Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P31002

- IMDH_ACICA

UniProt

P31002 - IMDH_ACICA

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Acinetobacter calcoaceticus
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.UniRule 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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei247 – 2471NADUniRule annotation
    Metal bindingi299 – 2991Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi301 – 3011Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei302 – 3021IMPUniRule annotation
    Active sitei304 – 3041Thioimidate intermediateUniRule annotation
    Metal bindingi304 – 3041Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei416 – 4161IMPUniRule annotation
    Metal bindingi470 – 4701Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi471 – 4711Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi472 – 4721Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi297 – 2993NADUniRule annotation

    GO - Molecular functioni

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

    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
    OrganismiAcinetobacter calcoaceticus
    Taxonomic identifieri471 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 488488Inosine-5'-monophosphate dehydrogenasePRO_0000093688Add
    BLAST

    Proteomic databases

    PRIDEiP31002.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliP31002.
    SMRiP31002. Positions 4-486.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini93 – 14856CBS 1UniRule annotationAdd
    BLAST
    Domaini152 – 21059CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni336 – 3383IMP bindingUniRule annotation
    Regioni359 – 3602IMP bindingUniRule annotation
    Regioni383 – 3875IMP bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the IMPDH/GMPR family.UniRule annotation
    Contains 2 CBS domains.UniRule annotation

    Keywords - Domaini

    CBS domain, Repeat

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01964. IMPDH.
    InterProiIPR013785. Aldolase_TIM.
    IPR000644. CBS_dom.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view]
    PfamiPF00571. CBS. 2 hits.
    PF00478. IMPDH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000130. IMPDH. 1 hit.
    SMARTiSM00116. CBS. 2 hits.
    [Graphical view]
    TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
    PROSITEiPS51371. CBS. 2 hits.
    PS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P31002-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLTIVQEALT FDDVLLLPAY STVLPKDVSL KTRLTRGIYL NIPLVSAAMD    50
    TVTESRMAIA MAQNGGIGIL HKNMDIAAQA AEVRRVKKFE AGMVKDPITV 100
    SPETTVRELI AITSANNISG VPVVKDSKVV GIVTGRDTRF ETNLEQPVSN 150
    IMTGQDRLVT VREGESKENI QALLQKHRIE KVLVVGESNE LKGLITVTDF 200
    RKAESYPNSC KDDLGRLRVG AAVGTGADTP SRVEALVEAG VDVIVVDTAH 250
    GHSAGVIERV RWVKQNFPQV QVIGGNIATG DAALALLDAG ADAVKVGIGP 300
    GSICTTRIVA GIGMPQISAI DSVASALKDQ IPLIADGGIP FSGDMAKAIG 350
    AGASTIMVGS LLAGTEEAPG EVEFFQGRYY KAYRGMGSLG AMAGRTGSAD 400
    RYFQDSKAGA EKLVPEGIEG RVPYKGPMGN IVHQMMGGLR SSMGYTGSAV 450
    IEDLRQNAKF VKITSAGMSE SHVHDVTITK EAPNYRVG 488
    Length:488
    Mass (Da):51,530
    Last modified:July 1, 1993 - v1
    Checksum:i3DE0F8F9B5157A03
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66859 Genomic DNA. Translation: CAA47328.1.
    PIRiS23226.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66859 Genomic DNA. Translation: CAA47328.1 .
    PIRi S23226.

    3D structure databases

    ProteinModelPortali P31002.
    SMRi P31002. Positions 4-486.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P31002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_01964. IMPDH.
    InterProi IPR013785. Aldolase_TIM.
    IPR000644. CBS_dom.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view ]
    Pfami PF00571. CBS. 2 hits.
    PF00478. IMPDH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000130. IMPDH. 1 hit.
    SMARTi SM00116. CBS. 2 hits.
    [Graphical view ]
    TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
    PROSITEi PS51371. CBS. 2 hits.
    PS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Anderegg U., Schnuck W.H., Asperger O., Kleber H.-P.
      Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: EB 104.

    Entry informationi

    Entry nameiIMDH_ACICA
    AccessioniPrimary (citable) accession number: P31002
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3