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Q59Q46 (IMDH_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Gene names
Name:IMH3
Synonyms:IMD3
ORF Names:CaO19.18, CaO19.7689
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length521 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.1

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. Also inhibited by ADP. Ref.1

Pathway

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

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_03156

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03156.

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 2 CBS domains.

Biophysicochemical properties

Kinetic parameters:

KM=60 µM for Inosine 5'-phosphate Ref.1

KM=3500 µM for NAD+

Sequence caution

The sequence EAK92581.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EAK92603.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 521521Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_03156
PRO_0000415684

Regions

Domain119 – 17860CBS 1
Domain182 – 23857CBS 2
Nucleotide binding276 – 2783NAD By similarity
Nucleotide binding326 – 3283NAD By similarity
Region366 – 3683IMP binding By similarity
Region389 – 3902IMP binding By similarity
Region413 – 4175IMP binding By similarity

Sites

Active site3331Thioimidate intermediate By similarity
Metal binding3281Potassium; via carbonyl oxygen By similarity
Metal binding3301Potassium; via carbonyl oxygen By similarity
Metal binding3331Potassium; via carbonyl oxygen By similarity
Metal binding5061Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5071Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5081Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site3311IMP By similarity
Binding site4471IMP By similarity

Experimental info

Mutagenesis2511A → T in MPA-resistant strain; decreases the K(M) values for both substrates. Decreases sensitivity to MPA 4-fold, but increases sensitivity to mizoribine monophosphate 40-fold. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q59Q46 [UniParc].

Last modified February 22, 2012. Version 2.
Checksum: 5F1E52611B1E1418

FASTA52156,239
        10         20         30         40         50         60 
MVFETSKATS YLKDYPKKDG LSVKELIDST NFGGLTYNDF LILPGLINFP SSAVSLETKL 

        70         80         90        100        110        120 
TKKITLKSPF VSSPMDTVTE ENMAIHMALL GGIGIIHHNC TSEEQAEMVR KVKKYENGFI 

       130        140        150        160        170        180 
NDPVVISPEV TVGEVKKMGE VLGFTSFPVT ENGKVGGKLV GIITSRDIQF HEDNKSPVSE 

       190        200        210        220        230        240 
VMTKDLVVGK KGISLTDGNE LLRSSKKGKL PIVDAEGNLV SLISRTDLQK NQDYPNASKS 

       250        260        270        280        290        300 
FHSKQLLCGA AIGTIDADRE RLDKLVEAGL DVVVLDSSNG SSVFQLNMIK WIKEKYPELQ 

       310        320        330        340        350        360 
VIAGNVVTRE QAALLIEAGA DALRIGMGSG SICITQEVMA CGRPQGTAVY GVTEFANKFG 

       370        380        390        400        410        420 
VPCIADGGIG NIGHITKALA LGASCVMMGG LLAGTAETPG DYFYRDGKRL KTYRGMGSID 

       430        440        450        460        470        480 
AMQQTNTNAN ASTSRYFSEA DKVLVAQGVS GSVVDKGSIT KFVPYLYNGL QHSLQDIGIK 

       490        500        510        520 
SIDELRENVD NGEIRFEFRT ASAQFEGGVH GLHSYEKRLH N 

« Hide

References

« Hide 'large scale' references
[1]"The functional basis of mycophenolic acid resistance in Candida albicans IMP dehydrogenase."
Koehler G.A., Gong X., Bentink S., Theiss S., Pagani G.M., Agabian N., Hedstrom L.
J. Biol. Chem. 280:11295-11302(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ENZYME REGULATION, MUTAGENESIS OF ALA-251, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: SC5314 / CAI4 / ATCC MYA-682.
[2]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY864854 Genomic DNA. Translation: AAW65379.1.
AACQ01000181 Genomic DNA. Translation: EAK92581.1. Sequence problems.
AACQ01000180 Genomic DNA. Translation: EAK92603.1. Sequence problems.
RefSeqXP_711803.1. XM_706711.1.
XP_711825.1. XM_706733.1.

3D structure databases

ProteinModelPortalQ59Q46.
SMRQ59Q46. Positions 9-519.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3646555.
3646575.
KEGGcal:CaO19.18.
cal:CaO19.7689.

Organism-specific databases

CGDCAL0069897. IMH3.

Phylogenomic databases

KOK00088.
OrthoDBEOG793BHK.

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_CANAL
AccessionPrimary (citable) accession number: Q59Q46
Secondary accession number(s): Q5G1M4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: February 22, 2012
Last modified: April 16, 2014
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Candida albicans

Candida albicans: entries and gene names