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P0C0H6

- IMDH_STRPY

UniProt

P0C0H6 - IMDH_STRPY

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Streptococcus pyogenes
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      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

    Kineticsi

    1. KM=62 µM for Inosine 5'-phosphate1 Publication
    2. KM=1180 µM for NAD+1 Publication

    pH dependencei

    Optimum pH is 7.8.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei253 – 2531NADUniRule annotation
    Metal bindingi305 – 3051Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi307 – 3071Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei308 – 3081IMP1 PublicationUniRule annotation
    Active sitei310 – 3101Thioimidate intermediateUniRule annotation
    Metal bindingi310 – 3101Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei421 – 4211IMPUniRule annotation
    Metal bindingi475 – 4751Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi476 – 4761Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi477 – 4771Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi303 – 3053NADUniRule 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

    SABIO-RKP0C0H6.
    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
    Synonyms:impD
    OrganismiStreptococcus pyogenes
    Taxonomic identifieri1314 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi406 – 4061R → A: No activity. 1 Publication
    Mutagenesisi421 – 4211E → Q: No activity. 1 Publication
    Mutagenesisi450 – 4501Y → A: No effect. 1 Publication
    Mutagenesisi450 – 4501Y → D: Reduces activity by 75%. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 493492Inosine-5'-monophosphate dehydrogenasePRO_0000093714Add
    BLAST

    Proteomic databases

    PRIDEiP0C0H6.

    Interactioni

    Subunit structurei

    Homotetramer.1 PublicationUniRule annotation

    Structurei

    Secondary structure

    1
    493
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 64
    Helixi15 – 173
    Beta strandi18 – 203
    Helixi29 – 313
    Beta strandi36 – 394
    Beta strandi42 – 509
    Turni54 – 563
    Helixi59 – 679
    Beta strandi71 – 744
    Helixi80 – 9314
    Turni94 – 974
    Beta strandi98 – 1003
    Beta strandi106 – 1094
    Helixi110 – 11910
    Beta strandi123 – 1297
    Turni131 – 1333
    Beta strandi135 – 1417
    Helixi142 – 1476
    Beta strandi151 – 1544
    Turni155 – 1573
    Helixi173 – 18210
    Beta strandi186 – 1916
    Beta strandi195 – 2028
    Helixi203 – 2119
    Beta strandi226 – 2294
    Helixi235 – 24511
    Beta strandi248 – 2525
    Helixi260 – 27213
    Beta strandi274 – 2763
    Beta strandi278 – 2836
    Helixi286 – 2949
    Beta strandi298 – 3025
    Helixi312 – 3154
    Helixi322 – 33514
    Beta strandi339 – 3446
    Helixi349 – 3579
    Beta strandi361 – 3666
    Turni367 – 3715
    Beta strandi372 – 3743
    Beta strandi379 – 3824
    Beta strandi385 – 3917
    Helixi396 – 3994
    Beta strandi424 – 4285
    Helixi433 – 45018
    Helixi456 – 4627
    Beta strandi465 – 4673
    Helixi470 – 4767

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZFJX-ray1.90A2-492[»]
    ProteinModelPortaliP0C0H6.
    SMRiP0C0H6. Positions 2-491.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0C0H6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini97 – 15559CBS 1UniRule annotationAdd
    BLAST
    Domaini159 – 21961CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni343 – 3453IMP binding
    Regioni366 – 3672IMP binding
    Regioni390 – 3945IMP binding

    Sequence similaritiesi

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

    Keywords - Domaini

    CBS domain, Repeat

    Phylogenomic databases

    eggNOGiCOG0517.

    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]
    PANTHERiPTHR11911:SF6. PTHR11911:SF6. 1 hit.
    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.

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

    P0C0H6-1 [UniParc]FASTAAdd to Basket

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    MSNWDTKFLK KGYTFDDVLL IPAESHVLPN EVDLKTKLAD NLTLNIPIIT    50
    AAMDTVTGSK MAIAIARAGG LGVIHKNMSI TEQAEEVRKV KRSENGVIID 100
    PFFLTPEHKV SEAEELMQRY RISGVPIVET LANRKLVGII TNRDMRFISD 150
    YNAPISEHMT SEHLVTAAVG TDLETAERIL HEHRIEKLPL VDNSGRLSGL 200
    ITIKDIEKVI EFPHAAKDEF GRLLVAAAVG VTSDTFERAE ALFEAGADAI 250
    VIDTAHGHSA GVLRKIAEIR AHFPNRTLIA GNIATAEGAR ALYDAGVDVV 300
    KVGIGPGSIC TTRVVAGVGV PQVTAIYDAA AVAREYGKTI IADGGIKYSG 350
    DIVKALAAGG NAVMLGSMFA GTDEAPGETE IYQGRKFKTY RGMGSIAAMK 400
    KGSSDRYFQG SVNEANKLVP EGIEGRVAYK GAASDIVFQM LGGIRSGMGY 450
    VGAGDIQELH ENAQFVEMSG AGLIESHPHD VQITNEAPNY SVH 493
    Length:493
    Mass (Da):52,807
    Last modified:January 23, 2007 - v2
    Checksum:i9C317AD598CB5740
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti419 – 4191V → L no nucleotide entry (PubMed:10200156)Curated

    Mass spectrometryi

    Molecular mass is 52328 Da from positions 2 - 493. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U26056 Genomic DNA. Translation: AAB03846.1.
    PIRiJC4372.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U26056 Genomic DNA. Translation: AAB03846.1 .
    PIRi JC4372.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZFJ X-ray 1.90 A 2-492 [» ]
    ProteinModelPortali P0C0H6.
    SMRi P0C0H6. Positions 2-491.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P0C0H6.

    Proteomic databases

    PRIDEi P0C0H6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0517.

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    SABIO-RK P0C0H6.

    Miscellaneous databases

    EvolutionaryTracei P0C0H6.

    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 ]
    PANTHERi PTHR11911:SF6. PTHR11911:SF6. 1 hit.
    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. "Cloning, sequence analysis and expression of the group A streptococcal guaB gene encoding inosine monophosphate dehydrogenase."
      Ashbaugh C.D., Wessels M.R.
      Gene 165:57-60(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase."
      Zhang R.G., Evans G., Rotella F.J., Westbrook E.M., Beno D., Huberman E., Joachimiak A., Collart F.R.
      Biochemistry 38:4691-4700(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH IMP, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, SUBUNIT, MUTAGENESIS OF ARG-406; GLU-421 AND TYR-450.

    Entry informationi

    Entry nameiIMDH_STRPY
    AccessioniPrimary (citable) accession number: P0C0H6
    Secondary accession number(s): P50099, P68838
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 58 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

    3D-structure, Direct protein sequencing

    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