METAA_CATMR
ID METAA_CATMR Reviewed; 312 AA.
AC E2NPN0;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00295};
DE Short=HAT {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000303|PubMed:28581482};
DE EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000269|PubMed:28581482};
DE AltName: Full=Homoserine transacetylase {ECO:0000255|HAMAP-Rule:MF_00295};
DE Short=HTA {ECO:0000255|HAMAP-Rule:MF_00295};
GN Name=metAA {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000303|PubMed:28581482};
GN Synonyms=metA {ECO:0000312|EMBL:EEF94800.1};
GN ORFNames=CATMIT_00521 {ECO:0000312|EMBL:EEF94800.1};
OS Catenibacterium mitsuokai (strain DSM 15897 / JCM 10609 / CIP 106738 /
OS RCA14-39).
OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Catenibacterium.
OX NCBI_TaxID=451640;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15897 / JCM 10609 / CIP 106738 / RCA14-39;
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
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_00295,
CC ECO:0000269|PubMed:28581482}.
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_00295,
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_00295}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00295}.
CC -!- SIMILARITY: Belongs to the MetA family. {ECO:0000255|HAMAP-
CC Rule:MF_00295}.
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DR EMBL; ACCK01000034; EEF94800.1; -; Genomic_DNA.
DR RefSeq; WP_006504746.1; NZ_ACCK01000034.1.
DR AlphaFoldDB; E2NPN0; -.
DR SMR; E2NPN0; -.
DR EnsemblBacteria; EEF94800; EEF94800; CATMIT_00521.
DR GeneID; 66218439; -.
DR OrthoDB; 1601420at2; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000004579; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008899; F:homoserine O-succinyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019281; P:L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine; IEA:InterPro.
DR CDD; cd03131; GATase1_HTS; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00295; MetA_acyltransf; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR005697; HST_MetA.
DR InterPro; IPR033752; MetA_family.
DR PANTHER; PTHR20919; PTHR20919; 1.
DR Pfam; PF04204; HTS; 1.
DR PIRSF; PIRSF000450; H_ser_succinyltr; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR01001; metA; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Transferase.
FT CHAIN 1..312
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000440338"
FT ACT_SITE 142
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT ACT_SITE 237
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT ACT_SITE 239
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT SITE 111
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT SITE 194
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
SQ SEQUENCE 312 AA; 36882 MW; 3282E687B7071DAC CRC64;
MPINIPDDLP AYKVLTAENI FVMNQTRATT QRIRPLKILI VNIMPLKITT ETQLLRLLSN
TPLQLEVELI HMSTHDSKNV PKEHLLTFYK TFKDIKENSY DGMIITGAPV EQMPFEEVDY
WNELSEIFEW AKTHVFSSFF ICWASQAALH YYYDIDKYLL KHKLTGVYRH HTNQRKMRRK
ILRGFDYQFY APHSRYTTVL KEDISSNPNL DILAESDDAG VYLVASKDGS QFFVTGHPEY
DPDTLDKEYK RDKEKPGVIA ELPKNYYLDD DPSQEIQVKW RSHAYLLFSN WLNYYVYQET
PYDLSDLHER KK
