ID A0A1Q3RPS5_9FIRM Unreviewed; 334 AA.
AC A0A1Q3RPS5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Phosphate acetyltransferase {ECO:0000256|ARBA:ARBA00021528};
DE EC=2.3.1.8 {ECO:0000256|ARBA:ARBA00012707};
DE AltName: Full=Phosphotransacetylase {ECO:0000256|ARBA:ARBA00031108};
GN ORFNames=BGO41_09165 {ECO:0000313|EMBL:OJV66087.1};
OS Clostridiales bacterium 38-18.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1895746 {ECO:0000313|EMBL:OJV66087.1, ECO:0000313|Proteomes:UP000185881};
RN [1] {ECO:0000313|EMBL:OJV66087.1, ECO:0000313|Proteomes:UP000185881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=38-18 {ECO:0000313|EMBL:OJV66087.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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 Evidence={ECO:0000256|ARBA:ARBA00000705};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from acetate: step 2/2. {ECO:0000256|ARBA:ARBA00004989}.
CC -!- SIMILARITY: Belongs to the phosphate acetyltransferase and
CC butyryltransferase family. {ECO:0000256|ARBA:ARBA00005656}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJV66087.1}.
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DR EMBL; MKTL01000002; OJV66087.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3RPS5; -.
DR STRING; 1895746.BGO41_09165; -.
DR Proteomes; UP000185881; Unassembled WGS sequence.
DR GO; GO:0016407; F:acetyltransferase activity; IEA:InterPro.
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 {ECO:0000256|ARBA:ARBA00023315};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OJV66087.1}.
FT DOMAIN 3..325
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 334 AA; 35494 MW; 31F79650C23D11A0 CRC64;
MAFLDKVIEV AKKDIQTIVL PEAFDPRTIE ATHKILEAGI ANIILVGDKE EILSTAGEWK
IEGATFINPK TFDQLDAFAA ELANLRKSKG MTVEEAKEIL IDSELFFGVM LVKMGFAGGM
VAGAANSTAN VLRPALQILK TAPGTKLVSA VFLMEVPNCE FGEEGIFIFG DCALNPNPTS
EELAHIAISS AKTFESIVHA EPKVAMLSFS SMGSASHADV DKVVEATRIA KELAPELALD
GELQFDAAIV PSVGKKKAPE SKVAGEANVI IFPDLDAGNI GYKLVQRLAK ANAYGPICQG
LAMPVNDLSR GCYADDIVGT VALTALQAQM QSKK
//
