PTAS_CORGL
ID PTAS_CORGL Reviewed; 329 AA.
AC P77844;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Phosphate acetyltransferase;
DE EC=2.3.1.8;
DE AltName: Full=Phosphotransacetylase;
GN Name=pta; OrderedLocusNames=Cgl2753, cg3048;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=10075432; DOI=10.1099/13500872-145-2-503;
RA Reinscheid D.J., Schnicke S., Rittmann D., Zahnow U., Sahm H.,
RA Eikmanns B.J.;
RT "Cloning, sequence analysis, expression and inactivation of the
RT Corynebacterium glutamicum pta-ack operon encoding phosphotransacetylase
RT and acetate kinase.";
RL Microbiology 145:503-513(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [4]
RP INDUCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=15090522; DOI=10.1128/jb.186.9.2798-2809.2004;
RA Gerstmeir R., Cramer A., Dangel P., Schaffer S., Eikmanns B.J.;
RT "RamB, a novel transcriptional regulator of genes involved in acetate
RT metabolism of Corynebacterium glutamicum.";
RL J. Bacteriol. 186:2798-2809(2004).
RN [5]
RP INDUCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=16179344; DOI=10.1074/jbc.m508693200;
RA Wennerhold J., Krug A., Bott M.;
RT "The AraC-type regulator RipA represses aconitase and other iron proteins
RT from Corynebacterium under iron limitation and is itself repressed by
RT DtxR.";
RL J. Biol. Chem. 280:40500-40508(2005).
RN [6]
RP INDUCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=16547043; DOI=10.1128/jb.188.7.2554-2567.2006;
RA Cramer A., Gerstmeir R., Schaffer S., Bott M., Eikmanns B.J.;
RT "Identification of RamA, a novel LuxR-type transcriptional regulator of
RT genes involved in acetate metabolism of Corynebacterium glutamicum.";
RL J. Bacteriol. 188:2554-2567(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 -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from acetate: step 2/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Activated by RamA and repressed by RipA and RamB.
CC {ECO:0000269|PubMed:15090522, ECO:0000269|PubMed:16179344,
CC ECO:0000269|PubMed:16547043}.
CC -!- SIMILARITY: Belongs to the phosphate acetyltransferase and
CC butyryltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAF20775.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X89084; CAA61455.1; -; Genomic_DNA.
DR EMBL; BA000036; BAC00147.1; -; Genomic_DNA.
DR EMBL; BX927156; CAF20775.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_601948.1; NC_003450.3.
DR AlphaFoldDB; P77844; -.
DR SMR; P77844; -.
DR STRING; 196627.cg3048; -.
DR KEGG; cgb:cg3048; -.
DR KEGG; cgl:Cgl2753; -.
DR PATRIC; fig|196627.13.peg.2684; -.
DR eggNOG; COG0280; Bacteria.
DR HOGENOM; CLU_019723_0_1_11; -.
DR OMA; TMLVKMG; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008959; F:phosphate acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.10750; -; 1.
DR Gene3D; 3.40.50.10950; -; 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 Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF000428; P_Ac_trans; 1.
DR TIGRFAMs; TIGR00651; pta; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..329
FT /note="Phosphate acetyltransferase"
FT /id="PRO_0000179128"
SQ SEQUENCE 329 AA; 35238 MW; EE6E8C6F95432E06 CRC64;
MSAELFENWL LKRARAEHSH IVLPEGDDDR ILMAAHQLLD QDICDITILG DPVKIKERAT
ELGLHLNTAY LVNPLTDPRL EEFAEQFAEL RKSKSVTIDE AREIMKDISY FGTMMVHNGD
ADGMVSGAAN TTAHTIKPSF QIIKTVPEAS VVSSIFLMVL RGRLWAFGDC AVNPNPTAEQ
LGEIAVVSAK TAAQFGIDPR VAILSYSTGN SGGGSDVDRA IDALAEARRL NPELCVDGPL
QFDAAVDPGV ARKKMPDSDV AGQANVFIFP DLEAGNIGYK TAQRTGHALA VGPILQGLNK
PVNDLSRGAT VPDIVNTVAI TAIQAGGRS
