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Q5KP44 (IMDH_CRYNJ) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Ordered Locus Names:CNA04240
OrganismCryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans) [Reference proteome]
Taxonomic identifier214684 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTremellalesTremellaceaeFilobasidiellaFilobasidiella/Cryptococcus neoformans species complex

Protein attributes

Sequence length544 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_03156

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 By similarity. HAMAP-Rule MF_03156

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.

Ontologies

Keywords
   Biological processGMP biosynthesis
Purine biosynthesis
   Cellular componentCytoplasm
   DomainCBS domain
Repeat
   LigandMetal-binding
NAD
Potassium
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionIMP dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

adenyl nucleotide binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 544544Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_03156
PRO_0000415685

Regions

Domain132 – 19261CBS 1
Domain194 – 25057CBS 2
Nucleotide binding288 – 2903NAD By similarity
Nucleotide binding338 – 3403NAD By similarity
Region378 – 3803IMP binding By similarity
Region401 – 4022IMP binding By similarity
Region425 – 4295IMP binding By similarity

Sites

Active site3451Thioimidate intermediate By similarity
Metal binding3401Potassium; via carbonyl oxygen By similarity
Metal binding3421Potassium; via carbonyl oxygen By similarity
Metal binding3451Potassium; via carbonyl oxygen By similarity
Metal binding5291Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5301Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5311Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site3431IMP By similarity
Binding site4701IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5KP44 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: E5AB349D78F302AB

FASTA54457,899
        10         20         30         40         50         60 
MADTNPNAPP RSDSLLNPAD ALKYLEEYPR GDGLSLQELM DSRKNGGLTY NDFLVLPGHI 

        70         80         90        100        110        120 
SFPASDVSLQ SRATKNIVLN TPFLSSPMDT VTEDRMAIAL ALHGGLGIIH HNCSAEEQAA 

       130        140        150        160        170        180 
MVRRVKKYEN GFITDPLCLG PDATVGDVLE IKAKFGFCGV PITETGAPNS KLLGIVTGRD 

       190        200        210        220        230        240 
VQFQDAETPI KSVMTTEVVT GSSPITLEKA NSLLRETKKG KLPIVDSNGH LVSLVARSDL 

       250        260        270        280        290        300 
LKNQNYPYAS KVPESKQLYC GAAIGTRPGD KDRLKLLAEA GLDVVVLDSS QGDSVYQIEF 

       310        320        330        340        350        360 
IKWIKQTYPK IEIIAGNVVT REQAAQLIAA GADGLRIGMG SGSICITQEV MAVGRPQGTA 

       370        380        390        400        410        420 
VYAVAEFASR FGIPCIADGG IGNIGHIAKA LALGASAVMM GGLLAGTTES PGEYFYHEGK 

       430        440        450        460        470        480 
RVKVYRGMGS IEAMEHTQRG SASGKRSILN LDNAATARYF SEADAVKVAQ GVSGDVADKG 

       490        500        510        520        530        540 
SINKFVPYLF TGLQHSFQDA GVKSVSELHS CARSGSLRFE LRTASAQLEG GVHGLNSYTK 


RLFA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017341 Genomic DNA. Translation: AAW40949.1.
RefSeqXP_566768.1. XM_566768.1.
UniGeneFne.7688.

3D structure databases

ProteinModelPortalQ5KP44.
SMRQ5KP44. Positions 28-129, 242-543.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING214684.CNA04240.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiAAW40949; AAW40949; CNA04240.
GeneID3253376.
KEGGcne:CNA04240.

Phylogenomic databases

HOGENOMHOG000165752.
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_CRYNJ
AccessionPrimary (citable) accession number: Q5KP44
Secondary accession number(s): Q55ZT3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: February 15, 2005
Last modified: June 11, 2014
This is version 82 of the entry and version 1 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