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METE_PSEPW
ID   METE_PSEPW              Reviewed;         766 AA.
AC   B1J2V4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=PputW619_0802;
OS   Pseudomonas putida (strain W619).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=390235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W619;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA   Richardson P.;
RT   "Complete sequence of Pseudomonas putida W619.";
RL   Submitted (FEB-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: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;
CC         Evidence={ECO:0000255|HAMAP-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}.
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DR   EMBL; CP000949; ACA71307.1; -; Genomic_DNA.
DR   RefSeq; WP_012312730.1; NC_010501.1.
DR   AlphaFoldDB; B1J2V4; -.
DR   SMR; B1J2V4; -.
DR   STRING; 390235.PputW619_0802; -.
DR   EnsemblBacteria; ACA71307; ACA71307; PputW619_0802.
DR   KEGG; ppw:PputW619_0802; -.
DR   eggNOG; COG0620; Bacteria.
DR   HOGENOM; CLU_013175_0_0_6; -.
DR   OMA; KVMKGML; -.
DR   OrthoDB; 577156at2; -.
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   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; Metal-binding; Methionine biosynthesis;
KW   Methyltransferase; Repeat; Transferase; Zinc.
FT   CHAIN           1..766
FT                   /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT                   methyltransferase"
FT                   /id="PRO_1000097833"
FT   ACT_SITE        706
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         122
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         443..445
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         443..445
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         496
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         496
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         527..528
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         573
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         611
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         611
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         617
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         653
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         655
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         677
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         738
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
SQ   SEQUENCE   766 AA;  85725 MW;  C206000A030DA6DA CRC64;
     MALAHNLGFP RIGRDRELKK AQEAFWKGEL DEAGLRKVGR DLRAAHWQAQ KDAGIELLPV
     GDFAWYDQVL THSLTFGVIP ERFRGHDGAK PTLQTLFAMA RGVATGRSAN CCGGAHAQEM
     TKWFDTNYHY LVPEFTVDQQ FALSWEQLFE EVDEAKALGH AAKPVVIGPL TYLWLGKAKG
     GDFDKLELLD RLLPVYDEIL NRLAGQGVEW VQIDEPILVL DLPQEWKNAY ERVYNILQRA
     PLKKLVATYF GGLEENLGLA ANLPVDGLHI DLVRAPEQYP TILDRLPAYK ILSLGLVNGR
     NVWACDLEKA VDVLRHAAER LGDRLWVAPS CSLLHSPVDL GREDQLDTEL KSWLAFAVQK
     CQEVAVLAKA VNQPDAAEVA AALARSRAIQ AGRASSPRIH KPAVQARVHA IKPGDSQRQS
     AFGQRIAKQR AGLNLPAYPT TTIGSFPQTP AIRLARQAFK QGKLTEADYV EAMHSEIRHA
     VQIQENLGLD VLVHGEAERN DMVEYFAEQL DGYVFTRFGW VQSYGSRCVK PAVIYGDLSR
     PEAMTVAWIR YAQGLTRKVM KGMLTGPVTM LMWSFPREDV SRETQARQLA LAIRDEVLDL
     EAADIKIVQI DEAAFREGLP LRRSAWPAYL EWATEAFRLC ASGVRDETQI HTHMCYSEFN
     DVIESIAAMD ADVITIETSR SDMELLEAFE KFDYPNEIGP GVYDIHSPRV PSREEMVKLL
     RKAALRIPAE RLWVNPDCGL KTRAWPETEA ALVNMVAAAR ELRATA
 
 
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