METE_THEAC
ID METE_THEAC Reviewed; 343 AA.
AC P57704; Q9HJJ0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=Ta0977;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(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}.
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DR EMBL; AL445066; CAC12106.1; -; Genomic_DNA.
DR RefSeq; WP_010901388.1; NC_002578.1.
DR AlphaFoldDB; P57704; -.
DR SMR; P57704; -.
DR STRING; 273075.Ta0977; -.
DR EnsemblBacteria; CAC12106; CAC12106; CAC12106.
DR GeneID; 1456503; -.
DR KEGG; tac:Ta0977; -.
DR eggNOG; arCOG01876; Archaea.
DR HOGENOM; CLU_040013_3_2_2; -.
DR OMA; THPDEMD; -.
DR OrthoDB; 21172at2157; -.
DR UniPathway; UPA00051; -.
DR Proteomes; UP000001024; 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; Reference proteome; Transferase; Zinc.
FT CHAIN 1..343
FT /note="Methionine synthase"
FT /id="PRO_0000098694"
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 343 AA; 40061 MW; 844C5D4CEA8FDF70 CRC64;
MTALITQEIG SFRKPDYLAK EFHKIERTPK FTELAERATR ETLEVFERSG LDNIGIGGEM
FRWEMYEHPA ERIKGIIFYG MVRSFDNRYY RKGSAIDRLE RREPFHVDEV KFVAGTTKKP
LKVPITGPYT MMEWSFNDYY DSREDLAMEF ARIINEELKD IASVWKQVSG GRRLEIQIDE
PATTTHPDEM DIVVDSINRS VQGVDGEISM HVCYSSDYRL LYDRIPDLKI DGYNLEYSNR
DTLERGLTDD KRVGFQDLKY FAQINESLQR KKFIGIGVTD VHIDYVEPVE LIEDRINYAL
KIIGDPDLVR INPDCGLRTR SREIGEQKLR NMVMARNNIL KQL