ID   A1VJN1_POLNA            Unreviewed;       308 AA.
AC   A1VJN1;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=serine O-acetyltransferase {ECO:0000256|ARBA:ARBA00013266};
DE            EC=2.3.1.30 {ECO:0000256|ARBA:ARBA00013266};
GN   OrderedLocusNames=Pnap_0539 {ECO:0000313|EMBL:ABM35859.1};
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044 {ECO:0000313|EMBL:ABM35859.1, ECO:0000313|Proteomes:UP000000644};
RN   [1] {ECO:0000313|Proteomes:UP000000644}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2 {ECO:0000313|Proteomes:UP000000644};
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(2009).
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}.
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DR   EMBL; CP000529; ABM35859.1; -; Genomic_DNA.
DR   RefSeq; WP_011799959.1; NC_008781.1.
DR   AlphaFoldDB; A1VJN1; -.
DR   STRING; 365044.Pnap_0539; -.
DR   KEGG; pna:Pnap_0539; -.
DR   eggNOG; COG1045; Bacteria.
DR   HOGENOM; CLU_051638_1_0_4; -.
DR   OrthoDB; 9801456at2; -.
DR   Proteomes; UP000000644; Chromosome.
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   ECO:0000313|EMBL:ABM35859.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000644};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABM35859.1}.
FT   REGION          289..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   308 AA;  33346 MW;  EB49F4B4503FA101 CRC64;
     MAVFDIEHIV GALHAVRQDW RESQKRSREP GGRELPSRDA LAQVVEALKG ALFPMRLGPL
     DLRQESEDIY VAHTLDSALH QLLAQIRLEL TYSARHQMRN GSDLEAEALT TTRSFGAALP
     EIRKLLDSDV LAAYHGDPAA RSVDEVLLCY PGILAMIHHR LAHQLYRLGL PLLARIVAEL
     AHAVTGIDIH PGAQIGASFF IDHGTGVVIG ETAVIGQRVR LYQAVTLGAK RFPTDEEGNL
     QKGLPRHPVV EDDVVIYAGA TVLGRVTLGR GATIGGNVWL THDVPPGGNV TQAVSREAGQ
     GSAARQRP
//