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Protein

Cyclic pyranopterin monophosphate synthase

Gene

moaC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).UniRule annotation1 Publication

Catalytic activityi

(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate.UniRule annotation1 Publication

Kineticsi

kcat is 0.56 min(-1).1 Publication
  1. KM=0.21 µM for (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate1 Publication

    Pathwayi: molybdopterin biosynthesis

    This protein is involved in the pathway molybdopterin biosynthesis, which is part of Cofactor biosynthesis.UniRule annotation
    View all proteins of this organism that are known to be involved in the pathway molybdopterin biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei128UniRule annotation1

    GO - Molecular functioni

    • cyclic pyranopterin monophosphate synthase activity Source: EcoCyc
    • identical protein binding Source: EcoCyc

    GO - Biological processi

    • Mo-molybdopterin cofactor biosynthetic process Source: EcoCyc
    • protein hexamerization Source: EcoCyc

    Keywordsi

    Molecular functionLyase
    Biological processMolybdenum cofactor biosynthesis

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11666-MONOMER.
    MetaCyc:EG11666-MONOMER.
    UniPathwayiUPA00344.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclic pyranopterin monophosphate synthaseUniRule annotationCurated (EC:4.6.1.17UniRule annotation1 Publication)
    Alternative name(s):
    Molybdenum cofactor biosynthesis protein CUniRule annotation
    Gene namesi
    Name:moaC
    Synonyms:chlA3
    Ordered Locus Names:b0783, JW0766
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11666. moaC.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi17D → A: Loss of activity by 70%. 1 Publication1
    Mutagenesisi21K → A: Loss of activity by 85%. 1 Publication1
    Mutagenesisi26R → A: Loss of activity by 80%. 1 Publication1
    Mutagenesisi51K → A: Complete loss of activity. 1 Publication1
    Mutagenesisi52G → A: Reduced activity. 1 Publication1
    Mutagenesisi67K → A: Reduced activity. 1 Publication1
    Mutagenesisi76C → A: Reduced activity. 1 Publication1
    Mutagenesisi77H → A: Complete loss of activity. 1 Publication1
    Mutagenesisi112E → A: Complete loss of activity. 1 Publication1
    Mutagenesisi114E → A: Loss of activity. 1 Publication1
    Mutagenesisi128D → A: Complete loss of activity. 1 Publication1
    Mutagenesisi131K → A: Complete loss of activity. 1 Publication1
    Mutagenesisi147K → A: Loss of activity by 90%. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00000977982 – 161Cyclic pyranopterin monophosphate synthaseAdd BLAST160

    Proteomic databases

    PaxDbiP0A738.
    PRIDEiP0A738.

    Expressioni

    Inductioni

    By anaerobiosis, repressed by the molybdenum cofactor.

    Interactioni

    Subunit structurei

    Homohexamer; trimer of dimers.UniRule annotation1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    rplAP0A7L02EBI-554314,EBI-543771

    GO - Molecular functioni

    • identical protein binding Source: EcoCyc

    Protein-protein interaction databases

    BioGridi4262176. 8 interactors.
    DIPiDIP-10230N.
    IntActiP0A738. 20 interactors.
    MINTiMINT-1231800.
    STRINGi316385.ECDH10B_0851.

    Structurei

    Secondary structure

    1161
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi19 – 21Combined sources3
    Beta strandi24 – 35Combined sources12
    Helixi38 – 46Combined sources9
    Turni47 – 49Combined sources3
    Beta strandi50 – 52Combined sources3
    Helixi54 – 67Combined sources14
    Helixi69 – 72Combined sources4
    Beta strandi82 – 91Combined sources10
    Helixi92 – 94Combined sources3
    Beta strandi96 – 109Combined sources14
    Helixi112 – 130Combined sources19
    Turni131 – 133Combined sources3
    Beta strandi138 – 145Combined sources8

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1EKRX-ray2.00A1-161[»]
    1EKSX-ray2.50A1-161[»]
    4PYAX-ray1.79A3-161[»]
    4PYDX-ray3.19A/B/C/D/E/F1-161[»]
    ProteinModelPortaliP0A738.
    SMRiP0A738.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A738.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni75 – 77Substrate bindingUniRule annotation1 Publication3
    Regioni113 – 114Substrate bindingUniRule annotation1 Publication2

    Sequence similaritiesi

    Belongs to the MoaC family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4108YXW. Bacteria.
    COG0315. LUCA.
    HOGENOMiHOG000228417.
    InParanoidiP0A738.
    KOiK03637.
    PhylomeDBiP0A738.

    Family and domain databases

    CDDicd01420. MoaC_PE. 1 hit.
    Gene3Di3.30.70.640. 1 hit.
    HAMAPiMF_01224_B. MoaC_B. 1 hit.
    InterProiView protein in InterPro
    IPR023045. Mo_CF_biosynth-C.
    IPR036522. MoaC_sf.
    IPR002820. Mopterin_CF_biosynth-C_dom.
    PfamiView protein in Pfam
    PF01967. MoaC. 1 hit.
    SUPFAMiSSF55040. SSF55040. 1 hit.
    TIGRFAMsiTIGR00581. moaC. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P0A738-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSQLTHINAA GEAHMVDVSA KAETVREARA EAFVTMRSET LAMIIDGRHH
    60 70 80 90 100
    KGDVFATARI AGIQAAKRTW DLIPLCHPLM LSKVEVNLQA EPEHNRVRIE
    110 120 130 140 150
    TLCRLTGKTG VEMEALTAAS VAALTIYDMC KAVQKDMVIG PVRLLAKSGG
    160
    KSGDFKVEAD D
    Length:161
    Mass (Da):17,467
    Last modified:January 23, 2007 - v2
    Checksum:i280DAC1EFAAA04AD
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti17D → N in CAA49863 (PubMed:8361352).Curated1
    Sequence conflicti92 – 97PEHNRV → RAQSG in CAA49863 (PubMed:8361352).Curated6

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X70420 Genomic DNA. Translation: CAA49863.1.
    U00096 Genomic DNA. Translation: AAC73870.1.
    AP009048 Genomic DNA. Translation: BAA35441.1.
    PIRiG64814.
    RefSeqiNP_415304.1. NC_000913.3.
    WP_000080885.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73870; AAC73870; b0783.
    BAA35441; BAA35441; BAA35441.
    GeneIDi945397.
    KEGGiecj:JW0766.
    eco:b0783.
    PATRICifig|1411691.4.peg.1495.

    Similar proteinsi

    Entry informationi

    Entry nameiMOAC_ECOLI
    AccessioniPrimary (citable) accession number: P0A738
    Secondary accession number(s): P30747, P77530
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: January 23, 2007
    Last modified: October 25, 2017
    This is version 112 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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