ID   CYSE_SHIFL              Reviewed;         273 AA.
AC   P0A9D7; P05796;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Serine acetyltransferase;
DE            Short=SAT;
DE            EC=2.3.1.30;
GN   Name=cysE; OrderedLocusNames=SF3646, S4122;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 1/2.
CC   -!- SUBUNIT: Homohexamer. Dimer of a homotrimer (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE005674; AAN45093.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP19099.1; -; Genomic_DNA.
DR   RefSeq; NP_709386.1; NC_004337.2.
DR   RefSeq; WP_001277561.1; NZ_WPGW01000082.1.
DR   AlphaFoldDB; P0A9D7; -.
DR   SMR; P0A9D7; -.
DR   STRING; 198214.SF3646; -.
DR   EnsemblBacteria; AAN45093; AAN45093; SF3646.
DR   EnsemblBacteria; AAP19099; AAP19099; S4122.
DR   GeneID; 1026265; -.
DR   GeneID; 66672495; -.
DR   KEGG; sfl:SF3646; -.
DR   KEGG; sfx:S4122; -.
DR   PATRIC; fig|198214.7.peg.4305; -.
DR   HOGENOM; CLU_051638_0_1_6; -.
DR   OMA; HPKIRHG; -.
DR   OrthoDB; 1639008at2; -.
DR   UniPathway; UPA00136; UER00199.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR045304; LbH_SAT.
DR   InterPro; IPR010493; Ser_AcTrfase_N.
DR   InterPro; IPR042122; Ser_AcTrfase_N_sf.
DR   InterPro; IPR005881; Ser_O-AcTrfase.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF06426; SATase_N; 1.
DR   SMART; SM00971; SATase_N; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   TIGRFAMs; TIGR01172; cysE; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN           1..273
FT                   /note="Serine acetyltransferase"
FT                   /id="PRO_0000068673"
SQ   SEQUENCE   273 AA;  29317 MW;  466EB898750EF709 CRC64;
     MSCEELEIVW NNIKAEARTL ADCEPMLASF YHATLLKHEN LGSALSYMLA NKLSSPIMPA
     IAIREVVEEA YAADPEMIAS AACDIQAVRT RDPAVDKYST PLLYLKGFHA LQAYRIGHWL
     WNQGRRALAI FLQNQVSVTF QVDIHPAAKI GRGIMLDHAT GIVVGETAVI ENDVSILQSV
     TLGGTGKSGG DRHPKIREGV MIGAGAKILG NIEVGRGAKI GAGSVVLQPV PPHTTAAGVP
     ARIVGKPDSD KPSMDMDQHF NGINHTFEYG DGI