Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P49058 (IMDH_BORBU)

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 Publications

Catalytic activityi

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.1 Publication

Cofactori

K+1 Publication

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.By similarity

Kineticsi

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

    Pathwayi: XMP biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Inosine-5'-monophosphate dehydrogenase (guaB)
    This subpathway is part of the pathway XMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from IMP, the pathway XMP biosynthesis via de novo pathway and in Purine metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei172NADBy similarity1
    Metal bindingi224Potassium; via carbonyl oxygenBy similarity1
    Metal bindingi226Potassium; via carbonyl oxygenBy similarity1
    Binding sitei227IMPBy similarity1
    Active sitei229Thioimidate intermediateBy similarity1
    Metal bindingi229Potassium; via carbonyl oxygenBy similarity1
    Active sitei325Proton acceptorBy similarity1
    Binding sitei340IMPBy similarity1
    Metal bindingi394Potassium; via carbonyl oxygen; shared with tetrameric partnerBy similarity1
    Metal bindingi395Potassium; via carbonyl oxygen; shared with tetrameric partnerBy similarity1
    Metal bindingi396Potassium; via carbonyl oxygen; shared with tetrameric partnerBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi222 – 224NADBy similarity3

    GO - Molecular functioni

    Complete GO annotation...

    GO - Biological processi

    Complete GO annotation...

    Keywordsi

    Molecular functionOxidoreductase
    Biological processGMP biosynthesis, Purine biosynthesis
    LigandMetal-binding, NAD, Potassium

    Enzyme and pathway databases

    BRENDAi1.1.1.205. 902.
    UniPathwayiUPA00601; UER00295.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inosine-5'-monophosphate dehydrogenase1 Publication (EC:1.1.1.2051 Publication)
    Short name:
    IMP dehydrogenase
    Short name:
    IMPD
    Short name:
    IMPDH1 Publication
    Gene namesi
    Name:guaB1 Publication
    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 lineageiBacteria › Spirochaetes › Spirochaetales › Borreliaceae › Borreliella ›
    Proteomesi
    • UP000001807 Componenti: Plasmid cp26

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00000936922 – 404Inosine-5'-monophosphate dehydrogenaseAdd BLAST403

    Proteomic databases

    PRIDEiP49058.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Chemistry databases

    BindingDBiP49058.

    Structurei

    Secondary structure

    1404
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi12 – 14Combined sources3
    Beta strandi15 – 17Combined sources3
    Helixi26 – 28Combined sources3
    Beta strandi33 – 38Combined sources6
    Beta strandi40 – 47Combined sources8
    Turni51 – 53Combined sources3
    Helixi56 – 65Combined sources10
    Beta strandi67 – 71Combined sources5
    Beta strandi73 – 75Combined sources3
    Helixi77 – 88Combined sources12
    Beta strandi145 – 148Combined sources4
    Helixi154 – 163Combined sources10
    Beta strandi167 – 171Combined sources5
    Helixi179 – 191Combined sources13
    Beta strandi196 – 202Combined sources7
    Helixi205 – 212Combined sources8
    Turni213 – 215Combined sources3
    Beta strandi217 – 221Combined sources5
    Helixi230 – 235Combined sources6
    Helixi241 – 252Combined sources12
    Beta strandi258 – 263Combined sources6
    Helixi268 – 277Combined sources10
    Beta strandi280 – 284Combined sources5
    Helixi286 – 289Combined sources4
    Beta strandi294 – 296Combined sources3
    Beta strandi298 – 301Combined sources4
    Beta strandi304 – 307Combined sources4
    Helixi352 – 370Combined sources19
    Helixi375 – 380Combined sources6
    Beta strandi384 – 386Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1EEPX-ray2.40A/B1-404[»]
    ProteinModelPortaliP49058.
    SMRiP49058.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49058.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni262 – 264IMP bindingBy similarity3
    Regioni285 – 286IMP bindingBy similarity2
    Regioni309 – 313IMP bindingBy similarity5

    Sequence similaritiesi

    Belongs to the IMPDH/GMPR family.Curated

    Phylogenomic databases

    KOiK00088.
    OMAiGIGIVHK.

    Family and domain databases

    CDDicd00381. IMPDH. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    InterProiView protein in InterPro
    IPR013785. Aldolase_TIM.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    PfamiView protein in Pfam
    PF00478. IMPDH. 1 hit.
    PIRSFiPIRSF000130. IMPDH. 1 hit.
    PROSITEiView protein in PROSITE
    PS00487. IMP_DH_GMP_RED. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P49058-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPNKITKEAL TFDDVSLIPR KSSVLPSEVS LKTQLTKNIS LNIPFLSSAM 
            60         70         80         90        100
    DTVTESQMAI AIAKEGGIGI IHKNMSIEAQ RKEIEKVKTY KFQKTINTNG 
           110        120        130        140        150
    DTNEQKPEIF TAKQHLEKSD AYKNAEHKED FPNACKDLNN KLRVGAAVSI 
           160        170        180        190        200
    DIDTIERVEE LVKAHVDILV IDSAHGHSTR IIELIKKIKT KYPNLDLIAG 
           210        220        230        240        250
    NIVTKEAALD LISVGADCLK VGIGPGSICT TRIVAGVGVP QITAICDVYE 
           260        270        280        290        300
    ACNNTNICII ADGGIRFSGD VVKAIAAGAD SVMIGNLFAG TKESPSEEII 
           310        320        330        340        350
    YNGKKFKSYV GMGSISAMKR GSKSRYFQLE NNEPKKLVPE GIEGMVPYSG 
           360        370        380        390        400
    KLKDILTQLK GGLMSGMGYL GAATISDLKI NSKFVKISHS SLKESHPHDV 

    FSIT
    Length:404
    Mass (Da):43,768
    Last modified:February 1, 1996 - v1
    Checksum:iA91D6D6C5CE522F1
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.
    PATRICifig|224326.49.peg.1605.

    Similar proteinsi

    Entry informationi

    Entry nameiIMDH_BORBU
    AccessioniPrimary (citable) accession number: P49058
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: August 30, 2017
    This is version 131 of the entry and version 1 of the sequence. See 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