CYSE_ECOLI
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 03-AUG-2022, entry version 127.
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; Proteobacteria; 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}.
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; 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; P0A9D4; -.
DR PRIDE; P0A9D4; -.
DR EnsemblBacteria; AAC76631; AAC76631; b3607.
DR EnsemblBacteria; BAE77685; BAE77685; BAE77685.
DR GeneID; 66672495; -.
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; HPKIRHG; -.
DR PhylomeDB; P0A9D4; -.
DR BioCyc; EcoCyc:SERINE-O-ACETTRAN-MON; -.
DR BioCyc; MetaCyc:SERINE-O-ACETTRAN-MON; -.
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; 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 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
