METXA_THET2
ID METXA_THET2 Reviewed; 380 AA.
AC Q9RA51;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00296};
DE Short=HAT {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000303|PubMed:28581482};
DE EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000269|PubMed:28581482};
DE AltName: Full=Homoserine transacetylase {ECO:0000255|HAMAP-Rule:MF_00296};
DE Short=HTA {ECO:0000255|HAMAP-Rule:MF_00296};
GN Name=metXA {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000303|PubMed:28581482};
GN Synonyms=met2 {ECO:0000303|PubMed:16232856}; OrderedLocusNames=TT_C0407;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=16232856; DOI=10.1016/s1389-1723(00)80081-x;
RA Kosuge T., Gao D., Hoshino T.;
RT "Analysis of the methionine biosynthetic pathway in the extremely
RT thermophilic eubacterium Thermus thermophilus.";
RL J. Biosci. Bioeng. 90:271-279(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28581482; DOI=10.1038/nchembio.2397;
RA Bastard K., Perret A., Mariage A., Bessonnet T., Pinet-Turpault A.,
RA Petit J.L., Darii E., Bazire P., Vergne-Vaxelaire C., Brewee C., Debard A.,
RA Pellouin V., Besnard-Gonnet M., Artiguenave F., Medigue C., Vallenet D.,
RA Danchin A., Zaparucha A., Weissenbach J., Salanoubat M., de Berardinis V.;
RT "Parallel evolution of non-homologous isofunctional enzymes in methionine
RT biosynthesis.";
RL Nat. Chem. Biol. 13:858-866(2017).
CC -!- FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine,
CC forming acetyl-L-homoserine. {ECO:0000255|HAMAP-Rule:MF_00296,
CC ECO:0000269|PubMed:28581482, ECO:0000305|PubMed:16232856}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine;
CC Xref=Rhea:RHEA:13701, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57476, ChEBI:CHEBI:57716; EC=2.3.1.31;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00296,
CC ECO:0000269|PubMed:28581482};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000269|PubMed:16232856}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- DISRUPTION PHENOTYPE: Methionine auxotroph.
CC {ECO:0000269|PubMed:16232856}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000255|HAMAP-Rule:MF_00296}.
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DR EMBL; AB029372; BAA88676.1; -; Genomic_DNA.
DR EMBL; AE017221; AAS80755.1; -; Genomic_DNA.
DR RefSeq; WP_011172855.1; NC_005835.1.
DR AlphaFoldDB; Q9RA51; -.
DR SMR; Q9RA51; -.
DR STRING; 262724.TT_C0407; -.
DR ESTHER; theth-metx; Homoserine_transacetylase.
DR EnsemblBacteria; AAS80755; AAS80755; TT_C0407.
DR KEGG; tth:TT_C0407; -.
DR eggNOG; COG2021; Bacteria.
DR HOGENOM; CLU_028760_1_2_0; -.
DR OMA; TRFCVVS; -.
DR OrthoDB; 536745at2; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_00296; MetX_acyltransf; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR008220; HAT_MetX-like.
DR PANTHER; PTHR32268; PTHR32268; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01392; homoserO_Ac_trn; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Transferase.
FT CHAIN 1..380
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000155744"
FT DOMAIN 70..366
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 186
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 333
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 361
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT CONFLICT 276..277
FT /note="TY -> IH (in Ref. 1; BAA88676)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="T -> N (in Ref. 1; BAA88676)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 42251 MW; D6F64EC2A77C0673 CRC64;
MSEIALEAWG EHEALLLKPP RSPLSIPPPK PRTAVLFPRR EGFYTELGGY LPEVRLRFET
YGTLSRRRDN AVLVFHALTG SAHLAGTYDE ETFRSLSPLE QAFGREGWWD SLVGPGRILD
PALYYVVSAN HLGSCYGSTG PLSLDPHTGR PYGRDFPPLT IRDLARAQAR LLDHLGVEKA
IVIGGSLGGM VALEFALMYP ERVKKLVVLA APARHGPWAR AFNHLSRQAI LQDPEYQKGN
PAPKGMALAR GIAMMSYRAP EGFEARWGAE PELGETYLDY QGEKFLRRFH AESYLVLSRA
MDTHDVGRGR GGVEEALKRL RAIPSLFVGI DTDLLYPAWE VRQAAKAAGA RYREIKSPHG
HDAFLIETDQ VEEILDAFLP
