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PTAS_ACET2
ID   PTAS_ACET2              Reviewed;         332 AA.
AC   O52593; A3DE82;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=Cthe_1029;
OS   Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS   103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=203119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Stevens D.R., Guerinot M.L., Lynd L.R.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC   B-4536 / VPI 7372;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA   Newcomb M., Richardson P.;
RT   "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL   Submitted (FEB-2007) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABN52261.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF041841; AAB96951.1; -; Genomic_DNA.
DR   EMBL; CP000568; ABN52261.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041734229.1; NC_009012.1.
DR   AlphaFoldDB; O52593; -.
DR   SMR; O52593; -.
DR   STRING; 203119.Cthe_1029; -.
DR   EnsemblBacteria; ABN52261; ABN52261; Cthe_1029.
DR   KEGG; cth:Cthe_1029; -.
DR   eggNOG; COG0280; Bacteria.
DR   HOGENOM; CLU_019723_0_1_9; -.
DR   OMA; TMLVKMG; -.
DR   OrthoDB; 1301815at2; -.
DR   BRENDA; 2.3.1.8; 1530.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000002145; 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..332
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000179126"
SQ   SEQUENCE   332 AA;  35396 MW;  ED97F638D6C84583 CRC64;
     MSFLEQIIER AKSDVKTIVL PESTDLRVIK AASMIMKKGI AKVVLIGNEK EIKSLAGDID
     LEGVMIEDSL NSEKLEDYAN TLYELRKSKG MTIEAARETI KDPLYYGVMM VKKGEADGMV
     AGAVNSTANT LRPALQILKT APGTKLVSSF FVMVVPNCEY GHNGTFVYAD CGLVENPDAD
     QLSEIAISAS KSFEMLVGAK PQVAMLSYSS YGSAKSELTE KVIKATQLAK EKAPHLAIDG
     ELQVDAAIVP EVAKSKAKGS SVAGKANVLI FPDLDAGNIA YKLTQRLAKA EAYGPITQGL
     ARPVNDLSRG CSAEDIVGVA AITAVQAQYV KA
 
 
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