CYSE_SALTY
ID CYSE_SALTY Reviewed; 273 AA.
AC P29847;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Serine acetyltransferase;
DE Short=SAT;
DE EC=2.3.1.30 {ECO:0000269|PubMed:4977445};
DE AltName: Full=Serine transacetylase {ECO:0000303|PubMed:4977445};
GN Name=cysE; OrderedLocusNames=STM3699;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RA Sivaprasad A.V., Kuczek E.S., Bawden C.S., Rogers G.E.;
RL Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Rogers G.E.;
RT "Cysteine biosynthesis in transgenic animals.";
RL Patent number GB2227243, 25-JUL-1990.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBUNIT.
RC STRAIN=LT2;
RX PubMed=4977445; DOI=10.1016/s0021-9258(19)78241-6;
RA Kredich N.M., Becker M.A., Tomkins G.M.;
RT "Purification and characterization of cysteine synthetase, a bifunctional
RT protein complex, from Salmonella typhimurium.";
RL J. Biol. Chem. 244:2428-2439(1969).
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:4977445};
CC -!- ACTIVITY REGULATION: Sensitive to feedback inhibition by L-cysteine.
CC {ECO:0000269|PubMed:4977445}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.9 mM for L-serine as isolated subunit
CC {ECO:0000269|PubMed:4977445};
CC KM=7.4 mM for L-serine in complex with CysK
CC {ECO:0000269|PubMed:4977445};
CC KM=1.2 mM for acetyl-CoA as isolated subunit and in complex with CysK
CC {ECO:0000269|PubMed:4977445};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 1/2.
CC -!- SUBUNIT: Part of the cysteine synthase complex formed at a ratio of 1
CC copy of this protein and 2 copies of O-acetylserine sulfhydrylase
CC (cysK). The complex reversibly dissociates in the presence of O-acetyl-
CC L-serine in the absence of hydrogen sulfide.
CC {ECO:0000269|PubMed:4977445}.
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; X59594; CAA42163.1; -; Genomic_DNA.
DR EMBL; A00198; CAA00039.1; -; Unassigned_DNA.
DR EMBL; AE006468; AAL22558.1; -; Genomic_DNA.
DR PIR; S29568; S29568.
DR RefSeq; NP_462599.1; NC_003197.2.
DR RefSeq; WP_001112113.1; NC_003197.2.
DR PDB; 4LI3; X-ray; 2.59 A; A=266-273.
DR PDB; 4NU8; X-ray; 2.07 A; A=266-273.
DR PDB; 4ZU1; X-ray; 2.20 A; A=264-273.
DR PDB; 4ZU6; X-ray; 2.03 A; B=264-273.
DR PDB; 5DBE; X-ray; 2.25 A; A=264-273.
DR PDB; 6AIF; X-ray; 2.30 A; B=264-273.
DR PDBsum; 4LI3; -.
DR PDBsum; 4NU8; -.
DR PDBsum; 4ZU1; -.
DR PDBsum; 4ZU6; -.
DR PDBsum; 5DBE; -.
DR PDBsum; 6AIF; -.
DR AlphaFoldDB; P29847; -.
DR SMR; P29847; -.
DR STRING; 99287.STM3699; -.
DR PaxDb; P29847; -.
DR EnsemblBacteria; AAL22558; AAL22558; STM3699.
DR GeneID; 1255223; -.
DR KEGG; stm:STM3699; -.
DR PATRIC; fig|99287.12.peg.3912; -.
DR HOGENOM; CLU_051638_0_1_6; -.
DR OMA; HPKIRHG; -.
DR PhylomeDB; P29847; -.
DR BioCyc; SENT99287:STM3699-MON; -.
DR BRENDA; 2.3.1.30; 5542.
DR UniPathway; UPA00136; UER00199.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009001; F:serine O-acetyltransferase activity; IBA:GO_Central.
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 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_0000068672"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:4NU8"
SQ SEQUENCE 273 AA; 29291 MW; 6A5736E656FBD25B CRC64;
MPCEELEIVW KNIKAEARAL ADCEPMLASF YHATLLKHEN LGSALSYMLA NKLASPIMPA
IAIREVVEEA YAADPEMIAS AACDIQAVRT RDPAVDKYST PLLYLKGFHA LQAYRIGHWL
WNKGRRALAI FLQNQVSVSF QVDIHPAAKI GRGIMLDHAT GIVVGETAVI EDDVSILQSV
TLGGTGKTSG DRHPKIREGV MIGAGAKILG NIEVGRGAKI GAGSVVLQPV PPHTTAAGVP
ARIVGKPGSD KPSMDMDQHF NGIHHTFEYG DGI
