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P21879

- IMDH_BACSU

UniProt

P21879 - IMDH_BACSU

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (29 Aug 2003)
      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.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 sitei251 – 2511NADUniRule annotation
    Metal bindingi303 – 3031Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi305 – 3051Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei306 – 3061IMPUniRule annotation
    Active sitei308 – 3081Thioimidate intermediateUniRule annotation
    Metal bindingi308 – 3081Potassium; 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 bindingi301 – 3033NADUniRule 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

    BioCyciBSUB:BSU00090-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
    Alternative name(s):
    Superoxide-inducible protein 12
    Short name:
    SOI12
    Gene namesi
    Name:guaBUniRule annotation
    Synonyms:gnaB
    Ordered Locus Names:BSU00090
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU00090. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 488488Inosine-5'-monophosphate dehydrogenasePRO_0000093691Add
    BLAST

    Proteomic databases

    PaxDbiP21879.
    PRIDEiP21879.

    Expressioni

    Inductioni

    By superoxide.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    IntActiP21879. 1 interaction.
    MINTiMINT-8365336.
    STRINGi224308.BSU00090.

    Structurei

    3D structure databases

    ProteinModelPortaliP21879.
    SMRiP21879. Positions 2-486.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini95 – 15359CBS 1UniRule annotationAdd
    BLAST
    Domaini157 – 21458CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni341 – 3433IMP bindingUniRule annotation
    Regioni364 – 3652IMP bindingUniRule annotation
    Regioni388 – 3925IMP bindingUniRule annotation

    Sequence similaritiesi

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

    Keywords - Domaini

    CBS domain, Repeat

    Phylogenomic databases

    eggNOGiCOG0517.
    HOGENOMiHOG000165754.
    KOiK00088.
    OMAiHGHSKNI.
    OrthoDBiEOG6GTZPV.
    PhylomeDBiP21879.

    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.

    P21879-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWESKFSKEG LTFDDVLLVP AKSEVLPRDV DLSVELTKTL KLNIPVISAG    50
    MDTVTESAMA IAMARQGGLG IIHKNMSIEQ QAEQVDKVKR SERGVITNPF 100
    FLTPDHQVFD AEHLMGKYRI SGVPIVNNEE DQKLVGIITN RDLRFISDYS 150
    MKISDVMTKE ELVTASVGTT LDEAEKILQK HKIEKLPLVD DQNKLKGLIT 200
    IKDIEKVIEF PNSSKDIHGR LIVGAAVGVT GDTMTRVKKL VEANVDVIVI 250
    DTAHGHSQGV LNTVTKIRET YPELNIIAGN VATAEATRAL IEAGADVVKV 300
    GIGPGSICTT RVVAGVGVPQ ITAIYDCATE ARKHGKTIIA DGGIKFSGDI 350
    TKALAAGGHA VMLGSLLAGT SESPGETEIY QGRRFKVYRG MGSVAAMEKG 400
    SKDRYFQEEN KKFVPEGIEG RTPYKGPVEE TVYQLVGGLR SGMGYCGSKD 450
    LRALREEAQF IRMTGAGLRE SHPHDVQITK ESPNYTIS 488
    Length:488
    Mass (Da):52,991
    Last modified:August 29, 2003 - v2
    Checksum:i34939E2758EA48B6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281R → H in CAA39204. (PubMed:1979163)Curated
    Sequence conflicti480 – 4889KESPNYTIS → VHRNKALPGLFGSHQKKTGF VYDECCQSGFFSSD in CAA39204. (PubMed:1979163)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55669 Genomic DNA. Translation: CAA39204.1.
    D26185 Genomic DNA. Translation: BAA05245.1.
    AL009126 Genomic DNA. Translation: CAB11785.1.
    PIRiS66039. DEBSMP.
    RefSeqiNP_387890.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB11785; CAB11785; BSU00090.
    GeneIDi938032.
    KEGGibsu:BSU00090.
    PATRICi18971477. VBIBacSub10457_0010.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55669 Genomic DNA. Translation: CAA39204.1 .
    D26185 Genomic DNA. Translation: BAA05245.1 .
    AL009126 Genomic DNA. Translation: CAB11785.1 .
    PIRi S66039. DEBSMP.
    RefSeqi NP_387890.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P21879.
    SMRi P21879. Positions 2-486.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P21879. 1 interaction.
    MINTi MINT-8365336.
    STRINGi 224308.BSU00090.

    Proteomic databases

    PaxDbi P21879.
    PRIDEi P21879.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB11785 ; CAB11785 ; BSU00090 .
    GeneIDi 938032.
    KEGGi bsu:BSU00090.
    PATRICi 18971477. VBIBacSub10457_0010.

    Organism-specific databases

    GenoListi BSU00090. [Micado ]

    Phylogenomic databases

    eggNOGi COG0517.
    HOGENOMi HOG000165754.
    KOi K00088.
    OMAi HGHSKNI.
    OrthoDBi EOG6GTZPV.
    PhylomeDBi P21879.

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    BioCyci BSUB:BSU00090-MONOMER.

    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. "Nucleotide sequence of the Bacillus subtilis IMP dehydrogenase gene."
      Kanzaki N., Miyagawa K.I.
      Nucleic Acids Res. 18:6710-6710(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin."
      Ogasawara N., Nakai S., Yoshikawa H.
      DNA Res. 1:1-14(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    4. "First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis."
      Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.
      Electrophoresis 18:1451-1463(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-25.
      Strain: 168 / IS58.

    Entry informationi

    Entry nameiIMDH_BACSU
    AccessioniPrimary (citable) accession number: P21879
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: August 29, 2003
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3