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Protein

Molybdenum cofactor guanylyltransferase

Gene

mobA

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

Functioni

Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor. Is also involved in the biosynthesis of the bis-MGD form of the Moco cofactor (Mo-bisMGD) in which the metal is symmetrically ligated by the dithiolene groups of two MGD molecules. Is necessary and sufficient for the in vitro activation of the DMSOR molybdoenzyme that uses the Mo-bisMGD form of molybdenum cofactor, which implies formation and efficient insertion of the cofactor into the enzyme without the need of a chaperone. Is specific for GTP since other nucleotides such as ATP and GMP cannot be utilized.4 Publications

Catalytic activityi

GTP + molybdenum cofactor = diphosphate + guanylyl molybdenum cofactor.2 Publications

Cofactori

Mg2+2 Publications, Mn2+2 PublicationsNote: Both divalent cations appear to be equally efficient in an vitro reconstitution assay.2 Publications

Kineticsi

  1. KM=6.5 µM for GTP1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei25GTP1
    Binding sitei53GTP1
    Binding sitei71GTP1
    Metal bindingi101Magnesium1
    Binding sitei101GTP1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi12 – 14GTP3

    GO - Molecular functioni

    • GTP binding Source: UniProtKB-HAMAP
    • magnesium ion binding Source: EcoCyc
    • molybdenum cofactor guanylyltransferase activity Source: EcoCyc

    GO - Biological processi

    • bis(molybdopterin guanine dinucleotide)molybdenum biosynthetic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Molybdenum cofactor biosynthesis

    Keywords - Ligandi

    GTP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11829-MONOMER.
    ECOL316407:JW3829-MONOMER.
    MetaCyc:EG11829-MONOMER.
    BRENDAi2.7.7.77. 2026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Molybdenum cofactor guanylyltransferase (EC:2.7.7.77)
    Short name:
    MoCo guanylyltransferase
    Alternative name(s):
    GTP:molybdopterin guanylyltransferase
    Mo-MPT guanylyltransferase
    Molybdopterin guanylyltransferase
    Molybdopterin-guanine dinucleotide biosynthesis protein A
    Molybdopterin-guanine dinucleotide synthase
    Short name:
    MGD synthase
    Protein FA
    Gene namesi
    Name:mobA
    Synonyms:chlB, mob, narB
    Ordered Locus Names:b3857, JW3829
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11829. mobA.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene are chlorate-resistant, fail to synthesize MGD and accumulate elevated quantities of MPT.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi12 – 14LAG → TAA: 7.5-fold decrease in affinity for GTP and nearly no effect on catalytic activity. Displays a 3-fold decrease in activity with GTP and gains a low activity with CTP as substrate; when associated with 79-LLTS-82. 1 Publication3
    Mutagenesisi15G → L: Complete loss of catalytic activity. Still capable of binding MPT and MGD and interacting with both MoeA and MobB. 1 Publication1
    Mutagenesisi19R → A: Slight reduction in catalytic activity. 1 Publication1
    Mutagenesisi22G → L: Nearly no effect on catalytic activity. 1 Publication1
    Mutagenesisi25K → A: Marked reduction in catalytic activity. Still capable of interacting with both MoeA and MobB. 1 Publication1
    Mutagenesisi78G → L: Nearly no effect on catalytic activity. 1 Publication1
    Mutagenesisi79 – 82PLAG → LLTS: 11-fold decrease in affinity for GTP and nearly no effect on catalytic activity. Displays a 3-fold decrease in activity with GTP and gains a low activity with CTP as substrate; when associated with 12-TAA-14. 1 Publication4
    Mutagenesisi82G → L: Slight reduction in catalytic activity. 1 Publication1
    Mutagenesisi101D → A: Complete loss of catalytic activity. 1 Publication1
    Mutagenesisi101D → N: Marked reduction in catalytic activity. Still capable of interacting with both MoeA and MobB. 1 Publication1
    Mutagenesisi156R → A: Nearly no effect on catalytic activity. 1 Publication1
    Mutagenesisi180N → D: Nearly no effect on catalytic activity. 1 Publication1
    Mutagenesisi182N → D: Nearly no effect on catalytic activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001348871 – 194Molybdenum cofactor guanylyltransferaseAdd BLAST194

    Proteomic databases

    PaxDbiP32173.
    PRIDEiP32173.

    Expressioni

    Inductioni

    Is expressed at very low levels under both aerobic and anaerobic growth conditions.1 Publication

    Interactioni

    Subunit structurei

    Monomer. An equilibrium exists between a monomeric and oligomeric form of the enzyme, which could be an octamer; whether this oligomeric arrangement is of functional relevance is unclear. Interacts with MoeA and MobB in vivo.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    moeAP122813EBI-1133881,EBI-554393

    Protein-protein interaction databases

    DIPiDIP-10233N.
    IntActiP32173. 10 interactors.
    MINTiMINT-1232345.
    STRINGi511145.b3857.

    Structurei

    Secondary structure

    1194
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi3 – 5Combined sources3
    Beta strandi6 – 12Combined sources7
    Beta strandi18 – 20Combined sources3
    Helixi25 – 27Combined sources3
    Beta strandi28 – 30Combined sources3
    Helixi35 – 46Combined sources12
    Beta strandi50 – 53Combined sources4
    Beta strandi55 – 57Combined sources3
    Helixi58 – 62Combined sources5
    Beta strandi67 – 69Combined sources3
    Helixi79 – 89Combined sources11
    Beta strandi92 – 99Combined sources8
    Helixi109 – 115Combined sources7
    Turni116 – 119Combined sources4
    Beta strandi121 – 126Combined sources6
    Beta strandi131 – 139Combined sources9
    Helixi142 – 151Combined sources10
    Helixi157 – 163Combined sources7
    Beta strandi167 – 170Combined sources4
    Turni175 – 178Combined sources4
    Helixi184 – 188Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1E5KX-ray1.35A1-194[»]
    1FR9X-ray1.65A1-194[»]
    1FRWX-ray1.75A1-194[»]
    1H4CX-ray1.65A1-194[»]
    1H4DX-ray1.74A1-194[»]
    1H4EX-ray1.65A1-194[»]
    1HJJX-ray1.65A1-194[»]
    1HJLX-ray2.00A1-194[»]
    ProteinModelPortaliP32173.
    SMRiP32173.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32173.

    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

    Sequence similaritiesi

    Belongs to the MobA family.Curated

    Phylogenomic databases

    eggNOGiENOG4105C6R. Bacteria.
    COG0746. LUCA.
    HOGENOMiHOG000280423.
    InParanoidiP32173.
    KOiK03752.
    OMAiDELPDFQ.
    PhylomeDBiP32173.

    Family and domain databases

    CDDicd02503. MobA. 1 hit.
    Gene3Di3.90.550.10. 1 hit.
    HAMAPiMF_00316. MobA. 1 hit.
    InterProiIPR025877. MobA-like_NTP_Trfase.
    IPR013482. Molybde_CF_guanTrfase.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    PfamiPF12804. NTP_transf_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF53448. SSF53448. 1 hit.
    TIGRFAMsiTIGR02665. molyb_mobA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P32173-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNLMTTITGV VLAGGKARRM GGVDKGLLEL NGKPLWQHVA DALMTQLSHV
    60 70 80 90 100
    VVNANRHQEI YQASGLKVIE DSLADYPGPL AGMLSVMQQE AGEWFLFCPC
    110 120 130 140 150
    DTPYIPPDLA ARLNHQRKDA PVVWVHDGER DHPTIALVNR AIEPLLLEYL
    160 170 180 190
    QAGERRVMVF MRLAGGHAVD FSDHKDAFVN VNTPEELARW QEKR
    Length:194
    Mass (Da):21,643
    Last modified:October 1, 1993 - v1
    Checksum:iB79B32DD7348DD48
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L19201 Genomic DNA. Translation: AAB02992.1.
    U00096 Genomic DNA. Translation: AAC76855.1.
    AP009048 Genomic DNA. Translation: BAE77451.1.
    PIRiS40803.
    RefSeqiNP_418294.1. NC_000913.3.
    WP_001052181.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76855; AAC76855; b3857.
    BAE77451; BAE77451; BAE77451.
    GeneIDi948349.
    KEGGiecj:JW3829.
    eco:b3857.
    PATRICi32123211. VBIEscCol129921_3966.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L19201 Genomic DNA. Translation: AAB02992.1.
    U00096 Genomic DNA. Translation: AAC76855.1.
    AP009048 Genomic DNA. Translation: BAE77451.1.
    PIRiS40803.
    RefSeqiNP_418294.1. NC_000913.3.
    WP_001052181.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1E5KX-ray1.35A1-194[»]
    1FR9X-ray1.65A1-194[»]
    1FRWX-ray1.75A1-194[»]
    1H4CX-ray1.65A1-194[»]
    1H4DX-ray1.74A1-194[»]
    1H4EX-ray1.65A1-194[»]
    1HJJX-ray1.65A1-194[»]
    1HJLX-ray2.00A1-194[»]
    ProteinModelPortaliP32173.
    SMRiP32173.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-10233N.
    IntActiP32173. 10 interactors.
    MINTiMINT-1232345.
    STRINGi511145.b3857.

    Proteomic databases

    PaxDbiP32173.
    PRIDEiP32173.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76855; AAC76855; b3857.
    BAE77451; BAE77451; BAE77451.
    GeneIDi948349.
    KEGGiecj:JW3829.
    eco:b3857.
    PATRICi32123211. VBIEscCol129921_3966.

    Organism-specific databases

    EchoBASEiEB1776.
    EcoGeneiEG11829. mobA.

    Phylogenomic databases

    eggNOGiENOG4105C6R. Bacteria.
    COG0746. LUCA.
    HOGENOMiHOG000280423.
    InParanoidiP32173.
    KOiK03752.
    OMAiDELPDFQ.
    PhylomeDBiP32173.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11829-MONOMER.
    ECOL316407:JW3829-MONOMER.
    MetaCyc:EG11829-MONOMER.
    BRENDAi2.7.7.77. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP32173.
    PROiP32173.

    Family and domain databases

    CDDicd02503. MobA. 1 hit.
    Gene3Di3.90.550.10. 1 hit.
    HAMAPiMF_00316. MobA. 1 hit.
    InterProiIPR025877. MobA-like_NTP_Trfase.
    IPR013482. Molybde_CF_guanTrfase.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    PfamiPF12804. NTP_transf_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF53448. SSF53448. 1 hit.
    TIGRFAMsiTIGR02665. molyb_mobA. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMOBA_ECOLI
    AccessioniPrimary (citable) accession number: P32173
    Secondary accession number(s): Q2M8F5, Q9LBV0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: November 2, 2016
    This is version 139 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    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.