ID METE_NITV9 Reviewed; 780 AA. AC B8DMM2; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 04-NOV-2026, entry version 83. 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=DvMF_2035; OS Nitratidesulfovibrio vulgaris (strain DSM 19637 / Miyazaki F) OS (Desulfovibrio vulgaris). OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia; OC Desulfovibrionales; Desulfovibrionaceae; Nitratidesulfovibrio. OX NCBI_TaxID=883; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19637 / Miyazaki F; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C., RA Richardson P.; RT "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. 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}. 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; CP001197; ACL08978.1; -; Genomic_DNA. DR AlphaFoldDB; B8DMM2; -. DR SMR; B8DMM2; -. DR STRING; 883.DvMF_2035; -. DR KEGG; dvm:DvMF_2035; -. DR eggNOG; COG0620; Bacteria. DR HOGENOM; CLU_013175_0_0_7; -. DR OMA; AAEMSKW; -. DR OrthoDB; 244285at2; -. DR UniPathway; UPA00051; UER00082. 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; metE; 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; Repeat; Transferase; Zinc. FT CHAIN 1..780 FT /note="5-methyltetrahydropteroyltriglutamate--homocysteine FT methyltransferase" FT /id="PRO_1000191196" FT ACT_SITE 720 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 15..18 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 114 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 457..459 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 457..459 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 510 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 510 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 541..542 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 587 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 625 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 625 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 631 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 667 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 669 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 691 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 752 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" SQ SEQUENCE 780 AA; 84734 MW; 78986F9D1A868056 CRC64; MRTHTLGFPR IGGNRELKKA VEDYWKGAAT RQQLEDAARA IRLRNWTLQR EAGIDVVPVG DFALYDHILD AALLLGVIPP RFRNDDAPRD IDLMFRMARG QGGDRPVAPL EMTKWFDTNY HYLVPELDAA TTFAPDAAPL LALIDEALAA GFTPKAVLPG PMTFLWLSKR VDGGTRWSLL PALLDAYGAL LRDVAARCPL IQLDEPILSL DLADDIRSRF VPAYARLRVA VPDATLLLAS YFAPVGDNLP VALSLPVDVV HLDLVRGPED LTPALDILTR AAARQPADSG LPQSGSQSGI ALSLGVINGR NVWRVDADKA AAPVRAAVAA LGPDRVWVAP SCSLLHCPVD LDAETGLDPE VAQWLAFARQ KCAEVRLVAD MCDLNGRADA PETAAALARN RAALAARAAS PVIHDPAVAV RAGTVTPEMG WRATPYTARI AAQRAALRLP VLPATTIGSF PQTVDIRAQR RKLRTGQITE AQYDAAMREA IATAIREQEA LGLDVLVHGE PERNDMVEYF GEQLRGFCIT ANGWVQSYGT RCVKPPLLYG DVARPGPMTV RWITHAQSLT QKPVKGMLTG PVTIACWSFV RDDVPRPVVF RQLALAIRDE VADLEAAGIG VIQIDEPALR EGLPLRRAAH AAYLDAAVGA FRLASSGVRD ATQIHTHMCY CDFHDIIDHV AALDADVISL EASRSRMELL DVFATHAYPN EVGPGVYDIH SPRVPSIDEM ETLLRAASRV LPLDRLWANP DCGLKTRDWP ETRASLAHLV AAATRVREGG //