ID   CYSE_BACLD              Reviewed;         216 AA.
AC   Q65PC9; Q62ZR7;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Serine acetyltransferase {ECO:0000312|EMBL:AAU21741.1};
DE            Short=SAT {ECO:0000250|UniProtKB:Q06750};
DE            EC=2.3.1.30;
GN   Name=cysE {ECO:0000312|EMBL:AAU39085.1};
GN   OrderedLocusNames=BLi00111, BL03268;
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1] {ECO:0000312|EMBL:AAU39085.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA   Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT   with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2] {ECO:0000312|EMBL:AAU21741.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
CC   -!- FUNCTION: Catalyzes the acetylation of serine by acetyl-CoA to produce
CC       O-acetylserine (OAS). {ECO:0000250|UniProtKB:Q06750}.
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:0000250|UniProtKB:Q06750};
CC   -!- ACTIVITY REGULATION: Inhibited by cysteine.
CC       {ECO:0000250|UniProtKB:Q06750}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 1/2. {ECO:0000250|UniProtKB:Q06750}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9D4}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000255}.
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DR   EMBL; AE017333; AAU39085.1; -; Genomic_DNA.
DR   EMBL; CP000002; AAU21741.1; -; Genomic_DNA.
DR   RefSeq; WP_003178282.1; NC_006322.1.
DR   AlphaFoldDB; Q65PC9; -.
DR   SMR; Q65PC9; -.
DR   STRING; 279010.BL03268; -.
DR   EnsemblBacteria; AAU21741; AAU21741; BL03268.
DR   GeneID; 66217743; -.
DR   KEGG; bld:BLi00111; -.
DR   KEGG; bli:BL03268; -.
DR   eggNOG; COG1045; Bacteria.
DR   HOGENOM; CLU_051638_10_1_9; -.
DR   OMA; GDDVMLY; -.
DR   OrthoDB; 1639008at2; -.
DR   BioCyc; BLIC279010:BLI_RS00565-MON; -.
DR   UniPathway; UPA00136; UER00199.
DR   Proteomes; UP000000606; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009001; F:serine O-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR   CDD; cd03354; LbH_SAT; 1.
DR   Gene3D; 1.10.3130.10; -; 1.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR045304; LbH_SAT.
DR   InterPro; IPR042122; Ser_AcTrfase_N_sf.
DR   InterPro; IPR005881; Ser_O-AcTrfase.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   Pfam; PF00132; Hexapep; 2.
DR   PIRSF; PIRSF000441; CysE; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   TIGRFAMs; TIGR01172; cysE; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN           1..216
FT                   /note="Serine acetyltransferase"
FT                   /id="PRO_0000404152"
SQ   SEQUENCE   216 AA;  24124 MW;  4C1AD0CC51F74B4C CRC64;
     MFFKMLKEDV DVVFDQDPAA RSYIEVILTY SGLHAIWAHR IAHALYKRKR FFIARAISQI
     ARFFTGIEIH PGAKIGRRFF IDHGMGVVIG ETCEIGNNVT VFQGVTLGGT GKEKGKRHPT
     IEDDALISTG AKVLGSITVG RGAKIGAGSV VLHDVPECST VVGIPGRVVV QNGKKIRRDL
     NHQDLPDPVA DRFRELENEI RQLKQELRRK EREDEL