CYSE_STAAC
ID CYSE_STAAC Reviewed; 213 AA.
AC Q5HIE6;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Serine acetyltransferase;
DE Short=SAT;
DE EC=2.3.1.30;
GN Name=cysE; OrderedLocusNames=SACOL0575;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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 -!- 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; CP000046; AAW37685.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5HIE6; -.
DR SMR; Q5HIE6; -.
DR EnsemblBacteria; AAW37685; AAW37685; SACOL0575.
DR KEGG; sac:SACOL0575; -.
DR HOGENOM; CLU_051638_10_0_9; -.
DR OMA; GDDVMLY; -.
DR UniPathway; UPA00136; UER00199.
DR Proteomes; UP000000530; 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; IPR045304; LbH_SAT.
DR InterPro; IPR042122; Ser_AcTrfase_N_sf.
DR InterPro; IPR005881; Ser_O-AcTrfase.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 2.
DR PIRSF; PIRSF000441; CysE; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR01172; cysE; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm;
KW Repeat; Transferase.
FT CHAIN 1..213
FT /note="Serine acetyltransferase"
FT /id="PRO_0000068677"
SQ SEQUENCE 213 AA; 23528 MW; 78490FFA1013A11F CRC64;
MLKRMRDDIK MVFEQDPAAR STLEVITTYA GLHAVWSHLI AHKLYNQKKY VAARAISQIS
RFFTGIEIHP GAKIGKRLFI DHGMGVVIGE TCTIGDNVTI YQGVTLGGTG KERGKRHPDI
GDNVLIAAGA KVLGNIKINS NVNIGANSVV LQSVPSYSTV VGIPGHIVKQ DGVRVGKTFD
HRHLPDPIYE QIKHLERQLE KTRNGEIQDD YII