ID   PTA_BUCAI               Reviewed;         708 AA.
AC   P57273;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=BU176;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
CC   -!- FUNCTION: Involved in acetate metabolism. {ECO:0000250}.
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   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The N-terminal region seems to be important for proper
CC       quaternary structure. The C-terminal region contains the substrate-
CC       binding site (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the CobB/CobQ family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the phosphate
CC       acetyltransferase and butyryltransferase family. {ECO:0000305}.
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DR   EMBL; BA000003; BAB12893.1; -; Genomic_DNA.
DR   RefSeq; NP_240007.1; NC_002528.1.
DR   RefSeq; WP_010895985.1; NC_002528.1.
DR   AlphaFoldDB; P57273; -.
DR   SMR; P57273; -.
DR   STRING; 563178.BUAP5A_173; -.
DR   EnsemblBacteria; BAB12893; BAB12893; BAB12893.
DR   KEGG; buc:BU176; -.
DR   PATRIC; fig|107806.10.peg.187; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0857; Bacteria.
DR   HOGENOM; CLU_019723_2_1_6; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000001806; 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; 3.40.50.10950; -; 1.
DR   Gene3D; 3.40.1390.20; HprK N-terminal domain-like; 1.
DR   Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   InterPro; IPR010766; DRTGG.
DR   InterPro; IPR016475; P-Actrans_bac.
DR   InterPro; IPR004614; P_AcTrfase.
DR   InterPro; IPR042113; P_AcTrfase_dom1.
DR   InterPro; IPR042112; P_AcTrfase_dom2.
DR   InterPro; IPR002505; PTA_PTB.
DR   InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
DR   NCBIfam; TIGR00651; pta; 1.
DR   PANTHER; PTHR43356; PHOSPHATE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR43356:SF3; PHOSPHATE ACETYLTRANSFERASE; 1.
DR   Pfam; PF13500; AAA_26; 1.
DR   Pfam; PF07085; DRTGG; 1.
DR   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF006107; PhpActrans_proteobac; 1.
DR   SUPFAM; SSF75138; HprK N-terminal domain-like; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..708
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000179122"
FT   REGION          388..708
FT                   /note="Phosphate acetyltransferase"
SQ   SEQUENCE   708 AA;  80770 MW;  1EDC4394824ED89A CRC64;
     MSRIIMLIPL DKDIGLTSIG LSIIYFFYQK KIKKKSVQSI LYFSCTQNSS NSTSHVINKY
     FSKIVHTVDY IDFSKVLFNS PEYSFLLNKV IDEHYNNKFL RELILIEGIK NNYCINSEEM
     NYDISQNLNA EVIFIANLEN SSPEYIKNKE KKINFFLKQK KYKNILGVIF NQINSPFLEN
     KYDFIKKLIV LKKIKNETKT IVPKKILKNN FFSIIACIPW NRNIVTTRVI DLFNFLNIQH
     TNLVQKKNHI IEEIIIFDTH HLNLLNKHSL NTLVIVSFSR VDVFLNVLNC NVNRSKVKCI
     ILTGILKLKK NIASLYKFLI KRSISIFFTE KNTIEILSQL QNFNFDISVK DITYIKKLQR
     YISNFFCHSS FMFFKKKYNI NVIYPPKEFC YNLKLLSQKK NKRIKLPESY EIRILKSVAI
     CSDSNIAQCV LLGDPKKIYS IANDNGINLK KNIEIIDPIS VRQEYLARFL EIRKGKNINE
     FSAKKQLEDN TVLATLILES NHVDGLVSGS INTTSDTIRP ALQIIKTNPQ SLLVSSIFFM
     LLPNQVLIYG DCAININPTA EELAVIAIQS ADSAKMFGIE PRIAMLSYST GCSGFGCQVE
     KVKEATSIIK NRRSDLIIDG PIQYDAAVSN KVAKLKAPSS PISGSANVFI FPDLNSGNIA
     YKAVQRSSRI VSIGPMLQGL RKPVNDLSRG ASVEDIIYTI ALTSIQSE
//