ID A4FN94_SACEN Unreviewed; 762 AA. AC A4FN94; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 02-SEP-2026, entry version 113. 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:CAM05519.1}; GN OrderedLocusNames=SACE_6349 {ECO:0000313|EMBL:CAM05519.1}; OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / OS NBRC 13426 / NCIMB 8594 / NRRL 2338). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales; OC Pseudonocardiaceae; Saccharopolyspora. OX NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM05519.1, ECO:0000313|Proteomes:UP000006728}; RN [1] {ECO:0000313|EMBL:CAM05519.1, ECO:0000313|Proteomes:UP000006728} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / RC NRRL 2338 {ECO:0000313|Proteomes:UP000006728}; RX PubMed=17369815; DOI=10.1038/nbt1297; RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S., RA Haydock S.F., Leadlay P.F.; RT "Complete genome sequence of the erythromycin-producing bacterium RT Saccharopolyspora erythraea NRRL23338."; RL Nat. Biotechnol. 25:447-453(2007). 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 = 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:0000256|HAMAP-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 --------------------------------------------------------------------------- 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; AM420293; CAM05519.1; -; Genomic_DNA. DR RefSeq; WP_009946026.1; NC_009142.1. DR AlphaFoldDB; A4FN94; -. DR STRING; 405948.SACE_6349; -. DR GeneID; 306462751; -. DR KEGG; sen:SACE_6349; -. DR eggNOG; COG0620; Bacteria. DR HOGENOM; CLU_013175_0_0_11; -. DR OrthoDB; 244285at2; -. DR UniPathway; UPA00051; UER00082. DR Proteomes; UP000006728; 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 {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:UP000006728}; KW Repeat {ECO:0000256|ARBA:ARBA00022737, 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 ACT_SITE 701 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172, FT ECO:0000256|PIRSR:PIRSR000382-3" FT BINDING 19..22 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 22 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1" 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 119 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 438..440 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 438..440 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 491 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 491 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 522..523 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 568 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 606 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 606 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 612 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 648 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 648 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 650 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 650 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 672 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 672 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 733 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 733 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 762 AA; 83407 MW; 5A3BA2851B93587F CRC64; MSSRIGSTVL GHPRIGPRRE LKRALEGYWA SRSTEAELRE VARSLRAGTW RELAAAGLDS VPGNTFSYYD QVLDTAATFG AVPRRFAELG LGPLDTYFAM ARGVESTPPL EMTKWFDTNY HYLVPEIGPG TTFSLADRTA VEDYREAAAD GVGTRPVVVG PLTFLLLSKS AEDAPKSFRP LDKLDELVQR YAELLTELHD AGAGWVQLDE PAFAADRTPE ELELLRGAYR TLSQLDRRPD ILVATYFGDP GDALPTLAST DVEGIAVDLV SNASTVDSLA RVDGLRSKTL VSGLVDGRNV WRTDLDAALG TAAALLEVAG EVAVSTSCSL LHVPYDVDAE ANLDPHVRPW LAFAKQKAAE VVTLGRALRE GRDSVADELA AARNAVQDRR SSERLRDNRV RGRLDALSAD SYRRSPYDAR RAAQRRTLDL PPLPTTTIGS FPQTPDVRKA RAALRNGSID QAAYDQRMLE EISRVIALQE ALGLDVLVHG EPERNDMVQY FAEHLDGFVS TENGWVQSYG SRCVRPPILF GDVSRPEPIT TRWAERAQRL TEKPVKGMLT GPITILAWSF VRDDQPLGET AAQVALAIRD EVRDLEAAGI RVIQVDEPAL RELLPLRAEQ HEDYLDWAVG SFRLATSGVA DRTQVHTHLC YSEFGEVIDA IVALDADVTS IEAARSRMEV LDDLNAVGFG RGVGPGVYDI HSPRVPSTEE IEGLLAAALR SVPAERLWVN PDCGLKTRGY AEVEPALRSM VEAAARMRAD LA //