ID   PTAS_RICTY              Reviewed;         349 AA.
AC   Q68XX7;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=RT0027;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + phosphate = acetyl phosphate + CoA;
CC         Xref=Rhea:RHEA:19521, ChEBI:CHEBI:22191, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.8;
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC       acetyl-CoA from acetate: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phosphate acetyltransferase and
CC       butyryltransferase family. {ECO:0000305}.
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DR   EMBL; AE017197; AAU03515.1; -; Genomic_DNA.
DR   RefSeq; WP_011190502.1; NC_006142.1.
DR   AlphaFoldDB; Q68XX7; -.
DR   SMR; Q68XX7; -.
DR   KEGG; rty:RT0027; -.
DR   eggNOG; COG0280; Bacteria.
DR   HOGENOM; CLU_056531_1_0_5; -.
DR   OrthoDB; 9800237at2; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000000604; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008959; F:phosphate acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR012147; P_Ac_Bu_trans.
DR   InterPro; IPR002505; PTA_PTB.
DR   PANTHER; PTHR43356; PHOSPHATE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR43356:SF2; PHOSPHATE ACETYLTRANSFERASE; 1.
DR   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF000428; P_Ac_trans; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Transferase.
FT   CHAIN           1..349
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000286663"
SQ   SEQUENCE   349 AA;  37938 MW;  428095D4635932B1 CRC64;
     MKKQHIINET FLDEILAQKL GTTYIPPTGI KDADFEQAAK HFINLLLRAD GLKPIKTAVV
     HPIDKESLLG AVRAAQFNVI KPVLIGPQHK IESVAKVNDV DLENYQVINA EHSHEAAKKA
     VELAKKREVS AIMKGALHTD ELMSAVVYKE NGLRTERRIS HAFLMAVATF PKPFIITDAA
     INIRPTLEDK RDIVQNAIDL MHMIKEDKQV RVAVLSAVET VTSAIPTTLD AAALSKMADR
     GQIMNAIVDG PLAFDNAISL FAAEAKGINS PVSGNADILV APDLESGNLL AKQLKYLGQA
     VMAGIVLGAR VPIILTSRAD PIDMRVISCV LASFIYNQTK AKLHIQASQ
//