ID Q03H89_PEDPA Unreviewed; 323 AA.
AC Q03H89;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
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 OrderedLocusNames=PEPE_0337 {ECO:0000313|EMBL:ABJ67433.1};
OS Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 /
OS 183-1w).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus.
OX NCBI_TaxID=278197 {ECO:0000313|EMBL:ABJ67433.1, ECO:0000313|Proteomes:UP000000773};
RN [1] {ECO:0000313|EMBL:ABJ67433.1, ECO:0000313|Proteomes:UP000000773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w
RC {ECO:0000313|Proteomes:UP000000773};
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA Kozyavkin S., Weimer B., Mills D.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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}.
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DR EMBL; CP000422; ABJ67433.1; -; Genomic_DNA.
DR RefSeq; WP_002832770.1; NC_008525.1.
DR AlphaFoldDB; Q03H89; -.
DR STRING; 278197.PEPE_0337; -.
DR GeneID; 33062488; -.
DR KEGG; ppe:PEPE_0337; -.
DR eggNOG; COG0280; Bacteria.
DR HOGENOM; CLU_019723_0_1_9; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000000773; Chromosome.
DR GO; GO:0008959; F:phosphate acetyltransferase activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:ABJ67433.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABJ67433.1}.
FT DOMAIN 4..320
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 323 AA; 34904 MW; 9A921F512D59C2B4 CRC64;
MDLFEGLKSK IKGQNRTVVF PEGEDVRVLA AAIRLADDGL VQSILLGVEA DIKATAEKHG
LNLENVQIID PSQYPEADQK EMIDKLVERR KGKNTEEQVI EMLKDVNYFG TMLVYLGKAD
AMVSGAVHAT GDTVRPALQI IKTKPGMRRI SGAFIMQREN ERYVFGDAAI NIDPDAETLA
EIAIQSAETA RLFDIDPKVA MLSFSTKGSA AGPMVDKVRE ATKVAQERDP KTPYDGELQF
DAAFVPAVGA SKAPDSEIAG HANVFIFPEL QSGNIGYKIA QRLGGFEAIG PILQGLNAPV
SDLSRGASEE DVYKVAIITA AQV
//
