METXA_PASMU
ID METXA_PASMU Reviewed; 360 AA.
AC P57884;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
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}; Synonyms=met2;
GN OrderedLocusNames=PM0866;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
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DR EMBL; AE004439; AAK02950.1; -; Genomic_DNA.
DR RefSeq; WP_010906895.1; NC_002663.1.
DR AlphaFoldDB; P57884; -.
DR SMR; P57884; -.
DR STRING; 747.DR93_1706; -.
DR ESTHER; pasmu-metx; Homoserine_transacetylase.
DR EnsemblBacteria; AAK02950; AAK02950; PM0866.
DR KEGG; pmu:PM0866; -.
DR PATRIC; fig|272843.6.peg.876; -.
DR HOGENOM; CLU_028760_1_2_6; -.
DR OMA; TRFCVVS; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000000809; 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 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..360
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000155736"
FT DOMAIN 41..344
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 144
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 305
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 338
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ SEQUENCE 360 AA; 40312 MW; 97F32CA067FA4B14 CRC64;
MAVQKVKLFT EAPFTLSLGG TLQDIEIAYQ TYGELNKEKT NAILICHALT GDAEPYFADH
SQRGWWQTFM GEGLALDTSQ YFFICSNVLG GCKGTTGPSS INPKTNKPYG SQFPNIIVQD
IVALQRALLT HLNIPRLHAV IGGSFGGMQA TQWAIDYPDD VSNVINLCSS LLFGAEAIGF
NHVMRQAVIN DPNFNGGDYY DSQPPEKGLA IARMLGMLTY RTDLQLTKAF GRATKAETEF
WGDYFQVESY LSYQGKKFLA RFDANSYLHL LRALDLYDPG FQYESLSAAL ARIKARYTLV
AVENDQLFKL TELQKSKKLL EESGVDLVYY QFSSDYGHDA FLVDYAFFEK KIRLALANQD