ID   PTA_VIBCH               Reviewed;         714 AA.
AC   Q9KT08;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=VC_1097;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(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; AE003852; AAF94256.1; -; Genomic_DNA.
DR   PIR; H82242; H82242.
DR   RefSeq; NP_230742.1; NC_002505.1.
DR   RefSeq; WP_000091710.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KT08; -.
DR   SMR; Q9KT08; -.
DR   STRING; 243277.VC_1097; -.
DR   DNASU; 2614367; -.
DR   EnsemblBacteria; AAF94256; AAF94256; VC_1097.
DR   GeneID; 69720211; -.
DR   KEGG; vch:VC_1097; -.
DR   PATRIC; fig|243277.26.peg.1047; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0857; Bacteria.
DR   HOGENOM; CLU_019723_2_1_6; -.
DR   UniPathway; UPA00340; UER00459.
DR   PHI-base; PHI:9842; -.
DR   Proteomes; UP000000584; Chromosome 1.
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   CDD; cd03109; DTBS; 1.
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   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   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.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..714
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000405554"
FT   REGION          390..714
FT                   /note="Phosphate acetyltransferase"
SQ   SEQUENCE   714 AA;  76892 MW;  18B90F0A6D87AC80 CRC64;
     MSRTIMLIPI SAGVGLTSVS MGLLRAMERK GVSVSFYKPI AQPRTGDDQP DLTSTVMSRN
     SDIKIGQPMS MSAAETLIGS EKMDVLLETV VERYNQINKD AEVTLIEGLV PTRKHPFANQ
     VNAEIANTLG AEIVFVATPG TDNPTQLKER IEVACSNFGG TKNKSISGVI INKLNAPVDE
     AGRTRPDLSE IFDDADHAKQ ANLEVMQIFN TSPIRVLGCV PWSIDLIATR AIDMAKHLKA
     EIINQGDINT RRIKSITFCA RSIPNMIEHF KPGSLLVTSA DRPDVIVAAA LAAMNGVEIG
     AVLLTGGYDI PRELVSLCKP AFDTGLPIFK AQGNTWQTSL NLQSFSLEVP ADDKERIEFI
     SEHVASHIDG PWVDSLTEGA QASRRLSPPA FRYQLTELAR SANKRIVLPE GDEPRTVKAA
     AICAERGIAQ CVLLGNPEEI KRVAAQQGVE LGSGIEIIDP KVAQEKYVAR LVELRKSKGM
     TEVVAREQLE DTVVLGTMML ERNEVDGLVS GAVHTTANTI RPPLQIIKTA PNASLVSSIF
     FMLLPDQVLV YGDCAINPDP NAEQLAEIAI QSADSAAAFG IEPRVAMISY STGTSGQGAD
     VDKVREATRI AKEKRPDLVI DGPLQYDAAI MENVAASKAP NSPVAGKATV FVFPDLNTGN
     TTYKAVQRSA DLVSIGPMLQ GMRKPVNDLS RGALVDDIVY TIALTAIQAG QEQK
//