ID A0A223KX45_9BACI Unreviewed; 231 AA.
AC A0A223KX45;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 18-JUN-2025, entry version 31.
DE RecName: Full=Serine acetyltransferase {ECO:0000256|ARBA:ARBA00018522, ECO:0000256|PIRNR:PIRNR000441};
DE EC=2.3.1.30 {ECO:0000256|ARBA:ARBA00013266, ECO:0000256|PIRNR:PIRNR000441};
GN ORFNames=BC6307_23585 {ECO:0000313|EMBL:AST94022.1};
OS Sutcliffiella cohnii.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Sutcliffiella.
OX NCBI_TaxID=33932 {ECO:0000313|EMBL:AST94022.1, ECO:0000313|Proteomes:UP000215224};
RN [1] {ECO:0000313|EMBL:AST94022.1, ECO:0000313|Proteomes:UP000215224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6307 {ECO:0000313|EMBL:AST94022.1,
RC ECO:0000313|Proteomes:UP000215224};
RA Lee Y.-J., Yi H., Bahn Y.-S., Kim J.F., Lee D.-W.;
RT "The whole genome sequencing and assembly of Bacillus cohnii DSM 6307T
RT strain.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the acetylation of serine by acetyl-CoA to produce
CC O-acetylserine (OAS). {ECO:0000256|ARBA:ARBA00053848}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine + acetyl-CoA = O-acetyl-L-serine + CoA;
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:0000256|ARBA:ARBA00049486,
CC ECO:0000256|PIRNR:PIRNR000441};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 1/2. {ECO:0000256|ARBA:ARBA00004876}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000256|ARBA:ARBA00007274, ECO:0000256|PIRNR:PIRNR000441}.
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DR EMBL; CP018866; AST94022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A223KX45; -.
DR STRING; 1314751.GCA_001591425_01427; -.
DR KEGG; bcoh:BC6307_23585; -.
DR UniPathway; UPA00136; UER00199.
DR Proteomes; UP000215224; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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 FunFam; 1.10.3130.10:FF:000002; Serine acetyltransferase; 1.
DR FunFam; 2.160.10.10:FF:000007; Serine acetyltransferase; 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; IPR053376; Serine_acetyltransferase.
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 Pfam; PF00132; Hexapep; 1.
DR Pfam; PF06426; SATase_N; 1.
DR PIRSF; PIRSF000441; CysE; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|PIRNR:PIRNR000441};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000215224};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000441}.
FT DOMAIN 5..47
FT /note="Serine acetyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06426"
SQ SEQUENCE 231 AA; 25664 MW; AC992C9C232DDE11 CRC64;
MHFTGKFKEG RKLFRLLKED IEVVFEQDPA ARSYLEVILT YSGLHAIWSH RLAHGLYKRK
FFFLARVISQ VSRFFTGIEI HPGAKIGRRF FIDHGMGVVI GETCEIGNNV TVFQGVTLGG
TGKEKGKRHP TIHDNALIAT GAKVLGSITI GENSKVGAGS VVLKDVPPHS TVVGIPGKVV
IQDGIKIARS KDLNHQDLPD PIADRFKELE KQMEELQKEL IKVTEREGTK E
//
