ID D3RQY1_ALLVD Unreviewed; 265 AA.
AC D3RQY1;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=serine O-acetyltransferase {ECO:0000256|ARBA:ARBA00013266};
DE EC=2.3.1.30 {ECO:0000256|ARBA:ARBA00013266};
GN OrderedLocusNames=Alvin_0863 {ECO:0000313|EMBL:ADC61809.1};
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477 {ECO:0000313|EMBL:ADC61809.1, ECO:0000313|Proteomes:UP000001441};
RN [1] {ECO:0000313|EMBL:ADC61809.1, ECO:0000313|Proteomes:UP000001441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D
RC {ECO:0000313|Proteomes:UP000001441};
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
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; CP001896; ADC61809.1; -; Genomic_DNA.
DR RefSeq; WP_012970085.1; NC_013851.1.
DR AlphaFoldDB; D3RQY1; -.
DR STRING; 572477.Alvin_0863; -.
DR KEGG; alv:Alvin_0863; -.
DR eggNOG; COG1045; Bacteria.
DR HOGENOM; CLU_051638_10_0_6; -.
DR OrthoDB; 9801456at2; -.
DR Proteomes; UP000001441; Chromosome.
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; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR045304; LbH_SAT.
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 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 ECO:0000313|EMBL:ADC61809.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001441};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADC61809.1}.
SQ SEQUENCE 265 AA; 29059 MW; E0B8AE06B46E0021 CRC64;
MFNRIREDIL CVFDRDPAAR NAFEILSTYP GLHAVMVHRI AHRLWRRDFK WSARVLSNIA
RLFTGIEIHP GAVIGRRFFI DHGMGVVIGE TAVIGDDCTL YHGVTLGGTS WQKGKRHPTL
GRDVVVGAGA KVLGPIEIGD GARIGSNAVV VKAVPPGATA VGVPGRIIEP ERDATTRRRA
DTAKRIGFDA YGATRDAPDP VANAINRMLD HIHHMDQRLE SMSRILEQHG LMEHFEHDGD
LDTVAIEPAT QPDAARPDDP TRARG
//