METE_SULIN
ID METE_SULIN Reviewed; 332 AA.
AC C3NGG0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 56.
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=YN1551_1114;
OS Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=419942;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y.N.15.51 / Yellowstone #2;
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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}.
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DR EMBL; CP001404; ACP48220.1; -; Genomic_DNA.
DR RefSeq; WP_012717342.1; NC_012623.1.
DR AlphaFoldDB; C3NGG0; -.
DR SMR; C3NGG0; -.
DR EnsemblBacteria; ACP48220; ACP48220; YN1551_1114.
DR GeneID; 7810845; -.
DR KEGG; sin:YN1551_1114; -.
DR HOGENOM; CLU_040013_3_2_2; -.
DR OMA; DPDCGMR; -.
DR UniPathway; UPA00051; -.
DR Proteomes; UP000006818; 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..332
FT /note="Methionine synthase"
FT /id="PRO_1000204857"
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 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
SQ SEQUENCE 332 AA; 38231 MW; 81CFD717C08496E7 CRC64;
MSKLPLLPTT VIGSYPRPKW LRESIRLHKA GKISDEDLQE AFSDAVIAVL KDHYNAGVDV
PTDGEVRRDE MVEFFAERIK GFKFYGPVRV WGTAYYRKPS VVSKIEYKKP MLVDEFTFAK
SVSYTDNLKI TITGPYTIAE WSYNEYYKNK KDLVFDLAKA INQEIKNLVE AGAKIIQIDE
PALHTRREDV SWGVEAVNEA VKGVNAKLVM HICYGEYSFV APYLNELKVD QINFAFKIYN
YKPLELLKRY GFDKELGAGV IDVHNRRIET SEEVANDIRK ILEYFTPEKV WINPDCGLKL
LSRKIAYQKL VSMVEGTKVV REELKRKGYS VD
