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Database: UniProt
Entry: A0A1A0FMF0_9GAMM
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ID   A0A1A0FMF0_9GAMM        Unreviewed;       264 AA.
AC   A0A1A0FMF0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Serine acetyltransferase {ECO:0000256|ARBA:ARBA00018522};
DE            EC=2.3.1.30 {ECO:0000256|ARBA:ARBA00013266};
GN   ORFNames=ADS46_09490 {ECO:0000313|EMBL:OBA00654.1};
OS   Halomonas sp. G11.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1684425 {ECO:0000313|EMBL:OBA00654.1, ECO:0000313|Proteomes:UP000092250};
RN   [1] {ECO:0000313|EMBL:OBA00654.1, ECO:0000313|Proteomes:UP000092250}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G11 {ECO:0000313|EMBL:OBA00654.1,
RC   ECO:0000313|Proteomes:UP000092250};
RA   Naifar M., Chouchane H., Najjari A., El Hidri D., Mahjoubi M., Ghedira K.,
RA   Soufi L., Salah A., Raddadi N., Sghaier H., Ouzari H.I.,
RA   Eddine Masmoudi A.S., Cherif A.;
RT   "Genomic basis for crude oil degradation, heavy metal resistance and high
RT   salt tolerance of Halomonas hydrocarbonoclasticus G11 isolated from
RT   Tunisian Chott El-Djerid salt lake.";
RL   Submitted (FEB-2016) 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:OBA00654.1}.
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DR   EMBL; LYXG01000002; OBA00654.1; -; Genomic_DNA.
DR   RefSeq; WP_066315236.1; NZ_LYXG01000002.1.
DR   AlphaFoldDB; A0A1A0FMF0; -.
DR   OrthoDB; 9801456at2; -.
DR   UniPathway; UPA00136; UER00199.
DR   Proteomes; UP000092250; Unassembled WGS sequence.
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   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; 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   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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OBA00654.1}.
FT   DOMAIN          7..111
FT                   /note="Serine acetyltransferase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00971"
SQ   SEQUENCE   264 AA;  28129 MW;  F67CDDAD20A05C57 CRC64;
     MQIEDATWQT LREEVRALAG SEPILASYLH ATVINHCELE DSLSYLLAGK LSSPDLPAMS
     LREVISQAFA DSPDIRKAIR NDLTAAADRD PAAHGLANPF LNHKGFHSLQ AYRVSHWFWT
     RGRRSLALYL QSRVSEVFAV DINPAAVLGD GIFIDHGNGV VIGETAVVGD NVSMLQGVTL
     GGTGKEEGDR HPKVESGVLL SAGVKVLGNI RIGAGSKVGA GSVVLQDVPR RTTVVGVPAR
     VVGKPGNEHP AICMDQRCEQ AGNT
//
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