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Database: UniProt
Entry: A0A0R2U1Z0_9GAMM
LinkDB: A0A0R2U1Z0_9GAMM
Original site: A0A0R2U1Z0_9GAMM 
ID   A0A0R2U1Z0_9GAMM        Unreviewed;       260 AA.
AC   A0A0R2U1Z0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Serine acetyltransferase {ECO:0000256|ARBA:ARBA00018522};
DE            EC=2.3.1.30 {ECO:0000256|ARBA:ARBA00013266};
GN   ORFNames=ABS24_03635 {ECO:0000313|EMBL:KRO93441.1};
OS   SAR92 bacterium BACL26 MAG-121220-bin70.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Porticoccaceae; SAR92 clade.
OX   NCBI_TaxID=1655626 {ECO:0000313|EMBL:KRO93441.1, ECO:0000313|Proteomes:UP000051213};
RN   [1] {ECO:0000313|EMBL:KRO93441.1, ECO:0000313|Proteomes:UP000051213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL26 MAG-121220-bin70 {ECO:0000313|EMBL:KRO93441.1};
RA   Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA   Andersson A.F.;
RT   "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL   Submitted (OCT-2015) 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         Evidence={ECO:0000256|ARBA:ARBA00000169};
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRO93441.1}.
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DR   EMBL; LICA01000255; KRO93441.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2U1Z0; -.
DR   UniPathway; UPA00136; UER00199.
DR   Proteomes; UP000051213; Unassembled WGS sequence.
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; 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; IPR011004; Trimer_LpxA-like_sf.
DR   NCBIfam; TIGR01172; cysE; 1.
DR   NCBIfam; NF041874; EPS_EpsC; 1.
DR   PANTHER; PTHR42811; SERINE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR42811:SF5; SERINE ACETYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF06426; SATase_N; 1.
DR   SMART; SM00971; SATase_N; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRO93441.1}.
FT   DOMAIN          7..111
FT                   /note="Serine acetyltransferase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00971"
SQ   SEQUENCE   260 AA;  27714 MW;  A114C6703D314BE4 CRC64;
     MTSDKPIWLL ITEEAKLSIA EEPLLSEFYQ RTILDHSDLD SSLSYNLANQ LSGSGIPFTT
     IEKLILDALT ADSGIGDSAR LDIIANVERD PACDKHLMPL LYFKGFQAMQ LYRISHWYWC
     NGRVALALFL QNQVAEIFAV DIHPGARMGS GIMIDHATGL VVGETAVIGD NVSILHSVTL
     GGSGRGNGDR HPQVGSGVMI AAGAKIIGNV KIGNGVKVGA GSLVIESVPP HVTVVGVPAR
     IVGARLKGPP SFDMNQHLDV
//
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