ID K8E295_CARML Unreviewed; 292 AA.
AC K8E295;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
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 Name=pta {ECO:0000313|EMBL:CCO10049.1};
GN ORFNames=BN424_559 {ECO:0000313|EMBL:CCO10049.1};
OS Carnobacterium maltaromaticum LMA28.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1234679 {ECO:0000313|EMBL:CCO10049.1, ECO:0000313|Proteomes:UP000000212};
RN [1] {ECO:0000313|Proteomes:UP000000212}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LMA28 {ECO:0000313|Proteomes:UP000000212};
RX PubMed=23405327; DOI=10.1128/genomeA.00115-12;
RA Cailliez-Grimal C., Chaillou S., Anba-Mondoloni J., Loux V., Afzal M.I.,
RA Rahman A., Kergourlay G., Champomier-Verges M.C., Zagorec M., Dalgaard P.,
RA Leisner J.J., Prevost H., Revol-Junelles A.M., Borges F.;
RT "Complete Chromosome Sequence of Carnobacterium maltaromaticum LMA 28.";
RL Genome Announc. 1:0-0(2013).
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; HE999757; CCO10049.1; -; Genomic_DNA.
DR AlphaFoldDB; K8E295; -.
DR STRING; 1234679.BN424_559; -.
DR KEGG; cml:BN424_559; -.
DR PATRIC; fig|1234679.3.peg.543; -.
DR eggNOG; COG0280; Bacteria.
DR HOGENOM; CLU_019723_0_1_9; -.
DR Proteomes; UP000000212; 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:CCO10049.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000212};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCO10049.1}.
FT DOMAIN 2..286
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 292 AA; 31517 MW; 7530002208B6823A CRC64;
MASEELVTPV LIGSEVAVKE AAKKRGFVVD NIEIIDPNNY PAMDEMVAAF VERRKGKATE
EQAREMLKDE NYFGTMLTYM GLTDGLVSGA VHSTGDTVRP ALQIIKTKPG VSRTSGAFIM
LRGRDNEKYL FSDCAINVNP NAQELAEIAV ESAKTAALFD IDPKVAMLSF STKGSANAPE
AKKVEEATKI AQEMAPEIQI DGELQFDAAY VASVGQQKAP DSEVAGHATV FVFPELQSGN
IGYKIAQRFG NFEAIGPILQ GLNKPVSDLS RGCNEEDVYK LSIITAAQSL MN
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