|
Name |
Accession |
Description |
Interval |
E-value |
| metH |
PRK09490 |
B12-dependent methionine synthase; Provisional |
16-1232 |
0e+00 |
|
B12-dependent methionine synthase; Provisional
Pssm-ID: 236539 [Multi-domain] Cd Length: 1229 Bit Score: 1624.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 16 LMEAAGREVLVLDGAMGTMIQRYGLSENDFRGERYAASDALLKGCNDALVLTRPDVIKDIHRKYLEAGAMIIETDSFNAN 95
Cdd:PRK09490 11 LRALLAERILVLDGAMGTMIQRYKLEEADYRGERFADWPCDLKGNNDLLVLTQPDVIEAIHRAYLEAGADIIETNTFNAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 96 AVSLGDYGLQHDVTALNHAAAKIAREAADEYMTQHPGAMRWVAGSIGPTSKSLTMGQGIDDPSAGVVDWDLLTETYIEQM 175
Cdd:PRK09490 91 TIAQADYGMESLVYELNFAAARLAREAADEWTAKTPDKPRFVAGVLGPTNRTASISPDVNDPGFRNVTFDELVAAYREQT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 176 KALIEGGVDALLIETIYDGLNAKAAIWAARRAMEIVGVRVPLMLSVTLTE-SGRTLSGQTLEAIIASMSFGEPMSIGLNC 254
Cdd:PRK09490 171 RGLIEGGADLILIETIFDTLNAKAAIFAVEEVFEELGVRLPVMISGTITDaSGRTLSGQTTEAFWNSLRHAKPLSIGLNC 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 255 GFGADAMMKYVEALQ----PYpyaVSVYPNAGLPNEMGEYDETPSMMADKIRVMLQRRWVNIVGGCCGTTPQHIKALAEL 330
Cdd:PRK09490 251 ALGADELRPYVEELSriadTY---VSAHPNAGLPNAFGEYDETPEEMAAQIGEFAESGFLNIVGGCCGTTPEHIAAIAEA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 331 CKQYAPRVVPEVEPEMTLAGLEPLCVTPRLNFVNVGERCNVAGSRKFLRLIKEGNIDEAIDIARNQVDAGAQIIDINMDD 410
Cdd:PRK09490 328 VAGLPPRKLPEIPVACRLSGLEPLNIDDDSLFVNVGERTNVTGSAKFARLIKEEDYDEALDVARQQVENGAQIIDINMDE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 411 AMLDARACMTSFLSRIGVEPDVARVPVMIDSSDWNVVIGGLKCVQGRPIVNSISLKEGEESFIKKARDIKEMGAAVVVMA 490
Cdd:PRK09490 408 GMLDSEAAMVRFLNLIASEPDIARVPIMIDSSKWEVIEAGLKCIQGKGIVNSISLKEGEEKFIEHARLVRRYGAAVVVMA 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 491 FDEKGQADTFERRIEVCDRAYRLLTGKVGFKGCDIVFDPNVLAVATGIEEHADYALDFIRAVEWIKSNLPGAKVSGGVSN 570
Cdd:PRK09490 488 FDEQGQADTRERKIEICKRAYDILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKQNLPHAKISGGVSN 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 571 LSFSFRGNNSVREAMHALFLYHAIAKGMDMAIVNAAAIMPVDDIPDELREAIDDVLLNRSHDATERLVAIAEKIKSGNVT 650
Cdd:PRK09490 568 VSFSFRGNNPVREAIHAVFLYHAIKAGMDMGIVNAGQLAIYDDIPPELREAVEDVVLNRRPDATERLLEIAEKYRGKGGK 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 651 VAAESPSEEPSLTPDKRVERMLVKGVVDGMERNLSDAMAMLGSAVKVIEGPLMAGMNSVGEMFGAGKMFLPQVVKSARTM 730
Cdd:PRK09490 648 KAKAEDLEWRSWPVEKRLEHALVKGITEFIEEDTEEARQQAARPLEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVM 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 731 KQAVGWLTPFIERER-RGKVSSKAGKMVIATVKGDVHDIGKNIVGVIMNCNGYDIIDMGVMVPAEDIVDKAIAENADFVG 809
Cdd:PRK09490 728 KQAVAYLEPFIEAKKeGGTDRKSNGKILMATVKGDVHDIGKNIVGVVLQCNNYEVIDLGVMVPAEKILETAKEENADIIG 807
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 810 LSGLITPSLEEMCNVARLMESKRMKIPLLIGGATTSELHTAVKIAPCYSGPVLYTRDAA-MMPAAVRRLGDE---AEVAR 885
Cdd:PRK09490 808 LSGLITPSLDEMVHVAKEMERQGFTIPLLIGGATTSKAHTAVKIAPNYSGPVVYVTDASrAVGVVSSLLSDEqrdAYVAE 887
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 886 LRDSQAELRRKHSSGAG---LLSLSEARSKRPRLSYPCY--PVAH-PGVHEL-NIDIAEAREFINWRAFLSAWkidasla 958
Cdd:PRK09490 888 TRAEYEKVREQHARKKPrkpLLTLEAARANRFKIDWEAYtpPKPKfLGVQVFeDYDLAELREYIDWTPFFQTW------- 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 959 svmDIKGcdhcraQWLASVPSEKVnkAAEAMQLLKEAGRVLDRLQRDivGGIKAK--VAFVEAASDgGDDI-LFNHDGET 1035
Cdd:PRK09490 961 ---ELAG------KYPAILEDEVV--GEEARKLFADAQAMLDKIIAE--KWLTARgvIGLFPANSV-GDDIeVYTDESRT 1026
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 1036 LRIAT---LRQQRpSERDGHCIALSDYIAPVESDgkLRDSMGMFAVTVGRDIERIIESYKNEGDDYSAILYQTVADRLVE 1112
Cdd:PRK09490 1027 EVLATlhhLRQQT-EKRGRPNYCLADFVAPKESG--KADYIGAFAVTAGLGEDELADRFEAAHDDYNAIMVKALADRLAE 1103
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 1113 AATEVMHRKVRVELWGYAPDESLSERHVLQQYYKGIRPAIGYPSLPDQS---LIFltdRVLRYSD-MGITLTESGAMSPA 1188
Cdd:PRK09490 1104 AFAEYLHERVRKEFWGYAPDENLSNEELIREKYQGIRPAPGYPACPDHTekaTLF---DLLDAEKnTGMKLTESYAMWPG 1180
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....
gi 1616153298 1189 ASTTGLIISHPDSRYFVVGDVDNGQRRLYAERRAMSLDELKRFL 1232
Cdd:PRK09490 1181 ASVSGWYFSHPESKYFAVGKIGRDQVEDYAARKGMSVEEVERWL 1224
|
|
| metH |
TIGR02082 |
5-methyltetrahydrofolate--homocysteine methyltransferase; This family represents ... |
22-1206 |
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: 1330.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 22 REVLVLDGAMGTMIQRYGLSENDFRGErYAASDALLKGCNDALVLTRPDVIKDIHRKYLEAGAMIIETDSFNANAVSLGD 101
Cdd:TIGR02082 3 QRILVLDGAMGTQLQSANLTEADFRGA-FADCHRELKGNNDILNLTKPEVIATIHRAYFEAGADIIETNTFNSTTISQAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 102 YGLQHDVTALNHAAAKIAREAADEYmTQHPGAMRWVAGSIGPTSKSLTMGQGIDDPSAGVVDWDLLTETYIEQMKALIEG 181
Cdd:TIGR02082 82 YDLEDLIYDLNFKGAKLARAVADEF-TLTPEKPRFVAGSMGPTNKTATLSPDVERPGFRNVTYDELVDAYTEQAKGLLDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 182 GVDALLIETIYDGLNAKAAIWAARRAMEIVGVRVPLMLSVTLTE-SGRTLSGQTLEAIIASMSFGEPMSIGLNCGFGADA 260
Cdd:TIGR02082 161 GVDLLLIETCFDTLNAKAALFAAETVFEEKGRELPIMISGTIVDtSGRTLSGQTIEAFLTSLEHAGIDMIGLNCALGPDE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 261 MMKYVEALQPY-PYAVSVYPNAGLPNEMGEYDETPSMMADKIRVMLQRRWVNIVGGCCGTTPQHIKALAELCKQYAPRVV 339
Cdd:TIGR02082 241 MRPHLKHLSEHaEAYVSCHPNAGLPNAFGEYDLTPDELAKALADFAAEGGLNIVGGCCGTTPDHIRAIAEAVKNIKPRQR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 340 PEVEPEMTLAGLEPLCVTPRLNFVNVGERCNVAGSRKFLRLIKEGNIDEAIDIARNQVDAGAQIIDINMDDAMLDARACM 419
Cdd:TIGR02082 321 PVLYEPSRLSGLEAITIAQDSNFVNIGERTNVAGSKKFRRLIIAEDYDEALDIAKQQVENGAQILDINVDYGMLDGVAAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 420 TSFLSRIGVEPDVARVPVMIDSSDWNVVIGGLKCVQGRPIVNSISLKEGEESFIKKARDIKEMGAAVVVMAFDEKGQADT 499
Cdd:TIGR02082 401 KRFLNLLASEPDISTVPLMLDSSEWAVLEAGLKCIQGKCIVNSISLKDGEERFIETAKLIKEYGAAVVVMAFDEEGQART 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 500 FERRIEVCDRAYRLLTGKVGFKGCDIVFDPNVLAVATGIEEHADYALDFIRAVEWIKSNLPGAKVSGGVSNLSFSFRGNN 579
Cdd:TIGR02082 481 ADRKIEICKRAYNILTEKVGFPPEDIIFDPNILTIATGIEEHRRYAINFIEAIRWIKEELPDAKISGGVSNVSFSFRGNP 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 580 SVREAMHALFLYHAIAKGMDMAIVNAAAIMPVDDIPDELREAIDDVLLNRSHDATERLVAIAEKIKSGNVTVAAES-PSE 658
Cdd:TIGR02082 561 AAREAMHSVFLYHAIRAGMDMGIVNAGKILPYDDIDPELRQVVEDLILNRRREATEPLLELAQLYEGTTTKSSKEAqQAE 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 659 EPSLTPDKRVERMLVKGVVDGMERNLSDAMAMLGSAVKVIEGPLMAGMNSVGEMFGAGKMFLPQVVKSARTMKQAVGWLT 738
Cdd:TIGR02082 641 WRNLPVEERLEYALVKGEREGIEEDLEEARKKLTRPLEIIEGPLMDGMKVVGDLFGSGKMFLPQVVKSARVMKKAVAYLE 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 739 PFIERERRGkvSSKAGKMVIATVKGDVHDIGKNIVGVIMNCNGYDIIDMGVMVPAEDIVDKAIAENADFVGLSGLITPSL 818
Cdd:TIGR02082 721 PHMEKEKSE--DSSKGKIVLATVKGDVHDIGKNIVGVVLSCNGYEVVDLGVMVPIEKILEAAKDHNADVIGLSGLITPSL 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 819 EEMCNVARLMESKRMKIPLLIGGATTSELHTAVKIAPCYSGPVLYTRDA--------AMMPAAVRrlgdEAEVARLRDSQ 890
Cdd:TIGR02082 799 DEMKEVAEEMNRRGITIPLLIGGAATSKTHTAVKIAPIYKGPVVYVLDAsravtvmdTLMSAKRK----DTENGRIKEEY 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 891 AELRRKHSSGAG---LLSLSEARSKR--PRLSYPCYPVAHP--GVHEL-NIDIAEAREFINWRAFLSAWKIdaslasvmd 962
Cdd:TIGR02082 875 DTAREKHGEQRSkriAASEQAARKNVfaPDWSDDIEPPAPPfwGTQIVeASDIAELRPYIDWTPFFLQWQL--------- 945
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 963 ikgcdhcRAQWLASVPSEKVNkaAEAMQLLKEAGRVLDRLQRDivGGIKAKVAF-VEAASDGGDDILFnHDGETLR---I 1038
Cdd:TIGR02082 946 -------RGKYPKILGDEYEG--LEAQKLFPDANEMLDKLSAE--NLLHARGVYgYFPAQSVGDDIEI-YTDETVEthpI 1013
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 1039 ATLR--QQRPSERDGHCIALSDYIAPVESDGklRDSMGMFAVTVGRDIERIIESYKNEGDDYSAILYQTVADRLVEAATE 1116
Cdd:TIGR02082 1014 ATVRylFHFPRQQSGRYLCLADFIAPKASGI--VDYIGAFAVTAGFGAEELADKLEAQHDDYDYIMVKAIADRLAEAFAE 1091
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 1117 VMHRKVRVELWGYAPDESLSERHVLQQYYKGIRPAIGYPSLPDQSLIFLTDRVLRYSDMGITLTESGAMSPAASTTGLII 1196
Cdd:TIGR02082 1092 YLHRRVRKELWGYAAEEPLSNEDLLKLRYQGIRPAPGYPACPDHTEKATMFELLEPERIGVRLTESLAMHPEQSVSGLYF 1171
|
1210
....*....|
gi 1616153298 1197 SHPDSRYFVV 1206
Cdd:TIGR02082 1172 AHPEAKYFAV 1181
|
|
| MetH2 |
COG1410 |
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; ... |
31-1206 |
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: 1298.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 31 MGTMIQRYGLSENDFRGERYAASDALLKGCNDALVLTRPDVIKDIHRKYLEAGAMIIETDSFNANAVSLGDYGLQHDVTA 110
Cdd:COG1410 1 MGTMIQLLKLRELDADGAMFTDLQLDLKGNNDLLGLTGPNEILEIHRPELEAGADIIETNTGADAAITAADGAAEALLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 111 LNHAAAKIAREAADEYMTQHPGAMRWVAGSIGPTSKSLTMGQGIDDPSAGVVDWDLLTETYIEQMKALIEGGVDALLIET 190
Cdd:COG1410 81 YNGAAAALALEAAAAAAAAAAAAARAVAGAPGPTGGTASPGPDVPGLGFRNFDFDELVEAYAEAGLGLGGGGADLLLTET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 191 IYDGLNAKAAIWAARRAMEIVGVRVPLMLSVTLTE-SGRTLSGQTLEAIIASMSFGEPMSIGLNCGFGADAMMKYVEALQ 269
Cdd:COG1410 161 IFDTLNAAAAAAAAAAAAEEEGVPIPVMVTGTITDgSGRTLSGQTAEAFLESLGHAAPGSNGLNCALGAEELRPYLEELS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 270 -PYPYAVSVYPNAGLPNEMGEYDETPSMMADKIRVMLQRRWVNIVGGCCGTTPQHIKALAELCKQYAPRVvPEVEPEMTL 348
Cdd:COG1410 241 rIPPSAVSNAPNAGLPNGFGEYDETPEEMAAALAEFAEEGGVNIVGGCCGTTPEHIRAIAEAVAGLKPRP-REKPPPAVL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 349 AGLEPLCVTPRLNFVNVGERCNVAGSRKFLRLIKEGNIDEAIDIARNQVDAGAQIIDINMDDAMLDARACMTSFLSRIGV 428
Cdd:COG1410 320 SGLEPVPIGQDSPFVNIGERTNVTGSKKFRELILEGDYDEALEVAREQVEAGAQILDVNVDEPGRDEVAAMVRFLNLLAS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 429 EpdvARVPVMIDSSDWNVVIGGLKCVQGRPIVNSISLKEGEESFIKKARDIKEMGAAVVVMAFDEKGQADTFERRIEVCD 508
Cdd:COG1410 400 E---VRVPLMIDSSKPEVIEAGLKCYQGKPIVNSISLEEGEERFEEVAPLAKKYGAAVVVLAIDEEGQADTAERKLEIAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 509 RAYRLLTGKVGFKGCDIVFDPNVLAVATGIEEHADYALDFIRAVEWIKSNLPGAKVSGGVSNLSFSFRGNnsVREAMHAL 588
Cdd:COG1410 477 RIYDLAVEEYGFPPEDIIFDPLVFTVATGIEEHRNYAVETIEAIRLIKEELPGAKTSLGVSNVSFGLPGN--VREALNSV 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 589 FLYHAIAKGMDMAIVNAAAIMPVDDIPDELREAIDDVLLNRSHDATERLVAIAEKIKSgnvTVAAESPSEEPSLTPDKRV 668
Cdd:COG1410 555 FLYHAIKAGLDMAIVNPGQLEPYDDIPPELRELAEDVLLNRRPDALERLIELFEGVKG---AKAKKADLEWRELPVEERL 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 669 ERMLVKGVVDGMERNLSDAMAMLGSAVKVIEGPLMAGMNSVGEMFGAGKMFLPQVVKSARTMKQAVGWLTPFIERErrGK 748
Cdd:COG1410 632 KHAIVKGIKEGIEEDTEEALAEGARPLEIINGPLMPGMNVVGDLFGAGKMFLPQVLKSAEVMKAAVAYLEPFMEKE--KG 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 749 VSSKAGKMVIATVKGDVHDIGKNIVGVIMNCNGYDIIDMGVMVPAEDIVDKAIAENADFVGLSGLITPSLEEMCNVARLM 828
Cdd:COG1410 710 ESSSKGKIVLATVKGDVHDIGKNIVGVVLENNGYEVIDLGVMVPAEKILEAAKEHKADIIGLSGLMTTSLDEMKEVAEEM 789
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 829 ESKRMKIPLLIGGATTSELHTAVKIAPCYSGPVLYTRDAAMMPAAVRRL----GDEAEVARLRDSQAELRRKHSS-GAGL 903
Cdd:COG1410 790 RRRGLDIPVLIGGAALTRAYTAVKIAPAYDGAVVYAKDASRAVRVADKLlskeRREAFVAEIKAEYEKLRERHAArKKKL 869
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 904 LSLSEARSKRPRlSYPCYPVAHPGVHEL-NIDIAEAREFINWRAFLSAWkidaslasvmDIKGcdhcraqwlasvpseKV 982
Cdd:COG1410 870 LSLEEARSNVDS-DYPPPTPPFLGTRVLkDIPLAELVPYIDWTPFFQQW----------GLKG---------------KY 923
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 983 NKAAEAMQLLKEAGRVLDRLQRDIVGGIKAKVAFVEAASDGGDDILFNHDG--ETLRIATLRQQRpserdGHCIALSDYI 1060
Cdd:COG1410 924 LDGEEARELFPDAQAMLDRIIEEKWLTARAVYGYFPANSEGDDIEVYDDESseELARFHFPRQQR-----GPNLCLADFV 998
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 1061 APVESdgKLRDSMGMFAVTVGRDIERIIESYKNEGDDYSAILYQTVADRLVEAATEVMHRKVRVElWGYAPDESLSERHV 1140
Cdd:COG1410 999 APKES--GERDYVGFFAVTAGIGIEELAAELEAAGDDYDAIMLHALADRLAEAFAEYLHERVRKE-WGYAPDEALTNEDL 1075
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1616153298 1141 LQQYYKGIRPAIGYPSLPDQSLIFLTDRVLRYSDMGITLTESGAMSPAASTTGLIISHPDSRYFVV 1206
Cdd:COG1410 1076 IKEKYRGIRPAPGYPACPDHTEKRKLFDLLDAERIGVTLTESFAMHPEASVSGIYFHHPEAKYFNV 1141
|
|
| MeTr |
cd00740 |
MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent ... |
362-618 |
6.87e-114 |
|
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: 355.55 E-value: 6.87e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 362 FVNVGERCNVAGSRKFLRLIKEGNIDEAIDIARNQVDAGAQIIDINMDDAMLDARACMTSFLSRIGVEPdvaRVPVMIDS 441
Cdd:cd00740 1 FLNIGERTNVTGSKKFRELIKAEDYDEALDVARQQVEGGAQILDLNVDYGGLDGVSAMKWLLNLLATEP---TVPLMLDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 442 SDWNVVIGGLKCVQGRPIVNSISLKEGEESFIKKARDIKEMGAAVVVMAFDEKGQADTFERRIEVCDRAYRLLTGKVGFK 521
Cdd:cd00740 78 TNWEVIEAGLKCCQGKCVVNSINLEDGEERFLKVARLAKEHGAAVVVLAFDEQGQAKTRDKKVEIAERAYEALTEFVGFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 522 GCDIVFDPNVLAVATGIEEHADYALDFIRAVEWIKSNLPGAKVSGGVSNLSFSFrgNNSVREAMHALFLYHAIAKGMDMA 601
Cdd:cd00740 158 PEDIIFDPLILPIATGIEEHRPYALETIDAIRMIKERLPAVKISLGVSNVSFGF--NPAAREALNSVFLYEAIKAGLDMA 235
|
250
....*....|....*..
gi 1616153298 602 IVNAAAIMPVDDIPDEL 618
Cdd:cd00740 236 IVNAGKLAPIEDIPEEL 252
|
|
| Met_synt_B12 |
pfam02965 |
Vitamin B12 dependent methionine synthase, activation domain; |
934-1221 |
1.06e-92 |
|
Vitamin B12 dependent methionine synthase, activation domain;
Pssm-ID: 460767 [Multi-domain] Cd Length: 273 Bit Score: 299.00 E-value: 1.06e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 934 DIAEAREFINWRAFLSAWkidaslasvmDIKGCDhcraqwlASVPSEKVnKAAEAMQLLKEAGRVLDRLQRDIVGGIKAK 1013
Cdd:pfam02965 1 DLAELVPYIDWTPFFQAW----------ELKGKY-------PAILDDEV-VGEEARKLFADAQAMLDRIIEEKWLTARGV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 1014 VAFVEAASDGgDDILFNHD----GETLRIATLRQQRPSERDGHCIALSDYIAPVESdGKlRDSMGMFAVTVGRDIERIIE 1089
Cdd:pfam02965 63 VGFFPANSVG-DDIEVYTDesrtEVLATFHTLRQQTEKPEGRPNLCLADFIAPKES-GI-ADYIGAFAVTAGIGIEELAA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 1090 SYKNEGDDYSAILYQTVADRLVEAATEVMHRKVRVELWGYAPDESLSERHVLQQYYKGIRPAIGYPSLPDQSLIFLTDRV 1169
Cdd:pfam02965 140 RFEAAHDDYSAIMVKALADRLAEAFAEYLHERVRKELWGYAPDENLSNEDLIKEKYQGIRPAPGYPACPDHTEKFTLFDL 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1616153298 1170 LrysDM----GITLTESGAMSPAASTTGLIISHPDSRYFVVGDVDNGQRRLYAERR 1221
Cdd:pfam02965 220 L---DAeeniGIRLTESFAMTPAASVSGLYFAHPESRYFAVGKIGKDQVEDYAKRK 272
|
|
| B12-binding_2 |
smart01018 |
B12 binding domain; Cobalamin-dependent methionine synthase is a large modular protein that ... |
662-745 |
4.62e-24 |
|
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: 97.16 E-value: 4.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 662 LTPDKRVERMLVKGVVDGMERNLSDAMAMLGSAVKVIEGPLMAGMNSVGEMFGAGKMFLPQVVKSARTMKQAVGWLTPFI 741
Cdd:smart01018 1 MPLLERLAEAIVDGDEEGVEELVEEALAEGVDPLEIINEGLIPGMNVVGDLFEAGEYFLPQVLMSAEAMKAAVAILKPLL 80
|
....
gi 1616153298 742 ERER 745
Cdd:smart01018 81 EKEK 84
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| metH |
PRK09490 |
B12-dependent methionine synthase; Provisional |
16-1232 |
0e+00 |
|
B12-dependent methionine synthase; Provisional
Pssm-ID: 236539 [Multi-domain] Cd Length: 1229 Bit Score: 1624.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 16 LMEAAGREVLVLDGAMGTMIQRYGLSENDFRGERYAASDALLKGCNDALVLTRPDVIKDIHRKYLEAGAMIIETDSFNAN 95
Cdd:PRK09490 11 LRALLAERILVLDGAMGTMIQRYKLEEADYRGERFADWPCDLKGNNDLLVLTQPDVIEAIHRAYLEAGADIIETNTFNAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 96 AVSLGDYGLQHDVTALNHAAAKIAREAADEYMTQHPGAMRWVAGSIGPTSKSLTMGQGIDDPSAGVVDWDLLTETYIEQM 175
Cdd:PRK09490 91 TIAQADYGMESLVYELNFAAARLAREAADEWTAKTPDKPRFVAGVLGPTNRTASISPDVNDPGFRNVTFDELVAAYREQT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 176 KALIEGGVDALLIETIYDGLNAKAAIWAARRAMEIVGVRVPLMLSVTLTE-SGRTLSGQTLEAIIASMSFGEPMSIGLNC 254
Cdd:PRK09490 171 RGLIEGGADLILIETIFDTLNAKAAIFAVEEVFEELGVRLPVMISGTITDaSGRTLSGQTTEAFWNSLRHAKPLSIGLNC 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 255 GFGADAMMKYVEALQ----PYpyaVSVYPNAGLPNEMGEYDETPSMMADKIRVMLQRRWVNIVGGCCGTTPQHIKALAEL 330
Cdd:PRK09490 251 ALGADELRPYVEELSriadTY---VSAHPNAGLPNAFGEYDETPEEMAAQIGEFAESGFLNIVGGCCGTTPEHIAAIAEA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 331 CKQYAPRVVPEVEPEMTLAGLEPLCVTPRLNFVNVGERCNVAGSRKFLRLIKEGNIDEAIDIARNQVDAGAQIIDINMDD 410
Cdd:PRK09490 328 VAGLPPRKLPEIPVACRLSGLEPLNIDDDSLFVNVGERTNVTGSAKFARLIKEEDYDEALDVARQQVENGAQIIDINMDE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 411 AMLDARACMTSFLSRIGVEPDVARVPVMIDSSDWNVVIGGLKCVQGRPIVNSISLKEGEESFIKKARDIKEMGAAVVVMA 490
Cdd:PRK09490 408 GMLDSEAAMVRFLNLIASEPDIARVPIMIDSSKWEVIEAGLKCIQGKGIVNSISLKEGEEKFIEHARLVRRYGAAVVVMA 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 491 FDEKGQADTFERRIEVCDRAYRLLTGKVGFKGCDIVFDPNVLAVATGIEEHADYALDFIRAVEWIKSNLPGAKVSGGVSN 570
Cdd:PRK09490 488 FDEQGQADTRERKIEICKRAYDILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKQNLPHAKISGGVSN 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 571 LSFSFRGNNSVREAMHALFLYHAIAKGMDMAIVNAAAIMPVDDIPDELREAIDDVLLNRSHDATERLVAIAEKIKSGNVT 650
Cdd:PRK09490 568 VSFSFRGNNPVREAIHAVFLYHAIKAGMDMGIVNAGQLAIYDDIPPELREAVEDVVLNRRPDATERLLEIAEKYRGKGGK 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 651 VAAESPSEEPSLTPDKRVERMLVKGVVDGMERNLSDAMAMLGSAVKVIEGPLMAGMNSVGEMFGAGKMFLPQVVKSARTM 730
Cdd:PRK09490 648 KAKAEDLEWRSWPVEKRLEHALVKGITEFIEEDTEEARQQAARPLEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVM 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 731 KQAVGWLTPFIERER-RGKVSSKAGKMVIATVKGDVHDIGKNIVGVIMNCNGYDIIDMGVMVPAEDIVDKAIAENADFVG 809
Cdd:PRK09490 728 KQAVAYLEPFIEAKKeGGTDRKSNGKILMATVKGDVHDIGKNIVGVVLQCNNYEVIDLGVMVPAEKILETAKEENADIIG 807
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 810 LSGLITPSLEEMCNVARLMESKRMKIPLLIGGATTSELHTAVKIAPCYSGPVLYTRDAA-MMPAAVRRLGDE---AEVAR 885
Cdd:PRK09490 808 LSGLITPSLDEMVHVAKEMERQGFTIPLLIGGATTSKAHTAVKIAPNYSGPVVYVTDASrAVGVVSSLLSDEqrdAYVAE 887
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 886 LRDSQAELRRKHSSGAG---LLSLSEARSKRPRLSYPCY--PVAH-PGVHEL-NIDIAEAREFINWRAFLSAWkidasla 958
Cdd:PRK09490 888 TRAEYEKVREQHARKKPrkpLLTLEAARANRFKIDWEAYtpPKPKfLGVQVFeDYDLAELREYIDWTPFFQTW------- 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 959 svmDIKGcdhcraQWLASVPSEKVnkAAEAMQLLKEAGRVLDRLQRDivGGIKAK--VAFVEAASDgGDDI-LFNHDGET 1035
Cdd:PRK09490 961 ---ELAG------KYPAILEDEVV--GEEARKLFADAQAMLDKIIAE--KWLTARgvIGLFPANSV-GDDIeVYTDESRT 1026
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 1036 LRIAT---LRQQRpSERDGHCIALSDYIAPVESDgkLRDSMGMFAVTVGRDIERIIESYKNEGDDYSAILYQTVADRLVE 1112
Cdd:PRK09490 1027 EVLATlhhLRQQT-EKRGRPNYCLADFVAPKESG--KADYIGAFAVTAGLGEDELADRFEAAHDDYNAIMVKALADRLAE 1103
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 1113 AATEVMHRKVRVELWGYAPDESLSERHVLQQYYKGIRPAIGYPSLPDQS---LIFltdRVLRYSD-MGITLTESGAMSPA 1188
Cdd:PRK09490 1104 AFAEYLHERVRKEFWGYAPDENLSNEELIREKYQGIRPAPGYPACPDHTekaTLF---DLLDAEKnTGMKLTESYAMWPG 1180
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....
gi 1616153298 1189 ASTTGLIISHPDSRYFVVGDVDNGQRRLYAERRAMSLDELKRFL 1232
Cdd:PRK09490 1181 ASVSGWYFSHPESKYFAVGKIGRDQVEDYAARKGMSVEEVERWL 1224
|
|
| metH |
TIGR02082 |
5-methyltetrahydrofolate--homocysteine methyltransferase; This family represents ... |
22-1206 |
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: 1330.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 22 REVLVLDGAMGTMIQRYGLSENDFRGErYAASDALLKGCNDALVLTRPDVIKDIHRKYLEAGAMIIETDSFNANAVSLGD 101
Cdd:TIGR02082 3 QRILVLDGAMGTQLQSANLTEADFRGA-FADCHRELKGNNDILNLTKPEVIATIHRAYFEAGADIIETNTFNSTTISQAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 102 YGLQHDVTALNHAAAKIAREAADEYmTQHPGAMRWVAGSIGPTSKSLTMGQGIDDPSAGVVDWDLLTETYIEQMKALIEG 181
Cdd:TIGR02082 82 YDLEDLIYDLNFKGAKLARAVADEF-TLTPEKPRFVAGSMGPTNKTATLSPDVERPGFRNVTYDELVDAYTEQAKGLLDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 182 GVDALLIETIYDGLNAKAAIWAARRAMEIVGVRVPLMLSVTLTE-SGRTLSGQTLEAIIASMSFGEPMSIGLNCGFGADA 260
Cdd:TIGR02082 161 GVDLLLIETCFDTLNAKAALFAAETVFEEKGRELPIMISGTIVDtSGRTLSGQTIEAFLTSLEHAGIDMIGLNCALGPDE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 261 MMKYVEALQPY-PYAVSVYPNAGLPNEMGEYDETPSMMADKIRVMLQRRWVNIVGGCCGTTPQHIKALAELCKQYAPRVV 339
Cdd:TIGR02082 241 MRPHLKHLSEHaEAYVSCHPNAGLPNAFGEYDLTPDELAKALADFAAEGGLNIVGGCCGTTPDHIRAIAEAVKNIKPRQR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 340 PEVEPEMTLAGLEPLCVTPRLNFVNVGERCNVAGSRKFLRLIKEGNIDEAIDIARNQVDAGAQIIDINMDDAMLDARACM 419
Cdd:TIGR02082 321 PVLYEPSRLSGLEAITIAQDSNFVNIGERTNVAGSKKFRRLIIAEDYDEALDIAKQQVENGAQILDINVDYGMLDGVAAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 420 TSFLSRIGVEPDVARVPVMIDSSDWNVVIGGLKCVQGRPIVNSISLKEGEESFIKKARDIKEMGAAVVVMAFDEKGQADT 499
Cdd:TIGR02082 401 KRFLNLLASEPDISTVPLMLDSSEWAVLEAGLKCIQGKCIVNSISLKDGEERFIETAKLIKEYGAAVVVMAFDEEGQART 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 500 FERRIEVCDRAYRLLTGKVGFKGCDIVFDPNVLAVATGIEEHADYALDFIRAVEWIKSNLPGAKVSGGVSNLSFSFRGNN 579
Cdd:TIGR02082 481 ADRKIEICKRAYNILTEKVGFPPEDIIFDPNILTIATGIEEHRRYAINFIEAIRWIKEELPDAKISGGVSNVSFSFRGNP 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 580 SVREAMHALFLYHAIAKGMDMAIVNAAAIMPVDDIPDELREAIDDVLLNRSHDATERLVAIAEKIKSGNVTVAAES-PSE 658
Cdd:TIGR02082 561 AAREAMHSVFLYHAIRAGMDMGIVNAGKILPYDDIDPELRQVVEDLILNRRREATEPLLELAQLYEGTTTKSSKEAqQAE 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 659 EPSLTPDKRVERMLVKGVVDGMERNLSDAMAMLGSAVKVIEGPLMAGMNSVGEMFGAGKMFLPQVVKSARTMKQAVGWLT 738
Cdd:TIGR02082 641 WRNLPVEERLEYALVKGEREGIEEDLEEARKKLTRPLEIIEGPLMDGMKVVGDLFGSGKMFLPQVVKSARVMKKAVAYLE 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 739 PFIERERRGkvSSKAGKMVIATVKGDVHDIGKNIVGVIMNCNGYDIIDMGVMVPAEDIVDKAIAENADFVGLSGLITPSL 818
Cdd:TIGR02082 721 PHMEKEKSE--DSSKGKIVLATVKGDVHDIGKNIVGVVLSCNGYEVVDLGVMVPIEKILEAAKDHNADVIGLSGLITPSL 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 819 EEMCNVARLMESKRMKIPLLIGGATTSELHTAVKIAPCYSGPVLYTRDA--------AMMPAAVRrlgdEAEVARLRDSQ 890
Cdd:TIGR02082 799 DEMKEVAEEMNRRGITIPLLIGGAATSKTHTAVKIAPIYKGPVVYVLDAsravtvmdTLMSAKRK----DTENGRIKEEY 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 891 AELRRKHSSGAG---LLSLSEARSKR--PRLSYPCYPVAHP--GVHEL-NIDIAEAREFINWRAFLSAWKIdaslasvmd 962
Cdd:TIGR02082 875 DTAREKHGEQRSkriAASEQAARKNVfaPDWSDDIEPPAPPfwGTQIVeASDIAELRPYIDWTPFFLQWQL--------- 945
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 963 ikgcdhcRAQWLASVPSEKVNkaAEAMQLLKEAGRVLDRLQRDivGGIKAKVAF-VEAASDGGDDILFnHDGETLR---I 1038
Cdd:TIGR02082 946 -------RGKYPKILGDEYEG--LEAQKLFPDANEMLDKLSAE--NLLHARGVYgYFPAQSVGDDIEI-YTDETVEthpI 1013
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 1039 ATLR--QQRPSERDGHCIALSDYIAPVESDGklRDSMGMFAVTVGRDIERIIESYKNEGDDYSAILYQTVADRLVEAATE 1116
Cdd:TIGR02082 1014 ATVRylFHFPRQQSGRYLCLADFIAPKASGI--VDYIGAFAVTAGFGAEELADKLEAQHDDYDYIMVKAIADRLAEAFAE 1091
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 1117 VMHRKVRVELWGYAPDESLSERHVLQQYYKGIRPAIGYPSLPDQSLIFLTDRVLRYSDMGITLTESGAMSPAASTTGLII 1196
Cdd:TIGR02082 1092 YLHRRVRKELWGYAAEEPLSNEDLLKLRYQGIRPAPGYPACPDHTEKATMFELLEPERIGVRLTESLAMHPEQSVSGLYF 1171
|
1210
....*....|
gi 1616153298 1197 SHPDSRYFVV 1206
Cdd:TIGR02082 1172 AHPEAKYFAV 1181
|
|
| MetH2 |
COG1410 |
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; ... |
31-1206 |
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: 1298.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 31 MGTMIQRYGLSENDFRGERYAASDALLKGCNDALVLTRPDVIKDIHRKYLEAGAMIIETDSFNANAVSLGDYGLQHDVTA 110
Cdd:COG1410 1 MGTMIQLLKLRELDADGAMFTDLQLDLKGNNDLLGLTGPNEILEIHRPELEAGADIIETNTGADAAITAADGAAEALLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 111 LNHAAAKIAREAADEYMTQHPGAMRWVAGSIGPTSKSLTMGQGIDDPSAGVVDWDLLTETYIEQMKALIEGGVDALLIET 190
Cdd:COG1410 81 YNGAAAALALEAAAAAAAAAAAAARAVAGAPGPTGGTASPGPDVPGLGFRNFDFDELVEAYAEAGLGLGGGGADLLLTET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 191 IYDGLNAKAAIWAARRAMEIVGVRVPLMLSVTLTE-SGRTLSGQTLEAIIASMSFGEPMSIGLNCGFGADAMMKYVEALQ 269
Cdd:COG1410 161 IFDTLNAAAAAAAAAAAAEEEGVPIPVMVTGTITDgSGRTLSGQTAEAFLESLGHAAPGSNGLNCALGAEELRPYLEELS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 270 -PYPYAVSVYPNAGLPNEMGEYDETPSMMADKIRVMLQRRWVNIVGGCCGTTPQHIKALAELCKQYAPRVvPEVEPEMTL 348
Cdd:COG1410 241 rIPPSAVSNAPNAGLPNGFGEYDETPEEMAAALAEFAEEGGVNIVGGCCGTTPEHIRAIAEAVAGLKPRP-REKPPPAVL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 349 AGLEPLCVTPRLNFVNVGERCNVAGSRKFLRLIKEGNIDEAIDIARNQVDAGAQIIDINMDDAMLDARACMTSFLSRIGV 428
Cdd:COG1410 320 SGLEPVPIGQDSPFVNIGERTNVTGSKKFRELILEGDYDEALEVAREQVEAGAQILDVNVDEPGRDEVAAMVRFLNLLAS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 429 EpdvARVPVMIDSSDWNVVIGGLKCVQGRPIVNSISLKEGEESFIKKARDIKEMGAAVVVMAFDEKGQADTFERRIEVCD 508
Cdd:COG1410 400 E---VRVPLMIDSSKPEVIEAGLKCYQGKPIVNSISLEEGEERFEEVAPLAKKYGAAVVVLAIDEEGQADTAERKLEIAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 509 RAYRLLTGKVGFKGCDIVFDPNVLAVATGIEEHADYALDFIRAVEWIKSNLPGAKVSGGVSNLSFSFRGNnsVREAMHAL 588
Cdd:COG1410 477 RIYDLAVEEYGFPPEDIIFDPLVFTVATGIEEHRNYAVETIEAIRLIKEELPGAKTSLGVSNVSFGLPGN--VREALNSV 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 589 FLYHAIAKGMDMAIVNAAAIMPVDDIPDELREAIDDVLLNRSHDATERLVAIAEKIKSgnvTVAAESPSEEPSLTPDKRV 668
Cdd:COG1410 555 FLYHAIKAGLDMAIVNPGQLEPYDDIPPELRELAEDVLLNRRPDALERLIELFEGVKG---AKAKKADLEWRELPVEERL 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 669 ERMLVKGVVDGMERNLSDAMAMLGSAVKVIEGPLMAGMNSVGEMFGAGKMFLPQVVKSARTMKQAVGWLTPFIERErrGK 748
Cdd:COG1410 632 KHAIVKGIKEGIEEDTEEALAEGARPLEIINGPLMPGMNVVGDLFGAGKMFLPQVLKSAEVMKAAVAYLEPFMEKE--KG 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 749 VSSKAGKMVIATVKGDVHDIGKNIVGVIMNCNGYDIIDMGVMVPAEDIVDKAIAENADFVGLSGLITPSLEEMCNVARLM 828
Cdd:COG1410 710 ESSSKGKIVLATVKGDVHDIGKNIVGVVLENNGYEVIDLGVMVPAEKILEAAKEHKADIIGLSGLMTTSLDEMKEVAEEM 789
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 829 ESKRMKIPLLIGGATTSELHTAVKIAPCYSGPVLYTRDAAMMPAAVRRL----GDEAEVARLRDSQAELRRKHSS-GAGL 903
Cdd:COG1410 790 RRRGLDIPVLIGGAALTRAYTAVKIAPAYDGAVVYAKDASRAVRVADKLlskeRREAFVAEIKAEYEKLRERHAArKKKL 869
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 904 LSLSEARSKRPRlSYPCYPVAHPGVHEL-NIDIAEAREFINWRAFLSAWkidaslasvmDIKGcdhcraqwlasvpseKV 982
Cdd:COG1410 870 LSLEEARSNVDS-DYPPPTPPFLGTRVLkDIPLAELVPYIDWTPFFQQW----------GLKG---------------KY 923
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 983 NKAAEAMQLLKEAGRVLDRLQRDIVGGIKAKVAFVEAASDGGDDILFNHDG--ETLRIATLRQQRpserdGHCIALSDYI 1060
Cdd:COG1410 924 LDGEEARELFPDAQAMLDRIIEEKWLTARAVYGYFPANSEGDDIEVYDDESseELARFHFPRQQR-----GPNLCLADFV 998
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 1061 APVESdgKLRDSMGMFAVTVGRDIERIIESYKNEGDDYSAILYQTVADRLVEAATEVMHRKVRVElWGYAPDESLSERHV 1140
Cdd:COG1410 999 APKES--GERDYVGFFAVTAGIGIEELAAELEAAGDDYDAIMLHALADRLAEAFAEYLHERVRKE-WGYAPDEALTNEDL 1075
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1616153298 1141 LQQYYKGIRPAIGYPSLPDQSLIFLTDRVLRYSDMGITLTESGAMSPAASTTGLIISHPDSRYFVV 1206
Cdd:COG1410 1076 IKEKYRGIRPAPGYPACPDHTEKRKLFDLLDAERIGVTLTESFAMHPEASVSGIYFHHPEAKYFNV 1141
|
|
| MetH1 |
COG0646 |
Methionine synthase I (cobalamin-dependent), methyltransferase domain [Amino acid transport ... |
15-837 |
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: 806.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 15 KLMEAAGREVLVLDGAMGTMIQRYGLSENDFRGEryaasdallKGCNDALVLTRPDVIKDIHRKYLEAGAMIIETDSFNA 94
Cdd:COG0646 5 ALLELLKERILILDGAMGTMLQAYGLTEGDFRGE---------KGCNELLNLTRPDVIREIHRAYLEAGADIIETNTFGA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 95 NAVSLGDYGLQHDVTALNHAAAKIAREAADEYmTQHPgamRWVAGSIGPTSKSLTmgqgiddpSAGVVDWDLLTETYIEQ 174
Cdd:COG0646 76 NRIKLADYGLEDRVYEINRAAARLAREAADEF-SDRP---RFVAGSIGPTGKLLS--------PLGNITFDELVEAYREQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 175 MKALIEGGVDALLIETIYDGLNAKAAIWAARRAMEIVGVRVPLMLSVTLTESGRTLSGQTLEAIIASMSFGEPMSIGLNC 254
Cdd:COG0646 144 AEGLIEGGVDLLLIETIFDTLEAKAAIFAAREAFEELGRDLPVMVSGTFDASGRTLSGQTPEAFATSLEHLGPDAIGLNC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 255 GFGADAMMKYVEALQPY-PYAVSVYPNAGLPNEMGE---YDETPSMMADKIRVMLQRRWVNIVGGCCGTTPQHIKALAEL 330
Cdd:COG0646 224 ALGPDEMRPHVEELSEVaDTPVSAYPNAGLPNLVGGrtvYDETPEEMAEYAEEFAEAGGVNIVGGCCGTTPEHIRAIAEA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 331 CKQYAPRVVPEVEPEMTLAGLEPLCVTPRLNFVNVGERCNVAGSRKFLRLIKEGNIDEAIDIARNQVDAGAQIIDINMDD 410
Cdd:COG0646 304 VKGLPPRKRPPPPPALRLSGLEPLTITQDSLFVNVGERTNVTGSKKFARLILEGDYDAALAVARQQVEAGAQVIDVNMDE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 411 AMLDARACMTSFLSRIGVEPDVARVPVMIDSSDWNVVIGGLKCVQGRPIVNSISLKEGEESFIKKARDIKEMGAAVVVMA 490
Cdd:COG0646 384 GMLDGEAAMVEFLNLIASEPDIPRVPDMIDSSKWEVIEAGLKGVQGKGIVNSISLKEGEEKFLELAKLVRRYGAAVVVMA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 491 FDEKGQADTFERRIEVCDRAYRLLTGKVGFKGCDIVFDPNVLAVATGIEEHADYALDFIRAVEWIKSNLPGAKVSGGVSN 570
Cdd:COG0646 464 FDEEGQADTAERKVEICARAYDLLTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKLNLPHALVSGGVSN 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 571 LSFSFRGNNSVREAMHALFLYHAIAKGMDMAIVNAAAIMPVDDIPDELREAIDDVLLNRSHDATERLVAIAEKIKSGNVT 650
Cdd:COG0646 544 VSFSFRGNNPVREAIHAVFLYHAIAAGMDMGIVNAGQLAIYEEIPEELLLLVEDVVLNRREDATERLLEIAEEVKGAGKA 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 651 VAAESPSEEPSLTPDKRVERMLVKGVVDGMERNLSDAMAMLGSAVKVIEGPLMAGMNSVGEMFGAGKMFLPQVVKSARTM 730
Cdd:COG0646 624 AEEEAEEERREEEEERLLELLLVGGIEIDEEDDEEAALLLAALELIIIELLLGGGMVVGGLGGGGGKLLLVVVVKAVVKK 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 731 KQAVGwLTPFIERERRGKVSSKAGKMVIATVKGDVHDIGKNIVGVIMNCNGYDIIDMGVMVPAEDIVDKAIAENADFVGL 810
Cdd:COG0646 704 KVAVA-LLKPEEEEKKKGGGKGGGVVVGVVVKVVVDDVDIIIVVVVVVVNNGIVVLVVVVIVVVALEAAAAAEAAVILLV 782
|
810 820
....*....|....*....|....*..
gi 1616153298 811 SGLITPSLEEMCNVARLMESKRMKIPL 837
Cdd:COG0646 783 GGLVLLLLEEEVLAAAEAAAEAAVLLL 809
|
|
| MeTr |
cd00740 |
MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent ... |
362-618 |
6.87e-114 |
|
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: 355.55 E-value: 6.87e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 362 FVNVGERCNVAGSRKFLRLIKEGNIDEAIDIARNQVDAGAQIIDINMDDAMLDARACMTSFLSRIGVEPdvaRVPVMIDS 441
Cdd:cd00740 1 FLNIGERTNVTGSKKFRELIKAEDYDEALDVARQQVEGGAQILDLNVDYGGLDGVSAMKWLLNLLATEP---TVPLMLDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 442 SDWNVVIGGLKCVQGRPIVNSISLKEGEESFIKKARDIKEMGAAVVVMAFDEKGQADTFERRIEVCDRAYRLLTGKVGFK 521
Cdd:cd00740 78 TNWEVIEAGLKCCQGKCVVNSINLEDGEERFLKVARLAKEHGAAVVVLAFDEQGQAKTRDKKVEIAERAYEALTEFVGFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 522 GCDIVFDPNVLAVATGIEEHADYALDFIRAVEWIKSNLPGAKVSGGVSNLSFSFrgNNSVREAMHALFLYHAIAKGMDMA 601
Cdd:cd00740 158 PEDIIFDPLILPIATGIEEHRPYALETIDAIRMIKERLPAVKISLGVSNVSFGF--NPAAREALNSVFLYEAIKAGLDMA 235
|
250
....*....|....*..
gi 1616153298 602 IVNAAAIMPVDDIPDEL 618
Cdd:cd00740 236 IVNAGKLAPIEDIPEEL 252
|
|
| methionine_synthase_B12_BD |
cd02069 |
B12 binding domain of methionine synthase. This domain binds methylcobalamin, which it uses as ... |
664-867 |
1.82e-97 |
|
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: 309.58 E-value: 1.82e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 664 PDKRVERMLVKGVVDGMERNLSDAMAMLGSAVKVIEGPLMAGMNSVGEMFGAGKMFLPQVVKSARTMKQAVGWLTPFIER 743
Cdd:cd02069 1 VEERLKHALVKGIRDGIEEDTEEARQQYARPLEIINGPLMDGMKVVGDLFGAGKMFLPQVLKSARVMKAAVAYLEPYMEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 744 ERRGkvSSKAGKMVIATVKGDVHDIGKNIVGVIMNCNGYDIIDMGVMVPAEDIVDKAIAENADFVGLSGLITPSLEEMCN 823
Cdd:cd02069 81 EKGE--NSSKGKIVLATVKGDVHDIGKNLVGVILSNNGYEVIDLGVMVPIEKILEAAKEHKADIIGLSGLLVPSLDEMVE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1616153298 824 VARLMESKRMKIPLLIGGATTSELHTAVKIAPCYSGPVLYTRDA 867
Cdd:cd02069 159 VAEEMNRRGIKIPLLIGGAATSRKHTAVKIAPEYDGPVVYVKDA 202
|
|
| Met_synt_B12 |
pfam02965 |
Vitamin B12 dependent methionine synthase, activation domain; |
934-1221 |
1.06e-92 |
|
Vitamin B12 dependent methionine synthase, activation domain;
Pssm-ID: 460767 [Multi-domain] Cd Length: 273 Bit Score: 299.00 E-value: 1.06e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 934 DIAEAREFINWRAFLSAWkidaslasvmDIKGCDhcraqwlASVPSEKVnKAAEAMQLLKEAGRVLDRLQRDIVGGIKAK 1013
Cdd:pfam02965 1 DLAELVPYIDWTPFFQAW----------ELKGKY-------PAILDDEV-VGEEARKLFADAQAMLDRIIEEKWLTARGV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 1014 VAFVEAASDGgDDILFNHD----GETLRIATLRQQRPSERDGHCIALSDYIAPVESdGKlRDSMGMFAVTVGRDIERIIE 1089
Cdd:pfam02965 63 VGFFPANSVG-DDIEVYTDesrtEVLATFHTLRQQTEKPEGRPNLCLADFIAPKES-GI-ADYIGAFAVTAGIGIEELAA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 1090 SYKNEGDDYSAILYQTVADRLVEAATEVMHRKVRVELWGYAPDESLSERHVLQQYYKGIRPAIGYPSLPDQSLIFLTDRV 1169
Cdd:pfam02965 140 RFEAAHDDYSAIMVKALADRLAEAFAEYLHERVRKELWGYAPDENLSNEDLIKEKYQGIRPAPGYPACPDHTEKFTLFDL 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1616153298 1170 LrysDM----GITLTESGAMSPAASTTGLIISHPDSRYFVVGDVDNGQRRLYAERR 1221
Cdd:pfam02965 220 L---DAeeniGIRLTESFAMTPAASVSGLYFAHPESRYFAVGKIGKDQVEDYAKRK 272
|
|
| S-methyl_trans |
pfam02574 |
Homocysteine S-methyltransferase; This is a family of related homocysteine ... |
25-331 |
4.81e-79 |
|
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: 260.94 E-value: 4.81e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 25 LVLDGAMGTMIQRYGLS-ENDFRgeryaasdallkgCNDalVLTRPDVIKDIHRKYLEAGAMIIETDSFNANAVSLGD-Y 102
Cdd:pfam02574 1 LILDGGMGTELQRRGLDlTEPLW-------------SNE--LLTRPEIIREIHRDYLEAGADIIETNTYQASPIKLAEgL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 103 GLQHDVTALNHAAAKIAREAADEYmtqhpgamrWVAGSIGPTSKSLTMGQGIddpsagvvDWDLLTETYIEQMKALIEGG 182
Cdd:pfam02574 66 EEEEAVYELNRAAVRLAREAADEY---------FVAGSIGPYGATLSDGYGL--------SFDELVDFHREQLEALLDGG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 183 VDALLIETIYDGLNAKaaiwAARRAMEIVgVRVPLMLSVTLTESGRTLSGQTLEAIIASM-SFGEPMSIGLNCGFgADAM 261
Cdd:pfam02574 129 VDLLLFETIPDLLEAK----AALELLAEE-PDLPVWISFTIEDGTRLRSGTTLEAAVAALlHATGPLAVGVNCAL-PEEM 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1616153298 262 MKYVEALQPY-PYAVSVYpnaglPNEMGE-YDETPSMMADKIRVMLQRRwVNIVGGCCGTTPQHIKALAELC 331
Cdd:pfam02574 203 LPLLKELAKDaPTPVSVY-----PNSTGEvYDLTPEEWAEYAEGWLEAG-ANIIGGCCGTTPEHIRAIAEAL 268
|
|
| PRK08645 |
PRK08645 |
bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; ... |
15-395 |
5.26e-61 |
|
bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; Reviewed
Pssm-ID: 236321 [Multi-domain] Cd Length: 612 Bit Score: 220.87 E-value: 5.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 15 KLMEAAGREVLVLDGAMGTMIQRYGLSendfrgeryaasdalLKGCNDALVLTRPDVIKDIHRKYLEAGAMIIETDSFNA 94
Cdd:PRK08645 3 KLLERLKERVLIADGAMGTLLYSRGVP---------------LDRCFEELNLSHPELILRIHREYIEAGADVIQTNTFGA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 95 NAVSLGDYGLQHDVTALNHAaakiareaadeymtqhpgAMR----------WVAGSIGPtsksltMGQGIDDPSagvVDW 164
Cdd:PRK08645 68 NRIKLKRYGLEDKVKEINRA------------------AVRlareaagddvYVAGTIGP------IGGRGPLGD---ISL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 165 DLLTETYIEQMKALIEGGVDALLIETIYDGLNAKAAIWAARRAMEIvgvrvPLMLSVTLTESGRTLSGQTLEAIIASMSF 244
Cdd:PRK08645 121 EEIRREFREQIDALLEEGVDGLLLETFYDLEELLLALEAAREKTDL-----PIIAQVAFHEDGVTQNGTSLEEALKELVA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 245 GEPMSIGLNCGFGADAMMKYVEALQ-PYPYAVSVYPNAGLPNEMGE---YDETPSMMADKIRVMLQRRwVNIVGGCCGTT 320
Cdd:PRK08645 196 AGADVVGLNCGLGPYHMLEALERIPiPENAPLSAYPNAGLPEYVDGryvYSANPEYFAEYALEFVEQG-VRLIGGCCGTT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 321 PQHIKALAELCKQYAPRVVPEVEPEMTLA-GLEPLCVTPRLnFVNVGERCNVA---------GSRKFL---RLIKEGNID 387
Cdd:PRK08645 275 PEHIRAMARALKGLKPVTEKEVKPRPKVVvTEEPLKAKSSL-LDKLKKGKTVIveldppkglDTDKFLegaKALKEAGVD 353
|
....*...
gi 1616153298 388 eAIDIARN 395
Cdd:PRK08645 354 -AITLADN 360
|
|
| Pterin_bind |
pfam00809 |
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ... |
366-604 |
1.32e-53 |
|
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: 187.49 E-value: 1.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 366 GERCNVAGSRKFLRLIKEgNIDEAIDIARNQVDAGAQIIDINMDDA-----MLDARACMTSFLSRIGVEPDVARVPVMID 440
Cdd:pfam00809 1 MGILNVTPDSFSDGGRFL-DLDKALAHARRMVEEGADIIDIGGESTrpgaeRVDGEEEMERVLPVLAALRDEADVPISVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 441 SSDWNVVIGGLKCvqGRPIVNSISLKEGeesFIKKARDIKEMGAAVVVMAFD--------EKGQADTFERRIEVCDRAYR 512
Cdd:pfam00809 80 TTKAEVAEAALKA--GADIINDISGGDG---DPEMAELAAEYGAAVVVMHMDgtpktmqeNEQQYEDVVEEVERFLRARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 513 LLTGKVGFKGCDIVFDPNVLavATGIEEHADYALDFIRAVEWIKsnlpGAKVSGGVSNLSFSFRGNN---SVREAMHALF 589
Cdd:pfam00809 155 AAAEEAGVPPEDIILDPGIG--FGKTEEHNLELLRTLDELRVIL----GVPVLLGVSRKSFIGRGLPlggEERDAGTAAF 228
|
250
....*....|....*
gi 1616153298 590 LYHAIAKGMDMAIVN 604
Cdd:pfam00809 229 LALAIAAGADIVRVH 243
|
|
| Pterin_binding |
cd00423 |
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and ... |
362-623 |
3.31e-47 |
|
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: 169.76 E-value: 3.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 362 FVNVGErCNVAGSrKFLRLIKEGNIDEAIDIARNQVDAGAQIIDINMDDAMLDARAC-MTSFLSRigVEP------DVAR 434
Cdd:cd00423 1 TLIMGI-LNVTPD-SFSDGGKFLSLDKALEHARRMVEEGADIIDIGGESTRPGAEPVsVEEELER--VIPvlralaGEPD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 435 VPVMIDSSDWNVVIGGLKCvqGRPIVNSISLKEGEEsfiKKARDIKEMGAAVVVMAFDEKGQ--------ADTFERRIEV 506
Cdd:cd00423 77 VPISVDTFNAEVAEAALKA--GADIINDVSGGRGDP---EMAPLAAEYGAPVVLMHMDGTPQtmqnnpyyADVVDEVVEF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 507 CDRAYRLLTGKVGFKGcDIVFDPNVLAVATgiEEHADYALDFIRAVEWIksnlPGAKVSGGVSNLSFSFR---GNNSVRE 583
Cdd:cd00423 152 LEERVEAATEAGIPPE-DIILDPGIGFGKT--EEHNLELLRRLDAFREL----PGLPLLLGVSRKSFLGDllsVGPKDRL 224
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1616153298 584 AMHALFLYHAIAKGMDMAIVNAAAimpvddipdELREAID 623
Cdd:cd00423 225 AGTAAFLAAAILNGADIVRVHDVK---------ELRDAIK 255
|
|
| corrinoid_protein_B12-BD |
cd02070 |
B12 binding domain of corrinoid proteins. A family of small methanogenic corrinoid proteins ... |
672-846 |
2.70e-44 |
|
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: 159.32 E-value: 2.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 672 LVKGVVDGMERN----LSDAMAMLGSAVKVIEGPLMAGMNSVGEMFGAGKMFLPQVVKSARTMKQAVGWLTPFIErerrG 747
Cdd:cd02070 1 LADAIVDGDEEEtvelVKKALEAGIDPQDIIEEGLAPGMDIVGDKYEEGEIFVPELLMAADAMKAGLDLLKPLLG----K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 748 KVSSKAGKMVIATVKGDVHDIGKNIVGVIMNCNGYDIIDMGVMVPAEDIVDKAIAENADFVGLSGLITPSLEEMCNVARL 827
Cdd:cd02070 77 SKSAKKGKVVIGTVEGDIHDIGKNLVATMLEANGFEVIDLGRDVPPEEFVEAVKEHKPDILGLSALMTTTMGGMKEVIEA 156
|
170 180
....*....|....*....|.
gi 1616153298 828 MESK--RMKIPLLIGGATTSE 846
Cdd:cd02070 157 LKEAglRDKVKVMVGGAPVNQ 177
|
|
| MtbC1 |
COG5012 |
Methanogenic corrinoid protein MtbC1 [Energy production and conversion]; |
660-877 |
3.40e-41 |
|
Methanogenic corrinoid protein MtbC1 [Energy production and conversion];
Pssm-ID: 444036 [Multi-domain] Cd Length: 219 Bit Score: 151.20 E-value: 3.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 660 PSLTPDKRVERMLVKGVVDGMERNLSD----AMAMLGSAVKVIEGPLMAGMNSVGEMFGAGKMFLPQVVKSARTMKQAVG 735
Cdd:COG5012 2 LTRPYGEELLESLADAVLEGDEDEALElvaeALAAGMDPEEIILDGLAPGMREVGELWEEGEIFVPEEHLAAAAMKAGLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 736 WLTPFIERERRgkvssKAGKMVIATVKGDVHDIGKNIVGVIMNCNGYDIIDMGVMVPAEDIVDKAIAENADFVGLSGLIT 815
Cdd:COG5012 82 ILKPLLAEEGG-----RKGKVVIGTVEGDLHDIGKNIVADMLRAAGFEVIDLGADVPPEEFVEAAKEEKPDIVGLSALLT 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616153298 816 PSLEEMCNVARLM--ESKRMKIPLLIGGATTSElHTAVKIapcysGPVLYTRDAAMMPAAVRRL 877
Cdd:COG5012 157 TTMPAMKELIEALreAGLRDKVKVIVGGAPVTE-ELAEEI-----GADAYAEDAADAVELAKEL 214
|
|
| MHT1 |
COG2040 |
Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) [Amino acid transport and ... |
19-335 |
2.40e-37 |
|
Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) [Amino acid transport and metabolism];
Pssm-ID: 441643 [Multi-domain] Cd Length: 301 Bit Score: 142.64 E-value: 2.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 19 AAGREVLVLDGAMGTMIQRYGLSEND--FrgeryaASDALLKgcndalvltRPDVIKDIHRKYLEAGAMIIETDSFNANA 96
Cdd:COG2040 8 LLMGRILLLDGGMGTELERRGGDLLDplW------SAFALLE---------APELVRAVHRDYFAAGADVITTNSYQASP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 97 VSLGDYGLQHD-VTALNHAAAKIAREAADEYMTQHPGamrWVAGSIGPTSKSLTMGQGIDDpsAGVVDWdlltetYIEQM 175
Cdd:COG2040 73 DGLAELGYSAEeAERLNRRAVALAREARDEYTPGPPV---LVAGSVGPYGDEYRPDYGLSA--EEAEAY------HRPRI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 176 KALIEGGVDALLIETIydglNAKAAIWAARRAMEIVGVrvPLMLSVTLTESGRTLSGQTLEAIIASM-SFGEPMSIGLNC 254
Cdd:COG2040 142 EALAEAGVDLLAAETI----PSLAEAIAIARAAAEAGK--PVWISFTVEDDGRLRSGEPLAEAIAAVdTDPGPAAVGVNC 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 255 gfgadAMMKYVEALQPYPYAVS-----VYPNAG----------LPNEMGEYDETPSMMADkirvmLQRRWVNIVGGCCGT 319
Cdd:COG2040 216 -----SHPEHFEAALEALAAWTgrpigVYANAGemsdaelktwGGLDDGDPEELAEQAAE-----WVAAGARIIGGCCGT 285
|
330
....*....|....*.
gi 1616153298 320 TPQHIKALAELCKQYA 335
Cdd:COG2040 286 GPRHIAAIARALRAAG 301
|
|
| B12-binding |
cd02067 |
B12 binding domain (B12-BD). This domain binds different cobalamid derivates, like B12 ... |
755-868 |
1.04e-35 |
|
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: 131.47 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 755 KMVIATVKGDVHDIGKNIVGVIMNCNGYDIIDMGVMVPAEDIVDKAIAENADFVGLSGLITPSLEEMCNVARLMESK-RM 833
Cdd:cd02067 1 KVVIATVGGDGHDIGKNIVARALRDAGFEVIDLGVDVPPEEIVEAAKEEDADAIGLSGLLTTHMTLMKEVIEELKEAgLD 80
|
90 100 110
....*....|....*....|....*....|....*
gi 1616153298 834 KIPLLIGGATTSELHTAVKiapcYSGPVLYTRDAA 868
Cdd:cd02067 81 DIPVLVGGAIVTRDFKFLK----EIGVDAYFGPAT 111
|
|
| PRK07534 |
PRK07534 |
betaine--homocysteine S-methyltransferase; |
20-343 |
6.73e-34 |
|
betaine--homocysteine S-methyltransferase;
Pssm-ID: 236045 [Multi-domain] Cd Length: 336 Bit Score: 133.72 E-value: 6.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 20 AGREVLVLDGAMGTMIQRYGLSendfrgeryaASDAllkgcNDALVLTRPDVIKDIHRKYLEAGAMIIETDSFNANAVSL 99
Cdd:PRK07534 10 AERGVLLADGATGTNLFNMGLE----------SGEA-----PELWNEDHPDNITALHQGFVDAGSDIILTNSFGGTAARL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 100 GDYGLQHDVTALNHAAAKIAREAADEymtqhPGAMRWVAGSIGPTSKsltmgqgIDDPsAGVVDWDLLTETYIEQMKALI 179
Cdd:PRK07534 75 KLHDAQDRVHELNRAAAEIAREVADK-----AGRKVIVAGSVGPTGE-------IMEP-MGALTHALAVEAFHEQAEGLK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 180 EGGVDALLIETIYDGLNAKAAIWAARRameivgVRVPLMLSVTLTESGRTLSGQTlEAIIASM--SFGE-PMSIGLNCGF 256
Cdd:PRK07534 142 AGGADVLWVETISAPEEIRAAAEAAKL------AGMPWCGTMSFDTAGRTMMGLT-PADLADLveKLGEpPLAFGANCGV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 257 GADAMMKYVE--ALQPYPYAVSVYPNAGLPNEMG---EYDETPSMMADkIRVMLQRRWVNIVGGCCGTTPQHIKALAELC 331
Cdd:PRK07534 215 GASDLLRTVLgfTAQGPERPIIAKGNAGIPKYVDghiHYDGTPELMAE-YAVLARDAGARIIGGCCGTMPEHLAAMRAAL 293
|
330
....*....|..
gi 1616153298 332 KQYAPRVVPEVE 343
Cdd:PRK07534 294 DARPRGPRPSLE 305
|
|
| pyl_corrinoid |
TIGR02370 |
methyltransferase cognate corrinoid proteins, Methanosarcina family; This model describes a ... |
672-846 |
5.04e-33 |
|
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: 126.84 E-value: 5.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 672 LVKGVVDGMERNLSDAMAMLGSAVKVIEGPLMAGMNSVGEMFGAGKMFLPQVVKSARTMKQAVGWLTPFIERerrGKVSS 751
Cdd:TIGR02370 6 IFEGEEDDVVEGAQKALDAGIDPIELIEKGLMAGMGVVGKLFEDGELFLPHVMMSADAMLAGIKVLTPEMEK---AVETE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 752 KAGKMVIATVKGDVHDIGKNIVGVIMNCNGYDIIDMGVMVPAEDIVDKAIAENADFVGLSGLITPSLEEMCNVA-RLMES 830
Cdd:TIGR02370 83 VLGKVVCGVAEGDVHDIGKNIVVTMLRANGFDVIDLGRDVPIDTVVEKVKKEKPLMLTGSALMTTTMYGQKDINdKLKEE 162
|
170
....*....|....*..
gi 1616153298 831 K-RMKIPLLIGGATTSE 846
Cdd:TIGR02370 163 GyRDSVKFMVGGAPVTQ 179
|
|
| B12-binding_like |
cd02065 |
B12 binding domain (B12-BD). Most of the members bind different cobalamid derivates, like B12 ... |
755-877 |
2.63e-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: 122.11 E-value: 2.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 755 KMVIATVKGDVHDIGKNIVGVIMNCNGYDIIDMGVMVPAEDIVDKAIAENADFVGLSGLITPSLEEMCNVARLMESKRMK 834
Cdd:cd02065 1 KVLGATVGGDVHDIGKNIVAIALRDNGFEVIDLGVDVPPEEIVEAAKEEDADVVGLSALSTTHMEAMKLVIEALKELGID 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1616153298 835 IPLLIGGATTSELHTAVKIAPCYSGPVLYTRDAAMMPAAVRRL 877
Cdd:cd02065 81 IPVVVGGAHPTADPEEPKVDAVVIGEGEYAGPALLEVEGIAYR 123
|
|
| mmuM |
PRK09485 |
homocysteine methyltransferase; Provisional |
15-333 |
1.59e-31 |
|
homocysteine methyltransferase; Provisional
Pssm-ID: 181899 [Multi-domain] Cd Length: 304 Bit Score: 126.12 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 15 KLMEA-AGREVLVLDGAMGTMIQRYGlsendfrgerYAASDALLKgcndALVLT-RPDVIKDIHRKYLEAGAMIIETDSF 92
Cdd:PRK09485 3 PFKELlAQGPVLILDGALATELEARG----------CDLNDSLWS----AKVLLeNPELIYQVHLDYFRAGADCAITASY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 93 NANAVSLGDYGL-QHDVTALNHAAAKIAREAADEYMTQHPgamrWVAGSIGPTSKSLTMG---QGiddpsagvvDWDLLT 168
Cdd:PRK09485 69 QATFQGFAARGLsEAEAEELIRRSVELAKEARDEFWAEKP----LVAGSVGPYGAYLADGseyRG---------DYGLSE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 169 ETYIE----QMKALIEGGVDALLIETIYDGLNAKAAIwaarRAMEIVGVRVPLMLSVTLTESGRTLSGQTLEAIIASM-S 243
Cdd:PRK09485 136 EELQDfhrpRIEALAEAGADLLACETIPNLDEAEALV----ELLKEEFPGVPAWLSFTLRDGTHISDGTPLAEAAALLaA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 244 FGEPMSIGLNCG--FGADAMMKYVEALQPYPyaVSVYPNAGlpnemGEYD---------ETPSMMADKIRvmlqrRW--- 309
Cdd:PRK09485 212 SPQVVAVGVNCTapELVTAAIAALRAVTDKP--LVVYPNSG-----EVYDavtktwhgpADDASLGELAP-----EWyaa 279
|
330 340
....*....|....*....|....*
gi 1616153298 310 -VNIVGGCCGTTPQHIKALAELCKQ 333
Cdd:PRK09485 280 gARLIGGCCRTTPEDIAALAAALKT 304
|
|
| PRK07535 |
PRK07535 |
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase; Validated |
365-629 |
4.69e-27 |
|
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase; Validated
Pssm-ID: 181022 [Multi-domain] Cd Length: 261 Bit Score: 111.87 E-value: 4.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 365 VGERCNvaGSRKFLRL-IKEGNIDEAIDIARNQVDAGAQIIDINMDDAMLDARACMTSFLSRIgvePDVARVPVMIDSSD 443
Cdd:PRK07535 4 IGERIN--GTRKSIAEaIEAKDAAFIQKLALKQAEAGADYLDVNAGTAVEEEPETMEWLVETV---QEVVDVPLCIDSPN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 444 WNVVIGGLKCVQGRPIVNSISLkEGE--ESFIKKardIKEMGAAVVVMAFDEKGQADTFERRIEVCDRAYRLLTgKVGFK 521
Cdd:PRK07535 79 PAAIEAGLKVAKGPPLINSVSA-EGEklEVVLPL---VKKYNAPVVALTMDDTGIPKDAEDRLAVAKELVEKAD-EYGIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 522 GCDIVFDPNVLAVATgIEEHADYALDFIRAvewIKSNLPGAKVSGGVSNLSFsfrgNNSVREAMHALFLYHAIAKGMDMA 601
Cdd:PRK07535 154 PEDIYIDPLVLPLSA-AQDAGPEVLETIRR---IKELYPKVHTTCGLSNISF----GLPNRKLINRAFLVMAMGAGMDSA 225
|
250 260
....*....|....*....|....*....
gi 1616153298 602 IVNaaaimPVD-DIPDELREAidDVLLNR 629
Cdd:PRK07535 226 ILD-----PLDrDLMGAIAAA--EALLGQ 247
|
|
| B12-binding_2 |
smart01018 |
B12 binding domain; Cobalamin-dependent methionine synthase is a large modular protein that ... |
662-745 |
4.62e-24 |
|
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: 97.16 E-value: 4.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 662 LTPDKRVERMLVKGVVDGMERNLSDAMAMLGSAVKVIEGPLMAGMNSVGEMFGAGKMFLPQVVKSARTMKQAVGWLTPFI 741
Cdd:smart01018 1 MPLLERLAEAIVDGDEEGVEELVEEALAEGVDPLEIINEGLIPGMNVVGDLFEAGEYFLPQVLMSAEAMKAAVAILKPLL 80
|
....
gi 1616153298 742 ERER 745
Cdd:smart01018 81 EKEK 84
|
|
| B12-binding |
pfam02310 |
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ... |
754-842 |
6.58e-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: 6.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 754 GKMVIATVKGDVHDIGKNIVGVIMNCNGYDIIDMGVMVPAEDIVDKAIAENADFVGLSGLITPSLEEMCNVARLMESKRM 833
Cdd:pfam02310 1 GKVVVATVGGDLHPLGLNYVAAALRAAGFEVIILGANVPPEDIVAAARDEKPDVVGLSALMTTTLPGAKELIRLLKGIRP 80
|
....*....
gi 1616153298 834 KIPLLIGGA 842
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 ... |
672-737 |
2.81e-14 |
|
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: 68.65 E-value: 2.81e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1616153298 672 LVKGVVDGMERNLSDAM--AMLGSAVKVIEGPLMAGMNSVGEMFGAGKMFLPQVVKSARTMKQAVGWL 737
Cdd:pfam02607 1 LLEALLEGDEEAAEELLeeALEIDPEEIIEDLLIPGMDEVGELWEAGEIFVPQEHLAAEAMKAALAVL 68
|
|
| PLN02489 |
PLN02489 |
homocysteine S-methyltransferase |
24-334 |
8.96e-11 |
|
homocysteine S-methyltransferase
Pssm-ID: 215269 Cd Length: 335 Bit Score: 65.03 E-value: 8.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 24 VLVLDGAMGTMIQRYGLSENDfrgERYAASdallkgcndaLVLTRPDVIKDIHRKYLEAGAMIIETDSFNANAVSLGDYG 103
Cdd:PLN02489 22 CAVIDGGFATELERHGADLND---PLWSAK----------CLITSPHLIRKVHLDYLEAGADIIITASYQATIQGFESRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 104 L----------------QHDVTALNHAAAKIAREAADEYMTQHPgamRWVAGSIGPTSKSLTMG---QGIDDPSagvVDW 164
Cdd:PLN02489 89 LsreesetllrksveiaCEARDIFWDKCQKGSTSRPGRELSYRP---ILVAASIGSYGAYLADGseySGDYGPS---VTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 165 DLLTETYIEQMKALIEGGVDALLIETIYDGLNAKAAIwaarRAMEIVGVRVPLMLSVTLTESGRTLSGQTL-EAIIASMS 243
Cdd:PLN02489 163 EKLKDFHRRRLQVLAEAGPDLIAFETIPNKLEAQAYV----ELLEEENIKIPAWISFNSKDGVNVVSGDSLlECASIADS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 244 FGEPMSIGLNCgfgadAMMKYVEAL-----QPYPYAVSVYPNAGlpnEmgEYD------ETPSMMADKIRVMLQRRW--- 309
Cdd:PLN02489 239 CKKVVAVGINC-----TPPRFIHGLilsirKVTSKPIVVYPNSG---E--TYDgeakewVESTGVSDEDFVSYVNKWrda 308
|
330 340
....*....|....*....|....*.
gi 1616153298 310 -VNIVGGCCGTTPQHIKALAELCKQY 334
Cdd:PLN02489 309 gASLIGGCCRTTPNTIRAISKALSER 334
|
|
| Sbm |
COG2185 |
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ... |
755-841 |
8.80e-09 |
|
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and metabolism];
Pssm-ID: 441788 [Multi-domain] Cd Length: 134 Bit Score: 55.15 E-value: 8.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 755 KMVIATVKGDVHDIGKNIVGVIMNCNGYDIIDMGVMVPAEDIVDKAIAENADFVGLSGL------ITPSLeemcnVARLM 828
Cdd:COG2185 12 RVLLAKPGLDGHDRGAKVIARALRDAGFEVIYLGLFQTPEEIVRAAIEEDADVIGVSSLdgghleLVPEL-----IELLK 86
|
90
....*....|...
gi 1616153298 829 ESKRMKIPLLIGG 841
Cdd:COG2185 87 EAGAGDILVVVGG 99
|
|
| MM_CoA_mut_B12_BD |
cd02071 |
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), ... |
755-841 |
2.31e-05 |
|
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), which initiates the conversion of succinyl CoA and methylmalonyl CoA by forming an adenosyl radical, which then undergoes a rearrangement exchanging a hydrogen atom with a group attached to a neighboring carbon atom. This family is present in both mammals and bacteria. Bacterial members are heterodimers and involved in the fermentation of pyruvate to propionate. Mammalian members are homodimers and responsible for the conversion of odd-chain fatty acids and branched-chain amino acids via propionyl CoA to succinyl CoA for further degradation.
Pssm-ID: 239022 [Multi-domain] Cd Length: 122 Bit Score: 44.89 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 755 KMVIATVKGDVHDIGKNIVGVIMNCNGYDIIDMGVMVPAEDIVDKAIAENADFVGLSGLITPSLE---EMcnVARLMESK 831
Cdd:cd02071 1 RILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRQTPEEIVEAAIQEDVDVIGLSSLSGGHMTlfpEV--IELLRELG 78
|
90
....*....|
gi 1616153298 832 RMKIPLLIGG 841
Cdd:cd02071 79 AGDILVVGGG 88
|
|
| PRK02261 |
PRK02261 |
methylaspartate mutase subunit S; Provisional |
755-813 |
4.29e-05 |
|
methylaspartate mutase subunit S; Provisional
Pssm-ID: 179400 [Multi-domain] Cd Length: 137 Bit Score: 44.56 E-value: 4.29e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1616153298 755 KMVIATVKGDVHDIGKNIVGVIMNCNGYDIIDMGVMVPAEDIVDKAIAENADFVGLSGL 813
Cdd:PRK02261 5 TVVLGVIGADCHAVGNKILDRALTEAGFEVINLGVMTSQEEFIDAAIETDADAILVSSL 63
|
|
| Glm_B12_BD |
cd02072 |
B12 binding domain of glutamate mutase (Glm). Glutamate mutase catalysis the conversion of (S) ... |
755-841 |
6.46e-05 |
|
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: 43.99 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616153298 755 KMVIATVKGDVHDIGKNIVGVIMNCNGYDIIDMGVMVPAEDIVDKAIAENADFVGLSGLI------TPSLEEMCNVARLM 828
Cdd:cd02072 1 TIVLGVIGSDCHAVGNKILDHAFTEAGFNVVNLGVLSPQEEFIDAAIETDADAILVSSLYghgeidCKGLREKCDEAGLK 80
|
90
....*....|...
gi 1616153298 829 EskrmkIPLLIGG 841
Cdd:cd02072 81 D-----ILLYVGG 88
|
|
| YgiQ |
COG1032 |
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only]; |
780-845 |
6.46e-03 |
|
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
Pssm-ID: 440655 [Multi-domain] Cd Length: 394 Bit Score: 40.31 E-value: 6.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1616153298 780 NGYD--IIDMGVMVPAEDIVDKAIAENADFVGLSgLITPSLEEMCNVARLMESKRMKIPLLIGGATTS 845
Cdd:COG1032 28 AGYEvrIVDLNAEDRSLEDLLKPLREDPDLVGIS-LYTPQYPNALELARLIKERNPGVPIVLGGPHAS 94
|
|
| |
