ID   CYSE_LACCA              Reviewed;         271 AA.
AC   A0A120HUS7;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2016, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Serine O-acetyltransferase {ECO:0000303|PubMed:26790714};
DE            Short=SAT {ECO:0000303|PubMed:26790714};
DE            EC=2.3.1.30 {ECO:0000269|PubMed:26790714};
GN   Name=cysE {ECO:0000303|PubMed:26790714};
OS   Lactobacillus casei.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1582 {ECO:0000312|EMBL:AMB19070.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC   STRAIN=FAM18110;
RX   PubMed=26790714; DOI=10.1093/femsle/fnw012;
RA   Bogicevic B., Berthoud H., Portmann R., Bavan T., Meile L., Irmler S.;
RT   "Cysteine biosynthesis in Lactobacillus casei: identification and
RT   characterization of a serine acetyltransferase.";
RL   FEMS Microbiol. Lett. 363:0-0(2016).
CC   -!- FUNCTION: Catalyzes the formation of O-acetylserine (OAS) from L-serine
CC       and acetyl-CoA. To a lesser extent, is also able to use succinyl-CoA
CC       and propionyl-CoA as acyl donors, but not butyryl-CoA. Does not acylate
CC       D-serine and L-homoserine. {ECO:0000269|PubMed:26790714}.
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:0000269|PubMed:26790714};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.13 mM for L-serine {ECO:0000269|PubMed:26790714};
CC         KM=0.021 mM for acetyl-CoA {ECO:0000269|PubMed:26790714};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 1/2. {ECO:0000305|PubMed:26790714}.
CC   -!- MISCELLANEOUS: Is able to complement an E.coli cysE mutant strain but
CC       not an E.coli metA mutant. {ECO:0000269|PubMed:26790714}.
CC   -!- SIMILARITY: Belongs to the MetA family. {ECO:0000305}.
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DR   EMBL; KU216159; AMB19070.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A120HUS7; -.
DR   SMR; A0A120HUS7; -.
DR   STRING; 1582.AAW28_13090; -.
DR   eggNOG; COG1897; Bacteria.
DR   UniPathway; UPA00136; UER00199.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0009001; F:serine O-acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IGI:UniProtKB.
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;
KW   Transferase.
FT   CHAIN           1..271
FT                   /note="Serine O-acetyltransferase"
FT                   /id="PRO_0000436850"
FT   ACT_SITE        112
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P07623"
FT   ACT_SITE        204
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P07623"
FT   ACT_SITE        206
FT                   /evidence="ECO:0000250|UniProtKB:P07623"
SQ   SEQUENCE   271 AA;  31522 MW;  38AEDBA73CA9F9E3 CRC64;
     MEKSPLKIGI LNVMHDKADT KTRLQHVLTH TAIPVDLHFY YPMTHYAGRT VPEAVSSILD
     PLDIHEVATM DGFIITGSPI ETLEFDQVHY IAEVRTLLKT LSQHVPNQLY LCWGGMVALN
     YFFGISKLIL PHKLFGVYPQ TILEPHPLLK GLKNDFKSPH ARYAEMDVRG IHADPRLTIN
     ATTTKGKLFM VTEPTDTQTF VFSHIEYDRW GLDSEYKREV AAHPEIDYVR AKHYYHHKND
     YDHPKFNWKK TQRTIFDNWI QHVADHRNDN H