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Protein

Molybdopterin-guanine dinucleotide biosynthesis adapter protein

Gene

mobB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GTP-binding protein that is not required for the biosynthesis of Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor, and not necessary for the formation of active molybdoenzymes using this form of molybdenum cofactor. May act as an adapter protein to achieve the efficient biosynthesis and utilization of MGD. Displays a weak intrinsic GTPase activity. Is also able to bind the nucleotides ATP, TTP and GDP, but with lower affinity than GTP.2 Publications

Kineticsi

kcat is 0.003 min(-1) for the GTPase activity.

  1. KM=7.5 µM for GTP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi17 – 215GTPCurated
    Nucleotide bindingi51 – 544GTPSequence analysis
    Nucleotide bindingi100 – 1034GTPSequence analysis

    GO - Molecular functioni

    • GTP binding Source: EcoCyc

    GO - Biological processi

    Complete GO annotation...

    Keywords - Biological processi

    Molybdenum cofactor biosynthesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11828-MONOMER.
    ECOL316407:JW5575-MONOMER.
    RETL1328306-WGS:GSTH-2421-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Molybdopterin-guanine dinucleotide biosynthesis adapter protein
    Short name:
    MGD biosynthesis adapter protein
    Alternative name(s):
    Molybdenum cofactor biosynthesis adapter protein
    Short name:
    Moco biosynthesis adapter protein
    Molybdopterin-guanine dinucleotide biosynthesis protein B
    Gene namesi
    Name:mobB
    Synonyms:yihC
    Ordered Locus Names:b3856, JW5575
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11828. mobB.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved2 Publications
    Chaini2 – 175174Molybdopterin-guanine dinucleotide biosynthesis adapter proteinPRO_0000096528Add
    BLAST

    Proteomic databases

    PaxDbiP32125.

    Expressioni

    Inductioni

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

    Interactioni

    Subunit structurei

    Homodimer. Interacts with MobA, MogA and MoeA in vivo.4 Publications

    Protein-protein interaction databases

    BioGridi4262618. 5 interactions.
    DIPiDIP-10234N.
    IntActiP32125. 4 interactions.
    MINTiMINT-1264474.
    STRINGi511145.b3856.

    Structurei

    Secondary structure

    1
    175
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 135Combined sources
    Beta strandi16 – 183Combined sources
    Helixi20 – 3314Combined sources
    Beta strandi38 – 436Combined sources
    Helixi54 – 585Combined sources
    Helixi60 – 634Combined sources
    Beta strandi66 – 716Combined sources
    Beta strandi73 – 819Combined sources
    Beta strandi83 – 853Combined sources
    Helixi90 – 967Combined sources
    Helixi99 – 1013Combined sources
    Beta strandi103 – 1097Combined sources
    Beta strandi115 – 1217Combined sources
    Helixi129 – 1313Combined sources
    Beta strandi138 – 1458Combined sources
    Beta strandi150 – 1556Combined sources
    Helixi159 – 17012Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NP6X-ray1.90A/B2-175[»]
    1P9NX-ray2.80A/B6-175[»]
    ProteinModelPortaliP32125.
    SMRiP32125. Positions 6-174.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32125.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the MobB family.Curated

    Phylogenomic databases

    eggNOGiENOG4105FNP. Bacteria.
    COG1763. LUCA.
    HOGENOMiHOG000280765.
    InParanoidiP32125.
    KOiK03753.
    OMAiHTHHNMD.
    OrthoDBiEOG6PKFG0.
    PhylomeDBiP32125.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR004435. MobB_dom.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF03205. MobB. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00176. mobB. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P32125-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAGKTMIPLL AFAAWSGTGK TTLLKKLIPA LCARGIRPGL IKHTHHDMDV
    60 70 80 90 100
    DKPGKDSYEL RKAGAAQTIV ASQQRWALMT ETPDEEELDL QFLASRMDTS
    110 120 130 140 150
    KLDLILVEGF KHEEIAKIVL FRDGAGHRPE ELVIDRHVIA VASDVPLNLD
    160 170
    VALLDINDVE GLADFVVEWM QKQNG
    Length:175
    Mass (Da):19,363
    Last modified:January 23, 2007 - v3
    Checksum:i41E0E4EFB2AE160C
    GO

    Sequence cautioni

    The sequence AAB02991.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence BAE77452.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L19201 Genomic DNA. Translation: AAB02991.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC76854.2.
    AP009048 Genomic DNA. Translation: BAE77452.1. Different initiation.
    PIRiS40802.
    RefSeqiNP_418293.2. NC_000913.3.
    WP_000907622.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76854; AAC76854; b3856.
    BAE77452; BAE77452; BAE77452.
    GeneIDi948343.
    KEGGiecj:JW5575.
    eco:b3856.
    PATRICi32123209. VBIEscCol129921_3965.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L19201 Genomic DNA. Translation: AAB02991.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC76854.2.
    AP009048 Genomic DNA. Translation: BAE77452.1. Different initiation.
    PIRiS40802.
    RefSeqiNP_418293.2. NC_000913.3.
    WP_000907622.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NP6X-ray1.90A/B2-175[»]
    1P9NX-ray2.80A/B6-175[»]
    ProteinModelPortaliP32125.
    SMRiP32125. Positions 6-174.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4262618. 5 interactions.
    DIPiDIP-10234N.
    IntActiP32125. 4 interactions.
    MINTiMINT-1264474.
    STRINGi511145.b3856.

    Proteomic databases

    PaxDbiP32125.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76854; AAC76854; b3856.
    BAE77452; BAE77452; BAE77452.
    GeneIDi948343.
    KEGGiecj:JW5575.
    eco:b3856.
    PATRICi32123209. VBIEscCol129921_3965.

    Organism-specific databases

    EchoBASEiEB1775.
    EcoGeneiEG11828. mobB.

    Phylogenomic databases

    eggNOGiENOG4105FNP. Bacteria.
    COG1763. LUCA.
    HOGENOMiHOG000280765.
    InParanoidiP32125.
    KOiK03753.
    OMAiHTHHNMD.
    OrthoDBiEOG6PKFG0.
    PhylomeDBiP32125.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11828-MONOMER.
    ECOL316407:JW5575-MONOMER.
    RETL1328306-WGS:GSTH-2421-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP32125.
    PROiP32125.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR004435. MobB_dom.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF03205. MobB. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00176. mobB. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "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], PROTEIN SEQUENCE OF 2-8, INDUCTION.
      Strain: K12.
    2. "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.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "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.
    5. "The product of the molybdenum cofactor gene mobB of Escherichia coli is a GTP-binding protein."
      Eaves D.J., Palmer T., Boxer D.H.
      Eur. J. Biochem. 246:690-697(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13, GTP-BINDING, GTPASE ACTIVITY, FUNCTION, SUBUNIT.
      Strain: K12 / JM109 / ATCC 53323.
    6. "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: NO ROLE IN ACTIVATION OF DMSOR.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    7. "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 MOBA; MOGA AND MOEA.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    8. "Molecules of Escherichia coli MobB assemble into densely packed hollow cylinders in a crystal lattice with 75% solvent content."
      Rangarajan S.E., Tocilj A., Li Y., Iannuzzi P., Matte A., Cygler M.
      Acta Crystallogr. D 59:2348-2352(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 6-174 IN COMPLEX WITH SULFATE, SUBUNIT.
    9. "Insight into the role of Escherichia coli MobB in molybdenum cofactor biosynthesis based on the high resolution crystal structure."
      McLuskey K., Harrison J.A., Schuttelkopf A.W., Boxer D.H., Hunter W.N.
      J. Biol. Chem. 278:23706-23713(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SULFATE, FUNCTION, SUBUNIT.

    Entry informationi

    Entry nameiMOBB_ECOLI
    AccessioniPrimary (citable) accession number: P32125
    Secondary accession number(s): P76770, Q2M8F4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: January 23, 2007
    Last modified: January 20, 2016
    This is version 138 of the entry and version 3 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.