ID   CYSE_ECO57              Reviewed;         273 AA.
AC   P0A9D6; P05796;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=Serine acetyltransferase;
DE            Short=SAT;
DE            EC=2.3.1.30;
GN   Name=cysE; OrderedLocusNames=Z5034, ECs4485;
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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}.
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DR   EMBL; AE005174; AAG58754.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37908.1; -; Genomic_DNA.
DR   PIR; E91189; E91189.
DR   PIR; F86036; F86036.
DR   RefSeq; NP_312512.1; NC_002695.1.
DR   RefSeq; WP_001277561.1; NZ_VOAI01000021.1.
DR   AlphaFoldDB; P0A9D6; -.
DR   SMR; P0A9D6; -.
DR   STRING; 155864.Z5034; -.
DR   GeneID; 75202179; -.
DR   GeneID; 915573; -.
DR   KEGG; ece:Z5034; -.
DR   KEGG; ecs:ECs_4485; -.
DR   PATRIC; fig|386585.9.peg.4700; -.
DR   eggNOG; COG1045; Bacteria.
DR   HOGENOM; CLU_051638_0_1_6; -.
DR   OMA; MPAIALR; -.
DR   SABIO-RK; P0A9D6; -.
DR   UniPathway; UPA00136; UER00199.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   Gene3D; 1.10.3130.10; serine acetyltransferase, domain 1; 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   NCBIfam; TIGR01172; cysE; 1.
DR   NCBIfam; NF041874; EPS_EpsC; 1.
DR   PANTHER; PTHR42811; SERINE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR42811:SF5; SERINE ACETYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF06426; SATase_N; 1.
DR   SMART; SM00971; SATase_N; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 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_0000068670"
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
//