Skip Header

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

Inosine-5'-monophosphate dehydrogenase

Gene

CNA04240

Organism
Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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 (CNA04240)
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 bindingi340Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi342Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei343IMPUniRule annotation1
Active sitei345Thioimidate intermediateUniRule annotation1
Metal bindingi345Potassium; via carbonyl oxygenUniRule annotation1
Active sitei458Proton acceptorUniRule annotation1
Binding sitei470IMPUniRule annotation1
Metal bindingi529Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi530Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi531Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi288 – 290NADUniRule annotation3
Nucleotide bindingi338 – 340NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

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
Ordered Locus Names:CNA04240
OrganismiCryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans)
Taxonomic identifieri214684 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTremellalesCryptococcaceaeCryptococcusCryptococcus neoformans species complex
Proteomesi
  • UP000002149 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiFungiDB:CNA04240.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004156851 – 544Inosine-5'-monophosphate dehydrogenaseAdd BLAST544

Proteomic databases

PaxDbiQ5KP44.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi214684.XP_566768.1.

Structurei

3D structure databases

ProteinModelPortaliQ5KP44.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini132 – 192CBS 1UniRule annotationAdd BLAST61
Domaini194 – 250CBS 2UniRule annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni378 – 380IMP bindingUniRule annotation3
Regioni401 – 402IMP bindingUniRule annotation2
Regioni425 – 429IMP bindingUniRule annotation5

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiKOG2550. Eukaryota.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165752.
InParanoidiQ5KP44.
KOiK00088.
OMAiYLEEYPR.
OrthoDBiEOG092C1U8P.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH. 1 hit.
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. 3 hits.
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.

Q5KP44-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADTNPNAPP RSDSLLNPAD ALKYLEEYPR GDGLSLQELM DSRKNGGLTY
60 70 80 90 100
NDFLVLPGHI SFPASDVSLQ SRATKNIVLN TPFLSSPMDT VTEDRMAIAL
110 120 130 140 150
ALHGGLGIIH HNCSAEEQAA MVRRVKKYEN GFITDPLCLG PDATVGDVLE
160 170 180 190 200
IKAKFGFCGV PITETGAPNS KLLGIVTGRD VQFQDAETPI KSVMTTEVVT
210 220 230 240 250
GSSPITLEKA NSLLRETKKG KLPIVDSNGH LVSLVARSDL LKNQNYPYAS
260 270 280 290 300
KVPESKQLYC GAAIGTRPGD KDRLKLLAEA GLDVVVLDSS QGDSVYQIEF
310 320 330 340 350
IKWIKQTYPK IEIIAGNVVT REQAAQLIAA GADGLRIGMG SGSICITQEV
360 370 380 390 400
MAVGRPQGTA VYAVAEFASR FGIPCIADGG IGNIGHIAKA LALGASAVMM
410 420 430 440 450
GGLLAGTTES PGEYFYHEGK RVKVYRGMGS IEAMEHTQRG SASGKRSILN
460 470 480 490 500
LDNAATARYF SEADAVKVAQ GVSGDVADKG SINKFVPYLF TGLQHSFQDA
510 520 530 540
GVKSVSELHS CARSGSLRFE LRTASAQLEG GVHGLNSYTK RLFA
Length:544
Mass (Da):57,899
Last modified:February 15, 2005 - v1
Checksum:iE5AB349D78F302AB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017341 Genomic DNA. Translation: AAW40949.1.
RefSeqiXP_566768.1. XM_566768.1.
UniGeneiFne.7688.

Genome annotation databases

EnsemblFungiiAAW40949; AAW40949; CNA04240.
GeneIDi3253376.
KEGGicne:CNA04240.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017341 Genomic DNA. Translation: AAW40949.1.
RefSeqiXP_566768.1. XM_566768.1.
UniGeneiFne.7688.

3D structure databases

ProteinModelPortaliQ5KP44.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi214684.XP_566768.1.

Proteomic databases

PaxDbiQ5KP44.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiAAW40949; AAW40949; CNA04240.
GeneIDi3253376.
KEGGicne:CNA04240.

Organism-specific databases

EuPathDBiFungiDB:CNA04240.

Phylogenomic databases

eggNOGiKOG2550. Eukaryota.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165752.
InParanoidiQ5KP44.
KOiK00088.
OMAiYLEEYPR.
OrthoDBiEOG092C1U8P.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH. 1 hit.
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. 3 hits.
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...

Entry informationi

Entry nameiIMDH_CRYNJ
AccessioniPrimary (citable) accession number: Q5KP44
Secondary accession number(s): Q55ZT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: February 15, 2005
Last modified: November 2, 2016
This is version 100 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.