|
Name |
Accession |
Description |
Interval |
E-value |
| metH |
TIGR02082 |
5-methyltetrahydrofolate--homocysteine methyltransferase; This family represents ... |
26-1169 |
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: 1412.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 26 VVVADGGMGTMLQAAEPSLDDFQ--------QLEGCNEVLNVTRPDIVRSVHQEYFDAGVDCVETNTFGANLAALGEYDI 97
Cdd:TIGR02082 5 ILVLDGAMGTQLQSANLTEADFRgafadchrELKGNNDILNLTKPEVIATIHRAYFEAGADIIETNTFNSTTISQADYDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 98 PERIAELSEAGARIARETADDCAARDGRQRWVLGSIGPGTKLPTLG---------HIRYADLRDAYQRNAEGLIAGGADA 168
Cdd:TIGR02082 85 EDLIYDLNFKGAKLARAVADEFTLTPEKPRFVAGSMGPTNKTATLSpdverpgfrNVTYDELVDAYTEQAKGLLDGGVDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 169 LLVETAQDLLQTKAAVLGARRAVAATGVDLPLVVQ-VTVETTGTMLLGSEIGAALTALEPLGIDMIGLNCATGPAEMSEH 247
Cdd:TIGR02082 165 LLIETCFDTLNAKAALFAAETVFEEKGRELPIMISgTIVDTSGRTLSGQTIEAFLTSLEHAGIDMIGLNCALGPDEMRPH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 248 LRYLSQHATIPISCMPNAGLPVLGKDgahYPLGPAELADAHQTFIGEFGLSLIGGCCGTTPEHLRQVVERVRGLTPGARD 327
Cdd:TIGR02082 245 LKHLSEHAEAYVSCHPNAGLPNAFGE---YDLTPDELAKALADFAAEGGLNIVGGCCGTTPDHIRAIAEAVKNIKPRQRP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 328 PRPEPGAASLYQTVPFRQDASYLAIGERTNANGSKKFREAMLEGRWEDCVELAREQIREGAHLLDLCVDYVGRDGAADMS 407
Cdd:TIGR02082 322 VLYEPSRLSGLEAITIAQDSNFVNIGERTNVAGSKKFRRLIIAEDYDEALDIAKQQVENGAQILDINVDYGMLDGVAAMK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 408 ELAGRLAT---ASTLPIVLDSTEPAVLEAGLERLGGRAVINSVNYEDGdgpDSRFAKVTRMAVEHGAALMALTIDERGQA 484
Cdd:TIGR02082 402 RFLNLLASepdISTVPLMLDSSEWAVLEAGLKCIQGKCIVNSISLKDG---EERFIETAKLIKEYGAAVVVMAFDEEGQA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 485 RTPEDKVAIAERIIADLTGNWGVAESDIIIDCLTFTICTGQEESRRDGVHTIEAIRELKRRHPQVQTTLGLSNISFGL-- 562
Cdd:TIGR02082 479 RTADRKIEICKRAYNILTEKVGFPPEDIIFDPNILTIATGIEEHRRYAINFIEAIRWIKEELPDAKISGGVSNVSFSFrg 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 563 NPAARLVLNSVFLDECVKAGLDSAIVHAAKILPIARIEDEQVQVALDLIHDRRREGYDPLQRFLELFEGVDAKSMRAGKT 642
Cdd:TIGR02082 559 NPAAREAMHSVFLYHAIRAGMDMGIVNAGKILPYDDIDPELRQVVEDLILNRRREATEPLLELAQLYEGTTTKSSKEAQQ 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 643 EELLALPLEERLRRRIVDGERKGLEADLDEALTT-RPALEIVNDTLLEGMKTVGELFGSGQMQLPFVLQSAEVMKTAVAH 721
Cdd:TIGR02082 639 AEWRNLPVEERLEYALVKGEREGIEEDLEEARKKlTRPLEIIEGPLMDGMKVVGDLFGSGKMFLPQVVKSARVMKKAVAY 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 722 LEPHMEKSD--DEGKGTIVLATVRGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVTAILDAAEEHRADVIGMSGLLVKST 799
Cdd:TIGR02082 719 LEPHMEKEKseDSSKGKIVLATVKGDVHDIGKNIVGVVLSCNGYEVVDLGVMVPIEKILEAAKDHNADVIGLSGLITPSL 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 800 VIMKENLEELNQRGMaaDYPVILGGAALTRAYVEQDLHEVYQGEVRYARDAFEGLRLMDALIAVKRGVP--GATLPELKK 877
Cdd:TIGR02082 799 DEMKEVAEEMNRRGI--TIPLLIGGAATSKTHTAVKIAPIYKGPVVYVLDASRAVTVMDTLMSAKRKDTenGRIKEEYDT 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 878 RRVAA-----RPAALPQEDTEEPVGRSATATDVPLPTAPFLGTRVIKGIPLKDYAAWLDEDALFKgQWGLKGSR-SGAGP 951
Cdd:TIGR02082 877 AREKHgeqrsKRIAASEQAARKNVFAPDWSDDIEPPAPPFWGTQIVEASDIAELRPYIDWTPFFL-QWQLRGKYpKILGD 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 952 DYEELLETEGRPRLRGWLDRLHTDNLLEAAVVYGYFPCHAEGQDLVILDEEGKE-------RTRFTFPRQRRGRRLCLAD 1024
Cdd:TIGR02082 956 EYEGLEAQKLFPDANEMLDKLSAENLLHARGVYGYFPAQSVGDDIEIYTDETVEthpiatvRYLFHFPRQQSGRYLCLAD 1035
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 1025 FFRPAESGETDVVALQAVTVGSRVSGATAELFAADAYRDYLELHGLSVQLAEALAEFWHARVRAEL-GIGGSDPAALAGM 1103
Cdd:TIGR02082 1036 FIAPKASGIVDYIGAFAVTAGFGAEELADKLEAQHDDYDYIMVKAIADRLAEAFAEYLHRRVRKELwGYAAEEPLSNEDL 1115
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818443726 1104 FRTEYQGCRYSLGYPACPDLEDRAKIAELLQPERIGVTLSEEFQLHPEQSTDAIILHHPEANYFNA 1169
Cdd:TIGR02082 1116 LKLRYQGIRPAPGYPACPDHTEKATMFELLEPERIGVRLTESLAMHPEQSVSGLYFAHPEAKYFAV 1181
|
|
| MetH2 |
COG1410 |
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; ... |
26-1169 |
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: 1396.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 26 VVVADGGMGTMLQAAEPSLDDFQQLEGCNEVLNVTRPDIVRSVHQEYFDAGVDCVETNTFGANLAALGEYDIPERIAELs 105
Cdd:COG1410 12 ELDADGAMFTDLQLDLKGNNDLLGLTGPNEILEIHRPELEAGADIIETNTGADAAITAADGAAEALLAEYNGAAAALAL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 106 EAGARIARETADDCAARDGRQRWVLGSIGPGTKLPTLGHIRYADLRDAYQRNAEGLIAGGADALLVETAQDLLQTKAAVL 185
Cdd:COG1410 91 EAAAAAAAAAAAAARAVAGAPGPTGGTASPGPDVPGLGFRNFDFDELVEAYAEAGLGLGGGGADLLLTETIFDTLNAAAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 186 GARRAVAATGVDLPLVVQVTVETTGTMLLGSEIGAALTALEPLGIDMIGLNCATGPAEMSEHLRYLSQHATIPISCMPNA 265
Cdd:COG1410 171 AAAAAAAAEEEGVPIPVMVTGTITDGSGRTLSGQTAEAFLESLGHAAPGSNGLNCALGAEELRPYLEELSRIPPSAVSNA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 266 GLPVLGKDGAHYPLGPAELADAHQTFIGEFGLSLIGGCCGTTPEHLRQVVERVRGLTPGARdPRPEPGAASLYQTVPFRQ 345
Cdd:COG1410 251 PNAGLPNGFGEYDETPEEMAAALAEFAEEGGVNIVGGCCGTTPEHIRAIAEAVAGLKPRPR-EKPPPAVLSGLEPVPIGQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 346 DASYLAIGERTNANGSKKFREAMLEGRWEDCVELAREQIREGAHLLDLCVDYVGRDGAADMSELAGRLATASTLPIVLDS 425
Cdd:COG1410 330 DSPFVNIGERTNVTGSKKFRELILEGDYDEALEVAREQVEAGAQILDVNVDEPGRDEVAAMVRFLNLLASEVRVPLMIDS 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 426 TEPAVLEAGLERLGGRAVINSVNYEDGDgpdSRFAKVTRMAVEHGAALMALTIDERGQARTPEDKVAIAERIIADLTGNW 505
Cdd:COG1410 410 SKPEVIEAGLKCYQGKPIVNSISLEEGE---ERFEEVAPLAKKYGAAVVVLAIDEEGQADTAERKLEIAERIYDLAVEEY 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 506 GVAESDIIIDCLTFTICTGQEESRRDGVHTIEAIRELKRRHPQVQTTLGLSNISFGLNPAARLVLNSVFLDECVKAGLDS 585
Cdd:COG1410 487 GFPPEDIIFDPLVFTVATGIEEHRNYAVETIEAIRLIKEELPGAKTSLGVSNVSFGLPGNVREALNSVFLYHAIKAGLDM 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 586 AIVHAAKILPIARIEDEQVQVALDLIHDRRRegyDPLQRFLELFEGVDAKSMRAgKTEELLALPLEERLRRRIVDGERKG 665
Cdd:COG1410 567 AIVNPGQLEPYDDIPPELRELAEDVLLNRRP---DALERLIELFEGVKGAKAKK-ADLEWRELPVEERLKHAIVKGIKEG 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 666 LEADLDEALTTRP-ALEIVNDTLLEGMKTVGELFGSGQMQLPFVLQSAEVMKTAVAHLEPHMEKSDD--EGKGTIVLATV 742
Cdd:COG1410 643 IEEDTEEALAEGArPLEIINGPLMPGMNVVGDLFGAGKMFLPQVLKSAEVMKAAVAYLEPFMEKEKGesSSKGKIVLATV 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 743 RGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVTAILDAAEEHRADVIGMSGLLVKSTVIMKENLEELNQRGMaaDYPVIL 822
Cdd:COG1410 723 KGDVHDIGKNIVGVVLENNGYEVIDLGVMVPAEKILEAAKEHKADIIGLSGLMTTSLDEMKEVAEEMRRRGL--DIPVLI 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 823 GGAALTRAYVEQDLHEVYQGEVRYARDAFEGLRLMDALIAVKRGVPGATLPELKKRRVAARPAALPQEDTEEPVGRSATA 902
Cdd:COG1410 801 GGAALTRAYTAVKIAPAYDGAVVYAKDASRAVRVADKLLSKERREAFVAEIKAEYEKLRERHAARKKKLLSLEEARSNVD 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 903 TDVPLPTAPFLGTRVIKGIPLKDYAAWLDEDALFKgQWGLKGSRSgagpDYEEllETEGRPRLRGWLDRLHTDNLLEAAV 982
Cdd:COG1410 881 SDYPPPTPPFLGTRVLKDIPLAELVPYIDWTPFFQ-QWGLKGKYL----DGEE--ARELFPDAQAMLDRIIEEKWLTARA 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 983 VYGYFPCHAEGQDLVILDEEG-KERTRFTFPRQRRGRRLCLADFFRPAESGETDVVALQAVTVGSRVSGATAELFAADAY 1061
Cdd:COG1410 954 VYGYFPANSEGDDIEVYDDESsEELARFHFPRQQRGPNLCLADFVAPKESGERDYVGFFAVTAGIGIEELAAELEAAGDD 1033
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 1062 RDYLELHGLSVQLAEALAEFWHARVRAELGIGGSDPAALAGMFRTEYQGCRYSLGYPACPDLEDRAKIAELLQPERIGVT 1141
Cdd:COG1410 1034 YDAIMLHALADRLAEAFAEYLHERVRKEWGYAPDEALTNEDLIKEKYRGIRPAPGYPACPDHTEKRKLFDLLDAERIGVT 1113
|
1130 1140
....*....|....*....|....*...
gi 818443726 1142 LSEEFQLHPEQSTDAIILHHPEANYFNA 1169
Cdd:COG1410 1114 LTESFAMHPEASVSGIYFHHPEAKYFNV 1141
|
|
| metH |
PRK09490 |
B12-dependent methionine synthase; Provisional |
26-1168 |
0e+00 |
|
B12-dependent methionine synthase; Provisional
Pssm-ID: 236539 [Multi-domain] Cd Length: 1229 Bit Score: 689.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 26 VVVADGGMGTMLQAAEPSLDDF---------QQLEGCNEVLNVTRPDIVRSVHQEYFDAGVDCVETNTFGANLAALGEYD 96
Cdd:PRK09490 19 ILVLDGAMGTMIQRYKLEEADYrgerfadwpCDLKGNNDLLVLTQPDVIEAIHRAYLEAGADIIETNTFNATTIAQADYG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 97 IPERIAELSEAGARIARETADDCAARD-GRQRWVLGSIGPGTKLPTLG---------HIRYADLRDAYQRNAEGLIAGGA 166
Cdd:PRK09490 99 MESLVYELNFAAARLAREAADEWTAKTpDKPRFVAGVLGPTNRTASISpdvndpgfrNVTFDELVAAYREQTRGLIEGGA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 167 DALLVETAQDLLQTKAAVLGARRAVAATGVDLPLVVQVTV-ETTGTMLLGSEIGA---ALTALEPLGIdmiGLNCATGPA 242
Cdd:PRK09490 179 DLILIETIFDTLNAKAAIFAVEEVFEELGVRLPVMISGTItDASGRTLSGQTTEAfwnSLRHAKPLSI---GLNCALGAD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 243 EMSEHLRYLSQHATIPISCMPNAGLP-VLGKdgahYPLGPAELADahqtFIGEFG----LSLIGGCCGTTPEHLRQVVER 317
Cdd:PRK09490 256 ELRPYVEELSRIADTYVSAHPNAGLPnAFGE----YDETPEEMAA----QIGEFAesgfLNIVGGCCGTTPEHIAAIAEA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 318 VRGLTPGARdPRPEPgAASLYQTVPF--RQDASYLAIGERTNANGSKKFREAMLEGRWEDCVELAREQIREGAHLLDLCV 395
Cdd:PRK09490 328 VAGLPPRKL-PEIPV-ACRLSGLEPLniDDDSLFVNVGERTNVTGSAKFARLIKEEDYDEALDVARQQVENGAQIIDINM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 396 DYVGRDGAADMSELAGRLAT---ASTLPIVLDSTEPAVLEAGLERLGGRAVINSVNYEDGDGPDSRFAKVTRmavEHGAA 472
Cdd:PRK09490 406 DEGMLDSEAAMVRFLNLIASepdIARVPIMIDSSKWEVIEAGLKCIQGKGIVNSISLKEGEEKFIEHARLVR---RYGAA 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 473 LMALTIDERGQARTPEDKVAIAERIIADLTGNWGVAESDIIIDCLTFTICTGQEESRRDGVHTIEAIRELKRRHPQVQTT 552
Cdd:PRK09490 483 VVVMAFDEQGQADTRERKIEICKRAYDILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKQNLPHAKIS 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 553 LGLSNISF---GLNPAaRLVLNSVFLDECVKAGLDSAIVHAAKILPIARIEDEQVQVALDLIHDRRRegyDPLQRFLELF 629
Cdd:PRK09490 563 GGVSNVSFsfrGNNPV-REAIHAVFLYHAIKAGMDMGIVNAGQLAIYDDIPPELREAVEDVVLNRRP---DATERLLEIA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 630 EGVdaKSMRAGKTEELLALPLEERLRRRI----VDGERKGLEADLDEA--LTTRPaLEIVNDTLLEGMKTVGELFGSGQM 703
Cdd:PRK09490 639 EKY--RGKGGKKAKAEDLEWRSWPVEKRLehalVKGITEFIEEDTEEArqQAARP-LEVIEGPLMDGMNVVGDLFGEGKM 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 704 QLPFVLQSAEVMKTAVAHLEPHMEK-----SDDEGKGTIVLATVRGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVTAIL 778
Cdd:PRK09490 716 FLPQVVKSARVMKQAVAYLEPFIEAkkeggTDRKSNGKILMATVKGDVHDIGKNIVGVVLQCNNYEVIDLGVMVPAEKIL 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 779 DAAEEHRADVIGMSGLLVKSTVIMKENLEELNQRGMaaDYPVILGGAALTRAYVEQDLHEVYQGEVRYardafeglrLMD 858
Cdd:PRK09490 796 ETAKEENADIIGLSGLITPSLDEMVHVAKEMERQGF--TIPLLIGGATTSKAHTAVKIAPNYSGPVVY---------VTD 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 859 ALIAVkrGVPGATLPELKKRRVAARPAALPQEDTEEPVGRSATATDVPL----------------PTAP-FLGTRVIKGI 921
Cdd:PRK09490 865 ASRAV--GVVSSLLSDEQRDAYVAETRAEYEKVREQHARKKPRKPLLTLeaaranrfkidweaytPPKPkFLGVQVFEDY 942
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 922 PLKDYAAWLDEDALFKgQWGLKGSrsgagpdYEELLE-----TEGRpRL----RGWLDRLHTDNLLEAAVVYGYFPCHAE 992
Cdd:PRK09490 943 DLAELREYIDWTPFFQ-TWELAGK-------YPAILEdevvgEEAR-KLfadaQAMLDKIIAEKWLTARGVIGLFPANSV 1013
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 993 GQDLVILDEEGKERTRFTFP--RQ---RRGR-RLCLADFFRPAESGETDVVALQAVTVGSRVSgATAELFAA--DAYRDY 1064
Cdd:PRK09490 1014 GDDIEVYTDESRTEVLATLHhlRQqteKRGRpNYCLADFVAPKESGKADYIGAFAVTAGLGED-ELADRFEAahDDYNAI 1092
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 1065 LeLHGLSVQLAEALAEFWHARVRAELGIGGSDPA-ALAGMFRTEYQGCRYSLGYPACPDLEDRAKIAELLQPE-RIGVTL 1142
Cdd:PRK09490 1093 M-VKALADRLAEAFAEYLHERVRKEFWGYAPDENlSNEELIREKYQGIRPAPGYPACPDHTEKATLFDLLDAEkNTGMKL 1171
|
1210 1220
....*....|....*....|....*.
gi 818443726 1143 SEEFQLHPEQSTDAIILHHPEANYFN 1168
Cdd:PRK09490 1172 TESYAMWPGASVSGWYFSHPESKYFA 1197
|
|
| MeTr |
cd00740 |
MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent ... |
349-603 |
1.85e-113 |
|
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: 353.24 E-value: 1.85e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 349 YLAIGERTNANGSKKFREAMLEGRWEDCVELAREQIREGAHLLDLCVDYVGRDGAADMSELAGRLATASTLPIVLDSTEP 428
Cdd:cd00740 1 FLNIGERTNVTGSKKFRELIKAEDYDEALDVARQQVEGGAQILDLNVDYGGLDGVSAMKWLLNLLATEPTVPLMLDSTNW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 429 AVLEAGLERLGGRAVINSVNYEDGDgpdSRFAKVTRMAVEHGAALMALTIDERGQARTPEDKVAIAERIIADLTGNWGVA 508
Cdd:cd00740 81 EVIEAGLKCCQGKCVVNSINLEDGE---ERFLKVARLAKEHGAAVVVLAFDEQGQAKTRDKKVEIAERAYEALTEFVGFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 509 ESDIIIDCLTFTICTGQEESRRDGVHTIEAIRELKRRHPQVQTTLGLSNISFGLNPAARLVLNSVFLDECVKAGLDSAIV 588
Cdd:cd00740 158 PEDIIFDPLILPIATGIEEHRPYALETIDAIRMIKERLPAVKISLGVSNVSFGFNPAAREALNSVFLYEAIKAGLDMAIV 237
|
250
....*....|....*
gi 818443726 589 HAAKILPIARIEDEQ 603
Cdd:cd00740 238 NAGKLAPIEDIPEEL 252
|
|
| S-methyl_trans |
pfam02574 |
Homocysteine S-methyltransferase; This is a family of related homocysteine ... |
27-318 |
3.55e-86 |
|
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: 280.20 E-value: 3.55e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 27 VVADGGMGTMLQAAEPSLDDfqqLEGCNEVLnvTRPDIVRSVHQEYFDAGVDCVETNTFGANLAALGE-YDIPERIAELS 105
Cdd:pfam02574 1 LILDGGMGTELQRRGLDLTE---PLWSNELL--TRPEIIREIHRDYLEAGADIIETNTYQASPIKLAEgLEEEEAVYELN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 106 EAGARIARETADDcaardgrqRWVLGSIGPGTKLPTLG-HIRYADLRDAYQRNAEGLIAGGADALLVETAQDLLQTKAAV 184
Cdd:pfam02574 76 RAAVRLAREAADE--------YFVAGSIGPYGATLSDGyGLSFDELVDFHREQLEALLDGGVDLLLFETIPDLLEAKAAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 185 lgarrAVAATGVDLPLVVQVTVETTGTMLLGSEIGAALTALEPL-GIDMIGLNCATgPAEMSEHLRYLSQHATIPISCMP 263
Cdd:pfam02574 148 -----ELLAEEPDLPVWISFTIEDGTRLRSGTTLEAAVAALLHAtGPLAVGVNCAL-PEEMLPLLKELAKDAPTPVSVYP 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 818443726 264 NAGlpvlgkdGAHYPLGPAELADAHQTFIgEFGLSLIGGCCGTTPEHLRQVVERV 318
Cdd:pfam02574 222 NST-------GEVYDLTPEEWAEYAEGWL-EAGANIIGGCCGTTPEHIRAIAEAL 268
|
|
| B12-binding_2 |
smart01018 |
B12 binding domain; Cobalamin-dependent methionine synthase is a large modular protein that ... |
655-730 |
1.24e-26 |
|
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: 104.47 E-value: 1.24e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818443726 655 RRRIVDGERKGLEADLDEALTT-RPALEIVNDTLLEGMKTVGELFGSGQMQLPFVLQSAEVMKTAVAHLEPHMEKSD 730
Cdd:smart01018 8 AEAIVDGDEEGVEELVEEALAEgVDPLEIINEGLIPGMNVVGDLFEAGEYFLPQVLMSAEAMKAAVAILKPLLEKEK 84
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| metH |
TIGR02082 |
5-methyltetrahydrofolate--homocysteine methyltransferase; This family represents ... |
26-1169 |
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: 1412.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 26 VVVADGGMGTMLQAAEPSLDDFQ--------QLEGCNEVLNVTRPDIVRSVHQEYFDAGVDCVETNTFGANLAALGEYDI 97
Cdd:TIGR02082 5 ILVLDGAMGTQLQSANLTEADFRgafadchrELKGNNDILNLTKPEVIATIHRAYFEAGADIIETNTFNSTTISQADYDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 98 PERIAELSEAGARIARETADDCAARDGRQRWVLGSIGPGTKLPTLG---------HIRYADLRDAYQRNAEGLIAGGADA 168
Cdd:TIGR02082 85 EDLIYDLNFKGAKLARAVADEFTLTPEKPRFVAGSMGPTNKTATLSpdverpgfrNVTYDELVDAYTEQAKGLLDGGVDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 169 LLVETAQDLLQTKAAVLGARRAVAATGVDLPLVVQ-VTVETTGTMLLGSEIGAALTALEPLGIDMIGLNCATGPAEMSEH 247
Cdd:TIGR02082 165 LLIETCFDTLNAKAALFAAETVFEEKGRELPIMISgTIVDTSGRTLSGQTIEAFLTSLEHAGIDMIGLNCALGPDEMRPH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 248 LRYLSQHATIPISCMPNAGLPVLGKDgahYPLGPAELADAHQTFIGEFGLSLIGGCCGTTPEHLRQVVERVRGLTPGARD 327
Cdd:TIGR02082 245 LKHLSEHAEAYVSCHPNAGLPNAFGE---YDLTPDELAKALADFAAEGGLNIVGGCCGTTPDHIRAIAEAVKNIKPRQRP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 328 PRPEPGAASLYQTVPFRQDASYLAIGERTNANGSKKFREAMLEGRWEDCVELAREQIREGAHLLDLCVDYVGRDGAADMS 407
Cdd:TIGR02082 322 VLYEPSRLSGLEAITIAQDSNFVNIGERTNVAGSKKFRRLIIAEDYDEALDIAKQQVENGAQILDINVDYGMLDGVAAMK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 408 ELAGRLAT---ASTLPIVLDSTEPAVLEAGLERLGGRAVINSVNYEDGdgpDSRFAKVTRMAVEHGAALMALTIDERGQA 484
Cdd:TIGR02082 402 RFLNLLASepdISTVPLMLDSSEWAVLEAGLKCIQGKCIVNSISLKDG---EERFIETAKLIKEYGAAVVVMAFDEEGQA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 485 RTPEDKVAIAERIIADLTGNWGVAESDIIIDCLTFTICTGQEESRRDGVHTIEAIRELKRRHPQVQTTLGLSNISFGL-- 562
Cdd:TIGR02082 479 RTADRKIEICKRAYNILTEKVGFPPEDIIFDPNILTIATGIEEHRRYAINFIEAIRWIKEELPDAKISGGVSNVSFSFrg 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 563 NPAARLVLNSVFLDECVKAGLDSAIVHAAKILPIARIEDEQVQVALDLIHDRRREGYDPLQRFLELFEGVDAKSMRAGKT 642
Cdd:TIGR02082 559 NPAAREAMHSVFLYHAIRAGMDMGIVNAGKILPYDDIDPELRQVVEDLILNRRREATEPLLELAQLYEGTTTKSSKEAQQ 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 643 EELLALPLEERLRRRIVDGERKGLEADLDEALTT-RPALEIVNDTLLEGMKTVGELFGSGQMQLPFVLQSAEVMKTAVAH 721
Cdd:TIGR02082 639 AEWRNLPVEERLEYALVKGEREGIEEDLEEARKKlTRPLEIIEGPLMDGMKVVGDLFGSGKMFLPQVVKSARVMKKAVAY 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 722 LEPHMEKSD--DEGKGTIVLATVRGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVTAILDAAEEHRADVIGMSGLLVKST 799
Cdd:TIGR02082 719 LEPHMEKEKseDSSKGKIVLATVKGDVHDIGKNIVGVVLSCNGYEVVDLGVMVPIEKILEAAKDHNADVIGLSGLITPSL 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 800 VIMKENLEELNQRGMaaDYPVILGGAALTRAYVEQDLHEVYQGEVRYARDAFEGLRLMDALIAVKRGVP--GATLPELKK 877
Cdd:TIGR02082 799 DEMKEVAEEMNRRGI--TIPLLIGGAATSKTHTAVKIAPIYKGPVVYVLDASRAVTVMDTLMSAKRKDTenGRIKEEYDT 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 878 RRVAA-----RPAALPQEDTEEPVGRSATATDVPLPTAPFLGTRVIKGIPLKDYAAWLDEDALFKgQWGLKGSR-SGAGP 951
Cdd:TIGR02082 877 AREKHgeqrsKRIAASEQAARKNVFAPDWSDDIEPPAPPFWGTQIVEASDIAELRPYIDWTPFFL-QWQLRGKYpKILGD 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 952 DYEELLETEGRPRLRGWLDRLHTDNLLEAAVVYGYFPCHAEGQDLVILDEEGKE-------RTRFTFPRQRRGRRLCLAD 1024
Cdd:TIGR02082 956 EYEGLEAQKLFPDANEMLDKLSAENLLHARGVYGYFPAQSVGDDIEIYTDETVEthpiatvRYLFHFPRQQSGRYLCLAD 1035
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 1025 FFRPAESGETDVVALQAVTVGSRVSGATAELFAADAYRDYLELHGLSVQLAEALAEFWHARVRAEL-GIGGSDPAALAGM 1103
Cdd:TIGR02082 1036 FIAPKASGIVDYIGAFAVTAGFGAEELADKLEAQHDDYDYIMVKAIADRLAEAFAEYLHRRVRKELwGYAAEEPLSNEDL 1115
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818443726 1104 FRTEYQGCRYSLGYPACPDLEDRAKIAELLQPERIGVTLSEEFQLHPEQSTDAIILHHPEANYFNA 1169
Cdd:TIGR02082 1116 LKLRYQGIRPAPGYPACPDHTEKATMFELLEPERIGVRLTESLAMHPEQSVSGLYFAHPEAKYFAV 1181
|
|
| MetH2 |
COG1410 |
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; ... |
26-1169 |
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: 1396.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 26 VVVADGGMGTMLQAAEPSLDDFQQLEGCNEVLNVTRPDIVRSVHQEYFDAGVDCVETNTFGANLAALGEYDIPERIAELs 105
Cdd:COG1410 12 ELDADGAMFTDLQLDLKGNNDLLGLTGPNEILEIHRPELEAGADIIETNTGADAAITAADGAAEALLAEYNGAAAALAL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 106 EAGARIARETADDCAARDGRQRWVLGSIGPGTKLPTLGHIRYADLRDAYQRNAEGLIAGGADALLVETAQDLLQTKAAVL 185
Cdd:COG1410 91 EAAAAAAAAAAAAARAVAGAPGPTGGTASPGPDVPGLGFRNFDFDELVEAYAEAGLGLGGGGADLLLTETIFDTLNAAAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 186 GARRAVAATGVDLPLVVQVTVETTGTMLLGSEIGAALTALEPLGIDMIGLNCATGPAEMSEHLRYLSQHATIPISCMPNA 265
Cdd:COG1410 171 AAAAAAAAEEEGVPIPVMVTGTITDGSGRTLSGQTAEAFLESLGHAAPGSNGLNCALGAEELRPYLEELSRIPPSAVSNA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 266 GLPVLGKDGAHYPLGPAELADAHQTFIGEFGLSLIGGCCGTTPEHLRQVVERVRGLTPGARdPRPEPGAASLYQTVPFRQ 345
Cdd:COG1410 251 PNAGLPNGFGEYDETPEEMAAALAEFAEEGGVNIVGGCCGTTPEHIRAIAEAVAGLKPRPR-EKPPPAVLSGLEPVPIGQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 346 DASYLAIGERTNANGSKKFREAMLEGRWEDCVELAREQIREGAHLLDLCVDYVGRDGAADMSELAGRLATASTLPIVLDS 425
Cdd:COG1410 330 DSPFVNIGERTNVTGSKKFRELILEGDYDEALEVAREQVEAGAQILDVNVDEPGRDEVAAMVRFLNLLASEVRVPLMIDS 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 426 TEPAVLEAGLERLGGRAVINSVNYEDGDgpdSRFAKVTRMAVEHGAALMALTIDERGQARTPEDKVAIAERIIADLTGNW 505
Cdd:COG1410 410 SKPEVIEAGLKCYQGKPIVNSISLEEGE---ERFEEVAPLAKKYGAAVVVLAIDEEGQADTAERKLEIAERIYDLAVEEY 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 506 GVAESDIIIDCLTFTICTGQEESRRDGVHTIEAIRELKRRHPQVQTTLGLSNISFGLNPAARLVLNSVFLDECVKAGLDS 585
Cdd:COG1410 487 GFPPEDIIFDPLVFTVATGIEEHRNYAVETIEAIRLIKEELPGAKTSLGVSNVSFGLPGNVREALNSVFLYHAIKAGLDM 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 586 AIVHAAKILPIARIEDEQVQVALDLIHDRRRegyDPLQRFLELFEGVDAKSMRAgKTEELLALPLEERLRRRIVDGERKG 665
Cdd:COG1410 567 AIVNPGQLEPYDDIPPELRELAEDVLLNRRP---DALERLIELFEGVKGAKAKK-ADLEWRELPVEERLKHAIVKGIKEG 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 666 LEADLDEALTTRP-ALEIVNDTLLEGMKTVGELFGSGQMQLPFVLQSAEVMKTAVAHLEPHMEKSDD--EGKGTIVLATV 742
Cdd:COG1410 643 IEEDTEEALAEGArPLEIINGPLMPGMNVVGDLFGAGKMFLPQVLKSAEVMKAAVAYLEPFMEKEKGesSSKGKIVLATV 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 743 RGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVTAILDAAEEHRADVIGMSGLLVKSTVIMKENLEELNQRGMaaDYPVIL 822
Cdd:COG1410 723 KGDVHDIGKNIVGVVLENNGYEVIDLGVMVPAEKILEAAKEHKADIIGLSGLMTTSLDEMKEVAEEMRRRGL--DIPVLI 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 823 GGAALTRAYVEQDLHEVYQGEVRYARDAFEGLRLMDALIAVKRGVPGATLPELKKRRVAARPAALPQEDTEEPVGRSATA 902
Cdd:COG1410 801 GGAALTRAYTAVKIAPAYDGAVVYAKDASRAVRVADKLLSKERREAFVAEIKAEYEKLRERHAARKKKLLSLEEARSNVD 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 903 TDVPLPTAPFLGTRVIKGIPLKDYAAWLDEDALFKgQWGLKGSRSgagpDYEEllETEGRPRLRGWLDRLHTDNLLEAAV 982
Cdd:COG1410 881 SDYPPPTPPFLGTRVLKDIPLAELVPYIDWTPFFQ-QWGLKGKYL----DGEE--ARELFPDAQAMLDRIIEEKWLTARA 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 983 VYGYFPCHAEGQDLVILDEEG-KERTRFTFPRQRRGRRLCLADFFRPAESGETDVVALQAVTVGSRVSGATAELFAADAY 1061
Cdd:COG1410 954 VYGYFPANSEGDDIEVYDDESsEELARFHFPRQQRGPNLCLADFVAPKESGERDYVGFFAVTAGIGIEELAAELEAAGDD 1033
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 1062 RDYLELHGLSVQLAEALAEFWHARVRAELGIGGSDPAALAGMFRTEYQGCRYSLGYPACPDLEDRAKIAELLQPERIGVT 1141
Cdd:COG1410 1034 YDAIMLHALADRLAEAFAEYLHERVRKEWGYAPDEALTNEDLIKEKYRGIRPAPGYPACPDHTEKRKLFDLLDAERIGVT 1113
|
1130 1140
....*....|....*....|....*...
gi 818443726 1142 LSEEFQLHPEQSTDAIILHHPEANYFNA 1169
Cdd:COG1410 1114 LTESFAMHPEASVSGIYFHHPEAKYFNV 1141
|
|
| MetH1 |
COG0646 |
Methionine synthase I (cobalamin-dependent), methyltransferase domain [Amino acid transport ... |
26-823 |
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: 738.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 26 VVVADGGMGTMLQAAEPSLDDFQQLEGCNEVLNVTRPDIVRSVHQEYFDAGVDCVETNTFGANLAALGEYDIPERIAELS 105
Cdd:COG0646 14 ILILDGAMGTMLQAYGLTEGDFRGEKGCNELLNLTRPDVIREIHRAYLEAGADIIETNTFGANRIKLADYGLEDRVYEIN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 106 EAGARIARETADDCAardGRQRWVLGSIGPGTKLPT-LGHIRYADLRDAYQRNAEGLIAGGADALLVETAQDLLQTKAAV 184
Cdd:COG0646 94 RAAARLAREAADEFS---DRPRFVAGSIGPTGKLLSpLGNITFDELVEAYREQAEGLIEGGVDLLLIETIFDTLEAKAAI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 185 LGARRAVAATGVDLPLVVQVTVETTGTMLLGSEIGAALTALEPLGIDMIGLNCATGPAEMSEHLRYLSQHATIPISCMPN 264
Cdd:COG0646 171 FAAREAFEELGRDLPVMVSGTFDASGRTLSGQTPEAFATSLEHLGPDAIGLNCALGPDEMRPHVEELSEVADTPVSAYPN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 265 AGLPVLGKDGAHYPLGPAELADAHQTFIGEFGLSLIGGCCGTTPEHLRQVVERVRGLTPGARDPRPEPGAASLYQTVPFR 344
Cdd:COG0646 251 AGLPNLVGGRTVYDETPEEMAEYAEEFAEAGGVNIVGGCCGTTPEHIRAIAEAVKGLPPRKRPPPPPALRLSGLEPLTIT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 345 QDASYLAIGERTNANGSKKFREAMLEGRWEDCVELAREQIREGAHLLDLCVDYVGRDGAADMSELAGRLATASTLPIVLD 424
Cdd:COG0646 331 QDSLFVNVGERTNVTGSKKFARLILEGDYDAALAVARQQVEAGAQVIDVNMDEGMLDGEAAMVEFLNLIASEPDIPRVPD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 425 STEPAVLEAGLERLGGRAVINSVNYEDGDGPDSRFAKVTRMAVEHGAALMALTIDERGQARTPEDKVAIAERIIADLTGN 504
Cdd:COG0646 411 MIDSSKWEVIEAGLKGVQGKGIVNSISLKEGEEKFLELAKLVRRYGAAVVVMAFDEEGQADTAERKVEICARAYDLLTEE 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 505 WGVAESDIIIDCLTFTICTGQEESRRDGVHTIEAIRELKRRHPQVQTTLGLSNISFGL--NPAARLVLNSVFLDECVKAG 582
Cdd:COG0646 491 VGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKLNLPHALVSGGVSNVSFSFrgNNPVREAIHAVFLYHAIAAG 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 583 LDSAIVHAAKILPIARIEDEQVQVALDLIHDRRRegYDPLQRFLELFEGVDAKSMRAGKTEELLALPLEERLRRRIVDGE 662
Cdd:COG0646 571 MDMGIVNAGQLAIYEEIPEELLLLVEDVVLNRRE--DATERLLEIAEEVKGAGKAAEEEAEEERREEEEERLLELLLVGG 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 663 RKGLEADLDEALTTRPALEIVNDTLLEGMKTVGELFGSGQMQLPFVLQSAEVMKTAVAHLEPHMEKSDDEGKGTIVLATV 742
Cdd:COG0646 649 IEIDEEDDEEAALLLAALELIIIELLLGGGMVVGGLGGGGGKLLLVVVVKAVVKKKVAVALLKPEEEEKKKGGGKGGGVV 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 743 RGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVTAILDAAEEHRADVIGMSGLLVKSTVIMKENLEELNQRGMAADYPVIL 822
Cdd:COG0646 729 VGVVVKVVVDDVDIIIVVVVVVVNNGIVVLVVVVIVVVALEAAAAAEAAVILLVGGLVLLLLEEEVLAAAEAAAEAAVLL 808
|
.
gi 818443726 823 G 823
Cdd:COG0646 809 L 809
|
|
| metH |
PRK09490 |
B12-dependent methionine synthase; Provisional |
26-1168 |
0e+00 |
|
B12-dependent methionine synthase; Provisional
Pssm-ID: 236539 [Multi-domain] Cd Length: 1229 Bit Score: 689.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 26 VVVADGGMGTMLQAAEPSLDDF---------QQLEGCNEVLNVTRPDIVRSVHQEYFDAGVDCVETNTFGANLAALGEYD 96
Cdd:PRK09490 19 ILVLDGAMGTMIQRYKLEEADYrgerfadwpCDLKGNNDLLVLTQPDVIEAIHRAYLEAGADIIETNTFNATTIAQADYG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 97 IPERIAELSEAGARIARETADDCAARD-GRQRWVLGSIGPGTKLPTLG---------HIRYADLRDAYQRNAEGLIAGGA 166
Cdd:PRK09490 99 MESLVYELNFAAARLAREAADEWTAKTpDKPRFVAGVLGPTNRTASISpdvndpgfrNVTFDELVAAYREQTRGLIEGGA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 167 DALLVETAQDLLQTKAAVLGARRAVAATGVDLPLVVQVTV-ETTGTMLLGSEIGA---ALTALEPLGIdmiGLNCATGPA 242
Cdd:PRK09490 179 DLILIETIFDTLNAKAAIFAVEEVFEELGVRLPVMISGTItDASGRTLSGQTTEAfwnSLRHAKPLSI---GLNCALGAD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 243 EMSEHLRYLSQHATIPISCMPNAGLP-VLGKdgahYPLGPAELADahqtFIGEFG----LSLIGGCCGTTPEHLRQVVER 317
Cdd:PRK09490 256 ELRPYVEELSRIADTYVSAHPNAGLPnAFGE----YDETPEEMAA----QIGEFAesgfLNIVGGCCGTTPEHIAAIAEA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 318 VRGLTPGARdPRPEPgAASLYQTVPF--RQDASYLAIGERTNANGSKKFREAMLEGRWEDCVELAREQIREGAHLLDLCV 395
Cdd:PRK09490 328 VAGLPPRKL-PEIPV-ACRLSGLEPLniDDDSLFVNVGERTNVTGSAKFARLIKEEDYDEALDVARQQVENGAQIIDINM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 396 DYVGRDGAADMSELAGRLAT---ASTLPIVLDSTEPAVLEAGLERLGGRAVINSVNYEDGDGPDSRFAKVTRmavEHGAA 472
Cdd:PRK09490 406 DEGMLDSEAAMVRFLNLIASepdIARVPIMIDSSKWEVIEAGLKCIQGKGIVNSISLKEGEEKFIEHARLVR---RYGAA 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 473 LMALTIDERGQARTPEDKVAIAERIIADLTGNWGVAESDIIIDCLTFTICTGQEESRRDGVHTIEAIRELKRRHPQVQTT 552
Cdd:PRK09490 483 VVVMAFDEQGQADTRERKIEICKRAYDILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKQNLPHAKIS 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 553 LGLSNISF---GLNPAaRLVLNSVFLDECVKAGLDSAIVHAAKILPIARIEDEQVQVALDLIHDRRRegyDPLQRFLELF 629
Cdd:PRK09490 563 GGVSNVSFsfrGNNPV-REAIHAVFLYHAIKAGMDMGIVNAGQLAIYDDIPPELREAVEDVVLNRRP---DATERLLEIA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 630 EGVdaKSMRAGKTEELLALPLEERLRRRI----VDGERKGLEADLDEA--LTTRPaLEIVNDTLLEGMKTVGELFGSGQM 703
Cdd:PRK09490 639 EKY--RGKGGKKAKAEDLEWRSWPVEKRLehalVKGITEFIEEDTEEArqQAARP-LEVIEGPLMDGMNVVGDLFGEGKM 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 704 QLPFVLQSAEVMKTAVAHLEPHMEK-----SDDEGKGTIVLATVRGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVTAIL 778
Cdd:PRK09490 716 FLPQVVKSARVMKQAVAYLEPFIEAkkeggTDRKSNGKILMATVKGDVHDIGKNIVGVVLQCNNYEVIDLGVMVPAEKIL 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 779 DAAEEHRADVIGMSGLLVKSTVIMKENLEELNQRGMaaDYPVILGGAALTRAYVEQDLHEVYQGEVRYardafeglrLMD 858
Cdd:PRK09490 796 ETAKEENADIIGLSGLITPSLDEMVHVAKEMERQGF--TIPLLIGGATTSKAHTAVKIAPNYSGPVVY---------VTD 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 859 ALIAVkrGVPGATLPELKKRRVAARPAALPQEDTEEPVGRSATATDVPL----------------PTAP-FLGTRVIKGI 921
Cdd:PRK09490 865 ASRAV--GVVSSLLSDEQRDAYVAETRAEYEKVREQHARKKPRKPLLTLeaaranrfkidweaytPPKPkFLGVQVFEDY 942
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 922 PLKDYAAWLDEDALFKgQWGLKGSrsgagpdYEELLE-----TEGRpRL----RGWLDRLHTDNLLEAAVVYGYFPCHAE 992
Cdd:PRK09490 943 DLAELREYIDWTPFFQ-TWELAGK-------YPAILEdevvgEEAR-KLfadaQAMLDKIIAEKWLTARGVIGLFPANSV 1013
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 993 GQDLVILDEEGKERTRFTFP--RQ---RRGR-RLCLADFFRPAESGETDVVALQAVTVGSRVSgATAELFAA--DAYRDY 1064
Cdd:PRK09490 1014 GDDIEVYTDESRTEVLATLHhlRQqteKRGRpNYCLADFVAPKESGKADYIGAFAVTAGLGED-ELADRFEAahDDYNAI 1092
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 1065 LeLHGLSVQLAEALAEFWHARVRAELGIGGSDPA-ALAGMFRTEYQGCRYSLGYPACPDLEDRAKIAELLQPE-RIGVTL 1142
Cdd:PRK09490 1093 M-VKALADRLAEAFAEYLHERVRKEFWGYAPDENlSNEELIREKYQGIRPAPGYPACPDHTEKATLFDLLDAEkNTGMKL 1171
|
1210 1220
....*....|....*....|....*.
gi 818443726 1143 SEEFQLHPEQSTDAIILHHPEANYFN 1168
Cdd:PRK09490 1172 TESYAMWPGASVSGWYFSHPESKYFA 1197
|
|
| MeTr |
cd00740 |
MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent ... |
349-603 |
1.85e-113 |
|
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: 353.24 E-value: 1.85e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 349 YLAIGERTNANGSKKFREAMLEGRWEDCVELAREQIREGAHLLDLCVDYVGRDGAADMSELAGRLATASTLPIVLDSTEP 428
Cdd:cd00740 1 FLNIGERTNVTGSKKFRELIKAEDYDEALDVARQQVEGGAQILDLNVDYGGLDGVSAMKWLLNLLATEPTVPLMLDSTNW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 429 AVLEAGLERLGGRAVINSVNYEDGDgpdSRFAKVTRMAVEHGAALMALTIDERGQARTPEDKVAIAERIIADLTGNWGVA 508
Cdd:cd00740 81 EVIEAGLKCCQGKCVVNSINLEDGE---ERFLKVARLAKEHGAAVVVLAFDEQGQAKTRDKKVEIAERAYEALTEFVGFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 509 ESDIIIDCLTFTICTGQEESRRDGVHTIEAIRELKRRHPQVQTTLGLSNISFGLNPAARLVLNSVFLDECVKAGLDSAIV 588
Cdd:cd00740 158 PEDIIFDPLILPIATGIEEHRPYALETIDAIRMIKERLPAVKISLGVSNVSFGFNPAAREALNSVFLYEAIKAGLDMAIV 237
|
250
....*....|....*
gi 818443726 589 HAAKILPIARIEDEQ 603
Cdd:cd00740 238 NAGKLAPIEDIPEEL 252
|
|
| methionine_synthase_B12_BD |
cd02069 |
B12 binding domain of methionine synthase. This domain binds methylcobalamin, which it uses as ... |
655-860 |
7.37e-105 |
|
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: 328.46 E-value: 7.37e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 655 RRRIVDGERKGLEADLDEALTTR-PALEIVNDTLLEGMKTVGELFGSGQMQLPFVLQSAEVMKTAVAHLEPHMEKSDDE- 732
Cdd:cd02069 6 KHALVKGIRDGIEEDTEEARQQYaRPLEIINGPLMDGMKVVGDLFGAGKMFLPQVLKSARVMKAAVAYLEPYMEKEKGEn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 733 -GKGTIVLATVRGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVTAILDAAEEHRADVIGMSGLLVKSTVIMKENLEELNQ 811
Cdd:cd02069 86 sSKGKIVLATVKGDVHDIGKNLVGVILSNNGYEVIDLGVMVPIEKILEAAKEHKADIIGLSGLLVPSLDEMVEVAEEMNR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 818443726 812 RGMaaDYPVILGGAALTRAYVEQDLHEVYQGEVRYARDAFEGLRLMDAL 860
Cdd:cd02069 166 RGI--KIPLLIGGAATSRKHTAVKIAPEYDGPVVYVKDASRALGVANKL 212
|
|
| S-methyl_trans |
pfam02574 |
Homocysteine S-methyltransferase; This is a family of related homocysteine ... |
27-318 |
3.55e-86 |
|
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: 280.20 E-value: 3.55e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 27 VVADGGMGTMLQAAEPSLDDfqqLEGCNEVLnvTRPDIVRSVHQEYFDAGVDCVETNTFGANLAALGE-YDIPERIAELS 105
Cdd:pfam02574 1 LILDGGMGTELQRRGLDLTE---PLWSNELL--TRPEIIREIHRDYLEAGADIIETNTYQASPIKLAEgLEEEEAVYELN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 106 EAGARIARETADDcaardgrqRWVLGSIGPGTKLPTLG-HIRYADLRDAYQRNAEGLIAGGADALLVETAQDLLQTKAAV 184
Cdd:pfam02574 76 RAAVRLAREAADE--------YFVAGSIGPYGATLSDGyGLSFDELVDFHREQLEALLDGGVDLLLFETIPDLLEAKAAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 185 lgarrAVAATGVDLPLVVQVTVETTGTMLLGSEIGAALTALEPL-GIDMIGLNCATgPAEMSEHLRYLSQHATIPISCMP 263
Cdd:pfam02574 148 -----ELLAEEPDLPVWISFTIEDGTRLRSGTTLEAAVAALLHAtGPLAVGVNCAL-PEEMLPLLKELAKDAPTPVSVYP 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 818443726 264 NAGlpvlgkdGAHYPLGPAELADAHQTFIgEFGLSLIGGCCGTTPEHLRQVVERV 318
Cdd:pfam02574 222 NST-------GEVYDLTPEEWAEYAEGWL-EAGANIIGGCCGTTPEHIRAIAEAL 268
|
|
| PRK08645 |
PRK08645 |
bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; ... |
26-345 |
3.32e-71 |
|
bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; Reviewed
Pssm-ID: 236321 [Multi-domain] Cd Length: 612 Bit Score: 250.15 E-value: 3.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 26 VVVADGGMGTMLQAAEPSLDDfqqlegCNEVLNVTRPDIVRSVHQEYFDAGVDCVETNTFGANLAALGEYDIPERIAELS 105
Cdd:PRK08645 12 VLIADGAMGTLLYSRGVPLDR------CFEELNLSHPELILRIHREYIEAGADVIQTNTFGANRIKLKRYGLEDKVKEIN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 106 EAGARIARETAddcaardGRQRWVLGSIGPGTKLPTLGHIRYADLRDAYQRNAEGLIAGGADALLVETAQDLLQTKAAVL 185
Cdd:PRK08645 86 RAAVRLAREAA-------GDDVYVAGTIGPIGGRGPLGDISLEEIRREFREQIDALLEEGVDGLLLETFYDLEELLLALE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 186 GARRAvaatgVDLPLVVQVTVETTGTMLLGSEIGAALTALEPLGIDMIGLNCATGPAEMSEHLRYLSQHATIPISCMPNA 265
Cdd:PRK08645 159 AAREK-----TDLPIIAQVAFHEDGVTQNGTSLEEALKELVAAGADVVGLNCGLGPYHMLEALERIPIPENAPLSAYPNA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 266 GLPVLGKDGAHYPLGPAELADAHQTFIgEFGLSLIGGCCGTTPEHLRQVVERVRGLTPGARD-----PRPEPGAASLYQT 340
Cdd:PRK08645 234 GLPEYVDGRYVYSANPEYFAEYALEFV-EQGVRLIGGCCGTTPEHIRAMARALKGLKPVTEKevkprPKVVVTEEPLKAK 312
|
....*
gi 818443726 341 VPFRQ 345
Cdd:PRK08645 313 SSLLD 317
|
|
| corrinoid_protein_B12-BD |
cd02070 |
B12 binding domain of corrinoid proteins. A family of small methanogenic corrinoid proteins ... |
658-859 |
2.46e-52 |
|
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: 182.44 E-value: 2.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 658 IVDGERKGLEADLDEALTT-RPALEIVNDTLLEGMKTVGELFGSGQMQLPFVLQSAEVMKTAVAHLEPHMEKSDDEGKGT 736
Cdd:cd02070 5 IVDGDEEETVELVKKALEAgIDPQDIIEEGLAPGMDIVGDKYEEGEIFVPELLMAADAMKAGLDLLKPLLGKSKSAKKGK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 737 IVLATVRGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVTAILDAAEEHRADVIGMSGLLVKSTVIMKENLEELNQRGMAA 816
Cdd:cd02070 85 VVIGTVEGDIHDIGKNLVATMLEANGFEVIDLGRDVPPEEFVEAVKEHKPDILGLSALMTTTMGGMKEVIEALKEAGLRD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 818443726 817 DYPVILGGAALTRAYVEqdlhevYQGEVRYARDAFEGLRLMDA 859
Cdd:cd02070 165 KVKVMVGGAPVNQEFAD------EIGADGYAEDAAEAVAIAKE 201
|
|
| Pterin_bind |
pfam00809 |
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ... |
353-589 |
9.79e-49 |
|
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: 173.63 E-value: 9.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 353 GERTNANGSKKFREAMLEgRWEDCVELAREQIREGAHLLDLCVDYV-----GRDGAADMSELAGRLA---TASTLPIVLD 424
Cdd:pfam00809 1 MGILNVTPDSFSDGGRFL-DLDKALAHARRMVEEGADIIDIGGESTrpgaeRVDGEEEMERVLPVLAalrDEADVPISVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 425 STEPAVLEAGLERlgGRAVINSVNYEDGDgpdsrfAKVTRMAVEHGAALMALTIDER--------GQARTPEDKVAIAER 496
Cdd:pfam00809 80 TTKAEVAEAALKA--GADIINDISGGDGD------PEMAELAAEYGAAVVVMHMDGTpktmqeneQQYEDVVEEVERFLR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 497 IIADLTGNWGVAESDIIIDCLTFTicTGQEESRRDGVHTIEAIRELKrrhpQVQTTLGLSNISFGLNP-----AARLVLN 571
Cdd:pfam00809 152 ARVAAAEEAGVPPEDIILDPGIGF--GKTEEHNLELLRTLDELRVIL----GVPVLLGVSRKSFIGRGlplggEERDAGT 225
|
250
....*....|....*...
gi 818443726 572 SVFLDECVKAGLDSAIVH 589
Cdd:pfam00809 226 AAFLALAIAAGADIVRVH 243
|
|
| PRK07535 |
PRK07535 |
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase; Validated |
352-588 |
8.46e-47 |
|
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase; Validated
Pssm-ID: 181022 [Multi-domain] Cd Length: 261 Bit Score: 168.49 E-value: 8.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 352 IGERTNanGS-KKFREAMLEGRWEDCVELAREQIREGAHLLDLCVDYVGRDGAADMSELAGRLATASTLPIVLDSTEPAV 430
Cdd:PRK07535 4 IGERIN--GTrKSIAEAIEAKDAAFIQKLALKQAEAGADYLDVNAGTAVEEEPETMEWLVETVQEVVDVPLCIDSPNPAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 431 LEAGLERLGGRAVINSVNYEdgdgpDSRFAKVTRMAVEHGAALMALTIDERGQARTPEDKVAIAERIIADLTGNwGVAES 510
Cdd:PRK07535 82 IEAGLKVAKGPPLINSVSAE-----GEKLEVVLPLVKKYNAPVVALTMDDTGIPKDAEDRLAVAKELVEKADEY-GIPPE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818443726 511 DIIIDCLTFTICTGQEEsrrdGVHTIEAIRELKRRHPQVQTTLGLSNISFGLNpaARLVLNSVFLDECVKAGLDSAIV 588
Cdd:PRK07535 156 DIYIDPLVLPLSAAQDA----GPEVLETIRRIKELYPKVHTTCGLSNISFGLP--NRKLINRAFLVMAMGAGMDSAIL 227
|
|
| MtbC1 |
COG5012 |
Methanogenic corrinoid protein MtbC1 [Energy production and conversion]; |
658-865 |
1.50e-45 |
|
Methanogenic corrinoid protein MtbC1 [Energy production and conversion];
Pssm-ID: 444036 [Multi-domain] Cd Length: 219 Bit Score: 163.53 E-value: 1.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 658 IVDGERKGLEADLDEALTTR-PALEIVNDTLLEGMKTVGELFGSGQMQLPFVLQSAEVMKTAVAHLEPHMEKsDDEGKGT 736
Cdd:COG5012 18 VLEGDEDEALELVAEALAAGmDPEEIILDGLAPGMREVGELWEEGEIFVPEEHLAAAAMKAGLEILKPLLAE-EGGRKGK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 737 IVLATVRGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVTAILDAAEEHRADVIGMSGLLVKSTVIMKENLEELNQRGMAA 816
Cdd:COG5012 97 VVIGTVEGDLHDIGKNIVADMLRAAGFEVIDLGADVPPEEFVEAAKEEKPDIVGLSALLTTTMPAMKELIEALREAGLRD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 818443726 817 DYPVILGGAALTRAYVEqdlhEVyqGEVRYARDAFEGLRLMDALIAVKR 865
Cdd:COG5012 177 KVKVIVGGAPVTEELAE----EI--GADAYAEDAADAVELAKELLAERR 219
|
|
| PRK07534 |
PRK07534 |
betaine--homocysteine S-methyltransferase; |
26-332 |
1.56e-44 |
|
betaine--homocysteine S-methyltransferase;
Pssm-ID: 236045 [Multi-domain] Cd Length: 336 Bit Score: 164.54 E-value: 1.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 26 VVVADGGMGT----M-LQAAEPSlddfqqlegcnEVLNVTRPDIVRSVHQEYFDAGVDCVETNTFGANLAALGEYDIPER 100
Cdd:PRK07534 14 VLLADGATGTnlfnMgLESGEAP-----------ELWNEDHPDNITALHQGFVDAGSDIILTNSFGGTAARLKLHDAQDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 101 IAELSEAGARIARETADdcaaRDGRQRWVLGSIGP-GTKLPTLGHIRYADLRDAYQRNAEGLIAGGADALLVETAQDLLQ 179
Cdd:PRK07534 83 VHELNRAAAEIAREVAD----KAGRKVIVAGSVGPtGEIMEPMGALTHALAVEAFHEQAEGLKAGGADVLWVETISAPEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 180 TKAAvlgarrAVAATGVDLPLVVQVTVETTG-TML-LGSEIGAALTALEPLGIDMIGLNCATGPAE-MSEHLRYLSQHAT 256
Cdd:PRK07534 159 IRAA------AEAAKLAGMPWCGTMSFDTAGrTMMgLTPADLADLVEKLGEPPLAFGANCGVGASDlLRTVLGFTAQGPE 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818443726 257 IPISCMPNAGLPVLGKDGAHYPlGPAELADAHQTFIGEFGLSLIGGCCGTTPEHLRQVVErvrGLTPGARDPRPEP 332
Cdd:PRK07534 233 RPIIAKGNAGIPKYVDGHIHYD-GTPELMAEYAVLARDAGARIIGGCCGTMPEHLAAMRA---ALDARPRGPRPSL 304
|
|
| MHT1 |
COG2040 |
Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) [Amino acid transport and ... |
26-320 |
2.35e-41 |
|
Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) [Amino acid transport and metabolism];
Pssm-ID: 441643 [Multi-domain] Cd Length: 301 Bit Score: 154.20 E-value: 2.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 26 VVVADGGMGTMLQAAEpslDDFQQLEGCNEVLnVTRPDIVRSVHQEYFDAGVDCVETNTFGANLAALGEYDI-PERIAEL 104
Cdd:COG2040 13 ILLLDGGMGTELERRG---GDLLDPLWSAFAL-LEAPELVRAVHRDYFAAGADVITTNSYQASPDGLAELGYsAEEAERL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 105 SEAGARIARETADdcAARDGRQRWVLGSIGPgtklptLG-------HIRYADLRDAYQRNAEGLIAGGADALLVETAQDL 177
Cdd:COG2040 89 NRRAVALAREARD--EYTPGPPVLVAGSVGP------YGdeyrpdyGLSAEEAEAYHRPRIEALAEAGVDLLAAETIPSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 178 LQTKAAVlgarRAVAATGVdlPLVVQVTVETTGTMLLGSEIGAALTAL-EPLGIDMIGLNCATgPAEMSEHLRYLSQHAT 256
Cdd:COG2040 161 AEAIAIA----RAAAEAGK--PVWISFTVEDDGRLRSGEPLAEAIAAVdTDPGPAAVGVNCSH-PEHFEAALEALAAWTG 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818443726 257 IPISCMPNAGL---PVLGKDGAHYPLGPAELADAHQTFIgEFGLSLIGGCCGTTPEHLRQVVERVRG 320
Cdd:COG2040 234 RPIGVYANAGEmsdAELKTWGGLDDGDPEELAEQAAEWV-AAGARIIGGCCGTGPRHIAAIARALRA 299
|
|
| B12-binding |
cd02067 |
B12 binding domain (B12-BD). This domain binds different cobalamid derivates, like B12 ... |
736-859 |
3.29e-41 |
|
B12 binding domain (B12-BD). This domain binds different cobalamid derivates, like B12 (adenosylcobamide) or methylcobalamin or methyl-Co(III) 5-hydroxybenzimidazolylcobamide, it is found in several enzymes, such as glutamate mutase, methionine synthase and methylmalonyl-CoA mutase. Cobalamin undergoes a conformational change on binding the protein; the dimethylbenzimidazole group, which is coordinated to the cobalt in the free cofactor, moves away from the corrin and is replaced by a histidine contributed by the protein. The sequence Asp-X-His-X-X-Gly, which contains this histidine ligand, is conserved in many cobalamin-binding proteins.
Pssm-ID: 239018 [Multi-domain] Cd Length: 119 Bit Score: 147.27 E-value: 3.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 736 TIVLATVRGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVTAILDAAEEHRADVIGMSGLLVKSTVIMKENLEELNQRGmA 815
Cdd:cd02067 1 KVVIATVGGDGHDIGKNIVARALRDAGFEVIDLGVDVPPEEIVEAAKEEDADAIGLSGLLTTHMTLMKEVIEELKEAG-L 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 818443726 816 ADYPVILGGAALTRAYVEQDlhevYQGEVRYARDAFEGLRLMDA 859
Cdd:cd02067 80 DDIPVLVGGAIVTRDFKFLK----EIGVDAYFGPATEAVEVLKK 119
|
|
| Met_synt_B12 |
pfam02965 |
Vitamin B12 dependent methionine synthase, activation domain; |
969-1168 |
5.53e-38 |
|
Vitamin B12 dependent methionine synthase, activation domain;
Pssm-ID: 460767 [Multi-domain] Cd Length: 273 Bit Score: 143.77 E-value: 5.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 969 LDRLHTDNLLEAAVVYGYFPCHAEGQDLVILDEEGKERTRFTFP--RQRRGRR-----LCLADFFRPAESGETDVVALQA 1041
Cdd:pfam02965 48 LDRIIEEKWLTARGVVGFFPANSVGDDIEVYTDESRTEVLATFHtlRQQTEKPegrpnLCLADFIAPKESGIADYIGAFA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 1042 VTVGSRVSGATAELFAA-DAYRDYLeLHGLSVQLAEALAEFWHARVRAEL-GIGGSDPAALAGMFRTEYQGCRYSLGYPA 1119
Cdd:pfam02965 128 VTAGIGIEELAARFEAAhDDYSAIM-VKALADRLAEAFAEYLHERVRKELwGYAPDENLSNEDLIKEKYQGIRPAPGYPA 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 818443726 1120 CPDLEDRAKIAELLQPE-RIGVTLSEEFQLHPEQSTDAIILHHPEANYFN 1168
Cdd:pfam02965 207 CPDHTEKFTLFDLLDAEeNIGIRLTESFAMTPAASVSGLYFAHPESRYFA 256
|
|
| pyl_corrinoid |
TIGR02370 |
methyltransferase cognate corrinoid proteins, Methanosarcina family; This model describes a ... |
658-834 |
9.12e-37 |
|
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: 137.62 E-value: 9.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 658 IVDGERKGLEADLDEALTT-RPALEIVNDTLLEGMKTVGELFGSGQMQLPFVLQSAEVMKTAVAHLEPHMEK-SDDEGKG 735
Cdd:TIGR02370 6 IFEGEEDDVVEGAQKALDAgIDPIELIEKGLMAGMGVVGKLFEDGELFLPHVMMSADAMLAGIKVLTPEMEKaVETEVLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 736 TIVLATVRGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVTAILDAAEEHRADVIGMSGLLVKSTVIMKENLEELNQRGMA 815
Cdd:TIGR02370 86 KVVCGVAEGDVHDIGKNIVVTMLRANGFDVIDLGRDVPIDTVVEKVKKEKPLMLTGSALMTTTMYGQKDINDKLKEEGYR 165
|
170
....*....|....*....
gi 818443726 816 ADYPVILGGAALTRAYVEQ 834
Cdd:TIGR02370 166 DSVKFMVGGAPVTQDWADK 184
|
|
| B12-binding_like |
cd02065 |
B12 binding domain (B12-BD). Most of the members bind different cobalamid derivates, like B12 ... |
736-859 |
5.80e-32 |
|
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: 120.96 E-value: 5.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 736 TIVLATVRGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVTAILDAAEEHRADVIGMSGLLVKSTVIMKENLEELNQRGma 815
Cdd:cd02065 1 KVLGATVGGDVHDIGKNIVAIALRDNGFEVIDLGVDVPPEEIVEAAKEEDADVVGLSALSTTHMEAMKLVIEALKELG-- 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 818443726 816 ADYPVILGGAALTRAYVEQDLHEVYQGEVRYARDAF---EGLRLMDA 859
Cdd:cd02065 79 IDIPVVVGGAHPTADPEEPKVDAVVIGEGEYAGPALlevEGIAYRKN 125
|
|
| mmuM |
PRK09485 |
homocysteine methyltransferase; Provisional |
26-320 |
4.80e-27 |
|
homocysteine methyltransferase; Provisional
Pssm-ID: 181899 [Multi-domain] Cd Length: 304 Bit Score: 112.64 E-value: 4.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 26 VVVADGGMGTMLQAAepslddfqqleGCN--------EVLnVTRPDIVRSVHQEYFDAGVDCVETNTFGANLAALGEYDI 97
Cdd:PRK09485 13 VLILDGALATELEAR-----------GCDlndslwsaKVL-LENPELIYQVHLDYFRAGADCAITASYQATFQGFAARGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 98 PE-RIAELSEAGARIARETADDCAARDgrqRWVLGSIGP-GTklpTLG---------HIRYADLRDAYQRNAEGLIAGGA 166
Cdd:PRK09485 81 SEaEAEELIRRSVELAKEARDEFWAEK---PLVAGSVGPyGA---YLAdgseyrgdyGLSEEELQDFHRPRIEALAEAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 167 DALLVETAQDLLQTKAAVlgarRAVAATGVDLPLVVQVTVETT-----GTMLlgSEIGAALTALEPlgIDMIGLNCaTGP 241
Cdd:PRK09485 155 DLLACETIPNLDEAEALV----ELLKEEFPGVPAWLSFTLRDGthisdGTPL--AEAAALLAASPQ--VVAVGVNC-TAP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 242 AEMSEHLRYLSQHATIPISCMPNAGLPVlgkDGA----HYPLGPAELADAHQTFIgEFGLSLIGGCCGTTPEHLRQVVER 317
Cdd:PRK09485 226 ELVTAAIAALRAVTDKPLVVYPNSGEVY---DAVtktwHGPADDASLGELAPEWY-AAGARLIGGCCRTTPEDIAALAAA 301
|
...
gi 818443726 318 VRG 320
Cdd:PRK09485 302 LKT 304
|
|
| B12-binding_2 |
smart01018 |
B12 binding domain; Cobalamin-dependent methionine synthase is a large modular protein that ... |
655-730 |
1.24e-26 |
|
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: 104.47 E-value: 1.24e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818443726 655 RRRIVDGERKGLEADLDEALTT-RPALEIVNDTLLEGMKTVGELFGSGQMQLPFVLQSAEVMKTAVAHLEPHMEKSD 730
Cdd:smart01018 8 AEAIVDGDEEGVEELVEEALAEgVDPLEIINEGLIPGMNVVGDLFEAGEYFLPQVLMSAEAMKAAVAILKPLLEKEK 84
|
|
| B12-binding |
pfam02310 |
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ... |
735-855 |
6.65e-19 |
|
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: 83.53 E-value: 6.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 735 GTIVLATVRGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVTAILDAAEEHRADVIGMSGLLVKSTVIMKENLEELnqRGM 814
Cdd:pfam02310 1 GKVVVATVGGDLHPLGLNYVAAALRAAGFEVIILGANVPPEDIVAAARDEKPDVVGLSALMTTTLPGAKELIRLL--KGI 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 818443726 815 AADYPVILGGAALT---RAYVEQDLHEVYqGEVRYARDAFEGLR 855
Cdd:pfam02310 79 RPRVKVVVGGPHPTfdpEELLEARPGVDD-VVFGEGEDALEALL 121
|
|
| B12-binding_2 |
pfam02607 |
B12 binding domain; This B12 binding domain is found in methionine synthase EC:2.1.1.13, and ... |
655-722 |
1.43e-16 |
|
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: 75.20 E-value: 1.43e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818443726 655 RRRIVDGERKGLEADLDEALTTRPaLEIVNDTLLEGMKTVGELFGSGQMQLPFVLQSAEVMKTAVAHL 722
Cdd:pfam02607 2 LEALLEGDEEAAEELLEEALEIDP-EEIIEDLLIPGMDEVGELWEAGEIFVPQEHLAAEAMKAALAVL 68
|
|
| PRK02261 |
PRK02261 |
methylaspartate mutase subunit S; Provisional |
734-794 |
9.24e-10 |
|
methylaspartate mutase subunit S; Provisional
Pssm-ID: 179400 [Multi-domain] Cd Length: 137 Bit Score: 58.04 E-value: 9.24e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818443726 734 KGTIVLATVRGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVTAILDAAEEHRADVIGMSGL 794
Cdd:PRK02261 3 KKTVVLGVIGADCHAVGNKILDRALTEAGFEVINLGVMTSQEEFIDAAIETDADAILVSSL 63
|
|
| Glm_B12_BD |
cd02072 |
B12 binding domain of glutamate mutase (Glm). Glutamate mutase catalysis the conversion of (S) ... |
736-824 |
5.43e-09 |
|
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: 55.55 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 736 TIVLATVRGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVTAILDAAEEHRADVIGMSGLLVKSTVIMKENLEELNQRGMa 815
Cdd:cd02072 1 TIVLGVIGSDCHAVGNKILDHAFTEAGFNVVNLGVLSPQEEFIDAAIETDADAILVSSLYGHGEIDCKGLREKCDEAGL- 79
|
....*....
gi 818443726 816 ADYPVILGG 824
Cdd:cd02072 80 KDILLYVGG 88
|
|
| Sbm |
COG2185 |
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ... |
736-824 |
5.60e-09 |
|
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and metabolism];
Pssm-ID: 441788 [Multi-domain] Cd Length: 134 Bit Score: 55.53 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 736 TIVLATVRGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVTAILDAAEEHRADVIGMSGL------LVKSTVimkenlEEL 809
Cdd:COG2185 12 RVLLAKPGLDGHDRGAKVIARALRDAGFEVIYLGLFQTPEEIVRAAIEEDADVIGVSSLdgghleLVPELI------ELL 85
|
90
....*....|....*
gi 818443726 810 NQRGmAADYPVILGG 824
Cdd:COG2185 86 KEAG-AGDILVVVGG 99
|
|
| MM_CoA_mut_B12_BD |
cd02071 |
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), ... |
737-824 |
3.75e-08 |
|
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: 52.98 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 737 IVLATVRGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVTAILDAAEEHRADVIGMSGLLVKSTVIMKENLEELNQRGmAA 816
Cdd:cd02071 2 ILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRQTPEEIVEAAIQEDVDVIGLSSLSGGHMTLFPEVIELLRELG-AG 80
|
....*...
gi 818443726 817 DYPVILGG 824
Cdd:cd02071 81 DILVVGGG 88
|
|
| PLN02489 |
PLN02489 |
homocysteine S-methyltransferase |
26-312 |
5.70e-08 |
|
homocysteine S-methyltransferase
Pssm-ID: 215269 Cd Length: 335 Bit Score: 56.17 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 26 VVVADGGMGTMLQAAEPSLDDFQQLEGCnevLnVTRPDIVRSVHQEYFDAGVDCVETNTFGANLAALGEYDIPERIAE-L 104
Cdd:PLN02489 22 CAVIDGGFATELERHGADLNDPLWSAKC---L-ITSPHLIRKVHLDYLEAGADIIITASYQATIQGFESRGLSREESEtL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 105 SEAGARIARETADD---------CAARDG----RQRWVLGSIGP-GTKLPT----LGHirYAD------LRDAYQRNAEG 160
Cdd:PLN02489 98 LRKSVEIACEARDIfwdkcqkgsTSRPGRelsyRPILVAASIGSyGAYLADgseySGD--YGPsvtlekLKDFHRRRLQV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 161 LIAGGADALLVETAQDLLQTKAAVlgarRAVAATGVDLPLVVQVTVETTGTMLLGSEIGAALTALEPLG-IDMIGLNCaT 239
Cdd:PLN02489 176 LAEAGPDLIAFETIPNKLEAQAYV----ELLEEENIKIPAWISFNSKDGVNVVSGDSLLECASIADSCKkVVAVGINC-T 250
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250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818443726 240 GPAEMSEHLRYLSQHATIPISCMPNAGLPVLGKDGAHYPL-GPAElaDAHQTFIGEF---GLSLIGGCCGTTPEHLR 312
Cdd:PLN02489 251 PPRFIHGLILSIRKVTSKPIVVYPNSGETYDGEAKEWVEStGVSD--EDFVSYVNKWrdaGASLIGGCCRTTPNTIR 325
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|
| acid_CoA_mut_C |
TIGR00640 |
methylmalonyl-CoA mutase C-terminal domain; Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a ... |
737-824 |
3.22e-03 |
|
methylmalonyl-CoA mutase C-terminal domain; Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a reversible isomerization between L-methylmalonyl-CoA and succinyl-CoA. The enzyme uses an adenosylcobalamin cofactor. It may be a homodimer, as in mitochondrion, or a heterodimer with partially homologous beta chain that does not bind the adenosylcobalamin cofactor, as in Propionibacterium freudenreichii. The most similar archaeal sequences are separate chains, such as AF2215 and AF2219 of Archaeoglobus fulgidus, that correspond roughly to the first 500 and last 130 residues, respectively of known methylmalonyl-CoA mutases. This model describes the C-terminal domain subfamily. In a neighbor-joining tree (methylaspartate mutase S chain as the outgroup), AF2219 branches with a coenzyme B12-dependent enzyme known not to be 5.4.99.2.
Pssm-ID: 129726 [Multi-domain] Cd Length: 132 Bit Score: 38.93 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818443726 737 IVLATVRGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVTAILDAAEEHRADVIGMSGLLVKSTVIMKENLEELNQRGMaA 816
Cdd:TIGR00640 5 ILVAKMGQDGHDRGAKVIATALADLGFDVDYGPLFQTPEEIARQAVEADVHVVGVSSLAGGHLTLVPELIKELNKLGR-P 83
|
....*...
gi 818443726 817 DYPVILGG 824
Cdd:TIGR00640 84 DILVVVGG 91
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