ID   SAT_LACAI               Reviewed;         262 AA.
AC   A0A1D3PCK2;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2016, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Serine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305};
DE            Short=SAT {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000303|PubMed:28581482};
DE            EC=2.3.1.30 {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000303|PubMed:28581482};
DE   AltName: Full=Homoserine O-acetyltransferase {ECO:0000305};
DE            Short=HAT {ECO:0000303|PubMed:28581482};
DE            EC=2.3.1.31 {ECO:0000269|PubMed:28581482};
DE   AltName: Full=Homoserine transacetylase {ECO:0000305};
DE            Short=HTA {ECO:0000305};
GN   Name=metA {ECO:0000312|EMBL:SCN13863.1};
OS   Lactobacillus acidophilus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 4356 / DSM 20079 / JCM 1132 / NBRC 13951 / NCIMB 8690 / L917;
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-serine,
CC       forming acetyl-L-serine. In vitro, has also homoserine acetyl
CC       transferase activity. {ECO:0000269|PubMed:28581482}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-serine = CoA + O-acetyl-L-serine;
CC         Xref=Rhea:RHEA:24560, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:58340; EC=2.3.1.30;
CC         Evidence={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:0000269|PubMed:28581482};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 1/2.
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; LT613639; SCN13863.1; -; Genomic_DNA.
DR   RefSeq; WP_003547771.1; NZ_WPCN01000001.1.
DR   AlphaFoldDB; A0A1D3PCK2; -.
DR   SMR; A0A1D3PCK2; -.
DR   GeneID; 56942827; -.
DR   KEGG; laf:SD55_1232; -.
DR   UniPathway; UPA00136; UER00199.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004414; F:homoserine O-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009001; F:serine O-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:UniProtKB-UniRule.
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; 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.
PE   1: Evidence at protein level;
KW   Acyltransferase; Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm;
KW   Transferase.
FT   CHAIN           1..262
FT                   /note="Serine O-acetyltransferase"
FT                   /id="PRO_0000440362"
FT   ACT_SITE        107
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   ACT_SITE        200
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   ACT_SITE        202
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   BINDING         214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   SITE            76
FT                   /note="Important for acyl-CoA specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   SITE            156
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
SQ   SEQUENCE   262 AA;  30771 MW;  C0C8344D8467FE2F CRC64;
     MANKVKIGIL NLMHDKLDTQ SHFIKVLPNA DLTFFYPRMH YQNRPIPPEV NMTSEPLDIN
     RVSEFDGFII TGAPIDQIDF SKITYIEEIR YLLQALDNHK IQQLYFCWGA MAALNYFYGI
     KKKILAEKIF GVFPHLITEP HPLLSGLSQG FMAPHARYAE MDKKQIMQDE RLAINAVDDN
     SHLFMVSAKD NPERNFIFSH IEYGKDSLRD EYNREINAHP ERHYKKPINY SMSNPSFQWQ
     DTQKIFFNNW LKKVKDNKLV LN