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