ID A0A0R1M2Y5_9LACO Unreviewed; 324 AA.
AC A0A0R1M2Y5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=FD04_GL002324 {ECO:0000313|EMBL:KRK99505.1};
OS Secundilactobacillus odoratitofui DSM 19909 = JCM 15043.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1423776 {ECO:0000313|EMBL:KRK99505.1, ECO:0000313|Proteomes:UP000051160};
RN [1] {ECO:0000313|EMBL:KRK99505.1, ECO:0000313|Proteomes:UP000051160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19909 {ECO:0000313|EMBL:KRK99505.1,
RC ECO:0000313|Proteomes:UP000051160};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRK99505.1}.
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DR EMBL; AZEE01000010; KRK99505.1; -; Genomic_DNA.
DR RefSeq; WP_056946534.1; NZ_AZEE01000010.1.
DR AlphaFoldDB; A0A0R1M2Y5; -.
DR STRING; 1423776.FD04_GL002324; -.
DR PATRIC; fig|1423776.4.peg.2354; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000051160; 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}.
FT DOMAIN 4..320
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 324 AA; 34295 MW; 70FB93E8481F7923 CRC64;
MELFDSLKQK ISGLNKTVVL PEGEDIRIIG AASRLAADKL LQPVLLGNAD AIQAAASDKG
FDLTGVKIVD PNNASADEKQ KMLDALVARR KGKNTPEQAA KMLEDPNYWG TMMVYLGEAD
AMVSGAAHPT GDTIRPALQI IKTKPGVKRI SGYFILLKGD ERLFFADSAI NIDLDAEGMA
EVAVESAHTA KKYDIDPKVA LLSFSTKGSA KADQVTKVQE ATKLAQEQAP DVAIDGELQF
DAAVVPEVAA LKAPGSPVAG HANVFIFPEL EAGNIGYKIA QRLGGYEAIG PLLQGLNAPV
SDLSRGANEE DVYKVAIITA AQAE
//
