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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

IMD1

Organism
Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841) (Yeast)
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

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 annotation

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.UniRule annotation

Pathwayi: XMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Inosine-5'-monophosphate dehydrogenase (IMD1)
This subpathway is part of the pathway XMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from IMP, the pathway XMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi328Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi330Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei331IMPUniRule annotation1
Active sitei333Thioimidate intermediateUniRule annotation1
Metal bindingi333Potassium; via carbonyl oxygenUniRule annotation1
Active sitei435Proton acceptorUniRule annotation1
Binding sitei447IMPUniRule annotation1
Metal bindingi502Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi276 – 278NADUniRule annotation3
Nucleotide bindingi326 – 328NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductaseUniRule annotation
Biological processGMP biosynthesisUniRule annotation, Purine biosynthesis
LigandMetal-bindingUniRule annotation, NADUniRule annotation, PotassiumUniRule annotation

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:IMD1Imported
Ordered Locus Names:Cd36_20770Imported
ORF Names:CD36_20770Imported
OrganismiCandida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841) (Yeast)Imported
Taxonomic identifieri573826 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000002605 Componenti: Chromosome 2

Organism-specific databases

CGDiCAL0000160447. Cd36_20770.

Subcellular locationi

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi573826.XP_002418556.1.

Structurei

3D structure databases

ProteinModelPortaliB9WBT6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini119 – 178CBSInterPro annotationAdd BLAST60
Domaini182 – 238CBSInterPro annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni366 – 368IMP bindingUniRule annotation3
Regioni389 – 390IMP bindingUniRule annotation2
Regioni413 – 417IMP bindingUniRule annotation5

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation

Keywords - Domaini

CBS domainPROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2550. Eukaryota.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165752.
KOiK00088.
OrthoDBiEOG092C1U8P.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 2 hits.
HAMAPiMF_01964. IMPDH. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
PfamiView protein in Pfam
PF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
PIRSFiPIRSF000130. IMPDH. 1 hit.
SMARTiView protein in SMART
SM00116. CBS. 2 hits.
TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
PROSITEiView protein in PROSITE
PS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.

Sequencei

Sequence statusi: Complete.

B9WBT6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVFEASKATS YLKDYPKKDG LSVKELIDST NFGGLTYNDF LVLPGLINFP
60 70 80 90 100
SSAVSLETKL TKKITLKSPF VSSPMDTVTE ENMAIHMALL GGIGIIHHNC
110 120 130 140 150
TADEQAEMVR KVKKYENGFI NDPVVISPEV TVGEVKKMHE TLGFTSFPVT
160 170 180 190 200
ENGKVGGKLV GIITSRDIQF HEDDKSPVSE VMTRDLVVGK KGISLTDGNE
210 220 230 240 250
LLRSSKKGKL PIVDDEGNLV SLISRTDLQK NQDYPNASKS FHSKQLLCGA
260 270 280 290 300
AIGTIDADKE RLDKLVEAGL DVVVLDSSNG SSIFQLNMIK WIKEKYPELQ
310 320 330 340 350
VIAGNVVTRE QAALLIEAGA DALRIGMGSG SICITQEVMA CGRPQGTAVY
360 370 380 390 400
GVTEFSNKFG VPCIADGGIG NIGHITKALA LGASCVMMGG LLAGTAETPG
410 420 430 440 450
DYFYRDGKRL KTYRGMGSID AMQQTSSSAN ASTSRYFSEA DKVLVAQGVS
460 470 480 490 500
GSVVDKGSIT KFVPYLYNGL QHSLQDIGIK SIDELRQNVD NGEVRFEFRT
510 520
ASAQFEGGVH GLHSYEKRLH N
Length:521
Mass (Da):56,239
Last modified:March 24, 2009 - v1
Checksum:i6DBD9033A6E1FB51
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM992689 Genomic DNA. Translation: CAX43858.1.
RefSeqiXP_002418556.1. XM_002418511.1.

Genome annotation databases

EnsemblFungiiCAX43858; CAX43858; CD36_20770.
GeneIDi8046101.
KEGGicdu:CD36_20770.

Similar proteinsi

Entry informationi

Entry nameiB9WBT6_CANDC
AccessioniPrimary (citable) accession number: B9WBT6
Entry historyiIntegrated into UniProtKB/TrEMBL: March 24, 2009
Last sequence update: March 24, 2009
Last modified: March 28, 2018
This is version 71 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation

Keywords - Technical termi

Complete proteomeImported