SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q59Q46

- IMDH_CANAL

UniProt

Q59Q46 - IMDH_CANAL

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Inosine-5'-monophosphate dehydrogenase

Gene
IMH3, IMD3, CaO19.18, CaO19.7689
Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
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. Also inhibited by ADP.1 Publication

Kineticsi

  1. KM=60 µM for Inosine 5'-phosphate1 Publication
  2. KM=3500 µM for NAD+

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi328 – 3281Potassium; via carbonyl oxygen By similarity
Metal bindingi330 – 3301Potassium; via carbonyl oxygen By similarity
Binding sitei331 – 3311IMP By similarity
Active sitei333 – 3331Thioimidate intermediate By similarity
Metal bindingi333 – 3331Potassium; via carbonyl oxygen By similarity
Binding sitei447 – 4471IMP By similarity
Metal bindingi506 – 5061Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi507 – 5071Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi508 – 5081Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi276 – 2783NAD By similarity
Nucleotide bindingi326 – 3283NAD By similarity

GO - Molecular functioni

  1. adenyl nucleotide binding Source: InterPro
  2. IMP dehydrogenase activity Source: CGD
  3. metal ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. cellular response to drug Source: CGD
  2. cellular response to starvation Source: CGD
  3. filamentous growth Source: CGD
  4. filamentous growth of a population of unicellular organisms in response to biotic stimulus Source: CGD
  5. filamentous growth of a population of unicellular organisms in response to starvation Source: CGD
  6. GMP biosynthetic process Source: CGD
  7. induction by symbiont of host defense response Source: CGD
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
Name:IMH3
Synonyms:IMD3
ORF Names:CaO19.18, CaO19.7689
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
ProteomesiUP000000559: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0069897. IMH3.

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi251 – 2511A → 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. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 521521Inosine-5'-monophosphate dehydrogenaseUniRule annotationPRO_0000415684Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ59Q46.
SMRiQ59Q46. Positions 9-519.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini119 – 17860CBS 1Add
BLAST
Domaini182 – 23857CBS 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni366 – 3683IMP binding By similarity
Regioni389 – 3902IMP binding By similarity
Regioni413 – 4175IMP binding By similarity

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

KOiK00088.
OrthoDBiEOG793BHK.

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.

Q59Q46-1 [UniParc]FASTAAdd to Basket

« Hide

MVFETSKATS YLKDYPKKDG LSVKELIDST NFGGLTYNDF LILPGLINFP    50
SSAVSLETKL TKKITLKSPF VSSPMDTVTE ENMAIHMALL GGIGIIHHNC 100
TSEEQAEMVR KVKKYENGFI NDPVVISPEV TVGEVKKMGE VLGFTSFPVT 150
ENGKVGGKLV GIITSRDIQF HEDNKSPVSE VMTKDLVVGK KGISLTDGNE 200
LLRSSKKGKL PIVDAEGNLV SLISRTDLQK NQDYPNASKS FHSKQLLCGA 250
AIGTIDADRE RLDKLVEAGL DVVVLDSSNG SSVFQLNMIK WIKEKYPELQ 300
VIAGNVVTRE QAALLIEAGA DALRIGMGSG SICITQEVMA CGRPQGTAVY 350
GVTEFANKFG VPCIADGGIG NIGHITKALA LGASCVMMGG LLAGTAETPG 400
DYFYRDGKRL KTYRGMGSID AMQQTNTNAN ASTSRYFSEA DKVLVAQGVS 450
GSVVDKGSIT KFVPYLYNGL QHSLQDIGIK SIDELRENVD NGEIRFEFRT 500
ASAQFEGGVH GLHSYEKRLH N 521
Length:521
Mass (Da):56,239
Last modified:February 22, 2012 - v2
Checksum:i5F1E52611B1E1418
GO

Sequence cautioni

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 databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY864854 Genomic DNA. Translation: AAW65379.1.
AACQ01000181 Genomic DNA. Translation: EAK92581.1. Sequence problems.
AACQ01000180 Genomic DNA. Translation: EAK92603.1. Sequence problems.
RefSeqiXP_711803.1. XM_706711.1.
XP_711825.1. XM_706733.1.

Genome annotation databases

GeneIDi3646555.
3646575.
KEGGical:CaO19.18.
cal:CaO19.7689.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY864854 Genomic DNA. Translation: AAW65379.1 .
AACQ01000181 Genomic DNA. Translation: EAK92581.1 . Sequence problems.
AACQ01000180 Genomic DNA. Translation: EAK92603.1 . Sequence problems.
RefSeqi XP_711803.1. XM_706711.1.
XP_711825.1. XM_706733.1.

3D structure databases

ProteinModelPortali Q59Q46.
SMRi Q59Q46. Positions 9-519.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3646555.
3646575.
KEGGi cal:CaO19.18.
cal:CaO19.7689.

Organism-specific databases

CGDi CAL0069897. IMH3.

Phylogenomic databases

KOi K00088.
OrthoDBi EOG793BHK.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .

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

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SC5314 / ATCC MYA-2876.

Entry informationi

Entry nameiIMDH_CANAL
AccessioniPrimary (citable) accession number: Q59Q46
Secondary accession number(s): Q5G1M4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: February 22, 2012
Last modified: June 11, 2014
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi