ID   METE_PSEMZ              Reviewed;          22 AA.
AC   P85918;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase {ECO:0000250|UniProtKB:O50008};
DE            EC=2.1.1.14;
DE   AltName: Full=Cobalamin-independent methionine synthase isozyme {ECO:0000250|UniProtKB:O50008};
DE   AltName: Full=Vitamin-B12-independent methionine synthase isozyme {ECO:0000250|UniProtKB:O50008};
DE   Flags: Fragments;
OS   Pseudotsuga menziesii (Douglas-fir) (Abies menziesii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae;
OC   Pseudotsuga.
OX   NCBI_TaxID=3357;
RN   [1] {ECO:0000305}
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18602030; DOI=10.1016/j.jprot.2008.06.004;
RA   Islam M.A., Sturrock R.N., Ekramoddoullah A.K.M.;
RT   "A proteomics approach to identify proteins differentially expressed in
RT   Douglas-fir seedlings infected by Phellinus sulphurascens.";
RL   J. Proteomics 71:425-438(2008).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from 5-
CC       methyltetrahydrofolate to homocysteine resulting in methionine
CC       formation. {ECO:0000250|UniProtKB:O50008}.
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;
CC         Evidence={ECO:0000250|UniProtKB:O50008};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:O50008};
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:0000250|UniProtKB:O50008}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O50008}.
CC   -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC       family. {ECO:0000255}.
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DR   AlphaFoldDB; P85918; -.
DR   UniPathway; UPA00051; UER00082.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Cytoplasm; Metal-binding; Methionine biosynthesis;
KW   Methyltransferase; Transferase; Zinc.
FT   CHAIN           <1..>22
FT                   /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT                   methyltransferase"
FT                   /id="PRO_0000397958"
FT   NON_CONS        10..11
FT                   /evidence="ECO:0000303|PubMed:18602030"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:18602030"
FT   NON_TER         22
FT                   /evidence="ECO:0000303|PubMed:18602030"
SQ   SEQUENCE   22 AA;  2429 MW;  1990A9BF785869DA CRC64;
     FALESFWDGK GNASAHAMEM TK