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Q8T6T2

- IMDH_CRYPV

UniProt

Q8T6T2 - IMDH_CRYPV

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Protein
Inosine-5'-monophosphate dehydrogenase
Gene
56k.02, cgd6_20
Organism
Cryptosporidium parvum
Status
Reviewed - 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.1 Publication

Catalytic activityi

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

Cofactori

Potassium By similarity.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 By similarity. Resistant to mycophenolic acid (MPA) inhibition.1 Publication

Kineticsi

  1. KM=29 µM for Inosine 5'-phosphate1 Publication
  2. KM=150 µM for NAD+

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei163 – 1631NAD By similarity
Metal bindingi214 – 2141Potassium; via carbonyl oxygen By similarity
Metal bindingi216 – 2161Potassium; via carbonyl oxygen By similarity
Binding sitei217 – 2171IMP By similarity
Active sitei219 – 2191Thioimidate intermediate By similarity
Metal bindingi219 – 2191Potassium; via carbonyl oxygen By similarity
Binding sitei329 – 3291IMP By similarity
Metal bindingi383 – 3831Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi384 – 3841Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi385 – 3851Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi212 – 2143NAD By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. GMP biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

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 dehydrogenase (EC:1.1.1.205)
Short name:
IMP dehydrogenase
Short name:
IMPD
Short name:
IMPDH
Gene namesi
ORF Names:56k.02, cgd6_20
OrganismiCryptosporidium parvum
Taxonomic identifieri5807 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaConoidasidaCoccidiaEucoccidioridaEimeriorinaCryptosporidiidaeCryptosporidium

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 400400Inosine-5'-monophosphate dehydrogenaseUniRule annotation
PRO_0000415682Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84
Helixi12 – 143
Beta strandi15 – 173
Helixi26 – 283
Beta strandi33 – 364
Beta strandi39 – 479
Turni51 – 533
Helixi56 – 649
Beta strandi68 – 714
Beta strandi73 – 753
Helixi77 – 8812
Beta strandi133 – 1353
Beta strandi138 – 1414
Helixi146 – 1549
Beta strandi158 – 1636
Helixi170 – 18213
Beta strandi186 – 1927
Helixi195 – 2039
Beta strandi207 – 2115
Helixi221 – 2244
Helixi231 – 24515
Beta strandi249 – 2535
Helixi258 – 2669
Beta strandi270 – 2756
Helixi276 – 2794
Beta strandi288 – 2914
Beta strandi294 – 3007
Helixi305 – 3095
Beta strandi332 – 3365
Helixi341 – 35818
Helixi364 – 3707
Beta strandi373 – 3753
Helixi378 – 3847
Beta strandi388 – 3914

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FFSX-ray3.19A/B/C/D1-400[»]
4IXHX-ray2.10A/B/C/D1-89[»]
A/B/C/D135-400[»]
ProteinModelPortaliQ8T6T2.
SMRiQ8T6T2. Positions 7-377.

Miscellaneous databases

EvolutionaryTraceiQ8T6T2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni252 – 2543IMP binding By similarity
Regioni275 – 2762IMP binding By similarity
Regioni299 – 3035IMP binding By similarity

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.

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]
PfamiPF00478. IMPDH. 1 hit.
[Graphical view]
PROSITEiPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8T6T2-1 [UniParc]FASTAAdd to Basket

« Hide

MGTKNIGKGL TFEDILLVPN YSEVLPREVS LETKLTKNVS LKIPLISSAM    50
DTVTEHLMAV GMARLGGIGI IHKNMDMESQ VNEVLKVKNW ISNLEKNEST 100
PDQNLDKEST DGKDTKSNNN IDAYSNENLD NKGRLRVGAA IGVNEIERAK 150
LLVEAGVDVI VLDSAHGHSL NIIRTLKEIK SKMNIDVIVG NVVTEEATKE 200
LIENGADGIK VGIGPGSICT TRIVAGVGVP QITAIEKCSS VASKFGIPII 250
ADGGIRYSGD IGKALAVGAS SVMIGSILAG TEESPGEKEL IGDTVYKYYR 300
GMGSVGAMKS GSGDRYFQEK RPENKMVPEG IEGRVKYKGE MEGVVYQLVG 350
GLRSCMGYLG SASIEELWKK SSYVEITTSG LRESHVHDVE IVKEVMNYSK 400
Length:400
Mass (Da):43,081
Last modified:June 1, 2002 - v1
Checksum:iDAAF96B44050DD18
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF426177 Genomic DNA. Translation: AAL83208.1.
BX538350 Genomic DNA. Translation: CAD98604.1.
FX115298 mRNA. Translation: BAJ77401.1.
FX115945 mRNA. Translation: BAJ78048.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF426177 Genomic DNA. Translation: AAL83208.1 .
BX538350 Genomic DNA. Translation: CAD98604.1 .
FX115298 mRNA. Translation: BAJ77401.1 .
FX115945 mRNA. Translation: BAJ78048.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3FFS X-ray 3.19 A/B/C/D 1-400 [» ]
4IXH X-ray 2.10 A/B/C/D 1-89 [» ]
A/B/C/D 135-400 [» ]
ProteinModelPortali Q8T6T2.
SMRi Q8T6T2. Positions 7-377.
ModBasei Search...

Chemistry

BindingDBi Q8T6T2.
ChEMBLi CHEMBL6145.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .

Miscellaneous databases

EvolutionaryTracei Q8T6T2.

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 ]
Pfami PF00478. IMPDH. 1 hit.
[Graphical view ]
PROSITEi PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Iowa.
  2. "Integrated mapping, chromosomal sequencing and sequence analysis of Cryptosporidium parvum."
    Bankier A.T., Spriggs H.F., Fartmann B., Konfortov B.A., Madera M., Vogel C., Teichmann S.A., Ivens A., Dear P.H.
    Genome Res. 13:1787-1799(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Iowa.
  3. "Construction and analysis of full-length cDNA library of Cryptosporidium parvum."
    Yamagishi J., Wakaguri H., Sugano S., Kawano S., Fujisaki K., Sugimoto C., Watanabe J., Suzuki Y., Kimata I., Xuan X.
    Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: HNJ-1.
  4. "Cryptosporidium parvum IMP dehydrogenase: identification of functional, structural, and dynamic properties that can be exploited for drug design."
    Umejiego N.N., Li C., Riera T., Hedstrom L., Striepen B.
    J. Biol. Chem. 279:40320-40327(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ENZYME REGULATION.
  5. "The structural basis of Cryptosporidium-specific IMP dehydrogenase inhibitor selectivity."
    Macpherson I.S., Kirubakaran S., Gorla S.K., Riera T.V., D'Aquino J.A., Zhang M., Cuny G.D., Hedstrom L.
    J. Am. Chem. Soc. 132:1230-1231(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.19 ANGSTROMS).

Entry informationi

Entry nameiIMDH_CRYPV
AccessioniPrimary (citable) accession number: Q8T6T2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

Cryptosporidium IMPDH was acquired through lateral transfer from eubacteria, and predictably the sensitivity to MPA differs from that of mammalian IMPDH forms. This divergence of parasite and host enzymes is exploited to design more potent parasite-specific inhibitors.

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

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