ID   CYSE_ECOLI              Reviewed;         273 AA.
AC   P0A9D4; P05796; Q2M7S1;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Serine acetyltransferase;
DE            Short=SAT;
DE            EC=2.3.1.30;
GN   Name=cysE; OrderedLocusNames=b3607, JW3582;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3309158; DOI=10.1099/00221287-133-3-515;
RA   Denk D., Boeck A.;
RT   "L-cysteine biosynthesis in Escherichia coli: nucleotide sequence and
RT   expression of the serine acetyltransferase (cysE) gene from the wild-type
RT   and a cysteine-excreting mutant.";
RL   J. Gen. Microbiol. 133:515-525(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=2108679; DOI=10.1016/0006-291x(90)90615-t;
RA   Tei H., Murata K., Kimura A.;
RT   "Structure and expression of cysX, the second gene in the Escherichia coli
RT   K-12 cysE locus.";
RL   Biochem. Biophys. Res. Commun. 167:948-955(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA   Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT   from 76.0 to 81.5 minutes.";
RL   Nucleic Acids Res. 22:2576-2586(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   CHARACTERIZATION.
RX   PubMed=2125278; DOI=10.1016/0014-5793(90)80862-d;
RA   Wigley D.B., Derrick J.P., Shaw W.V.;
RT   "The serine acetyltransferase from Escherichia coli. Over-expression,
RT   purification and preliminary crystallographic analysis.";
RL   FEBS Lett. 277:267-271(1990).
RN   [7]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [8]
RP   SUBUNIT.
RX   PubMed=10617639; DOI=10.1074/jbc.275.1.461;
RA   Hindson V.J., Moody P.C., Rowe A.J., Shaw W.V.;
RT   "Serine acetyltransferase from Escherichia coli is a dimer of trimers.";
RL   J. Biol. Chem. 275:461-466(2000).
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   -!- ACTIVITY REGULATION: Sensitive to feedback inhibition by L-cysteine.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 1/2.
CC   -!- SUBUNIT: Homohexamer; dimer of a homotrimer (PubMed:10617639). Forms a
CC       cysteine synthase complex with 2 copies of CysK (By similarity).
CC       {ECO:0000250|UniProtKB:P29847, ECO:0000269|PubMed:10617639}.
CC   -!- INTERACTION:
CC       P0A9D4; P0ABK5: cysK; NbExp=4; IntAct=EBI-1133237, EBI-553933;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000305}.
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DR   EMBL; M15745; AAA23648.1; -; Genomic_DNA.
DR   EMBL; M34333; AAA23659.1; -; Genomic_DNA.
DR   EMBL; U00039; AAB18584.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76631.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77685.1; -; Genomic_DNA.
DR   PIR; A27896; XYECSA.
DR   RefSeq; NP_418064.1; NC_000913.3.
DR   RefSeq; WP_001277561.1; NZ_STEB01000024.1.
DR   PDB; 1T3D; X-ray; 2.20 A; A/B/C=1-273.
DR   PDBsum; 1T3D; -.
DR   AlphaFoldDB; P0A9D4; -.
DR   SASBDB; P0A9D4; -.
DR   SMR; P0A9D4; -.
DR   BioGRID; 4259493; 38.
DR   ComplexPortal; CPX-3742; cysEK cysteine synthase complex.
DR   DIP; DIP-9377N; -.
DR   IntAct; P0A9D4; 2.
DR   STRING; 511145.b3607; -.
DR   jPOST; P0A9D4; -.
DR   PaxDb; 511145-b3607; -.
DR   EnsemblBacteria; AAC76631; AAC76631; b3607.
DR   GeneID; 75202179; -.
DR   GeneID; 948126; -.
DR   KEGG; ecj:JW3582; -.
DR   KEGG; eco:b3607; -.
DR   PATRIC; fig|1411691.4.peg.3099; -.
DR   EchoBASE; EB0184; -.
DR   eggNOG; COG1045; Bacteria.
DR   HOGENOM; CLU_051638_0_1_6; -.
DR   InParanoid; P0A9D4; -.
DR   OMA; MPAIALR; -.
DR   OrthoDB; 9801456at2; -.
DR   PhylomeDB; P0A9D4; -.
DR   BioCyc; EcoCyc:SERINE-O-ACETTRAN-MONOMER; -.
DR   BioCyc; MetaCyc:SERINE-O-ACETTRAN-MONOMER; -.
DR   BRENDA; 2.3.1.30; 2026.
DR   SABIO-RK; P0A9D4; -.
DR   UniPathway; UPA00136; UER00199.
DR   EvolutionaryTrace; P0A9D4; -.
DR   PRO; PR:P0A9D4; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009333; C:cysteine synthase complex; IDA:EcoCyc.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0009001; F:serine O-acetyltransferase activity; IDA:EcoCyc.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IDA:ComplexPortal.
DR   GO; GO:0010165; P:response to X-ray; IMP:EcoCyc.
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   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Amino-acid biosynthesis;
KW   Cysteine biosynthesis; Cytoplasm; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..273
FT                   /note="Serine acetyltransferase"
FT                   /id="PRO_0000068669"
FT   HELIX           3..23
FT                   /evidence="ECO:0007829|PDB:1T3D"
FT   HELIX           25..27
FT                   /evidence="ECO:0007829|PDB:1T3D"
FT   HELIX           28..34
FT                   /evidence="ECO:0007829|PDB:1T3D"
FT   TURN            35..37
FT                   /evidence="ECO:0007829|PDB:1T3D"
FT   HELIX           41..53
FT                   /evidence="ECO:0007829|PDB:1T3D"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:1T3D"
FT   HELIX           60..73
FT                   /evidence="ECO:0007829|PDB:1T3D"
FT   HELIX           76..91
FT                   /evidence="ECO:0007829|PDB:1T3D"
FT   HELIX           99..104
FT                   /evidence="ECO:0007829|PDB:1T3D"
FT   HELIX           106..123
FT                   /evidence="ECO:0007829|PDB:1T3D"
FT   HELIX           126..140
FT                   /evidence="ECO:0007829|PDB:1T3D"
FT   STRAND          181..183
FT                   /evidence="ECO:0007829|PDB:1T3D"
FT   STRAND          186..188
FT                   /evidence="ECO:0007829|PDB:1T3D"
FT   STRAND          207..211
FT                   /evidence="ECO:0007829|PDB:1T3D"
FT   STRAND          235..237
FT                   /evidence="ECO:0007829|PDB:1T3D"
FT   TURN            238..241
FT                   /evidence="ECO:0007829|PDB:1T3D"
FT   STRAND          242..245
FT                   /evidence="ECO:0007829|PDB:1T3D"
FT   STRAND          248..250
FT                   /evidence="ECO:0007829|PDB:1T3D"
FT   HELIX           252..255
FT                   /evidence="ECO:0007829|PDB:1T3D"
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
//