ID METE_PSEA7 Reviewed; 763 AA. AC A6V1K5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 86. 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=PSPA7_1556; OS Pseudomonas aeruginosa (strain PA7). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=381754; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PA7; RA Dodson R.J., Harkins D., Paulsen I.T.; RL Submitted (JUN-2007) 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 = 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:0000255|HAMAP- CC 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; CP000744; ABR84681.1; -; Genomic_DNA. DR RefSeq; WP_012074732.1; NC_009656.1. DR AlphaFoldDB; A6V1K5; -. DR SMR; A6V1K5; -. DR KEGG; pap:PSPA7_1556; -. DR HOGENOM; CLU_013175_0_0_6; -. DR UniPathway; UPA00051; UER00082. DR Proteomes; UP000001582; 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 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; Metal-binding; Methionine biosynthesis; KW Methyltransferase; Repeat; Transferase; Zinc. FT CHAIN 1..763 FT /note="5-methyltetrahydropteroyltriglutamate--homocysteine FT methyltransferase" FT /id="PRO_1000017261" FT ACT_SITE 701 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 16..19 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 117 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 438..440 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 438..440 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 491 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 491 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 522..523 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 568 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 606 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 606 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 612 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 648 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 650 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 672 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 733 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" SQ SEQUENCE 763 AA; 86085 MW; 7F5BA32D334ED4FB CRC64; MALAHTLGFP RIGRDRELKK ALEAYWKGEL DQPGLLQVGR ELRRQHWQLQ KDAGIELLPV GDFAWYDQVL AHSLAFGVIP ERFRPADGQP TLDTLFAMAR GVAQGCCGGA HAQEMTKWFD TNYHYLVPEF TVDQAFSLSW TQLFEEVDEA LALGHAVKPV LIGPLSYLWL GKAKGGEFDR LELLERLLPV YGEIFQGLAA RGVEWVQIDE PILVLDLPQA WKNAFERAYN LIQREPLKKL VATYFGGLED NLGLAAGLPV DGLHIDLVRA PGQYPTILDR LPAYKVLSLG LVNGRNVWRC DLEKALEVLA HAHERLGERL WVAPSCSLLH SPVDLCREDQ LDEELQSWLA FAVQKCEEVA ILARALVEPE APEVRQAFEV SRRVEASRRR STRIHKREVQ ARLAAVRPQD SRRASAFAER AVQQRARLEL PAFPTTTIGS FPQTSAIRLA RQSWKQGRLS QAEYTEAMHS EIRHAVQVQE RLGLDVLVHG EAERNDMVEY FAEQLDGYAF TRFGWVQSYG SRCVKPAVIY GDLSRPRPMT VEWIRYAQSL TGKVMKGMLT GPVTMLMWSF PREDVSREVQ ARQLALALRD EVSDLEQAGI RIVQIDEAAF REGLPLRRAD WPHYLEWATE AFRLCASGVR DETQIHTHMC YSEFNDVIES IAAMDADVIT IETSRSDMEL LEAFEAFAYP NEIGPGVYDI HSPRVPAVED MVKLLSKAAE RIPAARLWVN PDCGLKTRAW AETEAALANM VAAARQLRQA NLA //