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P0A9M8 (PTA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphate acetyltransferase

EC=2.3.1.8
Alternative name(s):
Phosphotransacetylase
Gene names
Name:pta
Ordered Locus Names:b2297, JW2294
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length714 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in acetate metabolism. Catalyzes the reversible interconversion of acetyl-CoA and acetyl phosphate. The direction of the overall reaction changes depending on growth conditions. On minimal medium acetyl-CoA is generated. In rich medium acetyl-CoA is converted to acetate and allowing the cell to dump the excess of acetylation potential in exchange for energy in the form of ATP. Ref.8

Catalytic activity

Acetyl-CoA + phosphate = CoA + acetyl phosphate.

Enzyme regulation

Inhibited by NADH and ATP. Pyruvate and PEP act as activators of the acetyl phosphate forming reaction while inhibiting the formation of acetyl-CoA. Ref.10

Pathway

Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2.

Subunit structure

Homohexamer. Ref.10

Subcellular location

Cytoplasm Potential.

Domain

The N-terminal region seems to be important for proper quaternary structure. The C-terminal region contains the substrate-binding site. Ref.10

Disruption phenotype

Severe impairment of growth in anaerobic conditions, as well as in growth on minimal medium. Increased sensitivity to environmental changes. Poor starvation survival and slower growth on glucose, fructose, tryptone broth, or pyruvate, but normal growth on glycerol or succinate. Ref.7 Ref.9

Sequence similarities

In the N-terminal section; belongs to the CobB/CobQ family.

In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=67.2 µM for acetyl-CoA Ref.10

KM=44.9 µM for acetyl phosphate

Vmax=177.4 µM/h/mg enzyme for acetyl-CoA-forming reaction

Vmax=23.1 µM/h/mg enzyme for acetyl phosphate-forming reaction

Binary interactions

With

Entry

#Exp.

IntAct

Notes

napDP0A9I52EBI-555015,EBI-554985

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.2
Chain2 – 714713Phosphate acetyltransferase
PRO_0000179129

Regions

Region391 – 714324Phosphate acetyltransferase

Experimental info

Sequence conflict20 – 5031SLGVI…GGDAP → AWRDPCNGTQRRSSERFQTY RSAAYRWRCA in BAA04663. Ref.2
Sequence conflict208 – 2092KL → NV in BAA04502. Ref.1
Sequence conflict208 – 2092KL → NV in BAA04663. Ref.2
Sequence conflict263 – 2719SIPHMLEHF → QHSAHAGAL in BAA04663. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P0A9M8 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B45AF0C93494A04C

FASTA71477,172
        10         20         30         40         50         60 
MSRIIMLIPT GTSVGLTSVS LGVIRAMERK GVRLSVFKPI AQPRTGGDAP DQTTTIVRAN 

        70         80         90        100        110        120 
SSTTTAAEPL KMSYVEGLLS SNQKDVLMEE IVANYHANTK DAEVVLVEGL VPTRKHQFAQ 

       130        140        150        160        170        180 
SLNYEIAKTL NAEIVFVMSQ GTDTPEQLKE RIELTRNSFG GAKNTNITGV IVNKLNAPVD 

       190        200        210        220        230        240 
EQGRTRPDLS EIFDDSSKAK VNNVDPAKLQ ESSPLPVLGA VPWSFDLIAT RAIDMARHLN 

       250        260        270        280        290        300 
ATIINEGDIN TRRVKSVTFC ARSIPHMLEH FRAGSLLVTS ADRPDVLVAA CLAAMNGVEI 

       310        320        330        340        350        360 
GALLLTGGYE MDARISKLCE RAFATGLPVF MVNTNTWQTS LSLQSFNLEV PVDDHERIEK 

       370        380        390        400        410        420 
VQEYVANYIN ADWIESLTAT SERSRRLSPP AFRYQLTELA RKAGKRIVLP EGDEPRTVKA 

       430        440        450        460        470        480 
AAICAERGIA TCVLLGNPAE INRVAASQGV ELGAGIEIVD PEVVRESYVG RLVELRKNKG 

       490        500        510        520        530        540 
MTETVAREQL EDNVVLGTLM LEQDEVDGLV SGAVHTTANT IRPPLQLIKT APGSSLVSSV 

       550        560        570        580        590        600 
FFMLLPEQVY VYGDCAINPD PTAEQLAEIA IQSADSAAAF GIEPRVAMLS YSTGTSGAGS 

       610        620        630        640        650        660 
DVEKVREATR LAQEKRPDLM IDGPLQYDAA VMADVAKSKA PNSPVAGRAT VFIFPDLNTG 

       670        680        690        700        710 
NTTYKAVQRS ADLISIGPML QGMRKPVNDL SRGALVDDIV YTIALTAIQS AQQQ 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of the ackA (acetate kinase A)-pta (phosphotransacetylase) operon and complementation analysis of acetate utilization by an ackA-pta deletion mutant of Escherichia coli."
Kakuda H., Hosono K., Shiroishi K., Ichihara S.
J. Biochem. 116:916-922(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-12.
Strain: K12 / KH131.
[2]"Nucleotide sequence of the phosphotransacetylase gene of Escherichia coli strain K12."
Matsuyama A., Yamamoto-Otake H., Hewitt J., McGillivray R.T.A., Nakano E.
Biochim. Biophys. Acta 1219:559-562(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-9.
Strain: K12 / 1100.
[3]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Cloning, expression, and nucleotide sequence of the Escherichia coli K-12 ackA gene."
Matsuyama A., Yamamoto H., Nakano E.
J. Bacteriol. 171:577-580(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
Strain: K12.
[7]"Acetate metabolism in a pta mutant of Escherichia coli W3110: importance of maintaining acetyl coenzyme A flux for growth and survival."
Chang D.E., Shin S., Rhee J.S., Pan J.G.
J. Bacteriol. 181:6656-6663(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]"A defect in the acetyl coenzyme A<-->acetate pathway poisons recombinational repair-deficient mutants of Escherichia coli."
Shi I.Y., Stansbury J., Kuzminov A.
J. Bacteriol. 187:1266-1275(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"An insight into the role of phosphotransacetylase (pta) and the acetate/acetyl-CoA node in Escherichia coli."
Castano-Cerezo S., Pastor J.M., Renilla S., Bernal V., Iborra J.L., Canovas M.
Microb. Cell Fact. 8:54-54(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[10]"Functional dissection of Escherichia coli phosphotransacetylase structural domains and analysis of key compounds involved in activity regulation."
Campos-Bermudez V.A., Bologna F.P., Andreo C.S., Drincovich M.F.
FEBS J. 277:1957-1966(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D17576 Genomic DNA. Translation: BAA04502.1.
D21123 Genomic DNA. Translation: BAA04663.1.
U00096 Genomic DNA. Translation: AAC75357.1.
AP009048 Genomic DNA. Translation: BAA16136.1.
PIRG65001.
JX0357.
S50130.
RefSeqNP_416800.1. NC_000913.3.
YP_490539.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0A9M8.
SMRP0A9M8. Positions 403-710.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35815N.
IntActP0A9M8. 27 interactions.
MINTMINT-1263208.
STRING511145.b2297.

PTM databases

PhosSiteP0810425.

2D gel databases

SWISS-2DPAGEP0A9M8.

Proteomic databases

PaxDbP0A9M8.
PRIDEP0A9M8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75357; AAC75357; b2297.
BAA16136; BAA16136; BAA16136.
GeneID12932506.
946778.
KEGGecj:Y75_p2263.
eco:b2297.
PATRIC32119965. VBIEscCol129921_2392.

Organism-specific databases

EchoBASEEB4147.
EcoGeneEG20173. pta.

Phylogenomic databases

eggNOGCOG0280.
HOGENOMHOG000053797.
KOK13788.
OMAKPIAQPH.
OrthoDBEOG6BKJ5W.
PhylomeDBP0A9M8.

Enzyme and pathway databases

BioCycEcoCyc:PHOSACETYLTRANS-MONOMER.
ECOL316407:JW2294-MONOMER.
MetaCyc:PHOSACETYLTRANS-MONOMER.
UniPathwayUPA00340; UER00459.

Gene expression databases

GenevestigatorP0A9M8.

Family and domain databases

Gene3D3.40.1390.20. 1 hit.
3.40.50.300. 1 hit.
InterProIPR010766. DRTGG.
IPR016475. P-Actrans_bac.
IPR027417. P-loop_NTPase.
IPR004614. P_AcTrfase.
IPR002505. PTA_PTB.
IPR028979. Ser_kin/Pase_Hpr_N_like.
[Graphical view]
PfamPF07085. DRTGG. 1 hit.
PF01515. PTA_PTB. 1 hit.
[Graphical view]
PIRSFPIRSF006107. PhpActrans_proteobac. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
SSF75138. SSF75138. 1 hit.
TIGRFAMsTIGR00651. pta. 1 hit.
ProtoNetSearch...

Other

PROP0A9M8.

Entry information

Entry namePTA_ECOLI
AccessionPrimary (citable) accession number: P0A9M8
Secondary accession number(s): P39184 expand/collapse secondary AC list , P78091, P78189, P78190, Q9EUP2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene