ID A0A4P6PH65_9BACT Unreviewed; 755 AA. AC A0A4P6PH65; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 03-AUG-2022, entry version 13. 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 ECO:0000313|EMBL:QBG49077.1}; GN ORFNames=EGM51_17350 {ECO:0000313|EMBL:QBG49077.1}; OS Verrucomicrobia bacterium S94. OC Bacteria; Verrucomicrobia. OX NCBI_TaxID=2488809 {ECO:0000313|EMBL:QBG49077.1, ECO:0000313|Proteomes:UP000289135}; RN [1] {ECO:0000313|EMBL:QBG49077.1, ECO:0000313|Proteomes:UP000289135} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S94 {ECO:0000313|EMBL:QBG49077.1, RC ECO:0000313|Proteomes:UP000289135}; RA Baek K.; RT "Verrucomicrobia bacterium S94."; RL Submitted (NOV-2018) 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 --------------------------------------------------------------------------- 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; CP036201; QBG49077.1; -; Genomic_DNA. DR EnsemblBacteria; QBG49077; QBG49077; EGM51_17350. DR KEGG; vbs:EGM51_17350; -. DR UniPathway; UPA00051; UER00082. DR Proteomes; UP000289135; 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: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 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 Pfam; PF08267; Meth_synt_1; 1. DR Pfam; PF01717; Meth_synt_2; 1. DR PIRSF; PIRSF000382; MeTrfase_B12_ind; 1. DR SUPFAM; SSF51726; SSF51726; 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}; Reference proteome {ECO:0000313|Proteomes:UP000289135}; KW 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 3..307 FT /note="Meth_synt_1" FT /evidence="ECO:0000259|Pfam:PF08267" FT DOMAIN 426..747 FT /note="Meth_synt_2" FT /evidence="ECO:0000259|Pfam:PF01717" FT REGION 15..18 FT /note="5-methyltetrahydropteroyltri-L-glutamate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT REGION 431..433 FT /note="L-homocysteine binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT REGION 431..433 FT /note="L-methionine binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT REGION 515..516 FT /note="5-methyltetrahydropteroyltri-L-glutamate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT ACT_SITE 694 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 112 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 484 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 484 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 561 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 599 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 599 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 605 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 641 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" 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 665 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 726 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" SQ SEQUENCE 755 AA; 85517 MW; C853B36E6449CCDA CRC64; MKSHILGFPR IGSQRELKFA IEAYWRRACS ESELLLRTEQ IKLQNWTVQQ KAGLDYVCTG DFSLYDHVLD VSRMIGAVPA RFQTPGLSEL DIYFNMARGN AEAGIAPMEM TKWFDTNYHY IVPEIEADMQ LAYSSDTLVR ETEAALKQGF RPKPVVVGPL TYLALAKAAE GVNKWDALDA ITGVYSTLLE KLSGLTDCIQ LDEPILCTDL PTEIRERAEQ TYAVLRSHAR HTRLLLGTYF GGLNENLDLT ARLPVDVLHI DLVRAPGQLD DVLTKWPEHK DLSLGLIDGR NIWKADLAEL LKQIVKAKPT RHTDQLWIGS SCSLLHTPVS LEPETDLLPE LKAWMAFAVE KCSEVKTLTL AAQGCNVNEE LLENKKIISS RKNSPLSLDF EVRKRVEQVD ARMCRRARPF AERKKCQQAR LNLPLLPTTT IGSFPQTKEI RNIRKAFRNG DCDQSAYTQA MQQEICSVIQ EQELAGLDVL VHGEPERNDM VEYFGQQMNG FCFSQYGWVQ SYGSRCVKPP IIYGDVSRPA PMTLDWIQYA QSQTEKPLKG MLTGPVTMLC WSFVRDDLPR AAVCRQIALA IRDEVLDLEK AGIGMIQIDE AAFREGLPIR KDEQEEYLNW AVENFRLATS GVRDETQIHT HMCYSEFNTI LQEIAAMDAD VISIEASRSD MELLQAFETF HYPNDIGPGV WDIHSPRVPS VTEIRTLIEN ALKVIPKEQL WINPDCGLKT RGWPETRQAL RNMVEATTAV RKILQ //