ID B8E093_DICTD Unreviewed; 240 AA.
AC B8E093;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Serine acetyltransferase {ECO:0000256|ARBA:ARBA00018522};
DE EC=2.3.1.30 {ECO:0000256|ARBA:ARBA00013266};
GN OrderedLocusNames=Dtur_1260 {ECO:0000313|EMBL:ACK42538.1};
OS Dictyoglomus turgidum (strain DSM 6724 / Z-1310).
OC Bacteria; Dictyoglomota; Dictyoglomia; Dictyoglomales; Dictyoglomaceae;
OC Dictyoglomus.
OX NCBI_TaxID=515635 {ECO:0000313|EMBL:ACK42538.1, ECO:0000313|Proteomes:UP000007719};
RN [1] {ECO:0000313|Proteomes:UP000007719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6724 / Z-1310 {ECO:0000313|Proteomes:UP000007719};
RX PubMed=28066333; DOI=10.3389/fmicb.2016.01979;
RA Brumm P.J., Gowda K., Robb F.T., Mead D.A.;
RT "The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM
RT 6724 reveals a specialized carbohydrate fermentor.";
RL Front. Microbiol. 7:1979-1979(2016).
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}.
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DR EMBL; CP001251; ACK42538.1; -; Genomic_DNA.
DR RefSeq; YP_002353152.1; NC_011661.1.
DR AlphaFoldDB; B8E093; -.
DR STRING; 515635.Dtur_1260; -.
DR EnsemblBacteria; ACK42538; ACK42538; Dtur_1260.
DR KEGG; dtu:Dtur_1260; -.
DR PATRIC; fig|515635.4.peg.1300; -.
DR eggNOG; COG1045; Bacteria.
DR HOGENOM; CLU_051638_10_0_0; -.
DR InParanoid; B8E093; -.
DR OrthoDB; 9801456at2; -.
DR UniPathway; UPA00136; UER00199.
DR Proteomes; UP000007719; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009001; F:serine O-acetyltransferase activity; IBA:GO_Central.
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; 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 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 Pfam; PF06426; SATase_N; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000007719};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..53
FT /note="Serine acetyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06426"
FT COILED 212..239
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 240 AA; 26649 MW; 221754898833CEAB CRC64;
MLFLYQRSIN WGEKVMKKII ETIIADYKAV FEKDPAARNF LEVILCYPGF HAILLHRIAH
FLWKLKIPII PRLISHINRF LTGIEIHPGA KIGKGFFIDH GMGVVIGETT EIGDNVLIYQ
GVTLGGTGKE KGKRHPTIGN NVVIGAGAKV LGPITIGDNT RIGAGSVVLK SVPPNCTVVG
VPGRIVTQEG KKLTPKEMLE HGNIPDPELR LIEELNAKIE NLEKRINYLE NLIREKIKEM
//
