLKHALVKGIRDGIEEDTEEARQQYARPLEIINGPLMDGMKVVGDLFGAGKMFLPQVLKSARVMKAAVAYLEPYMEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 739 SKEQGSSNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPAEKILRTAREENADLIGLSGLITPSLDEMVNVA 818
Cdd:cd02069 81 EKGENSSKGKIVLATVKGDVHDIGKNLVGVILSNNGYEVIDLGVMVPIEKILEAAKEHKADIIGLSGLLVPSLDEMVEVA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578218282 819 KEMERQGFTIPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVSALL 871
Cdd:cd02069 161 EEMNRRGIKIPLLIGGAATSRKHTAVKIAPEYDGPVVYVKDASRALGVANKLL 213
|
|
| S-methyl_trans |
pfam02574 |
Homocysteine S-methyltransferase; This is a family of related homocysteine ... |
17-325 |
1.49e-92 |
|
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: 298.30 E-value: 1.49e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 17 LVLDGGMGTMIQ--GYRLSEqDFRgerfadwpcdlkgNNDLLVlsKPEVIREIHDAYFAAGADIIETNTFNSTTIAMAD- 93
Cdd:pfam02574 1 LILDGGMGTELQrrGLDLTE-PLW-------------SNELLT--RPEIIREIHRDYLEAGADIIETNTYQASPIKLAEg 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 94 YQMESLSAEINFAAAKLARASADAWtartpekprYVAGVLGPTNRTASISPDvndpafrnITFDQLVAAYRESTKALVEG 173
Cdd:pfam02574 65 LEEEEAVYELNRAAVRLAREAADEY---------FVAGSIGPYGATLSDGYG--------LSFDELVDFHREQLEALLDG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 174 GSDLILIETVFDTLNAKAAIFAVKEEfealgVELPIMISGTITDAsGRTLSGQTTEAFYNSLRHA-DALTFGLNCALgPD 252
Cdd:pfam02574 128 GVDLLLFETIPDLLEAKAALELLAEE-----PDLPVWISFTIEDG-TRLRSGTTLEAAVAALLHAtGPLAVGVNCAL-PE 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578218282 253 ELRQYVQELSRIAECYVTAHpnaglPNAFGE-YDLDADTMAAQIREWAQAGfLNIVGGCCGTTPEHIAAMSRAV 325
Cdd:pfam02574 201 EMLPLLKELAKDAPTPVSVY-----PNSTGEvYDLTPEEWAEYAEGWLEAG-ANIIGGCCGTTPEHIRAIAEAL 268
|
|
| Pterin_bind |
pfam00809 |
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ... |
360-598 |
8.96e-76 |
|
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt a TIM barrel fold. The family includes dihydropteroate synthase EC:2.5.1.15 as well as a group methyltransferase enzymes including methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) that catalyzes a key step in the Wood-Ljungdahl pathway of carbon dioxide fixation. It transfers the N5-methyl group from methyltetrahydrofolate (CH3-H4folate) to a cob(I)amide centre in another protein, the corrinoid iron-sulfur protein. MeTr is a member of a family of proteins that includes methionine synthase and methanogenic enzymes that activate the methyl group of methyltetra-hydromethano(or -sarcino)pterin.
Pssm-ID: 395651 [Multi-domain] Cd Length: 243 Bit Score: 250.67 E-value: 8.96e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 360 GERTNVTGSAKFKRLIKEEkYSEALDVARQQVESGAQIIDINMDEG-----MLDAEAAMVRFLNLIAGEPDIARVPIMID 434
Cdd:pfam00809 1 MGILNVTPDSFSDGGRFLD-LDKALAHARRMVEEGADIIDIGGESTrpgaeRVDGEEEMERVLPVLAALRDEADVPISVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 435 SSKWEVIEKGLKCiqGKGIVNSISMKEGvepFIHHAKLVRRYGAAMVVMAFD--------EVGQADTRERKIEICRRAYK 506
Cdd:pfam00809 80 TTKAEVAEAALKA--GADIINDISGGDG---DPEMAELAAEYGAAVVVMHMDgtpktmqeNEQQYEDVVEEVERFLRARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 507 ILTEEVGFPPEDIIFDPNIFavATGIEEHNNYAQDFIGACEDIKrELPhalISGGVSNVSFSFRGN---DPVREAIHAVF 583
Cdd:pfam00809 155 AAAEEAGVPPEDIILDPGIG--FGKTEEHNLELLRTLDELRVIL-GVP---VLLGVSRKSFIGRGLplgGEERDAGTAAF 228
|
250
....*....|....*
gi 578218282 584 LYYAIRNGMDMGIVN 598
Cdd:pfam00809 229 LALAIAAGADIVRVH 243
|
|
| Pterin_binding |
cd00423 |
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and ... |
356-612 |
1.60e-66 |
|
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: 225.23 E-value: 1.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 356 FVNVGErTNVTGSaKFKRLIKEEKYSEALDVARQQVESGAQIIDINMDEG--------MLDAEAAMVRFLNLIAGEPDia 427
Cdd:cd00423 1 TLIMGI-LNVTPD-SFSDGGKFLSLDKALEHARRMVEEGADIIDIGGESTrpgaepvsVEEELERVIPVLRALAGEPD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 428 rVPIMIDSSKWEVIEKGLKCiqGKGIVNSISMKEGVEpfiHHAKLVRRYGAAMVVMAFDEVGQ--------ADTRERKIE 499
Cdd:cd00423 77 -VPISVDTFNAEVAEAALKA--GADIINDVSGGRGDP---EMAPLAAEYGAPVVLMHMDGTPQtmqnnpyyADVVDEVVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 500 ICRRAYKILTeEVGFPPEDIIFDPNIFAVATgiEEHNNYAQDFIGACedikRELPHALISGGVSNVSFSFR---GNDPVR 576
Cdd:cd00423 151 FLEERVEAAT-EAGIPPEDIILDPGIGFGKT--EEHNLELLRRLDAF----RELPGLPLLLGVSRKSFLGDllsVGPKDR 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 578218282 577 EAIHAVFLYYAIRNGMDMGIVNAgQLAIYDDLPGEL 612
Cdd:cd00423 224 LAGTAAFLAAAILNGADIVRVHD-VKELRDAIKVAE 258
|
|
| PRK08645 |
PRK08645 |
bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; ... |
10-330 |
1.75e-58 |
|
bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; Reviewed
Pssm-ID: 236321 [Multi-domain] Cd Length: 612 Bit Score: 213.17 E-value: 1.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 10 QQLRERILVLDGGMGTMiqgyrLSEQDFrgerfadwpcDLKGNNDLLVLSKPEVIREIHDAYFAAGADIIETNTFNSTTI 89
Cdd:PRK08645 6 ERLKERVLIADGAMGTL-----LYSRGV----------PLDRCFEELNLSHPELILRIHREYIEAGADVIQTNTFGANRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 90 AMADYQMESLSAEINfaaaklaraSADAWTARTP-EKPRYVAGVLGPTNRTASISPdvndpafrnITFDQLVAAYRESTK 168
Cdd:PRK08645 71 KLKRYGLEDKVKEIN---------RAAVRLAREAaGDDVYVAGTIGPIGGRGPLGD---------ISLEEIRREFREQID 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 169 ALVEGGSDLILIETVFDTLNAKAAIFAVKEEfealgVELPIMISGTITDAsGRTLSGQTTEAFYNSLRHADALTFGLNCA 248
Cdd:PRK08645 133 ALLEEGVDGLLLETFYDLEELLLALEAAREK-----TDLPIIAQVAFHED-GVTQNGTSLEEALKELVAAGADVVGLNCG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 249 LGPDELRQYVQELSRIAECYVTAHPNAGLPNAFGE---YDLDADTMAAQIREWAQAGfLNIVGGCCGTTPEHIAAMSRAV 325
Cdd:PRK08645 207 LGPYHMLEALERIPIPENAPLSAYPNAGLPEYVDGryvYSANPEYFAEYALEFVEQG-VRLIGGCCGTTPEHIRAMARAL 285
|
....*
gi 578218282 326 EGLPP 330
Cdd:PRK08645 286 KGLKP 290
|
|
| corrinoid_protein_B12-BD |
cd02070 |
B12 binding domain of corrinoid proteins. A family of small methanogenic corrinoid proteins ... |
666-839 |
6.98e-50 |
|
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: 175.50 E-value: 6.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 666 SLVKGITEFIEQDTEEARQQAERPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPYIEASKEQgsS 745
Cdd:cd02070 4 AIVDGDEEETVELVKKALEAGIDPQDIIEEGLAPGMDIVGDKYEEGEIFVPELLMAADAMKAGLDLLKPLLGKSKSA--K 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 746 NGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPAEKILRTAREENADLIGLSGLITPSLDEMVNVAKEMERQG 825
Cdd:cd02070 82 KGKVVIGTVEGDIHDIGKNLVATMLEANGFEVIDLGRDVPPEEFVEAVKEHKPDILGLSALMTTTMGGMKEVIEALKEAG 161
|
170
....*....|....*.
gi 578218282 826 FT--IPLLIGGATTSK 839
Cdd:cd02070 162 LRdkVKVMVGGAPVNQ 177
|
|
| MtbC1 |
COG5012 |
Methanogenic corrinoid protein MtbC1 [Energy production and conversion]; |
675-835 |
6.35e-46 |
|
Methanogenic corrinoid protein MtbC1 [Energy production and conversion];
Pssm-ID: 444036 [Multi-domain] Cd Length: 219 Bit Score: 164.68 E-value: 6.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 675 IEQDTEEARQQAER-------PIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPYIEASKEqgsSNG 747
Cdd:COG5012 19 LEGDEDEALELVAEalaagmdPEEIILDGLAPGMREVGELWEEGEIFVPEEHLAAAAMKAGLEILKPLLAEEGG---RKG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 748 KMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPAEKILRTAREENADLIGLSGLITPSLDEMVNVAKEMERQGFT 827
Cdd:COG5012 96 KVVIGTVEGDLHDIGKNIVADMLRAAGFEVIDLGADVPPEEFVEAAKEEKPDIVGLSALLTTTMPAMKELIEALREAGLR 175
|
170
....*....|
gi 578218282 828 --IPLLIGGA 835
Cdd:COG5012 176 dkVKVIVGGA 185
|
|
| B12-binding |
cd02067 |
B12 binding domain (B12-BD). This domain binds different cobalamid derivates, like B12 ... |
748-869 |
8.54e-44 |
|
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: 154.59 E-value: 8.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 748 KMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPAEKILRTAREENADLIGLSGLITPSLDEMVNVAKEMERQGFT 827
Cdd:cd02067 1 KVVIATVGGDGHDIGKNIVARALRDAGFEVIDLGVDVPPEEIVEAAKEEDADAIGLSGLLTTHMTLMKEVIEELKEAGLD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578218282 828 -IPLLIGGATTSKAHTAVKieqnYSGPTVYVQNASRTVGVVSA 869
Cdd:cd02067 81 dIPVLVGGAIVTRDFKFLK----EIGVDAYFGPATEAVEVLKK 119
|
|
| MHT1 |
COG2040 |
Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) [Amino acid transport and ... |
11-325 |
3.88e-39 |
|
Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) [Amino acid transport and metabolism];
Pssm-ID: 441643 [Multi-domain] Cd Length: 301 Bit Score: 148.03 E-value: 3.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 11 QLRERILVLDGGMGTmiqgyrlsEQDFRGerfadwpCDLkgNNDL----LVLSKPEVIREIHDAYFAAGADIIETNTFNS 86
Cdd:COG2040 8 LLMGRILLLDGGMGT--------ELERRG-------GDL--LDPLwsafALLEAPELVRAVHRDYFAAGADVITTNSYQA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 87 TT--IAMADYQMESLsAEINFAAAKLARASADAWTARtpeKPRYVAGVLGPtnRTASISPDvndpafRNITFDQLVAAYR 164
Cdd:COG2040 71 SPdgLAELGYSAEEA-ERLNRRAVALAREARDEYTPG---PPVLVAGSVGP--YGDEYRPD------YGLSAEEAEAYHR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 165 ESTKALVEGGSDLILIETVFDTLNAKAAIFAVKEefealgVELPIMISGTITDAsGRTLSGQT-TEAF--YNSLRHADAl 241
Cdd:COG2040 139 PRIEALAEAGVDLLAAETIPSLAEAIAIARAAAE------AGKPVWISFTVEDD-GRLRSGEPlAEAIaaVDTDPGPAA- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 242 tFGLNCAlGPDELRQYVQELSRIAECYVTAHPNAG------LPNAFGEYDLDADTMAAQIREWAQAGfLNIVGGCCGTTP 315
Cdd:COG2040 211 -VGVNCS-HPEHFEAALEALAAWTGRPIGVYANAGemsdaeLKTWGGLDDGDPEELAEQAAEWVAAG-ARIIGGCCGTGP 287
|
330
....*....|
gi 578218282 316 EHIAAMSRAV 325
Cdd:COG2040 288 RHIAAIARAL 297
|
|
| pyl_corrinoid |
TIGR02370 |
methyltransferase cognate corrinoid proteins, Methanosarcina family; This model describes a ... |
667-861 |
9.86e-38 |
|
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: 140.32 E-value: 9.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 667 LVKGITEFIEQDTEEARQQA----ERPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPYIEASKEQ 742
Cdd:TIGR02370 2 LAKAIFEGEEDDVVEGAQKAldagIDPIELIEKGLMAGMGVVGKLFEDGELFLPHVMMSADAMLAGIKVLTPEMEKAVET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 743 gSSNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPAEKILRTAREENADLIGLSGLITPSLDEMVNVAKEME 822
Cdd:TIGR02370 82 -EVLGKVVCGVAEGDVHDIGKNIVVTMLRANGFDVIDLGRDVPIDTVVEKVKKEKPLMLTGSALMTTTMYGQKDINDKLK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578218282 823 RQGF--TIPLLIGGATTSKAHtAVKIeqnysGPTVYVQNAS 861
Cdd:TIGR02370 161 EEGYrdSVKFMVGGAPVTQDW-ADKI-----GADVYGENAS 195
|
|
| B12-binding_2 |
smart01018 |
B12 binding domain; Cobalamin-dependent methionine synthase is a large modular protein that ... |
657-740 |
8.74e-35 |
|
B12 binding domain; Cobalamin-dependent methionine synthase is a large modular protein that catalyses methyl transfer from methyltetrahydrofolate (CH3-H4folate) to homocysteine. During the catalytic cycle, it supports three distinct methyl transfer reactions, each involving the cobalamin (vitamin B12) cofactor and a substrate bound to its own functional unit. The cobalamin cofactor plays an essential role in this reaction, accepting the methyl group from CH3-H4folate to form methylcob(III)alamin, and in turn donating the methyl group to homocysteine to generate methionine and cob(I)alamin. Methionine synthase is a large enzyme composed of four structurally and functionally distinct modules: the first two modules bind homocysteine and CH3-H4folate, the third module binds the cobalamin cofactor and the C-terminal module binds S-adenosylmethionine. The cobalamin-binding module is composed of two structurally distinct domains: a 4-helical bundle cap domain (residues 651-740 in the Escherichia coli enzyme) and an alpha/beta B12-binding domain (residues 741-896). The 4-helical bundle forms a cap over the alpha/beta domain, which acts to shield the methyl ligand of cobalamin from solvent. Furthermore, in the conversion to the active conformation of this enzyme, the 4-helical cap rotates to allow the cobalamin cofactor to bind the activation domain. The alpha/beta domain is a common cobalamin-binding motif, whereas the 4-helical bundle domain with its methyl cap is a distinctive feature of methionine synthases.
Pssm-ID: 198086 [Multi-domain] Cd Length: 84 Bit Score: 127.59 E-value: 8.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 657 WDVKKRLEYSLVKGITEFIEQDTEEARQQAERPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPYI 736
Cdd:smart01018 1 MPLLERLAEAIVDGDEEGVEELVEEALAEGVDPLEIINEGLIPGMNVVGDLFEAGEYFLPQVLMSAEAMKAAVAILKPLL 80
|
....
gi 578218282 737 EASK 740
Cdd:smart01018 81 EKEK 84
|
|
| B12-binding_like |
cd02065 |
B12 binding domain (B12-BD). Most of the members bind different cobalamid derivates, like B12 ... |
748-864 |
8.74e-35 |
|
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: 129.04 E-value: 8.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 748 KMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPAEKILRTAREENADLIGLSGLITPSLDEMVNVAKEMERQGFT 827
Cdd:cd02065 1 KVLGATVGGDVHDIGKNIVAIALRDNGFEVIDLGVDVPPEEIVEAAKEEDADVVGLSALSTTHMEAMKLVIEALKELGID 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 578218282 828 IPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTV 864
Cdd:cd02065 81 IPVVVGGAHPTADPEEPKVDAVVIGEGEYAGPALLEV 117
|
|
| mmuM |
PRK09485 |
homocysteine methyltransferase; Provisional |
1-327 |
1.27e-31 |
|
homocysteine methyltransferase; Provisional
Pssm-ID: 181899 [Multi-domain] Cd Length: 304 Bit Score: 126.12 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 1 MSNKVEQLHQQlreRILVLDGGMGTmiqgyrlsEQDFRGerfadwpCDLkgNNDL----LVLSKPEVIREIHDAYFAAGA 76
Cdd:PRK09485 1 MNPFKELLAQG---PVLILDGALAT--------ELEARG-------CDL--NDSLwsakVLLENPELIYQVHLDYFRAGA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 77 DIIETNTFNSTTIAMAD--------YQMESLSAEInfaaaklarasadAWTART--PEKPRYVAGVLGPTNrtASISpdv 146
Cdd:PRK09485 61 DCAITASYQATFQGFAArglseaeaEELIRRSVEL-------------AKEARDefWAEKPLVAGSVGPYG--AYLA--- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 147 NDPAFR---NITFDQLVAAYRESTKALVEGGSDLILIETVFDTLNAKAAIFAVKEEFEalgvELPIMISGTITDasGRTL 223
Cdd:PRK09485 123 DGSEYRgdyGLSEEELQDFHRPRIEALAEAGADLLACETIPNLDEAEALVELLKEEFP----GVPAWLSFTLRD--GTHI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 224 SGQTteafynSLRHADAL--------TFGLNCAlGPDELRQYVQELSRIAECYVTAHPNAGlpnafGEYDL--------- 286
Cdd:PRK09485 197 SDGT------PLAEAAALlaaspqvvAVGVNCT-APELVTAAIAALRAVTDKPLVVYPNSG-----EVYDAvtktwhgpa 264
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 578218282 287 DADTMAAQIREWAQAGfLNIVGGCCGTTPEHIAAMSRAVEG 327
Cdd:PRK09485 265 DDASLGELAPEWYAAG-ARLIGGCCRTTPEDIAALAAALKT 304
|
|
| PRK07534 |
PRK07534 |
betaine--homocysteine S-methyltransferase; |
1-336 |
1.13e-30 |
|
betaine--homocysteine S-methyltransferase;
Pssm-ID: 236045 [Multi-domain] Cd Length: 336 Bit Score: 124.48 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 1 MSNkveQLHQQLRER-ILVLDGGMGTMIQGYRLSEqdfrgerfADWPcdlkgnnDLLVLSKPEVIREIHDAYFAAGADII 79
Cdd:PRK07534 1 MTN---ALSDLLAERgVLLADGATGTNLFNMGLES--------GEAP-------ELWNEDHPDNITALHQGFVDAGSDII 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 80 ETNTFNSTTIAMADYQMESLSAEINFAAAKLARASADAwtartPEKPRYVAGVLGPTNrtasispDVNDPAFRnITFDQL 159
Cdd:PRK07534 63 LTNSFGGTAARLKLHDAQDRVHELNRAAAEIAREVADK-----AGRKVIVAGSVGPTG-------EIMEPMGA-LTHALA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 160 VAAYRESTKALVEGGSDLILIETVFDTLNAKAAIFAVKEefealgVELPIMISGTItDASGRTLSGQTTEAFYN---SLR 236
Cdd:PRK07534 130 VEAFHEQAEGLKAGGADVLWVETISAPEEIRAAAEAAKL------AGMPWCGTMSF-DTAGRTMMGLTPADLADlveKLG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 237 HAdALTFGLNCALGPDELRQYVQELSRIA-ECYVTAHPNAGLPNAFG---EYDLDADTMAAQIREWAQAGfLNIVGGCCG 312
Cdd:PRK07534 203 EP-PLAFGANCGVGASDLLRTVLGFTAQGpERPIIAKGNAGIPKYVDghiHYDGTPELMAEYAVLARDAG-ARIIGGCCG 280
|
330 340
....*....|....*....|....
gi 578218282 313 TTPEHIAAMSRAVEGLPPRQLPEL 336
Cdd:PRK07534 281 TMPEHLAAMRAALDARPRGPRPSL 304
|
|
| PRK07535 |
PRK07535 |
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase; Validated |
359-599 |
1.64e-29 |
|
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase; Validated
Pssm-ID: 181022 [Multi-domain] Cd Length: 261 Bit Score: 118.80 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 359 VGERTNvtGSAK-FKRLIKEEKYSEALDVARQQVESGAQIIDINMDEGMLDAEAAMVRFLNLIAGEPDiarVPIMIDSSK 437
Cdd:PRK07535 4 IGERIN--GTRKsIAEAIEAKDAAFIQKLALKQAEAGADYLDVNAGTAVEEEPETMEWLVETVQEVVD---VPLCIDSPN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 438 WEVIEKGLKCIQGKGIVNSISM-KEGVEPFIhhaKLVRRYGAAMVVMAFDEVGQADTRERKIEICRRAYKILtEEVGFPP 516
Cdd:PRK07535 79 PAAIEAGLKVAKGPPLINSVSAeGEKLEVVL---PLVKKYNAPVVALTMDDTGIPKDAEDRLAVAKELVEKA-DEYGIPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 517 EDIIFDPNIFAVATGieehNNYAQDFIGACEDIKRELPHALISGGVSNVSFsfrgNDPVREAIHAVFLYYAIRNGMDMGI 596
Cdd:PRK07535 155 EDIYIDPLVLPLSAA----QDAGPEVLETIRRIKELYPKVHTTCGLSNISF----GLPNRKLINRAFLVMAMGAGMDSAI 226
|
...
gi 578218282 597 VNA 599
Cdd:PRK07535 227 LDP 229
|
|
| B12-binding |
pfam02310 |
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ... |
747-835 |
2.77e-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: 90.46 E-value: 2.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 747 GKMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPAEKILRTAREENADLIGLSGLITPSLDEMVNVAKEMERQGF 826
Cdd:pfam02310 1 GKVVVATVGGDLHPLGLNYVAAALRAAGFEVIILGANVPPEDIVAAARDEKPDVVGLSALMTTTLPGAKELIRLLKGIRP 80
|
....*....
gi 578218282 827 TIPLLIGGA 835
Cdd:pfam02310 81 RVKVVVGGP 89
|
|
| B12-binding_2 |
pfam02607 |
B12 binding domain; This B12 binding domain is found in methionine synthase EC:2.1.1.13, and ... |
663-732 |
9.12e-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: 84.06 E-value: 9.12e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 663 LEYSLVKGITEFIEQDTEEARqqAERPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYL 732
Cdd:pfam02607 1 LLEALLEGDEEAAEELLEEAL--EIDPEEIIEDLLIPGMDEVGELWEAGEIFVPQEHLAAEAMKAALAVL 68
|
|
| PLN02489 |
PLN02489 |
homocysteine S-methyltransferase |
17-325 |
7.42e-17 |
|
homocysteine S-methyltransferase
Pssm-ID: 215269 Cd Length: 335 Bit Score: 83.52 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 17 LVLDGGMGTmiqgyrlsEQDFRGerfadwpCDLkgnND-----LLVLSKPEVIREIHDAYFAAGADIIETNTFNSTTIA- 90
Cdd:PLN02489 23 AVIDGGFAT--------ELERHG-------ADL---NDplwsaKCLITSPHLIRKVHLDYLEAGADIIITASYQATIQGf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 91 ----MADYQMESL---SAEINFAAAKL--ARASADAWTARTPE---KPRYVAgvlgptnrtASI-------------SPD 145
Cdd:PLN02489 85 esrgLSREESETLlrkSVEIACEARDIfwDKCQKGSTSRPGRElsyRPILVA---------ASIgsygayladgseySGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 146 VNDpafrNITFDQLVAAYRESTKALVEGGSDLILIETVFDTLNAKAAIfavkEEFEALGVELPIMISGTITDASgRTLSG 225
Cdd:PLN02489 156 YGP----SVTLEKLKDFHRRRLQVLAEAGPDLIAFETIPNKLEAQAYV----ELLEEENIKIPAWISFNSKDGV-NVVSG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 226 qttEAFYNSLRHADALT----FGLNCAlGPdelrQYVQELSRIAEcYVTAHPNAGLPNAFGEYDLDA-----------DT 290
Cdd:PLN02489 227 ---DSLLECASIADSCKkvvaVGINCT-PP----RFIHGLILSIR-KVTSKPIVVYPNSGETYDGEAkewvestgvsdED 297
|
330 340 350
....*....|....*....|....*....|....*
gi 578218282 291 MAAQIREWAQAGfLNIVGGCCGTTPEHIAAMSRAV 325
Cdd:PLN02489 298 FVSYVNKWRDAG-ASLIGGCCRTTPNTIRAISKAL 331
|
|
| Sbm |
COG2185 |
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ... |
748-834 |
4.16e-09 |
|
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and metabolism];
Pssm-ID: 441788 [Multi-domain] Cd Length: 134 Bit Score: 55.92 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 748 KMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPAEKILRTAREENADLIGLSglitpSLDEMVN-----VAKEME 822
Cdd:COG2185 12 RVLLAKPGLDGHDRGAKVIARALRDAGFEVIYLGLFQTPEEIVRAAIEEDADVIGVS-----SLDGGHLelvpeLIELLK 86
|
90
....*....|...
gi 578218282 823 RQGFT-IPLLIGG 834
Cdd:COG2185 87 EAGAGdILVVVGG 99
|
|
| DHPS |
cd00739 |
DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional ... |
348-525 |
9.56e-09 |
|
DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), 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.
Pssm-ID: 238380 Cd Length: 257 Bit Score: 57.62 E-value: 9.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 348 LNIGDDSlFVNVGERTNVTgsakfkrlikeekysEALDVARQQVESGAQIIDI-----NMDEGMLDAEAAMVRFLNLIAG 422
Cdd:cd00739 7 LNVTPDS-FSDGGRFLSLD---------------KAVAHAEKMIAEGADIIDIggestRPGADPVSVEEELERVIPVLEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 423 EPDIARVPIMIDSSKWEVIEKGLKciQGKGIVNSISmkeGVEPFIHHAKLVRRYGAAMVVM-----------------AF 485
Cdd:cd00739 71 LRGELDVLISVDTFRAEVARAALE--AGADIINDVS---GGSDDPAMLEVAAEYGAPLVLMhmrgtpktmqenpyyedVV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 578218282 486 DEVgqADTRERKIEICRRAykilteevGFPPEDIIFDPNI 525
Cdd:cd00739 146 DEV--LSFLEARLEAAESA--------GVARNRIILDPGI 175
|
|
| MM_CoA_mut_B12_BD |
cd02071 |
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), ... |
748-834 |
6.98e-05 |
|
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: 43.74 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578218282 748 KMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPAEKILRTAREENADLIGLSGLITPSLDEMVNVAKEMERQGFT 827
Cdd:cd02071 1 RILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRQTPEEIVEAAIQEDVDVIGLSSLSGGHMTLFPEVIELLRELGAG 80
|
....*...
gi 578218282 828 -IPLLIGG 834
Cdd:cd02071 81 dILVVGGG 88
|
|
| PRK02261 |
PRK02261 |
methylaspartate mutase subunit S; Provisional |
748-806 |
9.75e-05 |
|
methylaspartate mutase subunit S; Provisional
Pssm-ID: 179400 [Multi-domain] Cd Length: 137 Bit Score: 43.40 E-value: 9.75e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 578218282 748 KMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPAEKILRTAREENADLIGLSGL 806
Cdd:PRK02261 5 TVVLGVIGADCHAVGNKILDRALTEAGFEVINLGVMTSQEEFIDAAIETDADAILVSSL 63
|
|
| Glm_B12_BD |
cd02072 |
B12 binding domain of glutamate mutase (Glm). Glutamate mutase catalysis the conversion of (S) ... |
748-806 |
7.06e-04 |
|
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: 40.91 E-value: 7.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 578218282 748 KMVIATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVPAEKILRTAREENADLIGLSGL 806
Cdd:cd02072 1 TIVLGVIGSDCHAVGNKILDHAFTEAGFNVVNLGVLSPQEEFIDAAIETDADAILVSSL 59
|
|
| |
