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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

IMH3

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: 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.UniRule annotation1 Publication

Catalytic activityi

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

Cofactori

K(+)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.UniRule annotation1 Publication

Kineticsi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi328 – 3281Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi330 – 3301Potassium; via carbonyl oxygenUniRule annotation
Binding sitei331 – 3311IMPUniRule annotation
Active sitei333 – 3331Thioimidate intermediateUniRule annotation
Metal bindingi333 – 3331Potassium; via carbonyl oxygenUniRule annotation
Binding sitei447 – 4471IMPUniRule annotation
Metal bindingi506 – 5061Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi507 – 5071Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi508 – 5081Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi276 – 2783NADUniRule annotation
Nucleotide bindingi326 – 3283NADUniRule annotation

GO - Molecular functioni

  1. IMP dehydrogenase activity Source: CGD
  2. metal ion binding Source: UniProtKB-HAMAP
  3. nucleotide 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: UniProtKB-HAMAP
  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 dehydrogenaseUniRule annotation (EC:1.1.1.205UniRule annotation)
Short name:
IMP dehydrogenaseUniRule annotation
Short name:
IMPDUniRule annotation
Short name:
IMPDHUniRule annotation
Gene namesi
Name:IMH3
Synonyms:IMD3
ORF Names:CaO19.18, CaO19.7689
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
ProteomesiUP000000559: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0069897. IMH3.

Subcellular locationi

Cytoplasm 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 dehydrogenasePRO_0000415684Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ59Q46.
SMRiQ59Q46. Positions 9-519.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni366 – 3683IMP bindingUniRule annotation
Regioni389 – 3902IMP bindingUniRule annotation
Regioni413 – 4175IMP bindingUniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

InParanoidiQ59Q46.
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

        10         20         30         40         50
MVFETSKATS YLKDYPKKDG LSVKELIDST NFGGLTYNDF LILPGLINFP
60 70 80 90 100
SSAVSLETKL TKKITLKSPF VSSPMDTVTE ENMAIHMALL GGIGIIHHNC
110 120 130 140 150
TSEEQAEMVR KVKKYENGFI NDPVVISPEV TVGEVKKMGE VLGFTSFPVT
160 170 180 190 200
ENGKVGGKLV GIITSRDIQF HEDNKSPVSE VMTKDLVVGK KGISLTDGNE
210 220 230 240 250
LLRSSKKGKL PIVDAEGNLV SLISRTDLQK NQDYPNASKS FHSKQLLCGA
260 270 280 290 300
AIGTIDADRE RLDKLVEAGL DVVVLDSSNG SSVFQLNMIK WIKEKYPELQ
310 320 330 340 350
VIAGNVVTRE QAALLIEAGA DALRIGMGSG SICITQEVMA CGRPQGTAVY
360 370 380 390 400
GVTEFANKFG VPCIADGGIG NIGHITKALA LGASCVMMGG LLAGTAETPG
410 420 430 440 450
DYFYRDGKRL KTYRGMGSID AMQQTNTNAN ASTSRYFSEA DKVLVAQGVS
460 470 480 490 500
GSVVDKGSIT KFVPYLYNGL QHSLQDIGIK SIDELRENVD NGEIRFEFRT
510 520
ASAQFEGGVH GLHSYEKRLH N
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. Curated
The sequence EAK92603.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ59Q46.
SMRiQ59Q46. Positions 9-519.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CGDiCAL0069897. IMH3.

Phylogenomic databases

InParanoidiQ59Q46.
KOiK00088.
OrthoDBiEOG793BHK.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.

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]
ProtoNetiSearch...

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: March 4, 2015
This is version 76 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.