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 03-AUG-2022, entry version 119.
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; Firmicutes; 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 EnsemblBacteria; AAK79708; AAK79708; 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 OMA; TMLVKMG; -.
DR OrthoDB; 1301815at2; -.
DR BioCyc; MetaCyc:PTACLOS-MON; -.
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; 3.40.50.10750; -; 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..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