ID   PTAS_MYCGE              Reviewed;         320 AA.
AC   P47541;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=MG299;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
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   -!- SIMILARITY: Belongs to the phosphate acetyltransferase and
CC       butyryltransferase family. {ECO:0000305}.
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DR   EMBL; L43967; AAC71521.1; -; Genomic_DNA.
DR   PIR; A64233; A64233.
DR   RefSeq; WP_009885878.1; NZ_AAGX01000008.1.
DR   AlphaFoldDB; P47541; -.
DR   SMR; P47541; -.
DR   STRING; 243273.MG_299; -.
DR   EnsemblBacteria; AAC71521; AAC71521; MG_299.
DR   KEGG; mge:MG_299; -.
DR   eggNOG; COG0280; Bacteria.
DR   HOGENOM; CLU_019723_0_1_14; -.
DR   OMA; NIGCKIA; -.
DR   OrthoDB; 1301815at2; -.
DR   BioCyc; MGEN243273:G1GJ2-368-MON; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000000807; 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; 3.40.50.10750; -; 1.
DR   Gene3D; 3.40.50.10950; -; 1.
DR   InterPro; IPR012147; P_Ac_Bu_trans.
DR   InterPro; IPR004614; P_AcTrfase.
DR   InterPro; IPR042113; P_AcTrfase_dom1.
DR   InterPro; IPR042112; P_AcTrfase_dom2.
DR   InterPro; IPR002505; PTA_PTB.
DR   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF000428; P_Ac_trans; 1.
DR   TIGRFAMs; TIGR00651; pta; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..320
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000179133"
SQ   SEQUENCE   320 AA;  35469 MW;  9091249E1661A888 CRC64;
     MSVIDIFKKR LQAVSKKPVI IFPEGWSASV LKAVEMLNES KLIQPAVIFH NRQEIPANFD
     KKITHYVIDE MDLTSYANFV YEKRKHKGMD LKEAQKFVRD PSSLAATLVA LKVVDGEVCG
     KEYATKDTLR PALQLLATGN FVSSVFIMEK GEERLYFTDC AFAVYPNSQE LATIAENTFN
     FAKSLNEDEI KMAFLSYSTL GSGKGEMVDK VVLATKLFLE KHPELHQSVC GELQFDAAFV
     EKVRLQKAPQ LTWKNSANIY VFPNLDAGNI AYKIAQRLGG YDAIGPIVLG LSSPVNDLSR
     GASVSDIFNV GIITAAQAIK