|
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: 2702.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 1 MSSKVEQLRAQLNERILVLDGGMGTMIQSYRLNEADFRGERFADWPCDLKGNNDLLVLSKPEVIAAIHNAYFEAGADIIE 80
Cdd:PRK09490 4 MSSRLAQLRALLAERILVLDGAMGTMIQRYKLEEADYRGERFADWPCDLKGNNDLLVLTQPDVIEAIHRAYLEAGADIIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 81 TNTFNSTTIAMADYQMESLSAEINFAAAKLARACADEWTARTPEKPRYVAGVLGPTNRTASISPDVNDPAFRNITFDQLV 160
Cdd:PRK09490 84 TNTFNATTIAQADYGMESLVYELNFAAARLAREAADEWTAKTPDKPRFVAGVLGPTNRTASISPDVNDPGFRNVTFDELV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 161 AAYRESTKALVEGGADLILIETVFDTLNAKAAVFAVKTEFEALGVELPIMISGTITDASGRTLSGQTTEAFYNSLRHAEA 240
Cdd:PRK09490 164 AAYREQTRGLIEGGADLILIETIFDTLNAKAAIFAVEEVFEELGVRLPVMISGTITDASGRTLSGQTTEAFWNSLRHAKP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 241 LTFGLNCALGPDELRQYVQELSRIAECYVTAHPNAGLPNAFGEYDLDADTMAKQIREWAQAGFLNIVGGCCGTTPQHIAA 320
Cdd:PRK09490 244 LSIGLNCALGADELRPYVEELSRIADTYVSAHPNAGLPNAFGEYDETPEEMAAQIGEFAESGFLNIVGGCCGTTPEHIAA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 321 MSRAVEGLAPRKLPEIPVACRLSGLEPLNIGDDSLFVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVENGAQIIDI 400
Cdd:PRK09490 324 IAEAVAGLPPRKLPEIPVACRLSGLEPLNIDDDSLFVNVGERTNVTGSAKFARLIKEEDYDEALDVARQQVENGAQIIDI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 401 NMDEGMLDAEAAMVRFLNLIAGEPDIARVPIMIDSSKWEVIEKGLKCIQGKGIVNSISMKEGVDAFIHHAKLLRRYGAAV 480
Cdd:PRK09490 404 NMDEGMLDSEAAMVRFLNLIASEPDIARVPIMIDSSKWEVIEAGLKCIQGKGIVNSISLKEGEEKFIEHARLVRRYGAAV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 481 VVMAFDEQGQADTRARKIEICRRAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISG 560
Cdd:PRK09490 484 VVMAFDEQGQADTRERKIEICKRAYDILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKQNLPHAKISG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 561 GVSNVSFSFRGNDPVREAIHAVFLYYAIRNGMDMGIVNAGQLAIYDDLPAELRDAVEDVILNRRDDGTERLLELAEKYRG 640
Cdd:PRK09490 564 GVSNVSFSFRGNNPVREAIHAVFLYHAIKAGMDMGIVNAGQLAIYDDIPPELREAVEDVVLNRRPDATERLLEIAEKYRG 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 641 SKtDDTANAQQAEWRSWEVNKRLEYSLVKGITEFIEQDTEEARQQATRPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVK 720
Cdd:PRK09490 644 KG-GKKAKAEDLEWRSWPVEKRLEHALVKGITEFIEEDTEEARQQAARPLEVIEGPLMDGMNVVGDLFGEGKMFLPQVVK 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 721 SARVMKQAVAYLEPFIEASKEQG---KTNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVN 797
Cdd:PRK09490 723 SARVMKQAVAYLEPFIEAKKEGGtdrKSNGKILMATVKGDVHDIGKNIVGVVLQCNNYEVIDLGVMVPAEKILETAKEEN 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 798 ADLIGLSGLITPSLDEMVNVAKEMERQGFTIPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVAALLSDTQRD 877
Cdd:PRK09490 803 ADIIGLSGLITPSLDEMVHVAKEMERQGFTIPLLIGGATTSKAHTAVKIAPNYSGPVVYVTDASRAVGVVSSLLSDEQRD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 878 DFVARTRKEYETVRIQHGRKKPRTPPVTLEAARDNDFAFDWQAYTPPVAHRLGVQEVEA-SIETLRNYIDWTPFFMTWSL 956
Cdd:PRK09490 883 AYVAETRAEYEKVREQHARKKPRKPLLTLEAARANRFKIDWEAYTPPKPKFLGVQVFEDyDLAELREYIDWTPFFQTWEL 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 957 AGKYPRILEDEVVGVEAQRLFKDANDMLDKLSAEKTLNPRGVVGLFPANRVGDDIEIYRDETRTHVINVSHHLRQQTEKT 1036
Cdd:PRK09490 963 AGKYPAILEDEVVGEEARKLFADAQAMLDKIIAEKWLTARGVIGLFPANSVGDDIEVYTDESRTEVLATLHHLRQQTEKR 1042
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 1037 GFANYCLADFVAPKLSGKADYIGAFAVTGGLEEDALADAFEAQHDDYNKIMVKALADRLAEAFAEYLHERVRKVYWGYAP 1116
Cdd:PRK09490 1043 GRPNYCLADFVAPKESGKADYIGAFAVTAGLGEDELADRFEAAHDDYNAIMVKALADRLAEAFAEYLHERVRKEFWGYAP 1122
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 1117 NENLSNEELIRENYQGIRPAPGYPACPEHTEKATIWELLEVEKHTGMKLTESFAMWPGASVSGWYFSHPDSKYYAVAQIQ 1196
Cdd:PRK09490 1123 DENLSNEELIREKYQGIRPAPGYPACPDHTEKATLFDLLDAEKNTGMKLTESYAMWPGASVSGWYFSHPESKYFAVGKIG 1202
|
1210 1220
....*....|....*....|....*..
gi 446018192 1197 RDQVEDYARRKGMSVSDVERWLAPNLG 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: 2080.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 12 LNERILVLDGGMGTMIQSYRLNEADFRGErFADWPCDLKGNNDLLVLSKPEVIAAIHNAYFEAGADIIETNTFNSTTIAM 91
Cdd:TIGR02082 1 LNQRILVLDGAMGTQLQSANLTEADFRGA-FADCHRELKGNNDILNLTKPEVIATIHRAYFEAGADIIETNTFNSTTISQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 92 ADYQMESLSAEINFAAAKLARACADEWTaRTPEKPRYVAGVLGPTNRTASISPDVNDPAFRNITFDQLVAAYRESTKALV 171
Cdd:TIGR02082 80 ADYDLEDLIYDLNFKGAKLARAVADEFT-LTPEKPRFVAGSMGPTNKTATLSPDVERPGFRNVTYDELVDAYTEQAKGLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 172 EGGADLILIETVFDTLNAKAAVFAVKTEFEALGVELPIMISGTITDASGRTLSGQTTEAFYNSLRHAEALTFGLNCALGP 251
Cdd:TIGR02082 159 DGGVDLLLIETCFDTLNAKAALFAAETVFEEKGRELPIMISGTIVDTSGRTLSGQTIEAFLTSLEHAGIDMIGLNCALGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 252 DELRQYVQELSRIAECYVTAHPNAGLPNAFGEYDLDADTMAKQIREWAQAGFLNIVGGCCGTTPQHIAAMSRAVEGLAPR 331
Cdd:TIGR02082 239 DEMRPHLKHLSEHAEAYVSCHPNAGLPNAFGEYDLTPDELAKALADFAAEGGLNIVGGCCGTTPDHIRAIAEAVKNIKPR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 332 KLPEIPVACRLSGLEPLNIGDDSLFVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVENGAQIIDINMDEGMLDAEA 411
Cdd:TIGR02082 319 QRPVLYEPSRLSGLEAITIAQDSNFVNIGERTNVAGSKKFRRLIIAEDYDEALDIAKQQVENGAQILDINVDYGMLDGVA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 412 AMVRFLNLIAGEPDIARVPIMIDSSKWEVIEKGLKCIQGKGIVNSISMKEGVDAFIHHAKLLRRYGAAVVVMAFDEQGQA 491
Cdd:TIGR02082 399 AMKRFLNLLASEPDISTVPLMLDSSEWAVLEAGLKCIQGKCIVNSISLKDGEERFIETAKLIKEYGAAVVVMAFDEEGQA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 492 DTRARKIEICRRAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISGGVSNVSFSFRG 571
Cdd:TIGR02082 479 RTADRKIEICKRAYNILTEKVGFPPEDIIFDPNILTIATGIEEHRRYAINFIEAIRWIKEELPDAKISGGVSNVSFSFRG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 572 NDPVREAIHAVFLYYAIRNGMDMGIVNAGQLAIYDDLPAELRDAVEDVILNRRDDGTERLLELAEKYRGSKTDDTANAQQ 651
Cdd:TIGR02082 559 NPAAREAMHSVFLYHAIRAGMDMGIVNAGKILPYDDIDPELRQVVEDLILNRRREATEPLLELAQLYEGTTTKSSKEAQQ 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 652 AEWRSWEVNKRLEYSLVKGITEFIEQDTEEARQQATRPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAY 731
Cdd:TIGR02082 639 AEWRNLPVEERLEYALVKGEREGIEEDLEEARKKLTRPLEIIEGPLMDGMKVVGDLFGSGKMFLPQVVKSARVMKKAVAY 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 732 LEPFIEASKEQGKTNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADLIGLSGLITPSL 811
Cdd:TIGR02082 719 LEPHMEKEKSEDSSKGKIVLATVKGDVHDIGKNIVGVVLSCNGYEVVDLGVMVPIEKILEAAKDHNADVIGLSGLITPSL 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 812 DEMVNVAKEMERQGFTIPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVAALLSDTQRDDFVARTRKEYETVR 891
Cdd:TIGR02082 799 DEMKEVAEEMNRRGITIPLLIGGAATSKTHTAVKIAPIYKGPVVYVLDASRAVTVMDTLMSAKRKDTENGRIKEEYDTAR 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 892 IQHGRKKPRTPPVTLEAARDNDFAFDWQ-AYTPPVAHRLGVQEVEAS-IETLRNYIDWTPFFMTWSLAGKYPRILEDEVV 969
Cdd:TIGR02082 879 EKHGEQRSKRIAASEQAARKNVFAPDWSdDIEPPAPPFWGTQIVEASdIAELRPYIDWTPFFLQWQLRGKYPKILGDEYE 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 970 GVEAQRLFKDANDMLDKLSAEKTLNPRGVVGLFPANRVGDDIEIYRDETR-THVINVS----HHLRQQTEKtgfaNYCLA 1044
Cdd:TIGR02082 959 GLEAQKLFPDANEMLDKLSAENLLHARGVYGYFPAQSVGDDIEIYTDETVeTHPIATVrylfHFPRQQSGR----YLCLA 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 1045 DFVAPKLSGKADYIGAFAVTGGLEEDALADAFEAQHDDYNKIMVKALADRLAEAFAEYLHERVRKVYWGYAPNENLSNEE 1124
Cdd:TIGR02082 1035 DFIAPKASGIVDYIGAFAVTAGFGAEELADKLEAQHDDYDYIMVKAIADRLAEAFAEYLHRRVRKELWGYAAEEPLSNED 1114
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446018192 1125 LIRENYQGIRPAPGYPACPEHTEKATIWELLEVEKhTGMKLTESFAMWPGASVSGWYFSHPDSKYYAV 1192
Cdd:TIGR02082 1115 LLKLRYQGIRPAPGYPACPDHTEKATMFELLEPER-IGVRLTESLAMHPEQSVSGLYFAHPEAKYFAV 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: 1767.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 23 MGTMIQSYRLNEADFRGERFADWPCDLKGNNDLLVLSKPEVIAAIHNAYFEAGADIIETNTFNSTTIAMADYQMESLSAE 102
Cdd:COG1410 1 MGTMIQLLKLRELDADGAMFTDLQLDLKGNNDLLGLTGPNEILEIHRPELEAGADIIETNTGADAAITAADGAAEALLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 103 INFAAAKLARACADEWTARTPEKPRYVAGVLGPTNRTASISPDVNDPAFRNITFDQLVAAYRESTKALVEGGADLILIET 182
Cdd:COG1410 81 YNGAAAALALEAAAAAAAAAAAAARAVAGAPGPTGGTASPGPDVPGLGFRNFDFDELVEAYAEAGLGLGGGGADLLLTET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 183 VFDTLNAKAAVFAVKTEFEALGVELPIMISGTITDASGRTLSGQTTEAFYNSLRHAEALTFGLNCALGPDELRQYVQELS 262
Cdd:COG1410 161 IFDTLNAAAAAAAAAAAAEEEGVPIPVMVTGTITDGSGRTLSGQTAEAFLESLGHAAPGSNGLNCALGAEELRPYLEELS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 263 RIAECYVTAHPNAGLPNAFGEYDLDADTMAKQIREWAQAGFLNIVGGCCGTTPQHIAAMSRAVEGLAPRKlPEIPVACRL 342
Cdd:COG1410 241 RIPPSAVSNAPNAGLPNGFGEYDETPEEMAAALAEFAEEGGVNIVGGCCGTTPEHIRAIAEAVAGLKPRP-REKPPPAVL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 343 SGLEPLNIGDDSLFVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVENGAQIIDINMDEGMLDAEAAMVRFLNLIAG 422
Cdd:COG1410 320 SGLEPVPIGQDSPFVNIGERTNVTGSKKFRELILEGDYDEALEVAREQVEAGAQILDVNVDEPGRDEVAAMVRFLNLLAS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 423 EpdiARVPIMIDSSKWEVIEKGLKCIQGKGIVNSISMKEGVDAFIHHAKLLRRYGAAVVVMAFDEQGQADTRARKIEICR 502
Cdd:COG1410 400 E---VRVPLMIDSSKPEVIEAGLKCYQGKPIVNSISLEEGEERFEEVAPLAKKYGAAVVVLAIDEEGQADTAERKLEIAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 503 RAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISGGVSNVSFSFRGNdpVREAIHAV 582
Cdd:COG1410 477 RIYDLAVEEYGFPPEDIIFDPLVFTVATGIEEHRNYAVETIEAIRLIKEELPGAKTSLGVSNVSFGLPGN--VREALNSV 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 583 FLYYAIRNGMDMGIVNAGQLAIYDDLPAELRDAVEDVILNRRDDGTERLLELAEKYRGSKtddtANAQQAEWRSWEVNKR 662
Cdd:COG1410 555 FLYHAIKAGLDMAIVNPGQLEPYDDIPPELRELAEDVLLNRRPDALERLIELFEGVKGAK----AKKADLEWRELPVEER 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 663 LEYSLVKGITEFIEQDTEEARQQATRPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPFIEASKEQ 742
Cdd:COG1410 631 LKHAIVKGIKEGIEEDTEEALAEGARPLEIINGPLMPGMNVVGDLFGAGKMFLPQVLKSAEVMKAAVAYLEPFMEKEKGE 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 743 GKTNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADLIGLSGLITPSLDEMVNVAKEME 822
Cdd:COG1410 711 SSSKGKIVLATVKGDVHDIGKNIVGVVLENNGYEVIDLGVMVPAEKILEAAKEHKADIIGLSGLMTTSLDEMKEVAEEMR 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 823 RQGFTIPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVAALLSDTQRDDFVARTRKEYETVRIQHGRKKprTP 902
Cdd:COG1410 791 RRGLDIPVLIGGAALTRAYTAVKIAPAYDGAVVYAKDASRAVRVADKLLSKERREAFVAEIKAEYEKLRERHAARK--KK 868
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 903 PVTLEAARDNDFAfdwqAYTPPVAHRLGVQEVEA-SIETLRNYIDWTPFFMTWSLAGKYpriLEdevvGVEAQRLFKDAN 981
Cdd:COG1410 869 LLSLEEARSNVDS----DYPPPTPPFLGTRVLKDiPLAELVPYIDWTPFFQQWGLKGKY---LD----GEEARELFPDAQ 937
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 982 DMLDKLSAEKTLNPRGVVGLFPANRVGDDIEIYRDETrTHVINVSHHLRQQTEktgfANYCLADFVAPKLSGKADYIGAF 1061
Cdd:COG1410 938 AMLDRIIEEKWLTARAVYGYFPANSEGDDIEVYDDES-SEELARFHFPRQQRG----PNLCLADFVAPKESGERDYVGFF 1012
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 1062 AVTGGLEEDALADAFEAQHDDYNKIMVKALADRLAEAFAEYLHERVRKVyWGYAPNENLSNEELIRENYQGIRPAPGYPA 1141
Cdd:COG1410 1013 AVTAGIGIEELAAELEAAGDDYDAIMLHALADRLAEAFAEYLHERVRKE-WGYAPDEALTNEDLIKEKYRGIRPAPGYPA 1091
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|.
gi 446018192 1142 CPEHTEKATIWELLEVEKhTGMKLTESFAMWPGASVSGWYFSHPDSKYYAV 1192
Cdd:COG1410 1092 CPDHTEKRKLFDLLDAER-IGVTLTESFAMHPEASVSGIYFHHPEAKYFNV 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: 559.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 937 SIETLRNYIDWTPFFMTWSLAGKYPRILEDEVVGVEAQRLFKDANDMLDKLSAEKTLNPRGVVGLFPANRVGDDIEIYRD 1016
Cdd:pfam02965 1 DLAELVPYIDWTPFFQAWELKGKYPAILDDEVVGEEARKLFADAQAMLDRIIEEKWLTARGVVGFFPANSVGDDIEVYTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 1017 ETRTHVINVSHHLRQQTEKT-GFANYCLADFVAPKLSGKADYIGAFAVTGGLEEDALADAFEAQHDDYNKIMVKALADRL 1095
Cdd:pfam02965 81 ESRTEVLATFHTLRQQTEKPeGRPNLCLADFIAPKESGIADYIGAFAVTAGIGIEELAARFEAAHDDYSAIMVKALADRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 1096 AEAFAEYLHERVRKVYWGYAPNENLSNEELIRENYQGIRPAPGYPACPEHTEKATIWELLEVEKHTGMKLTESFAMWPGA 1175
Cdd:pfam02965 161 AEAFAEYLHERVRKELWGYAPDENLSNEDLIKEKYQGIRPAPGYPACPDHTEKFTLFDLLDAEENIGIRLTESFAMTPAA 240
|
250 260 270
....*....|....*....|....*....|...
gi 446018192 1176 SVSGWYFSHPDSKYYAVAQIQRDQVEDYARRKG 1208
Cdd:pfam02965 241 SVSGLYFAHPESRYFAVGKIGKDQVEDYAKRKG 273
|
|
| MeTr |
cd00740 |
MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent ... |
356-612 |
9.22e-140 |
|
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: 423.73 E-value: 9.22e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 356 FVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVENGAQIIDINMDEGMLDAEAAMVRFLNLIAGEPdiaRVPIMIDS 435
Cdd:cd00740 1 FLNIGERTNVTGSKKFRELIKAEDYDEALDVARQQVEGGAQILDLNVDYGGLDGVSAMKWLLNLLATEP---TVPLMLDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 436 SKWEVIEKGLKCIQGKGIVNSISMKEGVDAFIHHAKLLRRYGAAVVVMAFDEQGQADTRARKIEICRRAYKILTEEVGFP 515
Cdd:cd00740 78 TNWEVIEAGLKCCQGKCVVNSINLEDGEERFLKVARLAKEHGAAVVVLAFDEQGQAKTRDKKVEIAERAYEALTEFVGFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 516 PEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISGGVSNVSFSFrgNDPVREAIHAVFLYYAIRNGMDMG 595
Cdd:cd00740 158 PEDIIFDPLILPIATGIEEHRPYALETIDAIRMIKERLPAVKISLGVSNVSFGF--NPAAREALNSVFLYEAIKAGLDMA 235
|
250
....*....|....*..
gi 446018192 596 IVNAGQLAIYDDLPAEL 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 |
4.34e-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: 128.36 E-value: 4.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 657 WEVNKRLEYSLVKGITEFIEQDTEEARQQATRPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPFI 736
Cdd:smart01018 1 MPLLERLAEAIVDGDEEGVEELVEEALAEGVDPLEIINEGLIPGMNVVGDLFEAGEYFLPQVLMSAEAMKAAVAILKPLL 80
|
....
gi 446018192 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: 2702.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 1 MSSKVEQLRAQLNERILVLDGGMGTMIQSYRLNEADFRGERFADWPCDLKGNNDLLVLSKPEVIAAIHNAYFEAGADIIE 80
Cdd:PRK09490 4 MSSRLAQLRALLAERILVLDGAMGTMIQRYKLEEADYRGERFADWPCDLKGNNDLLVLTQPDVIEAIHRAYLEAGADIIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 81 TNTFNSTTIAMADYQMESLSAEINFAAAKLARACADEWTARTPEKPRYVAGVLGPTNRTASISPDVNDPAFRNITFDQLV 160
Cdd:PRK09490 84 TNTFNATTIAQADYGMESLVYELNFAAARLAREAADEWTAKTPDKPRFVAGVLGPTNRTASISPDVNDPGFRNVTFDELV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 161 AAYRESTKALVEGGADLILIETVFDTLNAKAAVFAVKTEFEALGVELPIMISGTITDASGRTLSGQTTEAFYNSLRHAEA 240
Cdd:PRK09490 164 AAYREQTRGLIEGGADLILIETIFDTLNAKAAIFAVEEVFEELGVRLPVMISGTITDASGRTLSGQTTEAFWNSLRHAKP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 241 LTFGLNCALGPDELRQYVQELSRIAECYVTAHPNAGLPNAFGEYDLDADTMAKQIREWAQAGFLNIVGGCCGTTPQHIAA 320
Cdd:PRK09490 244 LSIGLNCALGADELRPYVEELSRIADTYVSAHPNAGLPNAFGEYDETPEEMAAQIGEFAESGFLNIVGGCCGTTPEHIAA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 321 MSRAVEGLAPRKLPEIPVACRLSGLEPLNIGDDSLFVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVENGAQIIDI 400
Cdd:PRK09490 324 IAEAVAGLPPRKLPEIPVACRLSGLEPLNIDDDSLFVNVGERTNVTGSAKFARLIKEEDYDEALDVARQQVENGAQIIDI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 401 NMDEGMLDAEAAMVRFLNLIAGEPDIARVPIMIDSSKWEVIEKGLKCIQGKGIVNSISMKEGVDAFIHHAKLLRRYGAAV 480
Cdd:PRK09490 404 NMDEGMLDSEAAMVRFLNLIASEPDIARVPIMIDSSKWEVIEAGLKCIQGKGIVNSISLKEGEEKFIEHARLVRRYGAAV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 481 VVMAFDEQGQADTRARKIEICRRAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISG 560
Cdd:PRK09490 484 VVMAFDEQGQADTRERKIEICKRAYDILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKQNLPHAKISG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 561 GVSNVSFSFRGNDPVREAIHAVFLYYAIRNGMDMGIVNAGQLAIYDDLPAELRDAVEDVILNRRDDGTERLLELAEKYRG 640
Cdd:PRK09490 564 GVSNVSFSFRGNNPVREAIHAVFLYHAIKAGMDMGIVNAGQLAIYDDIPPELREAVEDVVLNRRPDATERLLEIAEKYRG 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 641 SKtDDTANAQQAEWRSWEVNKRLEYSLVKGITEFIEQDTEEARQQATRPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVK 720
Cdd:PRK09490 644 KG-GKKAKAEDLEWRSWPVEKRLEHALVKGITEFIEEDTEEARQQAARPLEVIEGPLMDGMNVVGDLFGEGKMFLPQVVK 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 721 SARVMKQAVAYLEPFIEASKEQG---KTNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVN 797
Cdd:PRK09490 723 SARVMKQAVAYLEPFIEAKKEGGtdrKSNGKILMATVKGDVHDIGKNIVGVVLQCNNYEVIDLGVMVPAEKILETAKEEN 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 798 ADLIGLSGLITPSLDEMVNVAKEMERQGFTIPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVAALLSDTQRD 877
Cdd:PRK09490 803 ADIIGLSGLITPSLDEMVHVAKEMERQGFTIPLLIGGATTSKAHTAVKIAPNYSGPVVYVTDASRAVGVVSSLLSDEQRD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 878 DFVARTRKEYETVRIQHGRKKPRTPPVTLEAARDNDFAFDWQAYTPPVAHRLGVQEVEA-SIETLRNYIDWTPFFMTWSL 956
Cdd:PRK09490 883 AYVAETRAEYEKVREQHARKKPRKPLLTLEAARANRFKIDWEAYTPPKPKFLGVQVFEDyDLAELREYIDWTPFFQTWEL 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 957 AGKYPRILEDEVVGVEAQRLFKDANDMLDKLSAEKTLNPRGVVGLFPANRVGDDIEIYRDETRTHVINVSHHLRQQTEKT 1036
Cdd:PRK09490 963 AGKYPAILEDEVVGEEARKLFADAQAMLDKIIAEKWLTARGVIGLFPANSVGDDIEVYTDESRTEVLATLHHLRQQTEKR 1042
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 1037 GFANYCLADFVAPKLSGKADYIGAFAVTGGLEEDALADAFEAQHDDYNKIMVKALADRLAEAFAEYLHERVRKVYWGYAP 1116
Cdd:PRK09490 1043 GRPNYCLADFVAPKESGKADYIGAFAVTAGLGEDELADRFEAAHDDYNAIMVKALADRLAEAFAEYLHERVRKEFWGYAP 1122
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 1117 NENLSNEELIRENYQGIRPAPGYPACPEHTEKATIWELLEVEKHTGMKLTESFAMWPGASVSGWYFSHPDSKYYAVAQIQ 1196
Cdd:PRK09490 1123 DENLSNEELIREKYQGIRPAPGYPACPDHTEKATLFDLLDAEKNTGMKLTESYAMWPGASVSGWYFSHPESKYFAVGKIG 1202
|
1210 1220
....*....|....*....|....*..
gi 446018192 1197 RDQVEDYARRKGMSVSDVERWLAPNLG 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: 2080.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 12 LNERILVLDGGMGTMIQSYRLNEADFRGErFADWPCDLKGNNDLLVLSKPEVIAAIHNAYFEAGADIIETNTFNSTTIAM 91
Cdd:TIGR02082 1 LNQRILVLDGAMGTQLQSANLTEADFRGA-FADCHRELKGNNDILNLTKPEVIATIHRAYFEAGADIIETNTFNSTTISQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 92 ADYQMESLSAEINFAAAKLARACADEWTaRTPEKPRYVAGVLGPTNRTASISPDVNDPAFRNITFDQLVAAYRESTKALV 171
Cdd:TIGR02082 80 ADYDLEDLIYDLNFKGAKLARAVADEFT-LTPEKPRFVAGSMGPTNKTATLSPDVERPGFRNVTYDELVDAYTEQAKGLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 172 EGGADLILIETVFDTLNAKAAVFAVKTEFEALGVELPIMISGTITDASGRTLSGQTTEAFYNSLRHAEALTFGLNCALGP 251
Cdd:TIGR02082 159 DGGVDLLLIETCFDTLNAKAALFAAETVFEEKGRELPIMISGTIVDTSGRTLSGQTIEAFLTSLEHAGIDMIGLNCALGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 252 DELRQYVQELSRIAECYVTAHPNAGLPNAFGEYDLDADTMAKQIREWAQAGFLNIVGGCCGTTPQHIAAMSRAVEGLAPR 331
Cdd:TIGR02082 239 DEMRPHLKHLSEHAEAYVSCHPNAGLPNAFGEYDLTPDELAKALADFAAEGGLNIVGGCCGTTPDHIRAIAEAVKNIKPR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 332 KLPEIPVACRLSGLEPLNIGDDSLFVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVENGAQIIDINMDEGMLDAEA 411
Cdd:TIGR02082 319 QRPVLYEPSRLSGLEAITIAQDSNFVNIGERTNVAGSKKFRRLIIAEDYDEALDIAKQQVENGAQILDINVDYGMLDGVA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 412 AMVRFLNLIAGEPDIARVPIMIDSSKWEVIEKGLKCIQGKGIVNSISMKEGVDAFIHHAKLLRRYGAAVVVMAFDEQGQA 491
Cdd:TIGR02082 399 AMKRFLNLLASEPDISTVPLMLDSSEWAVLEAGLKCIQGKCIVNSISLKDGEERFIETAKLIKEYGAAVVVMAFDEEGQA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 492 DTRARKIEICRRAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISGGVSNVSFSFRG 571
Cdd:TIGR02082 479 RTADRKIEICKRAYNILTEKVGFPPEDIIFDPNILTIATGIEEHRRYAINFIEAIRWIKEELPDAKISGGVSNVSFSFRG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 572 NDPVREAIHAVFLYYAIRNGMDMGIVNAGQLAIYDDLPAELRDAVEDVILNRRDDGTERLLELAEKYRGSKTDDTANAQQ 651
Cdd:TIGR02082 559 NPAAREAMHSVFLYHAIRAGMDMGIVNAGKILPYDDIDPELRQVVEDLILNRRREATEPLLELAQLYEGTTTKSSKEAQQ 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 652 AEWRSWEVNKRLEYSLVKGITEFIEQDTEEARQQATRPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAY 731
Cdd:TIGR02082 639 AEWRNLPVEERLEYALVKGEREGIEEDLEEARKKLTRPLEIIEGPLMDGMKVVGDLFGSGKMFLPQVVKSARVMKKAVAY 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 732 LEPFIEASKEQGKTNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADLIGLSGLITPSL 811
Cdd:TIGR02082 719 LEPHMEKEKSEDSSKGKIVLATVKGDVHDIGKNIVGVVLSCNGYEVVDLGVMVPIEKILEAAKDHNADVIGLSGLITPSL 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 812 DEMVNVAKEMERQGFTIPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVAALLSDTQRDDFVARTRKEYETVR 891
Cdd:TIGR02082 799 DEMKEVAEEMNRRGITIPLLIGGAATSKTHTAVKIAPIYKGPVVYVLDASRAVTVMDTLMSAKRKDTENGRIKEEYDTAR 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 892 IQHGRKKPRTPPVTLEAARDNDFAFDWQ-AYTPPVAHRLGVQEVEAS-IETLRNYIDWTPFFMTWSLAGKYPRILEDEVV 969
Cdd:TIGR02082 879 EKHGEQRSKRIAASEQAARKNVFAPDWSdDIEPPAPPFWGTQIVEASdIAELRPYIDWTPFFLQWQLRGKYPKILGDEYE 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 970 GVEAQRLFKDANDMLDKLSAEKTLNPRGVVGLFPANRVGDDIEIYRDETR-THVINVS----HHLRQQTEKtgfaNYCLA 1044
Cdd:TIGR02082 959 GLEAQKLFPDANEMLDKLSAENLLHARGVYGYFPAQSVGDDIEIYTDETVeTHPIATVrylfHFPRQQSGR----YLCLA 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 1045 DFVAPKLSGKADYIGAFAVTGGLEEDALADAFEAQHDDYNKIMVKALADRLAEAFAEYLHERVRKVYWGYAPNENLSNEE 1124
Cdd:TIGR02082 1035 DFIAPKASGIVDYIGAFAVTAGFGAEELADKLEAQHDDYDYIMVKAIADRLAEAFAEYLHRRVRKELWGYAAEEPLSNED 1114
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446018192 1125 LIRENYQGIRPAPGYPACPEHTEKATIWELLEVEKhTGMKLTESFAMWPGASVSGWYFSHPDSKYYAV 1192
Cdd:TIGR02082 1115 LLKLRYQGIRPAPGYPACPDHTEKATMFELLEPER-IGVRLTESLAMHPEQSVSGLYFAHPEAKYFAV 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: 1767.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 23 MGTMIQSYRLNEADFRGERFADWPCDLKGNNDLLVLSKPEVIAAIHNAYFEAGADIIETNTFNSTTIAMADYQMESLSAE 102
Cdd:COG1410 1 MGTMIQLLKLRELDADGAMFTDLQLDLKGNNDLLGLTGPNEILEIHRPELEAGADIIETNTGADAAITAADGAAEALLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 103 INFAAAKLARACADEWTARTPEKPRYVAGVLGPTNRTASISPDVNDPAFRNITFDQLVAAYRESTKALVEGGADLILIET 182
Cdd:COG1410 81 YNGAAAALALEAAAAAAAAAAAAARAVAGAPGPTGGTASPGPDVPGLGFRNFDFDELVEAYAEAGLGLGGGGADLLLTET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 183 VFDTLNAKAAVFAVKTEFEALGVELPIMISGTITDASGRTLSGQTTEAFYNSLRHAEALTFGLNCALGPDELRQYVQELS 262
Cdd:COG1410 161 IFDTLNAAAAAAAAAAAAEEEGVPIPVMVTGTITDGSGRTLSGQTAEAFLESLGHAAPGSNGLNCALGAEELRPYLEELS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 263 RIAECYVTAHPNAGLPNAFGEYDLDADTMAKQIREWAQAGFLNIVGGCCGTTPQHIAAMSRAVEGLAPRKlPEIPVACRL 342
Cdd:COG1410 241 RIPPSAVSNAPNAGLPNGFGEYDETPEEMAAALAEFAEEGGVNIVGGCCGTTPEHIRAIAEAVAGLKPRP-REKPPPAVL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 343 SGLEPLNIGDDSLFVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVENGAQIIDINMDEGMLDAEAAMVRFLNLIAG 422
Cdd:COG1410 320 SGLEPVPIGQDSPFVNIGERTNVTGSKKFRELILEGDYDEALEVAREQVEAGAQILDVNVDEPGRDEVAAMVRFLNLLAS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 423 EpdiARVPIMIDSSKWEVIEKGLKCIQGKGIVNSISMKEGVDAFIHHAKLLRRYGAAVVVMAFDEQGQADTRARKIEICR 502
Cdd:COG1410 400 E---VRVPLMIDSSKPEVIEAGLKCYQGKPIVNSISLEEGEERFEEVAPLAKKYGAAVVVLAIDEEGQADTAERKLEIAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 503 RAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISGGVSNVSFSFRGNdpVREAIHAV 582
Cdd:COG1410 477 RIYDLAVEEYGFPPEDIIFDPLVFTVATGIEEHRNYAVETIEAIRLIKEELPGAKTSLGVSNVSFGLPGN--VREALNSV 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 583 FLYYAIRNGMDMGIVNAGQLAIYDDLPAELRDAVEDVILNRRDDGTERLLELAEKYRGSKtddtANAQQAEWRSWEVNKR 662
Cdd:COG1410 555 FLYHAIKAGLDMAIVNPGQLEPYDDIPPELRELAEDVLLNRRPDALERLIELFEGVKGAK----AKKADLEWRELPVEER 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 663 LEYSLVKGITEFIEQDTEEARQQATRPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPFIEASKEQ 742
Cdd:COG1410 631 LKHAIVKGIKEGIEEDTEEALAEGARPLEIINGPLMPGMNVVGDLFGAGKMFLPQVLKSAEVMKAAVAYLEPFMEKEKGE 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 743 GKTNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADLIGLSGLITPSLDEMVNVAKEME 822
Cdd:COG1410 711 SSSKGKIVLATVKGDVHDIGKNIVGVVLENNGYEVIDLGVMVPAEKILEAAKEHKADIIGLSGLMTTSLDEMKEVAEEMR 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 823 RQGFTIPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVAALLSDTQRDDFVARTRKEYETVRIQHGRKKprTP 902
Cdd:COG1410 791 RRGLDIPVLIGGAALTRAYTAVKIAPAYDGAVVYAKDASRAVRVADKLLSKERREAFVAEIKAEYEKLRERHAARK--KK 868
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 903 PVTLEAARDNDFAfdwqAYTPPVAHRLGVQEVEA-SIETLRNYIDWTPFFMTWSLAGKYpriLEdevvGVEAQRLFKDAN 981
Cdd:COG1410 869 LLSLEEARSNVDS----DYPPPTPPFLGTRVLKDiPLAELVPYIDWTPFFQQWGLKGKY---LD----GEEARELFPDAQ 937
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 982 DMLDKLSAEKTLNPRGVVGLFPANRVGDDIEIYRDETrTHVINVSHHLRQQTEktgfANYCLADFVAPKLSGKADYIGAF 1061
Cdd:COG1410 938 AMLDRIIEEKWLTARAVYGYFPANSEGDDIEVYDDES-SEELARFHFPRQQRG----PNLCLADFVAPKESGERDYVGFF 1012
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 1062 AVTGGLEEDALADAFEAQHDDYNKIMVKALADRLAEAFAEYLHERVRKVyWGYAPNENLSNEELIRENYQGIRPAPGYPA 1141
Cdd:COG1410 1013 AVTAGIGIEELAAELEAAGDDYDAIMLHALADRLAEAFAEYLHERVRKE-WGYAPDEALTNEDLIKEKYRGIRPAPGYPA 1091
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|.
gi 446018192 1142 CPEHTEKATIWELLEVEKhTGMKLTESFAMWPGASVSGWYFSHPDSKYYAV 1192
Cdd:COG1410 1092 CPDHTEKRKLFDLLDAER-IGVTLTESFAMHPEASVSGIYFHHPEAKYFNV 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: 1006.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 6 EQLRAQLNERILVLDGGMGTMIQSYRLNEADFRGErfadwpcdlKGNNDLLVLSKPEVIAAIHNAYFEAGADIIETNTFN 85
Cdd:COG0646 4 AALLELLKERILILDGAMGTMLQAYGLTEGDFRGE---------KGCNELLNLTRPDVIREIHRAYLEAGADIIETNTFG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 86 STTIAMADYQMESLSAEINFAAAKLARACADEWTartpEKPRYVAGVLGPTNRTASispdvndpAFRNITFDQLVAAYRE 165
Cdd:COG0646 75 ANRIKLADYGLEDRVYEINRAAARLAREAADEFS----DRPRFVAGSIGPTGKLLS--------PLGNITFDELVEAYRE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 166 STKALVEGGADLILIETVFDTLNAKAAVFAVKTEFEALGVELPIMISGTItDASGRTLSGQTTEAFYNSLRHAEALTFGL 245
Cdd:COG0646 143 QAEGLIEGGVDLLLIETIFDTLEAKAAIFAAREAFEELGRDLPVMVSGTF-DASGRTLSGQTPEAFATSLEHLGPDAIGL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 246 NCALGPDELRQYVQELSRIAECYVTAHPNAGLPNAFGE---YDLDADTMAKQIREWAQAGFLNIVGGCCGTTPQHIAAMS 322
Cdd:COG0646 222 NCALGPDEMRPHVEELSEVADTPVSAYPNAGLPNLVGGrtvYDETPEEMAEYAEEFAEAGGVNIVGGCCGTTPEHIRAIA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 323 RAVEGLAPRKLPEIPVACRLSGLEPLNIGDDSLFVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVENGAQIIDINM 402
Cdd:COG0646 302 EAVKGLPPRKRPPPPPALRLSGLEPLTITQDSLFVNVGERTNVTGSKKFARLILEGDYDAALAVARQQVEAGAQVIDVNM 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 403 DEGMLDAEAAMVRFLNLIAGEPDIARVPIMIDSSKWEVIEKGLKCIQGKGIVNSISMKEGVDAFIHHAKLLRRYGAAVVV 482
Cdd:COG0646 382 DEGMLDGEAAMVEFLNLIASEPDIPRVPDMIDSSKWEVIEAGLKGVQGKGIVNSISLKEGEEKFLELAKLVRRYGAAVVV 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 483 MAFDEQGQADTRARKIEICRRAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISGGV 562
Cdd:COG0646 462 MAFDEEGQADTAERKVEICARAYDLLTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKLNLPHALVSGGV 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 563 SNVSFSFRGNDPVREAIHAVFLYYAIRNGMDMGIVNAGQLAIYDDLPAELRDAVEDVILNRRDDGTERLLELAEKYRGsK 642
Cdd:COG0646 542 SNVSFSFRGNNPVREAIHAVFLYHAIAAGMDMGIVNAGQLAIYEEIPEELLLLVEDVVLNRREDATERLLEIAEEVKG-A 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 643 TDDTANAQQAEWRSWEVNKRLEYSLVKGITEFIEQDTEEARQQATRPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSA 722
Cdd:COG0646 621 GKAAEEEAEEERREEEEERLLELLLVGGIEIDEEDDEEAALLLAALELIIIELLLGGGMVVGGLGGGGGKLLLVVVVKAV 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 723 RVMKQAVAYLEPFIEASKE-QGKTNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADLI 801
Cdd:COG0646 701 VKKKVAVALLKPEEEEKKKgGGKGGGVVVGVVVKVVVDDVDIIIVVVVVVVNNGIVVLVVVVIVVVALEAAAAAEAAVIL 780
|
810 820
....*....|....*....|....*....
gi 446018192 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: 559.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 937 SIETLRNYIDWTPFFMTWSLAGKYPRILEDEVVGVEAQRLFKDANDMLDKLSAEKTLNPRGVVGLFPANRVGDDIEIYRD 1016
Cdd:pfam02965 1 DLAELVPYIDWTPFFQAWELKGKYPAILDDEVVGEEARKLFADAQAMLDRIIEEKWLTARGVVGFFPANSVGDDIEVYTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 1017 ETRTHVINVSHHLRQQTEKT-GFANYCLADFVAPKLSGKADYIGAFAVTGGLEEDALADAFEAQHDDYNKIMVKALADRL 1095
Cdd:pfam02965 81 ESRTEVLATFHTLRQQTEKPeGRPNLCLADFIAPKESGIADYIGAFAVTAGIGIEELAARFEAAHDDYSAIMVKALADRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 1096 AEAFAEYLHERVRKVYWGYAPNENLSNEELIRENYQGIRPAPGYPACPEHTEKATIWELLEVEKHTGMKLTESFAMWPGA 1175
Cdd:pfam02965 161 AEAFAEYLHERVRKELWGYAPDENLSNEDLIKEKYQGIRPAPGYPACPDHTEKFTLFDLLDAEENIGIRLTESFAMTPAA 240
|
250 260 270
....*....|....*....|....*....|...
gi 446018192 1176 SVSGWYFSHPDSKYYAVAQIQRDQVEDYARRKG 1208
Cdd:pfam02965 241 SVSGLYFAHPESRYFAVGKIGKDQVEDYAKRKG 273
|
|
| MeTr |
cd00740 |
MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent ... |
356-612 |
9.22e-140 |
|
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: 423.73 E-value: 9.22e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 356 FVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVENGAQIIDINMDEGMLDAEAAMVRFLNLIAGEPdiaRVPIMIDS 435
Cdd:cd00740 1 FLNIGERTNVTGSKKFRELIKAEDYDEALDVARQQVEGGAQILDLNVDYGGLDGVSAMKWLLNLLATEP---TVPLMLDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 436 SKWEVIEKGLKCIQGKGIVNSISMKEGVDAFIHHAKLLRRYGAAVVVMAFDEQGQADTRARKIEICRRAYKILTEEVGFP 515
Cdd:cd00740 78 TNWEVIEAGLKCCQGKCVVNSINLEDGEERFLKVARLAKEHGAAVVVLAFDEQGQAKTRDKKVEIAERAYEALTEFVGFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 516 PEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISGGVSNVSFSFrgNDPVREAIHAVFLYYAIRNGMDMG 595
Cdd:cd00740 158 PEDIIFDPLILPIATGIEEHRPYALETIDAIRMIKERLPAVKISLGVSNVSFGF--NPAAREALNSVFLYEAIKAGLDMA 235
|
250
....*....|....*..
gi 446018192 596 IVNAGQLAIYDDLPAEL 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 |
6.31e-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: 409.73 E-value: 6.31e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 659 VNKRLEYSLVKGITEFIEQDTEEARQQATRPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPFIEA 738
Cdd:cd02069 1 VEERLKHALVKGIRDGIEEDTEEARQQYARPLEIINGPLMDGMKVVGDLFGAGKMFLPQVLKSARVMKAAVAYLEPYMEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 739 SKEQGKTNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADLIGLSGLITPSLDEMVNVA 818
Cdd:cd02069 81 EKGENSSKGKIVLATVKGDVHDIGKNLVGVILSNNGYEVIDLGVMVPIEKILEAAKEHKADIIGLSGLLVPSLDEMVEVA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446018192 819 KEMERQGFTIPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVAALL 871
Cdd:cd02069 161 EEMNRRGIKIPLLIGGAATSRKHTAVKIAPEYDGPVVYVKDASRALGVANKLL 213
|
|
| S-methyl_trans |
pfam02574 |
Homocysteine S-methyltransferase; This is a family of related homocysteine ... |
17-325 |
6.70e-93 |
|
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: 299.07 E-value: 6.70e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 17 LVLDGGMGTMIQSYRLNEADfrgerfADWpcdlkgNNDLLVlsKPEVIAAIHNAYFEAGADIIETNTFNSTTIAMAD-YQ 95
Cdd:pfam02574 1 LILDGGMGTELQRRGLDLTE------PLW------SNELLT--RPEIIREIHRDYLEAGADIIETNTYQASPIKLAEgLE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 96 MESLSAEINFAAAKLARACADEWtartpekprYVAGVLGPTNRTASISPDvndpafrnITFDQLVAAYRESTKALVEGGA 175
Cdd:pfam02574 67 EEEAVYELNRAAVRLAREAADEY---------FVAGSIGPYGATLSDGYG--------LSFDELVDFHREQLEALLDGGV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 176 DLILIETVFDTLNAKAAVFAVKTEfealgVELPIMISGTITDAsGRTLSGQTTEAFYNSLRHA-EALTFGLNCALgPDEL 254
Cdd:pfam02574 130 DLLLFETIPDLLEAKAALELLAEE-----PDLPVWISFTIEDG-TRLRSGTTLEAAVAALLHAtGPLAVGVNCAL-PEEM 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446018192 255 RQYVQELSRIAECYVTAHpnaglPNAFGE-YDLDADTMAKQIREWAQAGfLNIVGGCCGTTPQHIAAMSRAV 325
Cdd:pfam02574 203 LPLLKELAKDAPTPVSVY-----PNSTGEvYDLTPEEWAEYAEGWLEAG-ANIIGGCCGTTPEHIRAIAEAL 268
|
|
| Pterin_bind |
pfam00809 |
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ... |
360-598 |
1.64e-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: 252.98 E-value: 1.64e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 360 GERTNVTGSAKFKRLIKEEkYSEALDVARQQVENGAQIIDINMDEG-----MLDAEAAMVRFLNLIAGEPDIARVPIMID 434
Cdd:pfam00809 1 MGILNVTPDSFSDGGRFLD-LDKALAHARRMVEEGADIIDIGGESTrpgaeRVDGEEEMERVLPVLAALRDEADVPISVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 435 SSKWEVIEKGLKCiqGKGIVNSISMKEGvdaFIHHAKLLRRYGAAVVVMAFD--------EQGQADTRARKIEICRRAYK 506
Cdd:pfam00809 80 TTKAEVAEAALKA--GADIINDISGGDG---DPEMAELAAEYGAAVVVMHMDgtpktmqeNEQQYEDVVEEVERFLRARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 507 ILTEEVGFPPEDIIFDPNIFavATGIEEHNNYAQDFIGACEDIKrELPhalISGGVSNVSFSFRGN---DPVREAIHAVF 583
Cdd:pfam00809 155 AAAEEAGVPPEDIILDPGIG--FGKTEEHNLELLRTLDELRVIL-GVP---VLLGVSRKSFIGRGLplgGEERDAGTAAF 228
|
250
....*....|....*
gi 446018192 584 LYYAIRNGMDMGIVN 598
Cdd:pfam00809 229 LALAIAAGADIVRVH 243
|
|
| Pterin_binding |
cd00423 |
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and ... |
356-612 |
4.37e-68 |
|
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: 229.85 E-value: 4.37e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 356 FVNVGErTNVTGSaKFKRLIKEEKYSEALDVARQQVENGAQIIDINMDEG--------MLDAEAAMVRFLNLIAGEPDia 427
Cdd:cd00423 1 TLIMGI-LNVTPD-SFSDGGKFLSLDKALEHARRMVEEGADIIDIGGESTrpgaepvsVEEELERVIPVLRALAGEPD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 428 rVPIMIDSSKWEVIEKGLKCiqGKGIVNSISMKEGVDAfihHAKLLRRYGAAVVVMAFDEQGQ--------ADTRARKIE 499
Cdd:cd00423 77 -VPISVDTFNAEVAEAALKA--GADIINDVSGGRGDPE---MAPLAAEYGAPVVLMHMDGTPQtmqnnpyyADVVDEVVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 500 ICRRAYKILTeEVGFPPEDIIFDPNIFAVATgiEEHNNYAQDFIGACedikRELPHALISGGVSNVSFSFR---GNDPVR 576
Cdd:cd00423 151 FLEERVEAAT-EAGIPPEDIILDPGIGFGKT--EEHNLELLRRLDAF----RELPGLPLLLGVSRKSFLGDllsVGPKDR 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 446018192 577 EAIHAVFLYYAIRNGMDMGIVNAgQLAIYDDLPAEL 612
Cdd:cd00423 224 LAGTAAFLAAAILNGADIVRVHD-VKELRDAIKVAE 258
|
|
| PRK08645 |
PRK08645 |
bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; ... |
8-330 |
7.73e-58 |
|
bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; Reviewed
Pssm-ID: 236321 [Multi-domain] Cd Length: 612 Bit Score: 211.63 E-value: 7.73e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 8 LRAQLNERILVLDGGMGTMIQSYRLneadfrgerfadwpcDLKGNNDLLVLSKPEVIAAIHNAYFEAGADIIETNTFNST 87
Cdd:PRK08645 4 LLERLKERVLIADGAMGTLLYSRGV---------------PLDRCFEELNLSHPELILRIHREYIEAGADVIQTNTFGAN 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 88 TIAMADYQMESLSAEINFAAAKLaracadewtARTP-EKPRYVAGVLGPTNRTASISPdvndpafrnITFDQLVAAYRES 166
Cdd:PRK08645 69 RIKLKRYGLEDKVKEINRAAVRL---------AREAaGDDVYVAGTIGPIGGRGPLGD---------ISLEEIRREFREQ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 167 TKALVEGGADLILIETVFDTLNAKAAVFAVKTEfealgVELPIMISGTITDAsGRTLSGQTTEAFYNSLRHAEALTFGLN 246
Cdd:PRK08645 131 IDALLEEGVDGLLLETFYDLEELLLALEAAREK-----TDLPIIAQVAFHED-GVTQNGTSLEEALKELVAAGADVVGLN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 247 CALGPDELRQYVQELSRIAECYVTAHPNAGLPNAFGE---YDLDADTMAKQIREWAQAGfLNIVGGCCGTTPQHIAAMSR 323
Cdd:PRK08645 205 CGLGPYHMLEALERIPIPENAPLSAYPNAGLPEYVDGryvYSANPEYFAEYALEFVEQG-VRLIGGCCGTTPEHIRAMAR 283
|
....*..
gi 446018192 324 AVEGLAP 330
Cdd:PRK08645 284 ALKGLKP 290
|
|
| corrinoid_protein_B12-BD |
cd02070 |
B12 binding domain of corrinoid proteins. A family of small methanogenic corrinoid proteins ... |
666-839 |
1.41e-49 |
|
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: 174.35 E-value: 1.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 666 SLVKGITEFIEQDTEEARQQATRPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPFIEASKEQGKt 745
Cdd:cd02070 4 AIVDGDEEETVELVKKALEAGIDPQDIIEEGLAPGMDIVGDKYEEGEIFVPELLMAADAMKAGLDLLKPLLGKSKSAKK- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 746 nGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADLIGLSGLITPSLDEMVNVAKEMERQG 825
Cdd:cd02070 83 -GKVVIGTVEGDIHDIGKNLVATMLEANGFEVIDLGRDVPPEEFVEAVKEHKPDILGLSALMTTTMGGMKEVIEALKEAG 161
|
170
....*....|....*.
gi 446018192 826 FT--IPLLIGGATTSK 839
Cdd:cd02070 162 LRdkVKVMVGGAPVNQ 177
|
|
| MtbC1 |
COG5012 |
Methanogenic corrinoid protein MtbC1 [Energy production and conversion]; |
658-835 |
9.74e-45 |
|
Methanogenic corrinoid protein MtbC1 [Energy production and conversion];
Pssm-ID: 444036 [Multi-domain] Cd Length: 219 Bit Score: 161.21 E-value: 9.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 658 EVNKRLEYSLVKGITEFIEQDTEEARQQATRPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPFIe 737
Cdd:COG5012 9 ELLESLADAVLEGDEDEALELVAEALAAGMDPEEIILDGLAPGMREVGELWEEGEIFVPEEHLAAAAMKAGLEILKPLL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 738 asKEQGKTNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADLIGLSGLITPSLDEMVNV 817
Cdd:COG5012 88 --AEEGGRKGKVVIGTVEGDLHDIGKNIVADMLRAAGFEVIDLGADVPPEEFVEAAKEEKPDIVGLSALLTTTMPAMKEL 165
|
170 180
....*....|....*....|
gi 446018192 818 AKEMERQGFT--IPLLIGGA 835
Cdd:COG5012 166 IEALREAGLRdkVKVIVGGA 185
|
|
| B12-binding |
cd02067 |
B12 binding domain (B12-BD). This domain binds different cobalamid derivates, like B12 ... |
748-869 |
4.57e-43 |
|
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: 152.66 E-value: 4.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 748 KMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADLIGLSGLITPSLDEMVNVAKEMERQGFT 827
Cdd:cd02067 1 KVVIATVGGDGHDIGKNIVARALRDAGFEVIDLGVDVPPEEIVEAAKEEDADAIGLSGLLTTHMTLMKEVIEELKEAGLD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446018192 828 -IPLLIGGATTSKAHTAVKieqnYSGPTVYVQNASRTVGVVAA 869
Cdd:cd02067 81 dIPVLVGGAIVTRDFKFLK----EIGVDAYFGPATEAVEVLKK 119
|
|
| pyl_corrinoid |
TIGR02370 |
methyltransferase cognate corrinoid proteins, Methanosarcina family; This model describes a ... |
667-861 |
2.10e-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: 142.25 E-value: 2.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 667 LVKGITEFIEQDTEEARQQA----TRPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPFIEASKEQ 742
Cdd:TIGR02370 2 LAKAIFEGEEDDVVEGAQKAldagIDPIELIEKGLMAGMGVVGKLFEDGELFLPHVMMSADAMLAGIKVLTPEMEKAVET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 743 GKTnGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADLIGLSGLITPSLDEMVNVAKEME 822
Cdd:TIGR02370 82 EVL-GKVVCGVAEGDVHDIGKNIVVTMLRANGFDVIDLGRDVPIDTVVEKVKKEKPLMLTGSALMTTTMYGQKDINDKLK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446018192 823 RQGF--TIPLLIGGATTSKAHtAVKIeqnysGPTVYVQNAS 861
Cdd:TIGR02370 161 EEGYrdSVKFMVGGAPVTQDW-ADKI-----GADVYGENAS 195
|
|
| MHT1 |
COG2040 |
Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) [Amino acid transport and ... |
11-329 |
4.57e-38 |
|
Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) [Amino acid transport and metabolism];
Pssm-ID: 441643 [Multi-domain] Cd Length: 301 Bit Score: 144.95 E-value: 4.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 11 QLNERILVLDGGMGTmiqsyrlnEADFRGerfadwpCDLkgNNDL----LVLSKPEVIAAIHNAYFEAGADIIETNTFNS 86
Cdd:COG2040 8 LLMGRILLLDGGMGT--------ELERRG-------GDL--LDPLwsafALLEAPELVRAVHRDYFAAGADVITTNSYQA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 87 TT--IAMADYQMESLsAEINFAAAKLARACADEWTARtpeKPRYVAGVLGPtnRTASISPDvndpafRNITFDQLVAAYR 164
Cdd:COG2040 71 SPdgLAELGYSAEEA-ERLNRRAVALAREARDEYTPG---PPVLVAGSVGP--YGDEYRPD------YGLSAEEAEAYHR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 165 ESTKALVEGGADLILIETVFDTLNAKAAVFAVKtefealGVELPIMISGTITDAsGRTLSGQT-TEAFYNSLRHAEALTF 243
Cdd:COG2040 139 PRIEALAEAGVDLLAAETIPSLAEAIAIARAAA------EAGKPVWISFTVEDD-GRLRSGEPlAEAIAAVDTDPGPAAV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 244 GLNCAlGPDELRQYVQELSRIAECYVTAHPNAG------LPNAFGEYDLDADTMAKQIREWAQAGfLNIVGGCCGTTPQH 317
Cdd:COG2040 212 GVNCS-HPEHFEAALEALAAWTGRPIGVYANAGemsdaeLKTWGGLDDGDPEELAEQAAEWVAAG-ARIIGGCCGTGPRH 289
|
330
....*....|..
gi 446018192 318 IAAMSRAVEGLA 329
Cdd:COG2040 290 IAAIARALRAAG 301
|
|
| B12-binding_2 |
smart01018 |
B12 binding domain; Cobalamin-dependent methionine synthase is a large modular protein that ... |
657-740 |
4.34e-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: 128.36 E-value: 4.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 657 WEVNKRLEYSLVKGITEFIEQDTEEARQQATRPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPFI 736
Cdd:smart01018 1 MPLLERLAEAIVDGDEEGVEELVEEALAEGVDPLEIINEGLIPGMNVVGDLFEAGEYFLPQVLMSAEAMKAAVAILKPLL 80
|
....
gi 446018192 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 ... |
748-868 |
2.85e-34 |
|
B12 binding domain (B12-BD). Most of the members bind different cobalamid derivates, like B12 (adenosylcobamide) or methylcobalamin or methyl-Co(III) 5-hydroxybenzimidazolylcobamide. This domain is found in several enzymes, such as glutamate mutase, methionine synthase and methylmalonyl-CoA mutase. Cobalamin undergoes a conformational change on binding the protein; the dimethylbenzimidazole group, which is coordinated to the cobalt in the free cofactor, moves away from the corrin and is replaced by a histidine contributed by the protein. The sequence Asp-X-His-X-X-Gly, which contains this histidine ligand, is conserved in many cobalamin-binding proteins. Not all members of this family contain the conserved binding motif.
Pssm-ID: 239016 [Multi-domain] Cd Length: 125 Bit Score: 127.89 E-value: 2.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 748 KMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADLIGLSGLITPSLDEMVNVAKEMERQGFT 827
Cdd:cd02065 1 KVLGATVGGDVHDIGKNIVAIALRDNGFEVIDLGVDVPPEEIVEAAKEEDADVVGLSALSTTHMEAMKLVIEALKELGID 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 446018192 828 IPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVA 868
Cdd:cd02065 81 IPVVVGGAHPTADPEEPKVDAVVIGEGEYAGPALLEVEGIA 121
|
|
| mmuM |
PRK09485 |
homocysteine methyltransferase; Provisional |
8-327 |
3.97e-31 |
|
homocysteine methyltransferase; Provisional
Pssm-ID: 181899 [Multi-domain] Cd Length: 304 Bit Score: 124.97 E-value: 3.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 8 LRAQLNER-ILVLDGGMGTmiqsyrlnEADFRGerfadwpCDLkgNNDL----LVLSKPEVIAAIHNAYFEAGADIIETN 82
Cdd:PRK09485 4 FKELLAQGpVLILDGALAT--------ELEARG-------CDL--NDSLwsakVLLENPELIYQVHLDYFRAGADCAITA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 83 TFNSTTIAMAD--------YQMESLSAEInfaaaklARACADEWTARTPekprYVAGVLGPTNrtASISpdvNDPAFR-- 152
Cdd:PRK09485 67 SYQATFQGFAArglseaeaEELIRRSVEL-------AKEARDEFWAEKP----LVAGSVGPYG--AYLA---DGSEYRgd 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 153 -NITFDQLVAAYRESTKALVEGGADLILIETVFDTLNAKAAVFAVKTEFEalgvELPIMISGTITDasGRTLSGQTteaf 231
Cdd:PRK09485 131 yGLSEEELQDFHRPRIEALAEAGADLLACETIPNLDEAEALVELLKEEFP----GVPAWLSFTLRD--GTHISDGT---- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 232 ynSLRHAEAL--------TFGLNCAlGPDELRQYVQELSRIAECYVTAHPNAGlpnafGEYDL---------DADTMAKQ 294
Cdd:PRK09485 201 --PLAEAAALlaaspqvvAVGVNCT-APELVTAAIAALRAVTDKPLVVYPNSG-----EVYDAvtktwhgpaDDASLGEL 272
|
330 340 350
....*....|....*....|....*....|...
gi 446018192 295 IREWAQAGfLNIVGGCCGTTPQHIAAMSRAVEG 327
Cdd:PRK09485 273 APEWYAAG-ARLIGGCCRTTPEDIAALAAALKT 304
|
|
| PRK07535 |
PRK07535 |
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase; Validated |
359-599 |
6.86e-30 |
|
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase; Validated
Pssm-ID: 181022 [Multi-domain] Cd Length: 261 Bit Score: 119.96 E-value: 6.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 359 VGERTNvtGSAK-FKRLIKEEKYSEALDVARQQVENGAQIIDINMDEGMLDAEAAMVRFLNLIAGEPDiarVPIMIDSSK 437
Cdd:PRK07535 4 IGERIN--GTRKsIAEAIEAKDAAFIQKLALKQAEAGADYLDVNAGTAVEEEPETMEWLVETVQEVVD---VPLCIDSPN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 438 WEVIEKGLKCIQGKGIVNSISM-KEGVDAFIhhaKLLRRYGAAVVVMAFDEQGQADTRARKIEICRRAYKILtEEVGFPP 516
Cdd:PRK07535 79 PAAIEAGLKVAKGPPLINSVSAeGEKLEVVL---PLVKKYNAPVVALTMDDTGIPKDAEDRLAVAKELVEKA-DEYGIPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 517 EDIIFDPNIFAVATGieehNNYAQDFIGACEDIKRELPHALISGGVSNVSFsfrgNDPVREAIHAVFLYYAIRNGMDMGI 596
Cdd:PRK07535 155 EDIYIDPLVLPLSAA----QDAGPEVLETIRRIKELYPKVHTTCGLSNISF----GLPNRKLINRAFLVMAMGAGMDSAI 226
|
...
gi 446018192 597 VNA 599
Cdd:PRK07535 227 LDP 229
|
|
| PRK07534 |
PRK07534 |
betaine--homocysteine S-methyltransferase; |
54-331 |
2.72e-29 |
|
betaine--homocysteine S-methyltransferase;
Pssm-ID: 236045 [Multi-domain] Cd Length: 336 Bit Score: 120.24 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 54 DLLVLSKPEVIAAIHNAYFEAGADIIETNTFNSTTIAMADYQMESLSAEINFAAAKLARACADEwtartPEKPRYVAGVL 133
Cdd:PRK07534 37 ELWNEDHPDNITALHQGFVDAGSDIILTNSFGGTAARLKLHDAQDRVHELNRAAAEIAREVADK-----AGRKVIVAGSV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 134 GPTNrtasispDVNDPAFRnITFDQLVAAYRESTKALVEGGADLILIETVFDTLNAKAAVFAVKTefealgVELPIMISG 213
Cdd:PRK07534 112 GPTG-------EIMEPMGA-LTHALAVEAFHEQAEGLKAGGADVLWVETISAPEEIRAAAEAAKL------AGMPWCGTM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 214 TItDASGRTLSGQTTEAFYN---SLRHAeALTFGLNCALGPDELRQYVQELSRIA-ECYVTAHPNAGLPNAFG---EYDL 286
Cdd:PRK07534 178 SF-DTAGRTMMGLTPADLADlveKLGEP-PLAFGANCGVGASDLLRTVLGFTAQGpERPIIAKGNAGIPKYVDghiHYDG 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446018192 287 DADTMAKQIREWAQAGfLNIVGGCCGTTPQHIAAMSRAVEGlAPR 331
Cdd:PRK07534 256 TPELMAEYAVLARDAG-ARIIGGCCGTMPEHLAAMRAALDA-RPR 298
|
|
| B12-binding |
pfam02310 |
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ... |
747-835 |
5.71e-20 |
|
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: 86.61 E-value: 5.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 747 GKMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADLIGLSGLITPSLDEMVNVAKEMERQGF 826
Cdd:pfam02310 1 GKVVVATVGGDLHPLGLNYVAAALRAAGFEVIILGANVPPEDIVAAARDEKPDVVGLSALMTTTLPGAKELIRLLKGIRP 80
|
....*....
gi 446018192 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 |
7.44e-20 |
|
B12 binding domain; This B12 binding domain is found in methionine synthase EC:2.1.1.13, and other shorter proteins that bind to B12. This domain is always found to the N-terminus of pfam02310. The structure of this domain is known, it is a 4 helix bundle. Many of the conserved residues in this domain are involved in B12 binding, such as those in the MXXVG motif.
Pssm-ID: 460617 [Multi-domain] Cd Length: 68 Bit Score: 84.45 E-value: 7.44e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 663 LEYSLVKGITEFIEQDTEEARqqATRPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYL 732
Cdd:pfam02607 1 LLEALLEGDEEAAEELLEEAL--EIDPEEIIEDLLIPGMDEVGELWEAGEIFVPQEHLAAEAMKAALAVL 68
|
|
| PLN02489 |
PLN02489 |
homocysteine S-methyltransferase |
17-325 |
1.08e-15 |
|
homocysteine S-methyltransferase
Pssm-ID: 215269 Cd Length: 335 Bit Score: 80.06 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 17 LVLDGGMGTMIQSyrlNEADFrgerfadwpcdlkgnND-----LLVLSKPEVIAAIHNAYFEAGADIIETNTFNSTTIA- 90
Cdd:PLN02489 23 AVIDGGFATELER---HGADL---------------NDplwsaKCLITSPHLIRKVHLDYLEAGADIIITASYQATIQGf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 91 ----MADYQMESL---SAEINFAAAKLARACADEWTARTPEK-----PRYVAgvlgptnrtASI-------------SPD 145
Cdd:PLN02489 85 esrgLSREESETLlrkSVEIACEARDIFWDKCQKGSTSRPGRelsyrPILVA---------ASIgsygayladgseySGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 146 VNDpafrNITFDQLVAAYRESTKALVEGGADLILIETVFDTLNAKAAVfavkTEFEALGVELPIMISGTITDASgRTLSG 225
Cdd:PLN02489 156 YGP----SVTLEKLKDFHRRRLQVLAEAGPDLIAFETIPNKLEAQAYV----ELLEEENIKIPAWISFNSKDGV-NVVSG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 226 qttEAFYNSLRHAEALT----FGLNCAlGPdelrQYVQELSRIAEcYVTAHPNAGLPNAFGEYDLDA-----------DT 290
Cdd:PLN02489 227 ---DSLLECASIADSCKkvvaVGINCT-PP----RFIHGLILSIR-KVTSKPIVVYPNSGETYDGEAkewvestgvsdED 297
|
330 340 350
....*....|....*....|....*....|....*
gi 446018192 291 MAKQIREWAQAGfLNIVGGCCGTTPQHIAAMSRAV 325
Cdd:PLN02489 298 FVSYVNKWRDAG-ASLIGGCCRTTPNTIRAISKAL 331
|
|
| DHPS |
cd00739 |
DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional ... |
348-525 |
4.94e-08 |
|
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: 55.69 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 348 LNIGDDSlFVNVGERTNVTgsakfkrlikeekysEALDVARQQVENGAQIIDI-----NMDEGMLDAEAAMVRFLNLIAG 422
Cdd:cd00739 7 LNVTPDS-FSDGGRFLSLD---------------KAVAHAEKMIAEGADIIDIggestRPGADPVSVEEELERVIPVLEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 423 EPDIARVPIMIDSSKWEVIEKGLKciQGKGIVNSISmkeGVDAFIHHAKLLRRYGAAVVVM-----------------AF 485
Cdd:cd00739 71 LRGELDVLISVDTFRAEVARAALE--AGADIINDVS---GGSDDPAMLEVAAEYGAPLVLMhmrgtpktmqenpyyedVV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446018192 486 DEQGqADTRARkIEICRRAykilteevGFPPEDIIFDPNI 525
Cdd:cd00739 146 DEVL-SFLEAR-LEAAESA--------GVARNRIILDPGI 175
|
|
| Sbm |
COG2185 |
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ... |
748-834 |
5.13e-07 |
|
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and metabolism];
Pssm-ID: 441788 [Multi-domain] Cd Length: 134 Bit Score: 50.14 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 748 KMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADLIGLSglitpSLDEMVN-----VAKEME 822
Cdd:COG2185 12 RVLLAKPGLDGHDRGAKVIARALRDAGFEVIYLGLFQTPEEIVRAAIEEDADVIGVS-----SLDGGHLelvpeLIELLK 86
|
90
....*....|...
gi 446018192 823 RQGFT-IPLLIGG 834
Cdd:COG2185 87 EAGAGdILVVVGG 99
|
|
| PRK02261 |
PRK02261 |
methylaspartate mutase subunit S; Provisional |
748-806 |
6.84e-05 |
|
methylaspartate mutase subunit S; Provisional
Pssm-ID: 179400 [Multi-domain] Cd Length: 137 Bit Score: 44.17 E-value: 6.84e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446018192 748 KMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADLIGLSGL 806
Cdd:PRK02261 5 TVVLGVIGADCHAVGNKILDRALTEAGFEVINLGVMTSQEEFIDAAIETDADAILVSSL 63
|
|
| MM_CoA_mut_B12_BD |
cd02071 |
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), ... |
748-834 |
4.05e-04 |
|
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), which initiates the conversion of succinyl CoA and methylmalonyl CoA by forming an adenosyl radical, which then undergoes a rearrangement exchanging a hydrogen atom with a group attached to a neighboring carbon atom. This family is present in both mammals and bacteria. Bacterial members are heterodimers and involved in the fermentation of pyruvate to propionate. Mammalian members are homodimers and responsible for the conversion of odd-chain fatty acids and branched-chain amino acids via propionyl CoA to succinyl CoA for further degradation.
Pssm-ID: 239022 [Multi-domain] Cd Length: 122 Bit Score: 41.42 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446018192 748 KMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADLIGLSGLITPSLDEMVNVAKEMERQGFT 827
Cdd:cd02071 1 RILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRQTPEEIVEAAIQEDVDVIGLSSLSGGHMTLFPEVIELLRELGAG 80
|
....*...
gi 446018192 828 -IPLLIGG 834
Cdd:cd02071 81 dILVVGGG 88
|
|
| Glm_B12_BD |
cd02072 |
B12 binding domain of glutamate mutase (Glm). Glutamate mutase catalysis the conversion of (S) ... |
748-806 |
4.81e-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: 41.30 E-value: 4.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446018192 748 KMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADLIGLSGL 806
Cdd:cd02072 1 TIVLGVIGSDCHAVGNKILDHAFTEAGFNVVNLGVLSPQEEFIDAAIETDADAILVSSL 59
|
|
| |
