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Database: UniProt
Entry: PTAS_CLOAB
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Original site: PTAS_CLOAB 
ID   PTAS_CLOAB              Reviewed;         333 AA.
AC   P71103;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=CA_C1742;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=8702268; DOI=10.1128/aem.62.8.2758-2766.1996;
RA   Boynton Z.L., Bennett G.N., Rudolph F.B.;
RT   "Cloning, sequencing, and expression of genes encoding
RT   phosphotransacetylase and acetate kinase from Clostridium acetobutylicum
RT   ATCC 824.";
RL   Appl. Environ. Microbiol. 62:2758-2766(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; U38234; AAB18300.1; -; Genomic_DNA.
DR   EMBL; AE001437; AAK79708.1; -; Genomic_DNA.
DR   PIR; A97115; A97115.
DR   RefSeq; NP_348368.1; NC_003030.1.
DR   RefSeq; WP_010965049.1; NC_003030.1.
DR   AlphaFoldDB; P71103; -.
DR   SMR; P71103; -.
DR   STRING; 272562.CA_C1742; -.
DR   GeneID; 44998237; -.
DR   KEGG; cac:CA_C1742; -.
DR   PATRIC; fig|272562.8.peg.1944; -.
DR   eggNOG; COG0280; Bacteria.
DR   HOGENOM; CLU_019723_0_1_9; -.
DR   OrthoDB; 9805787at2; -.
DR   BioCyc; MetaCyc:PTACLOS-MONOMER; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000000814; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008959; F:phosphate acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019413; P:acetate biosynthetic process; IDA:MENGO.
DR   GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.10950; -; 1.
DR   Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 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   NCBIfam; TIGR00651; pta; 1.
DR   PANTHER; PTHR43356; PHOSPHATE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR43356:SF3; 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   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..333
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000179125"
FT   CONFLICT        215
FT                   /note="S -> G (in Ref. 1; AAB18300)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        237
FT                   /note="D -> H (in Ref. 1; AAB18300)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        312
FT                   /note="G -> S (in Ref. 1; AAB18300)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   333 AA;  36140 MW;  EDB3FDE702BECC2D CRC64;
     MDLIESIWEC AKQDKKRIIL AEGEEKRNLI AADKIIKEGL AELVLVGDEN KIKEKASELN
     LDISKAEIMD PETSLKTETY ARDFYELRKH KGMTIEKSEK MVRDPLYFAT MALKDGYVDG
     MVSGAVHTTG DLLRPGLQII KTAPGVKIVS GFFVMIIPDC DYGEEGLLLF ADCAVNPNPT
     SDELADIAIT TAETARKLCN VEPKVAMLSF STMGSAKGEM VDKVKNAVEI TKKFRPDLAI
     DGELQLDAAI DSEVAALKAP SSNVAGNANV LVFPDLQTGN IGYKLVQRFA KAKAIGPICQ
     GFAKPINDLS RGCSSEDIVN VVAITVVQAQ RGI
//
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