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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

G210_1330

Organism
Candida maltosa (strain Xu316) (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

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Catalytic activityi

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

Cofactori

K+UniRule annotation

Activity 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 (G210_1330)
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 bindingi327Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi329Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei330IMPUniRule annotation1
Active sitei332Thioimidate intermediateUniRule annotation1
Metal bindingi332Potassium; via carbonyl oxygenUniRule annotation1
Active sitei434Proton acceptorUniRule annotation1
Binding sitei446IMPUniRule annotation1
Metal bindingi501Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi275 – 277NADUniRule annotation3
Nucleotide bindingi325 – 327NADUniRule 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

UniPathwayi
UPA00601;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
ORF Names:G210_1330Imported
OrganismiCandida maltosa (strain Xu316) (Yeast)Imported
Taxonomic identifieri1245528 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000011777 Componenti: Unassembled WGS sequence

Subcellular locationi

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini119 – 177CBSInterPro annotationAdd BLAST59
Domaini181 – 237CBSInterPro annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni365 – 367IMP bindingUniRule annotation3
Regioni388 – 389IMP bindingUniRule annotation2
Regioni412 – 416IMP bindingUniRule annotation5

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation

Keywords - Domaini

CBS domainPROSITE-ProRule annotation

Phylogenomic databases

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.

M3IVR6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAFETTKATS YLKEYPKKDG LSVKELIDST NFGGLTYNDF LVLPGLINFP
60 70 80 90 100
SSAVSLETRL TKKITLKSPF VSSPMDTVTE ENMAIHMALL GGIGIIHHNC
110 120 130 140 150
SAEEQAEMVR KVKKYENGFI NDPVVISPDV TVGEVKKMGE VLGFTSFPVT
160 170 180 190 200
SGKIGGKLVG IITSRDIQFH EDNASKVGDI MTTDLVVGKQ GITLNEGNET
210 220 230 240 250
LRSSKKGKLP IVDAKGNLVS LISRTDLQKN QDYPNASKSF HSKQLLCGAA
260 270 280 290 300
IGTIDADKER LAKLVEAGLD VVVLDSSNGS SVFQLNMIKW IKETYPELQV
310 320 330 340 350
IAGNVVTREQ AALLIEAGAD GLRIGMGSGS ICITQEVMAC GRPQGTAVFA
360 370 380 390 400
VTEFANKFGV PCIADGGIGN IGHITKALAL GASCVMMGGL LAGTSETPGD
410 420 430 440 450
YFYRDGKRLK TYRGMGSIDA MQQTNTNANA STSRYFSEAD KVLVAQGVSG
460 470 480 490 500
SVVDKGSITK FVPYLFNGLQ HSLQDIGMKS IDELRSSVDA GEVRFEFRTA
510 520
SAQFEGGVHG LHSYEKRLHN
Length:520
Mass (Da):55,789
Last modified:May 1, 2013 - v1
Checksum:iFCC2EDAFCC1DED9B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AOGT01000137 Genomic DNA Translation: EMG50726.1

Genome annotation databases

EnsemblFungiiEMG50726; EMG50726; G210_1330

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AOGT01000137 Genomic DNA Translation: EMG50726.1

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEMG50726; EMG50726; G210_1330

Phylogenomic databases

OrthoDBiEOG092C1U8P

Enzyme and pathway databases

UniPathwayi
UPA00601;UER00295

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
ProtoNetiSearch...

Entry informationi

Entry nameiM3IVR6_CANMX
AccessioniPrimary (citable) accession number: M3IVR6
Entry historyiIntegrated into UniProtKB/TrEMBL: May 1, 2013
Last sequence update: May 1, 2013
Last modified: September 12, 2018
This is version 34 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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