ID B4U5Z5_HYDS0 Unreviewed; 755 AA. AC B4U5Z5; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 94. 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 OrderedLocusNames=HY04AAS1_1502 {ECO:0000313|EMBL:ACG58185.1}; OS Hydrogenobaculum sp. (strain Y04AAS1). OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; OC Hydrogenobaculum. OX NCBI_TaxID=380749 {ECO:0000313|EMBL:ACG58185.1}; RN [1] {ECO:0000313|EMBL:ACG58185.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Y04AAS1 {ECO:0000313|EMBL:ACG58185.1}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Kiss H., Brettin T., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Resenback A.-L., Mead D.; RT "Complete sequence of Hydrogenobaculum sp. Y04AAS1."; RL Submitted (AUG-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: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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00172}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00172}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000382-2}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR000382- CC 2}; 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: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|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; CP001130; ACG58185.1; -; Genomic_DNA. DR AlphaFoldDB; B4U5Z5; -. DR STRING; 380749.HY04AAS1_1502; -. DR KEGG; hya:HY04AAS1_1502; -. DR eggNOG; COG0620; Bacteria. DR HOGENOM; CLU_013175_0_0_0; -. 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: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 NCBIfam; TIGR01371; met_syn_B12ind; 1. 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. 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 5..316 FT /note="Cobalamin-independent methionine synthase MetE N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF08267" FT DOMAIN 427..748 FT /note="Cobalamin-independent methionine synthase MetE C- FT terminal/archaeal" FT /evidence="ECO:0000259|Pfam:PF01717" FT ACT_SITE 695 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172, FT ECO:0000256|PIRSR:PIRSR000382-3" FT BINDING 15..18 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 18 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 104 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 109 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 432..434 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172, FT ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 432..434 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172, FT ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 485 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 485 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172, FT ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 562 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172, FT ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 600 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172, FT ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 600 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172, FT ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 606 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 641 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR000382-2" FT BINDING 643 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR000382-2" 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 656 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR000382-2" 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 665 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR000382-2" FT BINDING 727 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 727 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR000382-2" SQ SEQUENCE 755 AA; 87551 MW; BA44DC8C4E121C5B CRC64; MKALAYGYPK LGEKREFKNA LESFWKKAIT EEQFYEQMRN IEAQRIRAYS ESVDEIPVGE LSFYDFMLDT AVMVGMIPSR FGEYKGLETY FEMARGKSAM EMTKYFNTNY HYIVPELESN NFKLLENKPK RCYLNAKDKV QNPKPYLIAP FTFLKLSKTY KKTTKDGFSV LETSKIENEK TLYYFLEPLL EVYKDILKNL KTEGVNIVSL QDPGLVFDLK DYELNAVKKI YEELSQVSDI ELITYYDSVS AYKDIIDLPV KRIGLDLCSN AENLENLRKY GFPKDKELIA GIINGRQVWR ANLRDKLKLI DELSKIAPNL SISNSSPLFH LPVNVELETK MDKDLKDRLS FAKQKLEELK TLKNAFLGDK ESLKEVEASA KLFEGSFGKN QVVIDRIKAL KDSDFQRELP YKERIKLQQS ILNLPIFPTT TIGSFPQTEE VRKTRSAFRS GKISKQEYEA FIKSQIDNVI AFQEEIGLDV LVHGEFERTD MVEFFAEKLK GVATTEHGWI ISYGSRGYRP PIIYGDVYRD EPMTLNEILY AQSKTQKPVK GMLTGPVTIL NWSFYREDIP KKEVAYQIAL AILDEVKDLE KSGIKIIQID EPAFREGTPI KKKDWEDYFD WAIKSFRLSS KANPKTQIHT HMCYSEFNDI IDKIYDMDFD VISIEASRSK GEILEAFERF GKWDRQIGIG VYDIHSPTIP SVEEMEIVMK RAMKVLDKSL LWVNPDCGLK TRRWEEVKPA LKNMMEMALK LRKEA //