ID   PTAS_RHIML              Reviewed;         316 AA.
AC   Q9X448;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-MAY-2023, entry version 63.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta;
OS   Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=104A14;
RX   PubMed=10094701; DOI=10.1128/jb.181.7.2217-2224.1999;
RA   Summers M.L., Denton M.C., McDermott T.R.;
RT   "Genes coding for phosphotransacetylase and acetate kinase in Sinorhizobium
RT   meliloti are in an operon that is inducible by phosphate stress and
RT   controlled by phoB.";
RL   J. Bacteriol. 181:2217-2224(1999).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD24357.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF095903; AAD24357.1; ALT_FRAME; Genomic_DNA.
DR   UniPathway; UPA00340; UER00459.
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..316
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000179137"
SQ   SEQUENCE   316 AA;  33398 MW;  04AC70D7B077D86E CRC64;
     MRXRWPAQPS KYDRLIAAAR AEAPAVTIVA HPCDETSLGG AIEAAEMGLI TPILVAPEAK
     IRNVAAEHRL DLGRREIVDV PHSHAAAAKA VALIREGRGE LLMKGSLHTD ELMHEVAASA
     TGLRTQRRIS HVFVMDVPGH TDTLFITDAA INIFPDLEAK RDIVQNAIDL WVAIGLGEPR
     VAILSAVETV TAKIPSTIEA AALCKMAERG QITGGVLEGP LAFDNAIDQE AARIKGINSP
     VAGHAQILVV PDLEAGNMLA KNLTFLTHAD AAGLVLGARV PIVLTSRADS VRTRLASCAV
     AALYAARRRA AQVAAV
//