ID   PTA_SYNY3               Reviewed;         697 AA.
AC   P73662;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   10-JUN-2026, entry version 145.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=slr2132;
OS   Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Merismopediaceae; Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA17707.1; -; Genomic_DNA.
DR   PIR; S77149; S77149.
DR   AlphaFoldDB; P73662; -.
DR   SMR; P73662; -.
DR   STRING; 1148.gene:10498574; -.
DR   PaxDb; 1148-gene:10498574; -.
DR   EnsemblBacteria; BAA17707; BAA17707; BAA17707.
DR   KEGG; syn:slr2132; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0857; Bacteria.
DR   InParanoid; P73662; -.
DR   PhylomeDB; P73662; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
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   FunFam; 3.40.50.10750:FF:000001; Phosphate acetyltransferase; 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; IPR050500; Phos_Acetyltrans/Butyryltrans.
DR   InterPro; IPR002505; PTA_PTB.
DR   InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
DR   NCBIfam; NF004167; PRK05632.1; 1.
DR   NCBIfam; NF007233; PRK09653.1; 1.
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..697
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000179148"
FT   REGION          374..697
FT                   /note="Phosphate acetyltransferase"
SQ   SEQUENCE   697 AA;  76477 MW;  F77B4439F5DB671A CRC64;
     MTSSLYLSTT EARSGKSLVV LGILDLILKK TTRIAYFRPI IQDPVNGKHD NNIILVLENF
     RLQQTYTDSF GLYFHEAVSL ASDGAIDQVL DRILAKYRHL ADQVDFILCE GSDYLGEESA
     FEFDLNTTIA KMLNCPILLL GNAMGNTIAD SLQPIDMALN SYDQESCQVV GVIINRVQPE
     LATEIQAQLE QRYGDRPMVL GTIPQDIMLK SLRLREIVSG LNAQVLSGAD LLDNLVYHHL
     VVAMHIAHAL HWLHEKNTLI ITPGDRGDII LGVMQAHRSL NYPSIAGILL TADYHPEPAI
     MKLIEGLPDA PPLLLTSTHT HETSARLETL HPALSPTDNY KIRHSIALFQ QQIDGEKLLN
     YLKTIRSKGI TPKLFLYNLV QAATAAQRHI VLPEGEEIRI LKAAASLINH GIVRLTLLGN
     IEAIEQTVKI NHIDLDLSKV RLINPKTSPD RERYAETYYQ LRKHKGVTLA MARDILTDIS
     YFGTMMVHLG EADGMVSGSV NTTQHTVRPA LQIIKTQPGF SLVSSVFFMC LEDRVLVYGD
     CAVNPDPNAE QLAEIALTSA ATAKNFGIEP RVALLSYSSG SSGQGADVEK VRQATAIAKE
     REPDLALEGP IQYDAAVDST VAAQKMPGSA VAGKATVFIF PDLNTGNNTY KAVQRETKAI
     AIGPILQGLN KPVNDLSRGC LVEDIINTVV ITALQVK
//