ID   PTA_DEIGD               Reviewed;         703 AA.
AC   Q1J2D0;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=Dgeo_0051;
OS   Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=319795;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11300 / AG-3a;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA   Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; CP000359; ABF44354.1; -; Genomic_DNA.
DR   RefSeq; WP_011529201.1; NC_008025.1.
DR   AlphaFoldDB; Q1J2D0; -.
DR   SMR; Q1J2D0; -.
DR   STRING; 319795.Dgeo_0051; -.
DR   KEGG; dge:Dgeo_0051; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0857; Bacteria.
DR   HOGENOM; CLU_019723_2_1_0; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000002431; 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..703
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000405545"
FT   REGION          377..703
FT                   /note="Phosphate acetyltransferase"
SQ   SEQUENCE   703 AA;  74708 MW;  B27D3B9DC99BD169 CRC64;
     MKTLFIAPTR NGVGLTSTAL GLLRALERQG LKVAFLKPIA QTHEAAPDDS VHWARTLAHA
     VTPDPILLSV AEEQLSQGQE EELMENVVAL AREAAAGVTG GADVLVVEGL ALNERNVYAG
     PLNASLARNL EADVVLVSSL AGVTPATLAD ELEIAAQAYR RSDGSGLAGY VLNFAPLELD
     FGGLLADLRA RSRILASGEL PLLGVIAQSP TLAAPRTLDV ARHLGAEVLN EGEARLRRVT
     STVVTARSVP KMADLFTSGA LVVTPGDRED VVMAAALSHL SGVPLAGLLF TSGSTPEAAI
     ERLCRAALTS TLPVLRVETN SYNTASRLSR MEARVPHDDL ERMERTLDFI ADRLDTVPLG
     TRLRAPEGSE RRLPPSAFRY ELIQKARAAN KRIVLPEGDE PRTVRAAIRC VEKGIARCVL
     LAQPEKVRQV AEGQGLTLPD GLEIIDPDRV RANYVAPMVE LRKHKGLTAP QAEAQLEDNV
     VLGTMMLALD EVDGLVSGAV HTTANTVRPA LQLIKTAPGV RLVSSIFFML MPEQVVVYGD
     AAINPNPNAE ELADIAIQSA DSARAFGIPP RIAMLSYSTG ESGAGADVEK VRIATRLVRE
     RRPDLPVDGP LQYDAASVLS VGRQKAPNSP VAGRATVFIF PDLNTGNTTY KAVQRAAGVV
     AVGPMLQGLR KPVNDLSRGA LVDDIVYTIA LTAIQATQAR EGA
//