ID A0A1S2WMF9_MYCMA Unreviewed; 756 AA. AC A0A1S2WMF9; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 22-FEB-2023, entry version 21. DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase {ECO:0000256|HAMAP-Rule:MF_00172}; DE EC=2.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00172}; DE AltName: Full=Cobalamin-independent methionine synthase {ECO:0000256|HAMAP-Rule:MF_00172}; DE AltName: Full=Methionine synthase, vitamin-B12 independent isozyme {ECO:0000256|HAMAP-Rule:MF_00172}; GN Name=metE {ECO:0000256|HAMAP-Rule:MF_00172}; GN ORFNames=BMG05_09550 {ECO:0000313|EMBL:OIN81118.1}; OS Mycobacterium malmoense. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1780 {ECO:0000313|EMBL:OIN81118.1, ECO:0000313|Proteomes:UP000181742}; RN [1] {ECO:0000313|EMBL:OIN81118.1, ECO:0000313|Proteomes:UP000181742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CTRI-256 {ECO:0000313|EMBL:OIN81118.1, RC ECO:0000313|Proteomes:UP000181742}; RA Ustinova V., Smirnova T.G., Varlamov D.A., Larionova E., Chernousova L.N.; RT "Mycobacterium malmoense draft genome assembly."; RL Submitted (NOV-2016) 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:0000256|ARBA:ARBA00002777, ECO:0000256|HAMAP- CC Rule:MF_00172}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L- CC methionine + tetrahydropteroyltri-L-glutamate; Xref=Rhea:RHEA:21196, CC ChEBI:CHEBI:57844, ChEBI:CHEBI:58140, ChEBI:CHEBI:58199, CC ChEBI:CHEBI:58207; EC=2.1.1.14; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00172}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00172}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|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:0000256|ARBA:ARBA00004681, ECO:0000256|HAMAP-Rule:MF_00172}. CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase CC family. {ECO:0000256|ARBA:ARBA00009553, ECO:0000256|HAMAP- CC Rule:MF_00172}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OIN81118.1}. 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; MOWS01000080; OIN81118.1; -; Genomic_DNA. DR RefSeq; WP_071510390.1; NZ_MOWS01000080.1. DR AlphaFoldDB; A0A1S2WMF9; -. DR EnsemblBacteria; OIN81118; OIN81118; BMG05_09550. DR OrthoDB; 244285at2; -. DR UniPathway; UPA00051; UER00082. DR Proteomes; UP000181742; Unassembled WGS sequence. 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:0009086; P:methionine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. 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 PANTHER; PTHR30519; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE; 1. DR PANTHER; PTHR30519:SF0; 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. DR TIGRFAMs; TIGR01371; met_syn_B12ind; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00172}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00172}; KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP- KW Rule:MF_00172}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP- KW Rule:MF_00172}; Repeat {ECO:0000256|HAMAP-Rule:MF_00172}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00172}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00172}. FT DOMAIN 8..311 FT /note="Cobalamin-independent methionine synthase MetE N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF08267" FT DOMAIN 428..750 FT /note="Cobalamin-independent methionine synthase MetE C- FT terminal/archaeal" FT /evidence="ECO:0000259|Pfam:PF01717" FT REGION 406..428 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 696 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 20..23 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 114 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 433..435 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 433..435 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 486 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 486 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 517..518 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 563 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 601 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 601 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 607 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 643 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 645 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 667 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 728 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" SQ SEQUENCE 756 AA; 81616 MW; AF1512958B8C0FC2 CRC64; MTPQAFTATV TGSPRIGPKR ELKRATEGYW AGRTSRSELE SVAATLRRDT WAGLAAAGLD SVPVNTFSYY DQVLDTAVLL GALPTRVAKI SDDLDRYFAA ARGNDEVAPL EMTKWFDTNY HYLVPEIEPA TKFALHPDKV LSELKEALEQ GIPARPVVVG PVTFLLLSKG VDGGGAPIER LQELVPIYSE LLSLLADNGA QWVQFDEPAL VTDISPDAPA LAEAVYNALG SVSNRPAIYV ATYFGDPGDS LAGLARTPIE AIGVDLVAGA DTAVAGIPEL STKTLVAGVV DGRNVWRTDL ESALAKLATL LGSAATVAVS TSCSTMHVPY SLEPETGLDD NLRSWLAFGA EKVHEIVVLA RALHEDRDAV AEEIAASNAA VASRKSDPRL HNDRVRARID SIVASGAHRG DAAQRRASQD ARLHLPPLPT TTIGSYPQTS AIRKARAALR AGEIDEAEYV RRMKKEIADV IKLQEQLGLD VLVHGEPERN DMVQYFAEQL EGFFATQNGW VQSYGSRCVR PPILYGDVSR PHPMTVEWIT YAQSLTDKPV KGMLTGPVTI LAWSFVRDDQ PLADTANQVA LAIRDETVDL QAAGIGIIQV DEPALRELLP LRRAQQEDYL RWAVGSFRLA TSGVADSTQI HTHLCYSEFG EVIGAIADLD ADVTSIEAAR SHMEVLDDLN AVGFANSVGP GVYDIHSPRV PSTDEMAESL RAALRAVPPQ RLWVNPDCGL KTRNVDEVTA SLQHMVAAAQ EVRAGV //