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Protein

Molybdenum cofactor cytidylyltransferase

Gene

mocA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 can not 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)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi101 – 1011MagnesiumBy similarity

    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
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Molybdenum cofactor biosynthesis

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:G7496-MONOMER.
    ECOL316407:JW2845-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 113TAA → 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 Publication
    Mutagenesisi79 – 824LLTS → 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 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 192192Molybdenum cofactor cytidylyltransferasePRO_0000169355Add
    BLAST

    Proteomic databases

    PaxDbiQ46810.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi4259705. 99 interactions.
    IntActiQ46810. 2 interactions.
    STRINGi511145.b2877.

    Structurei

    3D structure databases

    ProteinModelPortaliQ46810.
    SMRiQ46810. Positions 4-138.
    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.
    OMAiEYCFLTH.
    OrthoDBiEOG689HR0.
    PhylomeDBiQ46810.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR017696. Mo_hydrolase_YgfJ.
    IPR025877. MobA-like_NTP_Trfase.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    PfamiPF12804. NTP_transf_3. 1 hit.
    [Graphical view]
    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.
    PATRICi32121164. VBIEscCol129921_2970.

    Cross-referencesi

    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.

    3D structure databases

    ProteinModelPortaliQ46810.
    SMRiQ46810. Positions 4-138.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259705. 99 interactions.
    IntActiQ46810. 2 interactions.
    STRINGi511145.b2877.

    Proteomic databases

    PaxDbiQ46810.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75915; AAC75915; b2877.
    BAE76943; BAE76943; BAE76943.
    GeneIDi947356.
    KEGGiecj:JW2845.
    eco:b2877.
    PATRICi32121164. VBIEscCol129921_2970.

    Organism-specific databases

    EchoBASEiEB2872.
    EcoGeneiEG13060. mocA.

    Phylogenomic databases

    eggNOGiENOG4105MFX. Bacteria.
    COG2068. LUCA.
    HOGENOMiHOG000280424.
    InParanoidiQ46810.
    KOiK07141.
    OMAiEYCFLTH.
    OrthoDBiEOG689HR0.
    PhylomeDBiQ46810.

    Enzyme and pathway databases

    BioCyciEcoCyc:G7496-MONOMER.
    ECOL316407:JW2845-MONOMER.
    MetaCyc:G7496-MONOMER.

    Miscellaneous databases

    PROiQ46810.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR017696. Mo_hydrolase_YgfJ.
    IPR025877. MobA-like_NTP_Trfase.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    PfamiPF12804. NTP_transf_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF53448. SSF53448. 1 hit.
    TIGRFAMsiTIGR03310. matur_MocA_YgfJ. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. "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.
    3. "MocA is a specific cytidylyltransferase involved in molybdopterin cytosine dinucleotide biosynthesis in Escherichia coli."
      Neumann M., Mittelstadt G., Seduk F., Iobbi-Nivol C., Leimkuhler S.
      J. Biol. Chem. 284:21891-21898(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, GENE NAME, SUBUNIT, DISRUPTION PHENOTYPE.
    4. "Molybdopterin dinucleotide biosynthesis in Escherichia coli: identification of amino acid residues of molybdopterin dinucleotide transferases that determine specificity for binding of guanine or cytosine nucleotides."
      Neumann M., Seduk F., Iobbi-Nivol C., Leimkuhler S.
      J. Biol. Chem. 286:1400-1408(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, INTERACTION WITH PAOD, MUTAGENESIS OF 9-THR--ALA-11 AND 79-LEU--SER-82.

    Entry informationi

    Entry nameiMOCA_ECOLI
    AccessioniPrimary (citable) accession number: Q46810
    Secondary accession number(s): Q2M9W3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: January 20, 2016
    This is version 96 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene

    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.