METXA_HALSA
ID METXA_HALSA Reviewed; 374 AA.
AC P57715; Q9HMR4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00296};
DE Short=HAT {ECO:0000255|HAMAP-Rule:MF_00296};
DE EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00296};
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}; OrderedLocusNames=VNG_2420G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
CC -!- FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine,
CC forming acetyl-L-homoserine. {ECO:0000255|HAMAP-Rule:MF_00296}.
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 -!- 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}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG20507.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE004437; AAG20507.1; ALT_INIT; Genomic_DNA.
DR PIR; G84392; G84392.
DR RefSeq; WP_012289504.1; NC_002607.1.
DR AlphaFoldDB; P57715; -.
DR SMR; P57715; -.
DR STRING; 64091.VNG_2420G; -.
DR ESTHER; halsp-metx; Homoserine_transacetylase.
DR PaxDb; P57715; -.
DR EnsemblBacteria; AAG20507; AAG20507; VNG_2420G.
DR GeneID; 5953379; -.
DR KEGG; hal:VNG_2420G; -.
DR PATRIC; fig|64091.14.peg.1875; -.
DR HOGENOM; CLU_028760_1_2_2; -.
DR InParanoid; P57715; -.
DR OrthoDB; 8770at2157; -.
DR PhylomeDB; P57715; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0009092; P:homoserine metabolic process; IBA:GO_Central.
DR GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central.
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 SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01392; homoserO_Ac_trn; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..374
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000155752"
FT DOMAIN 34..346
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 137
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 306
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 340
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ SEQUENCE 374 AA; 39365 MW; 6BF3706929B5778E CRC64;
MPTTELDGFT FACGDTVDSL TVAYRTYGDY TGSNAVLVCH ALTGSQHVRG RADGDDRGWW
PDIVGPGRPI DTTEYFVVCA NVPGSCHGTD GPPADGPGGD PWGTAFPPVT VPDWTRCQRR
LLDTLGVDRL HAVVGGSVGG MNALDWARRY PDDVHRIAAV ATAPRLDAQC LGLNAIARRA
IRGDPNWNDG DYYGGAHPDR GLALARQLGH VMYLSKASMA DKFGRRTATT DTALPADPAA
EFFATRDVES YLDYQADTFV ARFDANSYLY LLRAMDAYDL AAGRPSVADA LAAFDGDALV
LSFTGDWHFT AAQSATVADA FRAGGAAGVA HHVVDSDYGH DAFLVDSAAV GPPLADFLAA
GTDGAAVTDA TGGV
