ID A0A0Q5RIC3_9SPHN Unreviewed; 302 AA.
AC A0A0Q5RIC3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=serine O-acetyltransferase {ECO:0000256|ARBA:ARBA00013266};
DE EC=2.3.1.30 {ECO:0000256|ARBA:ARBA00013266};
GN ORFNames=ASG11_05665 {ECO:0000313|EMBL:KQS05195.1};
OS Sphingomonas sp. Leaf357.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736350 {ECO:0000313|EMBL:KQS05195.1, ECO:0000313|Proteomes:UP000051080};
RN [1] {ECO:0000313|EMBL:KQS05195.1, ECO:0000313|Proteomes:UP000051080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf357 {ECO:0000313|EMBL:KQS05195.1,
RC ECO:0000313|Proteomes:UP000051080};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS05195.1, ECO:0000313|Proteomes:UP000051080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf357 {ECO:0000313|EMBL:KQS05195.1,
RC ECO:0000313|Proteomes:UP000051080};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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 -!- 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:KQS05195.1}.
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DR EMBL; LMPM01000001; KQS05195.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q5RIC3; -.
DR STRING; 1736350.ASG11_05665; -.
DR Proteomes; UP000051080; Unassembled WGS sequence.
DR GO; GO:0009001; F:serine O-acetyltransferase activity; IEA:UniProtKB-EC.
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; IPR042122; Ser_AcTrfase_N_sf.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
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 SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Reference proteome {ECO:0000313|Proteomes:UP000051080};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KQS05195.1}.
SQ SEQUENCE 302 AA; 32497 MW; 03A323C1F7F9DF3C CRC64;
MADLRAARED WRARQDEARD VVSFPSRAAL EQIVRQLSAA LYPRRLGQFR GNLADEDNFV
AAKLLAALTD LEREIGNELG YWQPEAGLFD ADQAPAIVRL FAAALGDIRR LVDSDVEAAF
LGDPAARSVD EILVCYPGAI ASLHHRIAHE LNALGAPIVA RLISELANER TGIDIHPGAT
IGESFFIDHG TGVVIGETAI IGARVRLYQH VTLGARSPIG ATPHDVRERH ARHPIVGDDV
VIYAGATILG RVTIGARSTI GGNVWLLSDV PDDSVLVQPE AQRLDTEAGL ALRDVLLRAA
SA
//
