ID   CYSE_SYNE7              Reviewed;         244 AA.
AC   Q56002; Q31KG9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Serine acetyltransferase;
DE            Short=SAT;
DE            EC=2.3.1.30;
GN   Name=cysE; OrderedLocusNames=Synpcc7942_2420;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8661945; DOI=10.1007/s002030050355;
RA   Anandan S., Nalty M.S., Cogdell D.E., Golden S.S.;
RT   "Identification of two classes of transcriptional regulator genes in the
RT   cyanobacterium Synechococcus sp. strain PCC 7942.";
RL   Arch. Microbiol. 166:58-63(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000305}.
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DR   EMBL; L41665; AAB38543.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB58450.1; -; Genomic_DNA.
DR   RefSeq; WP_011243996.1; NC_007604.1.
DR   AlphaFoldDB; Q56002; -.
DR   SMR; Q56002; -.
DR   STRING; 1140.Synpcc7942_2420; -.
DR   PRIDE; Q56002; -.
DR   EnsemblBacteria; ABB58450; ABB58450; Synpcc7942_2420.
DR   KEGG; syf:Synpcc7942_2420; -.
DR   eggNOG; COG1045; Bacteria.
DR   HOGENOM; CLU_051638_10_0_3; -.
DR   OMA; GDDVMLY; -.
DR   OrthoDB; 1639008at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_2420-MON; -.
DR   UniPathway; UPA00136; UER00199.
DR   GO; GO:0031470; C:carboxysome; IEA:UniProt.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009001; F:serine O-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043886; F:structural constituent of carboxysome; IEA:UniProt.
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; 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.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm;
KW   Repeat; Transferase.
FT   CHAIN           1..244
FT                   /note="Serine acetyltransferase"
FT                   /id="PRO_0000068686"
SQ   SEQUENCE   244 AA;  26454 MW;  AB0B50491023EDB1 CRC64;
     MFKTLAADFR IIFERDPAAR NGLEVLLCYP GFQALVCHRV AHWLYQQRLP VIPRLLSHLS
     RLLTGVEIHP GARLGQGIFI DHGMGVVIGE TAIVGDYCLI YQGVTLGGTG KQSGKRHPTL
     ANNVVVGAGA KVLGNIQIGE NVRIGAGSVV LRDVPSDCTV VGIPGRVIYR SGVRVDPLDH
     SQMPDSEARV IRMLLDRIEA LEDQLEGLNL PPAEEAIDVT LAPVGDRCQL RDRTIEEFLD
     GAGI