ID   CYSE_BACSU              Reviewed;         217 AA.
AC   Q06750;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Serine acetyltransferase;
DE            Short=SAT;
DE            EC=2.3.1.30;
GN   Name=cysE; Synonyms=cysA; OrderedLocusNames=BSU00930;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7510287; DOI=10.1016/s0021-9258(17)37310-6;
RA   Gagnon Y., Breton R., Putzer H., Pelchat M., Grunberg-Manago M.,
RA   Lapointe J.;
RT   "Clustering and co-transcription of the Bacillus subtilis genes encoding
RT   the aminoacyl-tRNA synthetases specific for glutamate and for cysteine and
RT   the first enzyme for cysteine biosynthesis.";
RL   J. Biol. Chem. 269:7473-7482(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC   STRAIN=168;
RX   PubMed=18974048; DOI=10.1074/jbc.m805951200;
RA   Tanous C., Soutourina O., Raynal B., Hullo M.-F., Mervelet P.,
RA   Gilles A.-M., Noirot P., Danchin A., England P., Martin-Verstraete I.;
RT   "The CymR regulator in complex with the enzyme CysK controls cysteine
RT   metabolism in Bacillus subtilis.";
RL   J. Biol. Chem. 283:35551-35560(2008).
CC   -!- FUNCTION: Catalyzes the acetylation of serine by acetyl-CoA to produce
CC       O-acetylserine (OAS).
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:18974048};
CC   -!- ACTIVITY REGULATION: Inhibited by cysteine.
CC       {ECO:0000269|PubMed:18974048}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000305}.
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DR   EMBL; L14580; AAA21797.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05327.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11869.1; -; Genomic_DNA.
DR   PIR; B53402; B53402.
DR   RefSeq; NP_387974.1; NC_000964.3.
DR   RefSeq; WP_003225749.1; NZ_JNCM01000029.1.
DR   AlphaFoldDB; Q06750; -.
DR   SMR; Q06750; -.
DR   STRING; 224308.BSU00930; -.
DR   PaxDb; Q06750; -.
DR   PRIDE; Q06750; -.
DR   EnsemblBacteria; CAB11869; CAB11869; BSU_00930.
DR   GeneID; 64301931; -.
DR   GeneID; 936831; -.
DR   KEGG; bsu:BSU00930; -.
DR   PATRIC; fig|224308.179.peg.96; -.
DR   eggNOG; COG1045; Bacteria.
DR   InParanoid; Q06750; -.
DR   OMA; GDDVMLY; -.
DR   PhylomeDB; Q06750; -.
DR   BioCyc; BSUB:BSU00930-MON; -.
DR   UniPathway; UPA00136; UER00199.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0009001; F:serine O-acetyltransferase activity; IDA:CAFA.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IMP:CAFA.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR   GO; GO:0009087; P:methionine catabolic process; IMP:CAFA.
DR   CDD; cd03354; LbH_SAT; 1.
DR   Gene3D; 1.10.3130.10; -; 1.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR018357; Hexapep_transf_CS.
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.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN           1..217
FT                   /note="Serine acetyltransferase"
FT                   /id="PRO_0000068665"
SQ   SEQUENCE   217 AA;  24143 MW;  14EFA32FA1086D9D CRC64;
     MFFRMLKEDI DTVFDQDPAA RSYFEVILTY SGLHAIWAHR IAHALYKRKF YFLARLISQV
     SRFFTGIEIH PGATIGRRFF IDHGMGVVIG ETCEIGNNVT VFQGVTLGGT GKEKGKRHPT
     IKDDALIATG AKVLGSITVG EGSKIGAGSV VLHDVPDFST VVGIPGRVVV QNGKKVRRDL
     NHQDLPDPVA DRFKSLEQQI LELKAELEDR KERINQK