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P0A9M8

- PTA_ECOLI

UniProt

P0A9M8 - PTA_ECOLI

Protein

Phosphate acetyltransferase

Gene

pta

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Catalytic activityi

    Acetyl-CoA + phosphate = CoA + acetyl phosphate.

    Enzyme regulationi

    Inhibited by NADH and ATP. Pyruvate and PEP act as activators of the acetyl phosphate forming reaction while inhibiting the formation of acetyl-CoA.1 Publication

    Kineticsi

    1. KM=67.2 µM for acetyl-CoA1 Publication
    2. KM=44.9 µM for acetyl phosphate1 Publication

    Vmax=177.4 µM/h/mg enzyme for acetyl-CoA-forming reaction1 Publication

    Vmax=23.1 µM/h/mg enzyme for acetyl phosphate-forming reaction1 Publication

    Pathwayi

    GO - Molecular functioni

    1. phosphate acetyltransferase activity Source: EcoCyc
    2. protein binding Source: IntAct
    3. zinc ion binding Source: EcoliWiki

    GO - Biological processi

    1. acetate biosynthetic process Source: EcoCyc
    2. acetate catabolic process Source: EcoCyc
    3. acetate metabolic process Source: CACAO
    4. acetyl-CoA biosynthetic process from acetate Source: EcoCyc
    5. L-threonine catabolic process to propionate Source: EcoCyc

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciEcoCyc:PHOSACETYLTRANS-MONOMER.
    ECOL316407:JW2294-MONOMER.
    MetaCyc:PHOSACETYLTRANS-MONOMER.
    UniPathwayiUPA00340; UER00459.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphate acetyltransferase (EC:2.3.1.8)
    Alternative name(s):
    Phosphotransacetylase
    Gene namesi
    Name:pta
    Ordered Locus Names:b2297, JW2294
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG20173. pta.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    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.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 714713Phosphate acetyltransferasePRO_0000179129Add
    BLAST

    Proteomic databases

    PaxDbiP0A9M8.
    PRIDEiP0A9M8.

    2D gel databases

    SWISS-2DPAGEP0A9M8.

    PTM databases

    PhosSiteiP0810425.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A9M8.

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    napDP0A9I52EBI-555015,EBI-554985

    Protein-protein interaction databases

    DIPiDIP-35815N.
    IntActiP0A9M8. 27 interactions.
    MINTiMINT-1263208.
    STRINGi511145.b2297.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A9M8.
    SMRiP0A9M8. Positions 403-710.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni391 – 714324Phosphate acetyltransferaseAdd
    BLAST

    Domaini

    The N-terminal region seems to be important for proper quaternary structure. The C-terminal region contains the substrate-binding site.1 Publication

    Sequence similaritiesi

    In the N-terminal section; belongs to the CobB/CobQ family.Curated
    In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family.Curated

    Phylogenomic databases

    eggNOGiCOG0280.
    HOGENOMiHOG000053797.
    KOiK13788.
    OMAiKPIAQPH.
    OrthoDBiEOG6BKJ5W.
    PhylomeDBiP0A9M8.

    Family and domain databases

    Gene3Di3.40.1390.20. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR010766. DRTGG.
    IPR016475. P-Actrans_bac.
    IPR027417. P-loop_NTPase.
    IPR004614. P_AcTrfase.
    IPR002505. PTA_PTB.
    IPR028979. Ser_kin/Pase_Hpr_N_like.
    [Graphical view]
    PfamiPF07085. DRTGG. 1 hit.
    PF01515. PTA_PTB. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006107. PhpActrans_proteobac. 1 hit.
    SUPFAMiSSF52540. SSF52540. 1 hit.
    SSF75138. SSF75138. 1 hit.
    TIGRFAMsiTIGR00651. pta. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A9M8-1 [UniParc]FASTAAdd to Basket

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    MSRIIMLIPT GTSVGLTSVS LGVIRAMERK GVRLSVFKPI AQPRTGGDAP    50
    DQTTTIVRAN SSTTTAAEPL KMSYVEGLLS SNQKDVLMEE IVANYHANTK 100
    DAEVVLVEGL VPTRKHQFAQ SLNYEIAKTL NAEIVFVMSQ GTDTPEQLKE 150
    RIELTRNSFG GAKNTNITGV IVNKLNAPVD EQGRTRPDLS EIFDDSSKAK 200
    VNNVDPAKLQ ESSPLPVLGA VPWSFDLIAT RAIDMARHLN ATIINEGDIN 250
    TRRVKSVTFC ARSIPHMLEH FRAGSLLVTS ADRPDVLVAA CLAAMNGVEI 300
    GALLLTGGYE MDARISKLCE RAFATGLPVF MVNTNTWQTS LSLQSFNLEV 350
    PVDDHERIEK VQEYVANYIN ADWIESLTAT SERSRRLSPP AFRYQLTELA 400
    RKAGKRIVLP EGDEPRTVKA AAICAERGIA TCVLLGNPAE INRVAASQGV 450
    ELGAGIEIVD PEVVRESYVG RLVELRKNKG MTETVAREQL EDNVVLGTLM 500
    LEQDEVDGLV SGAVHTTANT IRPPLQLIKT APGSSLVSSV FFMLLPEQVY 550
    VYGDCAINPD PTAEQLAEIA IQSADSAAAF GIEPRVAMLS YSTGTSGAGS 600
    DVEKVREATR LAQEKRPDLM IDGPLQYDAA VMADVAKSKA PNSPVAGRAT 650
    VFIFPDLNTG NTTYKAVQRS ADLISIGPML QGMRKPVNDL SRGALVDDIV 700
    YTIALTAIQS AQQQ 714
    Length:714
    Mass (Da):77,172
    Last modified:January 23, 2007 - v2
    Checksum:iB45AF0C93494A04C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 5031SLGVI…GGDAP → AWRDPCNGTQRRSSERFQTY RSAAYRWRCA in BAA04663. (PubMed:7918659)CuratedAdd
    BLAST
    Sequence conflicti208 – 2092KL → NV in BAA04502. (PubMed:7883769)Curated
    Sequence conflicti208 – 2092KL → NV in BAA04663. (PubMed:7918659)Curated
    Sequence conflicti263 – 2719SIPHMLEHF → QHSAHAGAL in BAA04663. (PubMed:7918659)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D17576 Genomic DNA. Translation: BAA04502.1.
    D21123 Genomic DNA. Translation: BAA04663.1.
    U00096 Genomic DNA. Translation: AAC75357.1.
    AP009048 Genomic DNA. Translation: BAA16136.1.
    PIRiG65001.
    JX0357.
    S50130.
    RefSeqiNP_416800.1. NC_000913.3.
    YP_490539.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75357; AAC75357; b2297.
    BAA16136; BAA16136; BAA16136.
    GeneIDi12932506.
    946778.
    KEGGiecj:Y75_p2263.
    eco:b2297.
    PATRICi32119965. VBIEscCol129921_2392.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D17576 Genomic DNA. Translation: BAA04502.1 .
    D21123 Genomic DNA. Translation: BAA04663.1 .
    U00096 Genomic DNA. Translation: AAC75357.1 .
    AP009048 Genomic DNA. Translation: BAA16136.1 .
    PIRi G65001.
    JX0357.
    S50130.
    RefSeqi NP_416800.1. NC_000913.3.
    YP_490539.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P0A9M8.
    SMRi P0A9M8. Positions 403-710.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35815N.
    IntActi P0A9M8. 27 interactions.
    MINTi MINT-1263208.
    STRINGi 511145.b2297.

    PTM databases

    PhosSitei P0810425.

    2D gel databases

    SWISS-2DPAGE P0A9M8.

    Proteomic databases

    PaxDbi P0A9M8.
    PRIDEi P0A9M8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75357 ; AAC75357 ; b2297 .
    BAA16136 ; BAA16136 ; BAA16136 .
    GeneIDi 12932506.
    946778.
    KEGGi ecj:Y75_p2263.
    eco:b2297.
    PATRICi 32119965. VBIEscCol129921_2392.

    Organism-specific databases

    EchoBASEi EB4147.
    EcoGenei EG20173. pta.

    Phylogenomic databases

    eggNOGi COG0280.
    HOGENOMi HOG000053797.
    KOi K13788.
    OMAi KPIAQPH.
    OrthoDBi EOG6BKJ5W.
    PhylomeDBi P0A9M8.

    Enzyme and pathway databases

    UniPathwayi UPA00340 ; UER00459 .
    BioCyci EcoCyc:PHOSACETYLTRANS-MONOMER.
    ECOL316407:JW2294-MONOMER.
    MetaCyc:PHOSACETYLTRANS-MONOMER.

    Miscellaneous databases

    PROi P0A9M8.

    Gene expression databases

    Genevestigatori P0A9M8.

    Family and domain databases

    Gene3Di 3.40.1390.20. 1 hit.
    3.40.50.300. 1 hit.
    InterProi IPR010766. DRTGG.
    IPR016475. P-Actrans_bac.
    IPR027417. P-loop_NTPase.
    IPR004614. P_AcTrfase.
    IPR002505. PTA_PTB.
    IPR028979. Ser_kin/Pase_Hpr_N_like.
    [Graphical view ]
    Pfami PF07085. DRTGG. 1 hit.
    PF01515. PTA_PTB. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006107. PhpActrans_proteobac. 1 hit.
    SUPFAMi SSF52540. SSF52540. 1 hit.
    SSF75138. SSF75138. 1 hit.
    TIGRFAMsi TIGR00651. pta. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    Entry informationi

    Entry nameiPTA_ECOLI
    AccessioniPrimary (citable) accession number: P0A9M8
    Secondary accession number(s): P39184
    , P78091, P78189, P78190, Q9EUP2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 84 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3