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P0A6I6

- COAD_ECOLI

UniProt

P0A6I6 - COAD_ECOLI

Protein

Phosphopantetheine adenylyltransferase

Gene

coaD

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (29 Mar 2005)
      Previous versions | rss
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    Functioni

    Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.

    Catalytic activityi

    ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA.UniRule annotation

    Pathwayi

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. pantetheine-phosphate adenylyltransferase activity Source: EcoCyc

    GO - Biological processi

    1. coenzyme A biosynthetic process Source: EcoCyc

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Coenzyme A biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PANTEPADENYLYLTRAN-MONOMER.
    ECOL316407:JW3609-MONOMER.
    MetaCyc:PANTEPADENYLYLTRAN-MONOMER.
    SABIO-RKP0A6I6.
    UniPathwayiUPA00241; UER00355.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphopantetheine adenylyltransferaseUniRule annotation (EC:2.7.7.3UniRule annotation)
    Alternative name(s):
    Dephospho-CoA pyrophosphorylaseUniRule annotation
    Pantetheine-phosphate adenylyltransferaseUniRule annotation
    Short name:
    PPATUniRule annotation
    Gene namesi
    Name:coaDUniRule annotation
    Synonyms:kdtB, yicA
    Ordered Locus Names:b3634, JW3609
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11190. coaD.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 159159Phosphopantetheine adenylyltransferasePRO_0000156204Add
    BLAST

    Expressioni

    Gene expression databases

    GenevestigatoriP0A6I6.

    Interactioni

    Subunit structurei

    Homohexamer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    rplDP607231EBI-553173,EBI-545597

    Protein-protein interaction databases

    DIPiDIP-35966N.
    IntActiP0A6I6. 10 interactions.
    STRINGi511145.b3634.

    Structurei

    Secondary structure

    1
    159
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 96
    Helixi16 – 2611
    Beta strandi29 – 3810
    Helixi48 – 5811
    Turni59 – 613
    Beta strandi65 – 706
    Helixi74 – 807
    Beta strandi85 – 895
    Helixi96 – 10914
    Beta strandi113 – 1186
    Helixi122 – 1243
    Helixi129 – 1379
    Helixi143 – 1453
    Helixi148 – 15811

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B6TX-ray1.80A/B1-159[»]
    1GN8X-ray1.83A/B1-159[»]
    1H1TX-ray1.78A/B1-159[»]
    1QJCX-ray1.64A/B2-159[»]
    ProteinModelPortaliP0A6I6.
    SMRiP0A6I6. Positions 3-159.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6I6.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the bacterial CoaD family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0669.
    HOGENOMiHOG000006518.
    KOiK00954.
    OMAiTMDFEYE.
    OrthoDBiEOG6MH5J7.
    PhylomeDBiP0A6I6.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    HAMAPiMF_00151. PPAT_bact.
    InterProiIPR004821. Cyt_trans-like.
    IPR001980. LPS_biosynth.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PfamiPF01467. CTP_transf_2. 1 hit.
    [Graphical view]
    PRINTSiPR01020. LPSBIOSNTHSS.
    TIGRFAMsiTIGR01510. coaD_prev_kdtB. 1 hit.
    TIGR00125. cyt_tran_rel. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0A6I6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQKRAIYPGT FDPITNGHID IVTRATQMFD HVILAIAASP SKKPMFTLEE    50
    RVALAQQATA HLGNVEVVGF SDLMANFARN QHATVLIRGL RAVADFEYEM 100
    QLAHMNRHLM PELESVFLMP SKEWSFISSS LVKEVARHQG DVTHFLPENV 150
    HQALMAKLA 159
    Length:159
    Mass (Da):17,837
    Last modified:March 29, 2005 - v1
    Checksum:iC4D7B8715A061B91
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60670 Genomic DNA. Translation: AAA24044.1.
    M86305 Genomic DNA. Translation: AAA03746.1.
    U00039 Genomic DNA. Translation: AAB18611.1.
    U00096 Genomic DNA. Translation: AAC76658.1.
    AP009048 Genomic DNA. Translation: BAE77658.1.
    PIRiJU0468.
    RefSeqiNP_418091.1. NC_000913.3.
    YP_491799.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76658; AAC76658; b3634.
    BAE77658; BAE77658; BAE77658.
    GeneIDi12934385.
    947386.
    KEGGiecj:Y75_p3540.
    eco:b3634.
    PATRICi32122755. VBIEscCol129921_3754.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60670 Genomic DNA. Translation: AAA24044.1 .
    M86305 Genomic DNA. Translation: AAA03746.1 .
    U00039 Genomic DNA. Translation: AAB18611.1 .
    U00096 Genomic DNA. Translation: AAC76658.1 .
    AP009048 Genomic DNA. Translation: BAE77658.1 .
    PIRi JU0468.
    RefSeqi NP_418091.1. NC_000913.3.
    YP_491799.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B6T X-ray 1.80 A/B 1-159 [» ]
    1GN8 X-ray 1.83 A/B 1-159 [» ]
    1H1T X-ray 1.78 A/B 1-159 [» ]
    1QJC X-ray 1.64 A/B 2-159 [» ]
    ProteinModelPortali P0A6I6.
    SMRi P0A6I6. Positions 3-159.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35966N.
    IntActi P0A6I6. 10 interactions.
    STRINGi 511145.b3634.

    Chemistry

    BindingDBi P0A6I6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76658 ; AAC76658 ; b3634 .
    BAE77658 ; BAE77658 ; BAE77658 .
    GeneIDi 12934385.
    947386.
    KEGGi ecj:Y75_p3540.
    eco:b3634.
    PATRICi 32122755. VBIEscCol129921_3754.

    Organism-specific databases

    EchoBASEi EB1176.
    EcoGenei EG11190. coaD.

    Phylogenomic databases

    eggNOGi COG0669.
    HOGENOMi HOG000006518.
    KOi K00954.
    OMAi TMDFEYE.
    OrthoDBi EOG6MH5J7.
    PhylomeDBi P0A6I6.

    Enzyme and pathway databases

    UniPathwayi UPA00241 ; UER00355 .
    BioCyci EcoCyc:PANTEPADENYLYLTRAN-MONOMER.
    ECOL316407:JW3609-MONOMER.
    MetaCyc:PANTEPADENYLYLTRAN-MONOMER.
    SABIO-RK P0A6I6.

    Miscellaneous databases

    EvolutionaryTracei P0A6I6.
    PROi P0A6I6.

    Gene expression databases

    Genevestigatori P0A6I6.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    HAMAPi MF_00151. PPAT_bact.
    InterProi IPR004821. Cyt_trans-like.
    IPR001980. LPS_biosynth.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    Pfami PF01467. CTP_transf_2. 1 hit.
    [Graphical view ]
    PRINTSi PR01020. LPSBIOSNTHSS.
    TIGRFAMsi TIGR01510. coaD_prev_kdtB. 1 hit.
    TIGR00125. cyt_tran_rel. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "A gene coding for 3-deoxy-D-manno-octulosonic-acid transferase in Escherichia coli. Identification, mapping, cloning, and sequencing."
      Clementz T., Raetz C.R.H.
      J. Biol. Chem. 266:9687-9696(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
      Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
      Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "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.
    5. "Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli."
      Geerlof A., Lewendon A., Shaw W.V.
      J. Biol. Chem. 274:27105-27111(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-10, CHARACTERIZATION.
    6. "Genetic analysis of the genes involved in synthesis of the lipopolysaccharide core in Escherichia coli K-12: three operons in the rfa locus."
      Roncero C., Casadaban M.J.
      J. Bacteriol. 174:3250-3260(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENETIC CHARACTERIZATION.
      Strain: K12.
    7. "The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivity."
      Izard T., Geerlof A.
      EMBO J. 18:2021-2030(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    8. "The crystal structures of phosphopantetheine adenylyltransferase with bound substrates reveal the enzyme's catalytic mechanism."
      Izard T.
      J. Mol. Biol. 315:487-495(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS).

    Entry informationi

    Entry nameiCOAD_ECOLI
    AccessioniPrimary (citable) accession number: P0A6I6
    Secondary accession number(s): P23875, Q2M7U8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: March 29, 2005
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally thought to have an essential function in lipopolysaccharides biosynthesis.Curated

    Keywords - Technical termi

    3D-structure, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3