ID   PTA_HAEIN               Reviewed;         711 AA.
AC   P45107;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=HI_1203;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC22857.1; -; Genomic_DNA.
DR   PIR; B64169; B64169.
DR   RefSeq; NP_439359.1; NC_000907.1.
DR   AlphaFoldDB; P45107; -.
DR   SMR; P45107; -.
DR   STRING; 71421.HI_1203; -.
DR   DNASU; 950151; -.
DR   EnsemblBacteria; AAC22857; AAC22857; HI_1203.
DR   KEGG; hin:HI_1203; -.
DR   PATRIC; fig|71421.8.peg.1255; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0857; Bacteria.
DR   HOGENOM; CLU_019723_2_1_6; -.
DR   OrthoDB; 9808984at2; -.
DR   PhylomeDB; P45107; -.
DR   BioCyc; HINF71421:G1GJ1-1234-MONOMER; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000000579; 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   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..711
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000179130"
FT   REGION          390..711
FT                   /note="Phosphate acetyltransferase"
SQ   SEQUENCE   711 AA;  76517 MW;  4C684C943E2870CB CRC64;
     MSRTIILIPV STGVGLTSIS LGLIHSLEQK GTKVAFMKPV SQPSTGEDKL DRTTSIIRTS
     TSLETAEPFM LSVAESLIGQ NQSDVLLEKI VANHQQLTKN NDIVVVEGLI PTRKHGYANS
     INYEIAQALD AEIVLVAAPA TETPTELKDR VEAAASLFGG KNNPNLLGVV VNKFNAPVDE
     SGRTRPDLAE IFDSFQHNHI SETEVNKLFA GSAIKLLACV PWNANLIATR AIDLVKHLGA
     SIINEGEINR RIRGITFCAR SLPNMVEHFR AGSLLVASAD RPDVLVAAAL AASNGIEIGG
     ILLTGGYKID AQINKLCRPT FEKAKLPIFR IEGNTWQTAL SLQSFNLEVP VDDKERIENI
     KQYISQHFNA DFINNLVADS SRLPRLSPPA FRFQLTELAR AAKKRIVLPE GDEPRTIKAA
     VLCAERGIAE CVLLADPASV QRVAEAQGVK LGKGITIINP ADVRENYVDR LVELRKAKGM
     TETAAREQLE DTVVLGTMML EANEVDGLVS GAVHTTANTI RPPMQIIKTA PGSSIVSSIF
     FMLLPDQVLV YGDCAVNPDP TAEQLAEIAI QSADSAKAFG IDPKVAMISY STGTSGSGAD
     VEKVKEATRI AKEKRPDLLI DGPLQYDAAV MEDVARSKAP NSPVAGKATV FVFPDLNTGN
     TTYKAVQRSA DLVSIGPMLQ GMRKPVNDLS RGALVDDIVY TIALTAIQAT Q
//