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
//