Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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 can not 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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei25 – 251GTP
    Binding sitei53 – 531GTP
    Binding sitei71 – 711GTP
    Metal bindingi101 – 1011Magnesium
    Binding sitei101 – 1011GTP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 143GTP

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi12 – 143LAG → 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 Publication
    Mutagenesisi15 – 151G → L: Complete loss of catalytic activity. Still capable of binding MPT and MGD and interacting with both MoeA and MobB. 1 Publication
    Mutagenesisi19 – 191R → A: Slight reduction in catalytic activity. 1 Publication
    Mutagenesisi22 – 221G → L: Nearly no effect on catalytic activity. 1 Publication
    Mutagenesisi25 – 251K → A: Marked reduction in catalytic activity. Still capable of interacting with both MoeA and MobB. 1 Publication
    Mutagenesisi78 – 781G → L: Nearly no effect on catalytic activity. 1 Publication
    Mutagenesisi79 – 824PLAG → 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 Publication
    Mutagenesisi82 – 821G → L: Slight reduction in catalytic activity. 1 Publication
    Mutagenesisi101 – 1011D → A: Complete loss of catalytic activity. 1 Publication
    Mutagenesisi101 – 1011D → N: Marked reduction in catalytic activity. Still capable of interacting with both MoeA and MobB. 1 Publication
    Mutagenesisi156 – 1561R → A: Nearly no effect on catalytic activity. 1 Publication
    Mutagenesisi180 – 1801N → D: Nearly no effect on catalytic activity. 1 Publication
    Mutagenesisi182 – 1821N → D: Nearly no effect on catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 194194Molybdenum cofactor guanylyltransferasePRO_0000134887Add
    BLAST

    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 interactions.
    MINTiMINT-1232345.
    STRINGi511145.b3857.

    Structurei

    Secondary structure

    1
    194
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 53Combined sources
    Beta strandi6 – 127Combined sources
    Beta strandi18 – 203Combined sources
    Helixi25 – 273Combined sources
    Beta strandi28 – 303Combined sources
    Helixi35 – 4612Combined sources
    Beta strandi50 – 534Combined sources
    Beta strandi55 – 573Combined sources
    Helixi58 – 625Combined sources
    Beta strandi67 – 693Combined sources
    Helixi79 – 8911Combined sources
    Beta strandi92 – 998Combined sources
    Helixi109 – 1157Combined sources
    Turni116 – 1194Combined sources
    Beta strandi121 – 1266Combined sources
    Beta strandi131 – 1399Combined sources
    Helixi142 – 15110Combined sources
    Helixi157 – 1637Combined sources
    Beta strandi167 – 1704Combined sources
    Turni175 – 1784Combined sources
    Helixi184 – 1885Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 4-191.
    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

    eggNOGiCOG0746.
    HOGENOMiHOG000280423.
    InParanoidiP32173.
    KOiK03752.
    OMAiQISINAN.
    OrthoDBiEOG6PKFG0.
    PhylomeDBiP32173.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    HAMAPiMF_00316. MobA.
    InterProiIPR025877. MobA-like_NTP_Trfase_dom.
    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.

    Genome annotation databases

    EnsemblBacteriaiAAC76855; AAC76855; b3857.
    BAE77451; BAE77451; BAE77451.
    GeneIDi948349.
    KEGGiecj:Y75_p3328.
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 4-191.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-10233N.
    IntActiP32173. 10 interactions.
    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:Y75_p3328.
    eco:b3857.
    PATRICi32123211. VBIEscCol129921_3966.

    Organism-specific databases

    EchoBASEiEB1776.
    EcoGeneiEG11829. mobA.

    Phylogenomic databases

    eggNOGiCOG0746.
    HOGENOMiHOG000280423.
    InParanoidiP32173.
    KOiK03752.
    OMAiQISINAN.
    OrthoDBiEOG6PKFG0.
    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

    Gene3Di3.90.550.10. 1 hit.
    HAMAPiMF_00316. MobA.
    InterProiIPR025877. MobA-like_NTP_Trfase_dom.
    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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
      Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "The mob locus of Escherichia coli K12 required for molybdenum cofactor biosynthesis is expressed at very low levels."
      Iobbi-Nivol C., Palmer T., Whitty P.W., McNairn E., Boxer D.H.
      Microbiology 141:1663-1671(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
      Strain: K12.
    5. "Isolation of protein FA, a product of the mob locus required for molybdenum cofactor biosynthesis in Escherichia coli."
      Palmer T., Vasishta A., Whitty P.W., Boxer D.H.
      Eur. J. Biochem. 222:687-692(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-5, FUNCTION IN MGD BIOSYNTHESIS, SUBUNIT.
    6. "Molybdenum cofactor biosynthesis in Escherichia coli. Requirement of the chlB gene product for the formation of molybdopterin guanine dinucleotide."
      Johnson J.L., Indermaur L.W., Rajagopalan K.V.
      J. Biol. Chem. 266:12140-12145(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MGD BIOSYNTHESIS, DISRUPTION PHENOTYPE.
      Strain: RK4353.
    7. "Mechanism of assembly of the bis(molybdopterin guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase."
      Temple C.A., Rajagopalan K.V.
      J. Biol. Chem. 275:40202-40210(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN BIS(MGD) AND MGD BIOSYNTHESIS, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    8. "In vivo interactions between gene products involved in the final stages of molybdenum cofactor biosynthesis in Escherichia coli."
      Magalon A., Frixon C., Pommier J., Giordano G., Blasco F.
      J. Biol. Chem. 277:48199-48204(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MOEA AND MOBB.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    9. "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: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, DOMAIN, MUTAGENESIS OF 12-LEU--GLY-14 AND 79-PRO--GLY-82.
    10. "The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis."
      Lake M.W., Temple C.A., Rajagopalan K.V., Schindelin H.
      J. Biol. Chem. 275:40211-40217(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH MN-GTP, COFACTOR, SUBUNIT.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    11. "Crystal structure of the molybdenum cofactor biosynthesis protein MobA from Escherichia coli at near-atomic resolution."
      Stevenson C.E., Sargent F., Buchanan G., Palmer T., Lawson D.M.
      Structure 8:1115-1125(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
      Strain: K12.
    12. "Biochemical and structural analysis of the molybdenum cofactor biosynthesis protein MobA."
      Guse A., Stevenson C.E., Kuper J., Buchanan G., Schwarz G., Giordano G., Magalon A., Mendel R.R., Lawson D.M., Palmer T.
      J. Biol. Chem. 278:25302-25307(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF MUTANTS ALA-19; LEU-22; ASN-101; ASP-180 AND ASP-182, MUTAGENESIS OF GLY-15; ARG-19; GLY-22; LYS-25; GLY-78; GLY-82; ASP-101; ARG-156; ASN-180 AND ASN-182.
      Strain: K12.

    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: June 24, 2015
    This is version 131 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

    External Data

    Dasty 3

    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 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.