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P21620 (IMDH_LEIDO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inosine-5'-monophosphate dehydrogenase

Short name=IMP dehydrogenase
Short name=IMPD
Short name=IMPDH
EC=1.1.1.205
OrganismLeishmania donovani
Taxonomic identifier5661 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Protein attributes

Sequence length514 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2

Catalytic activity

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH. HAMAP-Rule MF_03156

Cofactor

Potassium By similarity. HAMAP-Rule MF_03156

Enzyme regulation

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. Potently inhibited by MPA. Inhibited by XMP and GMP. Ref.2

Pathway

Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. HAMAP-Rule MF_03156

Subunit structure

Heterotetramer. Interacts with glycosomal protein sorting receptor PEX5. Ref.2

Subcellular location

Glycosome Ref.2.

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 2 CBS domains.

Biophysicochemical properties

Kinetic parameters:

KM=33 µM for Inosine 5'-phosphate Ref.2

KM=390 µM for NAD+

Ontologies

Keywords
   Biological processGMP biosynthesis
Purine biosynthesis
   Cellular componentGlycosome
Peroxisome
   DomainCBS domain
Repeat
   LigandMetal-binding
NAD
Potassium
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological_processGMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentglycosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionIMP dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

adenyl nucleotide binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 514514Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_03156
PRO_0000093675

Regions

Domain112 – 17160CBS 1
Domain175 – 23359CBS 2
Nucleotide binding270 – 2723NAD By similarity
Nucleotide binding320 – 3223NAD By similarity
Region360 – 3623IMP binding By similarity
Region383 – 3842IMP binding By similarity
Region407 – 4115IMP binding By similarity
Motif512 – 5143Microbody targeting signal Potential

Sites

Active site3271Thioimidate intermediate By similarity
Metal binding3221Potassium; via carbonyl oxygen By similarity
Metal binding3241Potassium; via carbonyl oxygen By similarity
Metal binding3271Potassium; via carbonyl oxygen By similarity
Metal binding4961Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4971Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4981Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site3251IMP By similarity
Binding site4371IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
P21620 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: E251FCC1362D60E5

FASTA51455,552
        10         20         30         40         50         60 
MATNNANYRI KTIKDGCTAE ELFRGDGLTY NDFIILPGFI DFGAADVNIS GQFTKRIRLH 

        70         80         90        100        110        120 
IPIVSSPMDT ITENEMAKTM ALMGGVGVLH NNCTVERQVE MVKSVKAYRN GFISKPKSVP 

       130        140        150        160        170        180 
PNTPISNIIR IKEEKGISGI LVTENGDPHG KLLGIVCTKD IDYVKNKDTP VSAVMTRREK 

       190        200        210        220        230        240 
MTVERAPIQL EEAMDVLNRS RYGYLPIVNE NDEVVNLCSR RDAVRARDYP HSTLDKSGRL 

       250        260        270        280        290        300 
ICAAATSTRP EDKRRVAALA DVGVDVLVLD SSQGNTIYQI AFIKWVKSTY PHLEVVAGNV 

       310        320        330        340        350        360 
VTQDQAKNLI DAGADGIRIG MGSGSICITQ EVLACGRPQG TAVYKVAQYC ASRGVPCTAD 

       370        380        390        400        410        420 
GGLRQVGDIC KALAIGANCA MLGGMLSGTT ETPGEYFFKG GVRLKVYRGM GSLEAMSQGK 

       430        440        450        460        470        480 
ESGKRYLSEN EAVQVAQGVS GNVVDKGSAA KLIAYVSKGL QQSAQDIGEI SFDAIREKMY 

       490        500        510 
AGQVLFSRRS PTAQGEGGVH SLHSYEKKLF AAKM 

« Hide

References

[1]"Amplification and molecular cloning of the IMP dehydrogenase gene of Leishmania donovani."
Wilson K.E., Collart F.R., Huberman E., Stringer J.R., Ullman B.
J. Biol. Chem. 266:1665-1671(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Kinetic characterization of inosine monophosphate dehydrogenase of Leishmania donovani."
Dobie F., Berg A., Boitz J.M., Jardim A.
Mol. Biochem. Parasitol. 152:11-21(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH PEX5, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55667 Genomic DNA. Translation: AAA29253.1.
PIRA38668.
RefSeqXP_003860332.1. XM_003860284.1.

3D structure databases

ProteinModelPortalP21620.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID13386143.
KEGGldo:LDBPK_191590.

Phylogenomic databases

KOK00088.

Enzyme and pathway databases

UniPathwayUPA00601; UER00295.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01964. IMPDH.
InterProIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERPTHR11911:SF6. PTHR11911:SF6. 1 hit.
PfamPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFPIRSF000130. IMPDH. 1 hit.
SMARTSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsTIGR01302. IMP_dehydrog. 1 hit.
PROSITEPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIMDH_LEIDO
AccessionPrimary (citable) accession number: P21620
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: February 19, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways