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METE_THEVO
ID   METE_THEVO              Reviewed;         344 AA.
AC   Q979L4;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Methionine synthase {ECO:0000255|HAMAP-Rule:MF_00288};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00288};
DE   AltName: Full=Homocysteine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00288};
GN   Name=metE {ECO:0000255|HAMAP-Rule:MF_00288}; OrderedLocusNames=TV1147;
GN   ORFNames=TVG1176554;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group to L-homocysteine
CC       resulting in methionine formation. The physiological methyl donor is
CC       unknown. {ECO:0000255|HAMAP-Rule:MF_00288}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00288};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00288};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway. {ECO:0000255|HAMAP-Rule:MF_00288}.
CC   -!- SIMILARITY: Belongs to the archaeal MetE family. {ECO:0000255|HAMAP-
CC       Rule:MF_00288, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB60289.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000011; BAB60289.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_010917381.1; NC_002689.2.
DR   AlphaFoldDB; Q979L4; -.
DR   SMR; Q979L4; -.
DR   STRING; 273116.14325385; -.
DR   DNASU; 1441263; -.
DR   EnsemblBacteria; BAB60289; BAB60289; BAB60289.
DR   GeneID; 1441263; -.
DR   KEGG; tvo:TVG1176554; -.
DR   eggNOG; arCOG01876; Archaea.
DR   HOGENOM; CLU_040013_3_2_2; -.
DR   OMA; THPDEMD; -.
DR   OrthoDB; 21172at2157; -.
DR   PhylomeDB; Q979L4; -.
DR   UniPathway; UPA00051; -.
DR   Proteomes; UP000001017; Chromosome.
DR   GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:InterPro.
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; -; 1.
DR   HAMAP; MF_00288; MetE; 1.
DR   InterPro; IPR002629; Met_Synth_C/arc.
DR   InterPro; IPR022921; MetE_arc.
DR   InterPro; IPR038071; UROD/MetE-like_sf.
DR   Pfam; PF01717; Meth_synt_2; 1.
DR   SUPFAM; SSF51726; SSF51726; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Metal-binding; Methionine biosynthesis;
KW   Methyltransferase; Transferase; Zinc.
FT   CHAIN           1..344
FT                   /note="Methionine synthase"
FT                   /id="PRO_0000098695"
FT   BINDING         211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
FT   BINDING         213
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
FT   BINDING         236
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
SQ   SEQUENCE   344 AA;  40153 MW;  7EF4BEE284F93902 CRC64;
     MAALITQEIG SFRKPEYLSM EFHKIEGTEK FKELAERATI DTLKIFENTG LDNVGIGGEM
     YRWEMYEHPA ERIKGLIFYG MVRSFDNRYY RKGSVIDKIE RRGSFHMDEV EFVAKSTKKP
     IKIPITGPYT MMDWSFNDHY NDRHELAMEF ARIINEELKE IQSKWPYISN GRKLEIQIDE
     PATTTHPDEM DIVVDSVNKS IEGIDAELSL HVCYSRDYRL LYDRIPELNI DGYNLEYSNR
     DTTDLGVEDA KRPGFQDIKY FNEVNESLQR KKFIGVGVTD VHIDFIEPVK LIEDRIKYVL
     NIIKDPELVK LNPDCGLRTR SRSIGEQKLR NMVIAKNNVL KDIS
 
 
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