ID J2SDX7_9PSED Unreviewed; 762 AA. AC J2SDX7; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 27-NOV-2024, entry version 52. 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=PMI31_05817 {ECO:0000313|EMBL:EJM65141.1}; OS Pseudomonas sp. GM55. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1144333 {ECO:0000313|EMBL:EJM65141.1, ECO:0000313|Proteomes:UP000007268}; RN [1] {ECO:0000313|EMBL:EJM65141.1, ECO:0000313|Proteomes:UP000007268} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GM55 {ECO:0000313|EMBL:EJM65141.1, RC ECO:0000313|Proteomes:UP000007268}; RX PubMed=23045501; DOI=10.1128/JB.01243-12; RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L., RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.; RT "Twenty-one genome sequences from Pseudomonas species and 19 genome RT sequences from diverse bacteria isolated from the rhizosphere and RT endosphere of Populus deltoides."; RL J. Bacteriol. 194:5991-5993(2012). 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; CC Evidence={ECO:0000256|HAMAP-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: 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:EJM65141.1}. 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; AKJJ01000147; EJM65141.1; -; Genomic_DNA. DR RefSeq; WP_008023334.1; NZ_AKJJ01000147.1. DR AlphaFoldDB; J2SDX7; -. DR PATRIC; fig|1144333.3.peg.5663; -. DR UniPathway; UPA00051; UER00082. DR Proteomes; UP000007268; 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 FunFam; 3.20.20.210:FF:000002; 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; 1. DR FunFam; 3.20.20.210:FF:000003; 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; 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 4..315 FT /note="Cobalamin-independent methionine synthase MetE N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF08267" FT DOMAIN 433..755 FT /note="Cobalamin-independent methionine synthase MetE C- FT terminal/archaeal" FT /evidence="ECO:0000259|Pfam:PF01717" FT ACT_SITE 701 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172, FT ECO:0000256|PIRSR:PIRSR000382-3" FT BINDING 16..19 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 19 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 117 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 122 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_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 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; 85937 MW; 50977FC3D366265D CRC64; MALAHSLGFP RIGRDRELKK AQEAFWKGEL DEAGLRAVGR DLRKTHWDLQ KKAGIELLPV GDFAWYDQVL THSLMFGVVP ERFRPHDGKA SLQTLFGMAR GVSDSCCGGA HAQEMTKWFD TNYHYLVPEF SADQQFQLGW EQLFEEVEEA RALGHDVKPV IIGPLTYLWL GKAKGVEFDK LELLDRLLPL YGQIFQRLAA QGVEWVQIDE PILVLDLPQA WKNAFERAYN LIQRDPLKKL VATYFGGLEE NLGLAANLPV DGLHIDLVRA PEQFPTILDR LPAYKVLSLG VVNGRNVWRC DLENALATLR YAQERLGDRL WVAPSCSLLH SPVDLGCEDQ LDSELKSWLA FAVQKCEEVA LLAQAVNEPE APKVLQALTQ SRAVQARRAA SPRIHKPAVQ ARVAAITARD SQRHSPFARR IEKQRAGLNL PLFPTTTIGS FPQTTSIRLA RQSFRQGKLT EAEYTEAMHS EIRHAVQVQE HLGLDVLVHG EAERNDMVEY FAEQLDGYVF TRFGWVQSYG SRCVKPAVIF GDLSRPKAMT VEWIRYAQGL TDKVMKGMLT GPVTMLMWSF PREDVSGEVQ ARQLALAIRD EVLDLEAAGI QIVQIDEAAF REGLPLRQAQ WQHYLDWATE VFRLCASGVR DETQIHTHMC YSEFNDVIES IAAMDADVIT IETSRSDMEL LDAFEAFAYP NEIGPGVYDI HSPRVPDASE MANLLRKAAK RIPADRLWVN PDCGLKTRGW AETEAALVHM VNAARQLRKE WA //