ID METE_MYCBO Reviewed; 759 AA. AC P65341; A0A1R3XXH6; O06584; X2BHF0; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 02-SEP-2026, entry version 114. DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00172}; DE EC=2.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00172}; DE AltName: Full=Cobalamin-independent methionine synthase {ECO:0000255|HAMAP-Rule:MF_00172}; DE AltName: Full=Methionine synthase, vitamin-B12 independent isozyme {ECO:0000255|HAMAP-Rule:MF_00172}; GN Name=metE {ECO:0000255|HAMAP-Rule:MF_00172}; GN OrderedLocusNames=BQ2027_MB1164C; OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=233413; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=12788972; DOI=10.1073/pnas.1130426100; RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J., RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.; RT "The complete genome sequence of Mycobacterium bovis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=28385856; DOI=10.1128/genomea.00157-17; RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R., RA Robbe-Austerman S., Gordon S.V.; RT "Updated reference genome sequence and annotation of Mycobacterium bovis RT AF2122/97."; RL Genome Announc. 5:E00157-E00157(2017). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5- CC methyltetrahydrofolate to homocysteine resulting in methionine CC formation. {ECO:0000255|HAMAP-Rule:MF_00172}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = CC tetrahydropteroyltri-L-glutamate + L-methionine; CC Xref=Rhea:RHEA:21196, ChEBI:CHEBI:57844, ChEBI:CHEBI:58140, CC ChEBI:CHEBI:58199, ChEBI:CHEBI:58207; EC=2.1.1.14; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00172}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00172}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00172}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo CC pathway; L-methionine from L-homocysteine (MetE route): step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00172}. CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase CC family. {ECO:0000255|HAMAP-Rule:MF_00172, ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LT708304; SIT99764.1; -; Genomic_DNA. DR RefSeq; WP_003405914.1; NC_002945.4. DR AlphaFoldDB; P65341; -. DR SMR; P65341; -. DR KEGG; mbo:BQ2027_MB1164C; -. DR PATRIC; fig|233413.5.peg.1274; -. DR UniPathway; UPA00051; UER00082. DR Proteomes; UP000001419; Chromosome. DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:InterPro. DR CDD; cd03311; CIMS_C_terminal_like; 1. DR CDD; cd03312; CIMS_N_terminal_like; 1. DR Gene3D; 3.20.20.210; -; 2. DR HAMAP; MF_00172; Meth_synth; 1. DR InterPro; IPR013215; Cbl-indep_Met_Synth_N. DR InterPro; IPR006276; Cobalamin-indep_Met_synthase. DR InterPro; IPR002629; Met_Synth_C/arc. DR InterPro; IPR038071; UROD/MetE-like_sf. DR NCBIfam; TIGR01371; met_syn_B12ind; 1. DR NCBIfam; NF003556; PRK05222.1; 1. DR PANTHER; PTHR30519; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE; 1. DR Pfam; PF08267; Meth_synt_1; 1. DR Pfam; PF01717; Meth_synt_2; 1. DR PIRSF; PIRSF000382; MeTrfase_B12_ind; 1. DR SUPFAM; SSF51726; UROD/MetE-like; 2. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Metal-binding; Methionine biosynthesis; KW Methyltransferase; Reference proteome; Repeat; Transferase; Zinc. FT CHAIN 1..759 FT /note="5-methyltetrahydropteroyltriglutamate--homocysteine FT methyltransferase" FT /id="PRO_0000098642" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..16 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 700 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 24..27 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 118 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 437..439 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 437..439 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 490 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 490 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 521..522 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 567 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 605 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 605 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 611 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 647 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 649 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 671 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 732 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" SQ SEQUENCE 759 AA; 81582 MW; 702F90BF79B25C8D CRC64; MTQPVRRQPF TATITGSPRI GPRRELKRAT EGYWAGRTSR SELEAVAATL RRDTWSALAA AGLDSVPVNT FSYYDQMLDT AVLLGALPPR VSPVSDGLDR YFAAARGTDQ IAPLEMTKWF DTNYHYLVPE IGPSTTFTLH PGKVLAELKE ALGQGIPARP VIIGPITFLL LSKAVDGAGA PIERLEELVP VYSELLSLLA DGGAQWVQFD EPALVTDLSP DAPALAEAVY TALCSVSNRP AIYVATYFGD PGAALPALAR TPVEAIGVDL VAGADTSVAG VPELAGKTLV AGVVDGRNVW RTDLEAALGT LATLLGSAAT VAVSTSCSTL HVPYSLEPET DLDDALRSWL AFGAEKVREV VVLARALRDG HDAVADEIAS SRAAIASRKR DPRLHNGQIR ARIEAIVASG AHRGNAAQRR ASQDARLHLP PLPTTTIGSY PQTSAIRVAR AALRAGEIDE AEYVRRMRQE ITEVIALQER LGLDVLVHGE PERNDMVQYF AEQLAGFFAT QNGWVQSYGS RCVRPPILYG DVSRPRAMTV EWITYAQSLT DKPVKGMLTG PVTILAWSFV RDDQPLADTA NQVALAIRDE TVDLQSAGIA VIQVDEPALR ELLPLRRADQ AEYLRWAVGA FRLATSGVSD ATQIHTHLCY SEFGEVIGAI ADLDADVTSI EAARSHMEVL DDLNAIGFAN GVGPGVYDIH SPRVPSAEEM ADSLRAALRA VPAERLWVNP DCGLKTRNVD EVTASLHNMV AAAREVRAG //