PTAS_MYCCT
ID PTAS_MYCCT Reviewed; 322 AA.
AC Q49112; Q2SSP7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Phosphate acetyltransferase;
DE EC=2.3.1.8;
DE AltName: Full=Phosphotransacetylase;
GN Name=pta; OrderedLocusNames=MCAP_0229;
OS Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS / NCTC 10154).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=340047;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8844861; DOI=10.1002/pro.5560050825;
RA Zhu P.P., Peterkofsky A.;
RT "Sequence and organization of genes encoding enzymes involved in pyruvate
RT metabolism in Mycoplasma capricolum.";
RL Protein Sci. 5:1719-1736(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; U62057; AAC44346.1; -; Genomic_DNA.
DR EMBL; CP000123; ABC01301.1; -; Genomic_DNA.
DR RefSeq; WP_011387117.1; NC_007633.1.
DR AlphaFoldDB; Q49112; -.
DR SMR; Q49112; -.
DR EnsemblBacteria; ABC01301; ABC01301; MCAP_0229.
DR GeneID; 23778818; -.
DR KEGG; mcp:MCAP_0229; -.
DR HOGENOM; CLU_019723_0_1_14; -.
DR OMA; NIGCKIA; -.
DR OrthoDB; 1301815at2; -.
DR PhylomeDB; Q49112; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000001928; 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; Transferase.
FT CHAIN 1..322
FT /note="Phosphate acetyltransferase"
FT /id="PRO_0000179132"
SQ SEQUENCE 322 AA; 35677 MW; 1FB392697E7A9F8E CRC64;
MYTLEEIKNQ LGLKSEKKSI VFPEAESEII QSVAKTLVDE KLGLPILLFK SSKEVPSEIK
NNSSIKTICL DEFDTKEFEE EFVKLRKGKA TIEVAHQVMQ LPNYIGAMLV KLNQADCMLS
GLNNTTADTI RPALQIIGTK PGYNIASSIF VMSKGNENYI FTDCALNIKP TSEQLVEITQ
MAVDFAKALN VKNVEAALLS YSTNGSGKGE DVDRVHQAVE ILKSKEKDYV CEGEIQFDAA
FDKKTRDKKF KNCSLLKQTP DIFVFPDINA GNIGYKIAQR MGGFEAIGPF VLGLNQPVND
LSRGATFVDV LNTAIMTLYL SY