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Protein

Molybdenum cofactor cytidylyltransferase

Gene

mocA

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

Functioni

Transfers a CMP moiety from CTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin cytosine dinucleotide (Mo-MCD) cofactor. Is specific for CTP; other nucleotides such as ATP and GTP cannot be utilized. Is also able to convert MPT to MCD in the absence of molybdate, however, with only one catalytic turnover.1 Publication

Catalytic activityi

CTP + molybdenum cofactor = diphosphate + cytidylyl molybdenum cofactor.1 Publication

Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Mg2+ is essential for activity. However, Mn2+ is able to functionally replace Mg2+ with a 50% reduced efficiency, whereas no MCD is produced with other divalent cations like Co2+ or Ni2+.1 Publication

Kineticsi

  1. KM=3.4 µM for CTP1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi101MagnesiumBy similarity1

    GO - Molecular functioni

    • magnesium ion binding Source: EcoCyc
    • molybdenum cofactor cytidylyltransferase activity Source: EcoCyc
    • nucleotide binding Source: UniProtKB-KW

    GO - Biological processi

    • Mo(VI)-molybdopterin cytosine dinucleotide biosynthetic process Source: EcoCyc
    • Mo-molybdopterin cofactor biosynthetic process Source: EcoCyc

    Keywordsi

    Molecular functionTransferase
    Biological processMolybdenum cofactor biosynthesis
    LigandMagnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:G7496-MONOMER
    MetaCyc:G7496-MONOMER

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Molybdenum cofactor cytidylyltransferase (EC:2.7.7.76)
    Short name:
    MoCo cytidylyltransferase
    Alternative name(s):
    CTP:molybdopterin cytidylyltransferase
    Mo-MPT cytidylyltransferase
    Molybdopterin cytidylyltransferase
    Molybdopterin-cytosine dinucleotide synthase
    Short name:
    MCD synthase
    Gene namesi
    Name:mocA
    Synonyms:ygfJ
    Ordered Locus Names:b2877, JW2845
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13060 mocA

    Pathology & Biotechi

    Disruption phenotypei

    A disruption in the mocA gene impairs MCD biosynthesis in E.coli, resulting in an inactive PaoABC aldehyde oxidoreductase devoid of MCD cofactor.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi9 – 11TAA → LAG: 12-fold decrease in affinity for CTP and 3-fold decrease in catalytic activity. Displays a 3-fold decrease in activity with CTP and gains a low activity with GTP as substrate; when associated with 79-P--G-82. 1 Publication3
    Mutagenesisi79 – 82LLTS → PLAG: 15-fold decrease in affinity for CTP and 1.5-fold decrease in catalytic activity. Displays a 3-fold decrease in activity with CTP and gains a low activity with GTP as substrate; when associated with 9-L--G-11. 1 Publication4

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001693551 – 192Molybdenum cofactor cytidylyltransferaseAdd BLAST192

    Proteomic databases

    PaxDbiQ46810
    PRIDEiQ46810

    Interactioni

    Subunit structurei

    Monomer. Interacts with the Moco-binding chaperone PaoD.2 Publications

    Protein-protein interaction databases

    BioGridi4259705, 103 interactors
    IntActiQ46810, 2 interactors
    STRINGi316385.ECDH10B_3052

    Structurei

    3D structure databases

    ProteinModelPortaliQ46810
    SMRiQ46810
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein. When the N-terminal domain of MobA is fused to the C-terminal domain of MocA, comparable kinetic constants as wild-type MobA are obtained with GTP, and the activity with CTP is completely lost. Consistent results are obtained when the N-terminal domain of MocA is fused to the C-terminal domain of MobA: the kinetic constants with CTP are comparable with the ones found for wild-type MocA, although no activity with GTP is detected.1 Publication

    Phylogenomic databases

    eggNOGiENOG4105MFX Bacteria
    COG2068 LUCA
    HOGENOMiHOG000280424
    InParanoidiQ46810
    KOiK07141
    OMAiTEYCFLT
    PhylomeDBiQ46810

    Family and domain databases

    Gene3Di3.90.550.10, 1 hit
    InterProiView protein in InterPro
    IPR017696 Mo_hydrolase_YgfJ
    IPR025877 MobA-like_NTP_Trfase
    IPR029044 Nucleotide-diphossugar_trans
    PfamiView protein in Pfam
    PF12804 NTP_transf_3, 1 hit
    SUPFAMiSSF53448 SSF53448, 1 hit
    TIGRFAMsiTIGR03310 matur_MocA_YgfJ, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Q46810-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSAIDCIITA AGLSSRMGQW KMMLPWEQGT ILDTSIKNAL QFCSRIILVT
    60 70 80 90 100
    GYRGNELHER YANQSNITII HNPDYAQGLL TSVKAAVPAV QTEHCFLTHG
    110 120 130 140 150
    DMPTLTIDIF RKIWSLRNDG AILPLHNGIP GHPILVSKPC LMQAIQRPNV
    160 170 180 190
    TNMRQALLMG DHYSVEIENA EIILDIDTPD DFITAKERYT EI
    Length:192
    Mass (Da):21,514
    Last modified:November 1, 1996 - v1
    Checksum:i5F8E4CDE6133ECD6
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U28375 Genomic DNA Translation: AAA83058.1
    U00096 Genomic DNA Translation: AAC75915.1
    AP009048 Genomic DNA Translation: BAE76943.1
    PIRiE65071
    RefSeqiNP_417353.1, NC_000913.3
    WP_001272828.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC75915; AAC75915; b2877
    BAE76943; BAE76943; BAE76943
    GeneIDi947356
    KEGGiecj:JW2845
    eco:b2877
    PATRICifig|1411691.4.peg.3857

    Entry informationi

    Entry nameiMOCA_ECOLI
    AccessioniPrimary (citable) accession number: Q46810
    Secondary accession number(s): Q2M9W3
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: March 28, 2018
    This is version 105 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

    Complete proteome, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health