ID   PTA_PSEPK               Reviewed;         695 AA.
AC   Q88PS4;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=PP_0774;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN66399.1; -; Genomic_DNA.
DR   RefSeq; NP_742935.1; NC_002947.4.
DR   RefSeq; WP_010952014.1; NC_002947.4.
DR   AlphaFoldDB; Q88PS4; -.
DR   SMR; Q88PS4; -.
DR   STRING; 160488.PP_0774; -.
DR   EnsemblBacteria; AAN66399; AAN66399; PP_0774.
DR   KEGG; ppu:PP_0774; -.
DR   PATRIC; fig|160488.4.peg.830; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0857; Bacteria.
DR   HOGENOM; CLU_019723_2_1_6; -.
DR   OMA; FFMCLAD; -.
DR   PhylomeDB; Q88PS4; -.
DR   BioCyc; PPUT160488:G1G01-850-MON; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000000556; 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; 3.40.1390.20; -; 1.
DR   Gene3D; 3.40.50.10750; -; 1.
DR   Gene3D; 3.40.50.10950; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR010766; DRTGG.
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   Pfam; PF07085; DRTGG; 1.
DR   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF006107; PhpActrans_proteobac; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF75138; SSF75138; 1.
DR   TIGRFAMs; TIGR00651; pta; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..695
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000405550"
FT   REGION          374..695
FT                   /note="Phosphate acetyltransferase"
SQ   SEQUENCE   695 AA;  74643 MW;  CE730933D3FFC209 CRC64;
     MQTFFIAPTD FGVGLTSISL GLVRTLERAG LKVGFFKPIA QPHPGDTGPE RSTELVARTH
     GIKPPVPLSL AHVERMLGDG QLDELLEEII RLYQQACVGN DVVVVEGMVP TRHASYAARV
     NLHLAKSLDA EVILVSAPEN EVLSELSGRV ELQAQLFGGP RDPKVLGVIL NKVRTDESMA
     DFATRLREHS PLLRGNDFRL LGCIPYQPEL NAPRTRDVAE LLGAQVLNAG DYEQRRMSKI
     IICARTVANT VPLLTSGTLV VTPGDRDDII LAVSLAAING VPLAGLLLTS DSKPDVRILG
     LCRGALQAGL PILSVSTGSY DTANQLNSLN REIPVDDRER AEFITDFVAS HLDAAWLHQR
     CGTPRELRLS PAVFRYQLIQ RAQQANKRIV LPEGAEPLLV QAAAICQARG IARCVLLAKP
     EDVDAVARAQ GITLPPGLEI LDPELIRGRY VEPMVELRKS KNLNAPMAEQ QLEDPVVIGT
     MMLALDEVDG LVSGLVHSTA NTIRPALQLI KTAPGSSLVS SVFFMLFPEQ VLVYGDCVMN
     PHPSAAELAE IAQQSAASAQ AFGIAPRVAM ISYSSDSASD EEVEKVREAT RLAQDAAQEL
     LIDGPLQYDA AANPAIAREL APASPVAGRA TVFVFPDLNT GNTTHKAVQR SADGVSLGPM
     LQGLRKPVND LPRGAQVDDI VHTIALTAIQ ASVAR