ID A0A1G1JWW3_9BACT Unreviewed; 327 AA.
AC A0A1G1JWW3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=A2987_04600 {ECO:0000313|EMBL:OGW85124.1};
OS Omnitrophica bacterium RIFCSPLOWO2_01_FULL_45_10.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801826 {ECO:0000313|EMBL:OGW85124.1, ECO:0000313|Proteomes:UP000176340};
RN [1] {ECO:0000313|EMBL:OGW85124.1, ECO:0000313|Proteomes:UP000176340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGW85124.1}.
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DR EMBL; MHFL01000012; OGW85124.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1JWW3; -.
DR STRING; 1801826.A2987_04600; -.
DR Proteomes; UP000176340; 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:OGW85124.1}.
FT DOMAIN 3..324
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 327 AA; 34901 MW; 03037D515853455B CRC64;
MSILDDIRKR AVKCSKKIVL PESEDARTLD AINIILNKKM TKIILVGEES LSRKIKGKNL
SGIEIINPTK YRDLEALISK YYELRKHKGI TIEEARDAVM NNFLIFGAML VRAGAADGFV
AGANNTTADV IRCGLRCLEI DKNIGVVSGA FLMEVPDPDY GEKGVFVFSD CAVNVEPDAK
QLAGIAVSAA GLFKQLVGPE PRVALLSYSS KGSAKGPLVE KVKEALKLAR TISPGILIDG
ELQADSAIVP EVALKKSAAS EVAGRANVLI FPDLNSGNIG YKLIQRLANA RAIGPLLQGF
TRPASDLSRG CSVDDIVDAA AIIAVRA
//
