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Protein

Phosphopantetheine adenylyltransferase

Gene

coaD

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.UniRule annotation2 Publications

Catalytic activityi

ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA.UniRule annotation2 Publications

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Regulated by Coenzyme A (CoA) through feedback inhibition.2 Publications

Kineticsi

kcat is 288.5 min(-1) for the reverse reaction, with diphosphate and 3'-dephospho-CoA as substrates, which is nearly identical to that of the forward reaction fitted to the Hill equation. The enzyme seems to utilize a nonrapid-equilibrium random bi-bi mechanism with a preferred pathway to the ternary complex. A sigmoidal response is observed when ATP was varied at different fixed concentrations of pantetheine 4'-phosphate. Also exhibits nonhyperbolic kinetics when pantetheine 4'-phosphate was varied at a fixed saturating concentration of ATP.1 Publication
  1. KM=6.7 µM for 3'-dephospho-CoA1 Publication

    Pathwayi: coenzyme A biosynthesis

    This protein is involved in step 4 of the subpathway that synthesizes CoA from (R)-pantothenate.UniRule annotation
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Pantothenate kinase (coaA), Type III pantothenate kinase (coaX), Pantothenate kinase (coaA), Type III pantothenate kinase (coaX)
    2. Coenzyme A biosynthesis bifunctional protein CoaBC (coaBC)
    3. Coenzyme A biosynthesis bifunctional protein CoaBC (coaBC)
    4. Phosphopantetheine adenylyltransferase (coaD), Phosphopantetheine adenylyltransferase (coaD)
    5. Dephospho-CoA kinase (coaE), Dephospho-CoA kinase (coaE)
    This subpathway is part of the pathway coenzyme A biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes CoA from (R)-pantothenate, the pathway coenzyme A biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei9SubstrateUniRule annotationCombined sources1 Publication1
    Binding sitei17ATPUniRule annotationCombined sources1 Publication1 Publication1
    Sitei17Transition state stabilizerUniRule annotation1
    Binding sitei41SubstrateUniRule annotation1
    Binding sitei73Substrate; via amide nitrogenUniRule annotationCombined sources1 Publication1
    Binding sitei87SubstrateUniRule annotation1
    Binding sitei98ATPUniRule annotationCombined sources1 Publication1
    Binding sitei105SubstrateCombined sources1 Publication1
    Binding sitei118ATPCombined sources1 Publication1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi9 – 10ATPUniRule annotationCombined sources1 Publication1 Publication2
    Nucleotide bindingi88 – 90ATPUniRule annotationCombined sources1 Publication1 Publication3
    Nucleotide bindingi122 – 128ATPUniRule annotationCombined sources1 Publication1 Publication7

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • pantetheine-phosphate adenylyltransferase activity Source: MTBBASE

    GO - Biological processi

    • coenzyme A biosynthetic process Source: MTBBASE
    • protein hexamerization Source: MTBBASE

    Keywordsi

    Molecular functionNucleotidyltransferase, Transferase
    Biological processCoenzyme A biosynthesis
    LigandATP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00241; UER00355.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphopantetheine adenylyltransferase2 PublicationsUniRule annotation (EC:2.7.7.3UniRule annotation2 Publications)
    Alternative name(s):
    Dephospho-CoA pyrophosphorylaseUniRule annotation
    Pantetheine-phosphate adenylyltransferaseUniRule annotation
    Short name:
    PPAT2 PublicationsUniRule annotation
    Gene namesi
    Name:coaDUniRule annotation
    Synonyms:kdtB1 Publication
    Ordered Locus Names:Rv2965c
    ORF Names:MTCY349.22, u0002e
    OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    Taxonomic identifieri83332 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    Proteomesi
    • UP000001584 Componenti: Chromosome

    Organism-specific databases

    TubercuListiRv2965c.

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources
    ChainiPRO_00001562422 – 161Phosphopantetheine adenylyltransferaseAdd BLAST160

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylthreonineCombined sources1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP9WPA5.

    Interactioni

    Subunit structurei

    Homohexamer; dimer of trimers.UniRule annotation1 Publication1 Publication

    Protein-protein interaction databases

    STRINGi83332.Rv2965c.

    Structurei

    Secondary structure

    1161
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 8Combined sources6
    Helixi15 – 27Combined sources13
    Beta strandi28 – 35Combined sources8
    Beta strandi39 – 41Combined sources3
    Helixi47 – 57Combined sources11
    Beta strandi64 – 68Combined sources5
    Helixi73 – 79Combined sources7
    Beta strandi84 – 89Combined sources6
    Helixi95 – 109Combined sources15
    Beta strandi112 – 117Combined sources6
    Helixi120 – 122Combined sources3
    Helixi127 – 135Combined sources9
    Helixi141 – 143Combined sources3
    Helixi146 – 156Combined sources11

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1TFUX-ray1.99A1-157[»]
    3LCJX-ray2.10A1-161[»]
    3NBAX-ray2.68A/B/C/D1-157[»]
    3NBKX-ray1.58A/B/C/D1-157[»]
    3PNBX-ray2.11A/B/C/D1-157[»]
    3RBAX-ray1.59A1-157[»]
    3RFFX-ray1.76A1-157[»]
    3RHSX-ray1.59A1-157[»]
    3UC5X-ray1.70A1-157[»]
    4E1AX-ray1.62A1-161[»]
    4R0NX-ray2.00A/C/E/G/I/K2-157[»]
    ProteinModelPortaliP9WPA5.
    SMRiP9WPA5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the bacterial CoaD family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4108ZEF. Bacteria.
    COG0669. LUCA.
    KOiK00954.
    OMAiEFQMALM.
    PhylomeDBiP9WPA5.

    Family and domain databases

    CDDicd02163. PPAT. 1 hit.
    Gene3Di3.40.50.620. 1 hit.
    HAMAPiMF_00151. PPAT_bact. 1 hit.
    InterProiView protein in InterPro
    IPR004821. Cyt_trans-like.
    IPR001980. PPAT.
    IPR014729. Rossmann-like_a/b/a_fold.
    PfamiView protein in Pfam
    PF01467. CTP_transf_like. 1 hit.
    PRINTSiPR01020. LPSBIOSNTHSS.
    TIGRFAMsiTIGR01510. coaD_prev_kdtB. 1 hit.
    TIGR00125. cyt_tran_rel. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P9WPA5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTGAVCPGSF DPVTLGHVDI FERAAAQFDE VVVAILVNPA KTGMFDLDER
    60 70 80 90 100
    IAMVKESTTH LPNLRVQVGH GLVVDFVRSC GMTAIVKGLR TGTDFEYELQ
    110 120 130 140 150
    MAQMNKHIAG VDTFFVATAP RYSFVSSSLA KEVAMLGGDV SELLPEPVNR
    160
    RLRDRLNTER T
    Length:161
    Mass (Da):17,628
    Last modified:April 16, 2014 - v1
    Checksum:iDE9F12E18D0C1721
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00024 Genomic DNA. Translation: AAA50946.1.
    AL123456 Genomic DNA. Translation: CCP45769.1.
    PIRiB70671.
    RefSeqiNP_217481.1. NC_000962.3.
    WP_003414998.1. NZ_KK339370.1.

    Genome annotation databases

    EnsemblBacteriaiCCP45769; CCP45769; Rv2965c.
    GeneIDi888423.
    KEGGimtu:Rv2965c.

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

    Entry informationi

    Entry nameiCOAD_MYCTU
    AccessioniPrimary (citable) accession number: P9WPA5
    Secondary accession number(s): L0TCR8
    , O08023, P0A530, Q50452
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2014
    Last sequence update: April 16, 2014
    Last modified: July 5, 2017
    This is version 23 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
    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