ID   PTAS_THEMA              Reviewed;         294 AA.
AC   Q9X0L4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=TM_1130;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-39, AND CHARACTERIZATION.
RX   PubMed=10074080; DOI=10.1128/jb.181.6.1861-1867.1999;
RA   Bock A.-K., Glasemacher J., Schmidt R., Schoenheit P.;
RT   "Purification and characterization of two extremely thermostable enzymes,
RT   phosphate acetyltransferase and acetate kinase, from the hyperthermophilic
RT   eubacterium Thermotoga maritima.";
RL   J. Bacteriol. 181:1861-1867(1999).
CC   -!- FUNCTION: In addition to acetyl-CoA (100%), the enzyme accepts
CC       propionyl-CoA (60%) and butyryl-CoA (30%).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 90 degrees Celsius.;
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC       acetyl-CoA from acetate: step 2/2.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phosphate acetyltransferase and
CC       butyryltransferase family. {ECO:0000305}.
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DR   EMBL; AE000512; AAD36206.1; -; Genomic_DNA.
DR   PIR; G72293; G72293.
DR   RefSeq; NP_228936.1; NC_000853.1.
DR   RefSeq; WP_004080280.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9X0L4; -.
DR   SMR; Q9X0L4; -.
DR   DIP; DIP-2900N; -.
DR   STRING; 243274.TM_1130; -.
DR   PaxDb; 243274-THEMA_08695; -.
DR   EnsemblBacteria; AAD36206; AAD36206; TM_1130.
DR   KEGG; tma:TM1130; -.
DR   eggNOG; COG0280; Bacteria.
DR   InParanoid; Q9X0L4; -.
DR   OrthoDB; 9774179at2; -.
DR   BioCyc; MetaCyc:MONOMER-427; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000008183; 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; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR012147; P_Ac_Bu_trans.
DR   InterPro; IPR002505; PTA_PTB.
DR   PANTHER; PTHR43356; PHOSPHATE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR43356:SF2; PHOSPHATE ACETYLTRANSFERASE; 1.
DR   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF000428; P_Ac_trans; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Cytoplasm; Direct protein sequencing; Reference proteome;
KW   Transferase.
FT   CHAIN           1..294
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000179149"
FT   CONFLICT        11
FT                   /note="R -> Y (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   294 AA;  32093 MW;  F4B98B3CAE120AFB CRC64;
     MFLEKLVEMA RGKGKKLAVA AANDDHVIEA VYRAWRERVC EPVLFGPEEE ITRIIEELVP
     EWKNPQIIDC PPEEAGRLAV EAVSKGECDF LMKGKIKTGD LMKIYLDERY GLRTGKTMAM
     VSVMEIPDFP RPLIISDPGM LISPTLEQKV DMIEHCVRVA NVMGLETPKV AVVGAIEVVN
     PKMPITMEAA ILSKMNQRGQ IKGCIVDGPF ALDNVVSEEA AKKKGIQSPV AGKADILILP
     DIEAANILYK ALVFLAKAKS ASTILGGKVP VVLTSRADSE ETKFYSIALS AVFA
//