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P49058

- IMDH_BORBU

UniProt

P49058 - IMDH_BORBU

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Essential for mouse infection by tick bite and critical for the survival in environments that appear to lack sufficient amounts of guanine, guanosine, and/or deoxyguanosine to support spirochete growth, such as mammalian host tissues.2 PublicationsUniRule annotation

    Catalytic activityi

    Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

    Cofactori

    Potassium.UniRule annotation

    Enzyme regulationi

    Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.UniRule annotation

    Kineticsi

    1. KM=29 µM for Inosine 5'-phosphate1 Publication
    2. KM=1100 µM for NAD+1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei172 – 1721NADUniRule annotation
    Metal bindingi224 – 2241Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi226 – 2261Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei227 – 2271IMPUniRule annotation
    Active sitei229 – 2291Thioimidate intermediateUniRule annotation
    Metal bindingi229 – 2291Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei340 – 3401IMPUniRule annotation
    Metal bindingi394 – 3941Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi395 – 3951Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi396 – 3961Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi222 – 2243NADUniRule annotation

    GO - Molecular functioni

    1. IMP dehydrogenase activity Source: UniProtKB-HAMAP
    2. metal ion binding Source: UniProtKB-HAMAP
    3. nucleotide binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. GMP biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    GMP biosynthesis, Purine biosynthesis

    Keywords - Ligandi

    Metal-binding, NAD, Potassium

    Enzyme and pathway databases

    BioCyciBBUR224326:G9SO-1498-MONOMER.
    UniPathwayiUPA00601; UER00295.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inosine-5'-monophosphate dehydrogenaseUniRule annotation (EC:1.1.1.205UniRule annotation)
    Short name:
    IMP dehydrogenaseUniRule annotation
    Short name:
    IMPDUniRule annotation
    Short name:
    IMPDHUniRule annotation
    Gene namesi
    Name:guaBUniRule annotation
    Ordered Locus Names:BB_B17
    Encoded oniPlasmid cp26 (circular 26 kb)0 Publication
    OrganismiBorrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
    Taxonomic identifieri224326 [NCBI]
    Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group
    ProteomesiUP000001807: Plasmid cp26

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 404403Inosine-5'-monophosphate dehydrogenasePRO_0000093692Add
    BLAST

    Proteomic databases

    PRIDEiP49058.

    Interactioni

    Subunit structurei

    Homotetramer.1 PublicationUniRule annotation

    Protein-protein interaction databases

    STRINGi224326.BBB17.

    Structurei

    Secondary structure

    1
    404
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi12 – 143
    Beta strandi15 – 173
    Helixi26 – 283
    Beta strandi33 – 386
    Beta strandi40 – 478
    Turni51 – 533
    Helixi56 – 6510
    Beta strandi67 – 715
    Beta strandi73 – 753
    Helixi77 – 8812
    Beta strandi145 – 1484
    Helixi154 – 16310
    Beta strandi167 – 1715
    Helixi179 – 19113
    Beta strandi196 – 2027
    Helixi205 – 2128
    Turni213 – 2153
    Beta strandi217 – 2215
    Helixi230 – 2356
    Helixi241 – 25212
    Beta strandi258 – 2636
    Helixi268 – 27710
    Beta strandi280 – 2845
    Helixi286 – 2894
    Beta strandi294 – 2963
    Beta strandi298 – 3014
    Beta strandi304 – 3074
    Helixi352 – 37019
    Helixi375 – 3806
    Beta strandi384 – 3863

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EEPX-ray2.40A/B1-404[»]
    ProteinModelPortaliP49058.
    SMRiP49058. Positions 3-389.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49058.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni262 – 2643IMP bindingUniRule annotation
    Regioni285 – 2862IMP bindingUniRule annotation
    Regioni309 – 3135IMP bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the IMPDH/GMPR family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0517.
    KOiK00088.
    OMAiHGHSKNI.
    OrthoDBiEOG6GTZPV.

    Family and domain databases

    Gene3Di3.20.20.70. 2 hits.
    HAMAPiMF_01964. IMPDH.
    InterProiIPR013785. Aldolase_TIM.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view]
    PANTHERiPTHR11911:SF6. PTHR11911:SF6. 1 hit.
    PfamiPF00478. IMPDH. 1 hit.
    [Graphical view]
    PROSITEiPS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P49058-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPNKITKEAL TFDDVSLIPR KSSVLPSEVS LKTQLTKNIS LNIPFLSSAM    50
    DTVTESQMAI AIAKEGGIGI IHKNMSIEAQ RKEIEKVKTY KFQKTINTNG 100
    DTNEQKPEIF TAKQHLEKSD AYKNAEHKED FPNACKDLNN KLRVGAAVSI 150
    DIDTIERVEE LVKAHVDILV IDSAHGHSTR IIELIKKIKT KYPNLDLIAG 200
    NIVTKEAALD LISVGADCLK VGIGPGSICT TRIVAGVGVP QITAICDVYE 250
    ACNNTNICII ADGGIRFSGD VVKAIAAGAD SVMIGNLFAG TKESPSEEII 300
    YNGKKFKSYV GMGSISAMKR GSKSRYFQLE NNEPKKLVPE GIEGMVPYSG 350
    KLKDILTQLK GGLMSGMGYL GAATISDLKI NSKFVKISHS SLKESHPHDV 400
    FSIT 404
    Length:404
    Mass (Da):43,768
    Last modified:February 1, 1996 - v1
    Checksum:iA91D6D6C5CE522F1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13372 Genomic DNA. Translation: AAA53247.1.
    AE000792 Genomic DNA. Translation: AAC66314.1.
    PIRiE70218.
    RefSeqiNP_047003.1. NC_001903.1.
    WP_010890582.1. NC_001903.1.

    Genome annotation databases

    EnsemblBacteriaiAAC66314; AAC66314; BB_B17.
    GeneIDi1194400.
    KEGGibbu:BB_B17.
    PATRICi20559101. VBIBorBur75917_1605.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13372 Genomic DNA. Translation: AAA53247.1 .
    AE000792 Genomic DNA. Translation: AAC66314.1 .
    PIRi E70218.
    RefSeqi NP_047003.1. NC_001903.1.
    WP_010890582.1. NC_001903.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EEP X-ray 2.40 A/B 1-404 [» ]
    ProteinModelPortali P49058.
    SMRi P49058. Positions 3-389.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224326.BBB17.

    Chemistry

    BindingDBi P49058.

    Proteomic databases

    PRIDEi P49058.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC66314 ; AAC66314 ; BB_B17 .
    GeneIDi 1194400.
    KEGGi bbu:BB_B17.
    PATRICi 20559101. VBIBorBur75917_1605.

    Phylogenomic databases

    eggNOGi COG0517.
    KOi K00088.
    OMAi HGHSKNI.
    OrthoDBi EOG6GTZPV.

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    BioCyci BBUR224326:G9SO-1498-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P49058.

    Family and domain databases

    Gene3Di 3.20.20.70. 2 hits.
    HAMAPi MF_01964. IMPDH.
    InterProi IPR013785. Aldolase_TIM.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view ]
    PANTHERi PTHR11911:SF6. PTHR11911:SF6. 1 hit.
    Pfami PF00478. IMPDH. 1 hit.
    [Graphical view ]
    PROSITEi PS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Plasmid location of Borrelia purine biosynthesis gene homologs."
      Margolis N., Hogan D., Tilly K., Rosa P.
      J. Bacteriol. 176:6427-6432(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
    3. "Expression, purification, and characterization of inosine 5'-monophosphate dehydrogenase from Borrelia burgdorferi."
      Zhou X., Cahoon M., Rosa P., Hedstrom L.
      J. Biol. Chem. 272:21977-21981(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-7, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
    4. "GuaA and GuaB are essential for Borrelia burgdorferi survival in the tick-mouse infection cycle."
      Jewett M.W., Lawrence K.A., Bestor A., Byram R., Gherardini F., Rosa P.A.
      J. Bacteriol. 191:6231-6241(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
    5. "Crystal structure at 2.4-A resolution of Borrelia burgdorferi inosine 5'-monophosphate dehydrogenase: evidence of a substrate-induced hinged-lid motion by loop 6."
      McMillan F.M., Cahoon M., White A., Hedstrom L., Petsko G.A., Ringe D.
      Biochemistry 39:4533-4542(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

    Entry informationi

    Entry nameiIMDH_BORBU
    AccessioniPrimary (citable) accession number: P49058
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 110 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, Plasmid, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    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