ID   PTA_BUCBP               Reviewed;         715 AA.
AC   Q89AS7;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=bbp_165;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO26898.1; -; Genomic_DNA.
DR   RefSeq; WP_011091299.1; NC_004545.1.
DR   AlphaFoldDB; Q89AS7; -.
DR   SMR; Q89AS7; -.
DR   STRING; 224915.bbp_165; -.
DR   KEGG; bab:bbp_165; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0857; Bacteria.
DR   HOGENOM; CLU_019723_3_0_6; -.
DR   OrthoDB; 9808984at2; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000000601; 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; IPR016475; P-Actrans_bac.
DR   InterPro; IPR027417; P-loop_NTPase.
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; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF006107; PhpActrans_proteobac; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..715
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000179124"
FT   REGION          392..715
FT                   /note="Phosphate acetyltransferase"
SQ   SEQUENCE   715 AA;  80489 MW;  EC82E2C55C0DAE1C CRC64;
     MTRTIMLVPI GKNIGLTTIS LSVISAMKRC KFNVKFLKSA IEYSNTNYNI DDTSLILKDT
     QSLSYINPLI VDFINQFSLK QIKQRIVDYI LSKVYAKKEK YDIFLIEGFD TKSHTYVLSN
     DINYYISKSI NVEIVFVCAV DRSSQLDINN IVYIINNVFK KNKNINIRGV IINELCQKVR
     NDYGNVNLFD MFKSSVKKIN FGDVKYDFLF QKNGIEVLGC VPWIHKLMEP SVKILCDKYL
     GANIIYDRCM NSQYIKTFII YDTNEDIKNA KKFHRSLLII PAISNDKIKE ICVQINKNKI
     LISAILLTNF LNVHDKCTDF IDQLKIANCT ICSTPNDVFT VVSLLHKFNF KLDNKNYQLN
     IIENDMSRHI NLDWIRSLKH SYQYNSICLP SLFIYNLKHL AKKFMKNILL PEGCELRIIK
     AASICSKNDI AYCTLLGNPK KIKNIAESNN IVLNSNIEII DPKLIRKNYV ERLCHLRRHH
     GITLAHANEL VKDNSILSTL ILESKKVDGL VSGSIGTTSS IILPALQLIK TSPGSSLISS
     VFFMLLSDYV TLYADCAVNI NPDATQLAEI AIQSSNTARL FGIFPKVAML SYATGCSGFG
     DTVDKVKEAT RIVQERSPNL IVDGPIQYDA AINRSVAKLK CPHSLVAGNA TVFIFPDLNS
     GNITYKAVQR SANILSIGPI LQGINQPVND LSRGSSVQDI VYTIAVTVLQ SSLSH
//