CYSE_BUCAP
ID CYSE_BUCAP Reviewed; 261 AA.
AC P32003;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Serine acetyltransferase;
DE Short=SAT;
DE EC=2.3.1.30;
GN Name=cysE; OrderedLocusNames=BUsg_051;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1398077; DOI=10.1016/0378-1119(92)90074-y;
RA Lai C.-Y., Baumann P.;
RT "Sequence analysis of a DNA fragment from Buchnera aphidicola (an
RT endosymbiont of aphids) containing genes homologous to dnaG, rpoD, cysE,
RT and secB.";
RL Gene 119:113-118(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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 -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 1/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
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DR EMBL; M90644; AAA73232.1; -; Genomic_DNA.
DR EMBL; AE013218; AAM67622.1; -; Genomic_DNA.
DR PIR; JC1293; JC1293.
DR AlphaFoldDB; P32003; -.
DR SMR; P32003; -.
DR STRING; 198804.BUsg_051; -.
DR EnsemblBacteria; AAM67622; AAM67622; BUsg_051.
DR KEGG; bas:BUsg_051; -.
DR eggNOG; COG1045; Bacteria.
DR HOGENOM; CLU_051638_0_1_6; -.
DR OMA; DVIMHDR; -.
DR UniPathway; UPA00136; UER00199.
DR Proteomes; UP000000416; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 1.10.3130.10; -; 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 Pfam; PF00132; Hexapep; 1.
DR Pfam; PF06426; SATase_N; 1.
DR SMART; SM00971; SATase_N; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR01172; cysE; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm;
KW Repeat; Transferase.
FT CHAIN 1..261
FT /note="Serine acetyltransferase"
FT /id="PRO_0000068667"
SQ SEQUENCE 261 AA; 28914 MW; DC02685464A25944 CRC64;
MCSLEELELW NMIKHKAQKI LKKEPILSNF YQKSILNHKK LSHSLSCILS DKLSTSMISE
KDIYNIFNKI YANNISIINS VVKDIKAASQ RDPVVKHYLT PLLYLKGFHA LEAYRLSHYL
WNIKRYELSA YLQSRISTVF SVDIHPAASI GSGIMLDHAT GIVIGEGVII ENDVSIFHSV
TLGGTGSNTG KNRHPIIRKN VTIGAGAKIL GNIEVGQGVK VGAGSIVLKN IPPFVTVVGV
PAKIIKKIKN SNKNLFQKEK K