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Q9GZH3 (IMDH_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
ORF Names:T22D1.3
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length534 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 – 534534Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_03156
PRO_0000415680

Regions

Domain117 – 18165CBS 1
Domain190 – 25566CBS 2
Nucleotide binding292 – 2943NAD By similarity
Nucleotide binding342 – 3443NAD By similarity
Region382 – 3843IMP binding By similarity
Region405 – 4062IMP binding By similarity
Region430 – 4345IMP binding By similarity

Sites

Active site3491Thioimidate intermediate By similarity
Metal binding3441Potassium; via carbonyl oxygen By similarity
Metal binding3461Potassium; via carbonyl oxygen By similarity
Metal binding3491Potassium; via carbonyl oxygen By similarity
Metal binding5201Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5211Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5221Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site3471IMP By similarity
Binding site4611IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9GZH3 [UniParc].

Last modified March 1, 2002. Version 2.
Checksum: 9462FBEE9119FD0B

FASTA53458,170
        10         20         30         40         50         60 
MVRPEDFNSL ELDNSLTDGE TVHEMMAHKA GLTYNDFNIL PGFINFGVHD VSLETNITKD 

        70         80         90        100        110        120 
LKIKAPLVSS PMDTVTESGM AIVMALYGGI GIIHGNFPKP EDQAAEVLKV KRFKQGYVMQ 

       130        140        150        160        170        180 
PHCLSRDSTA FDMIQIKKKY GYTGAPVTED GRVGSKLIGM VTSRDFDFIT MDVAGQKGTP 

       190        200        210        220        230        240 
ISDTNDVTPT TPITRIMVSV DQLHLGHIND APELSQKKLK EHRLGKLPIV NDNGELCALL 

       250        260        270        280        290        300 
CRSDLLKARD YPMASYDSKG QLLCGAAVNT RGESQYTVDR VVEAGVDVLI IDSSNGSSTY 

       310        320        330        340        350        360 
QISMLRYIKE KHPHVQVIAG NVVTRAQAKL LIDQGADGLR IGMGSGSICI TQDVMAVGRA 

       370        380        390        400        410        420 
QGTAVYDVAR YANQRGIPIV ADGGIRDVGY ITKAISLGAS AVMMGGLLAA TTEAPGEYFW 

       430        440        450        460        470        480 
GPGGVRVKKY RGMGSLDAME AHASSQDRYF TAESDQIKVA QGVSATMKDR GSCHKFIPYL 

       490        500        510        520        530 
IRGVQHGMQD IGVRSLRDFR EKVDNGIVKF ERRSTNAQLE GGVHSLHSFE KRLY 

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References

[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FO080211 Genomic DNA. Translation: CCD62017.1.
RefSeqNP_001023395.1. NM_001028224.3.
UniGeneCel.17245.

3D structure databases

ProteinModelPortalQ9GZH3.
SMRQ9GZH3. Positions 18-534.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9GZH3. 1 interaction.

Proteomic databases

PRIDEQ9GZH3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaT22D1.3a; T22D1.3a; WBGene00020682.
GeneID177457.
KEGGcel:CELE_T22D1.3.
UCSCT22D1.3b.1. c. elegans.

Organism-specific databases

CTD177457.
WormBaseT22D1.3a; CE30188; WBGene00020682.

Phylogenomic databases

GeneTreeENSGT00530000062923.
HOGENOMHOG000165752.
InParanoidQ9GZH3.
KOK00088.
OMAIMATYRI.
PhylomeDBQ9GZH3.

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...

Other

NextBio896908.
PROQ9GZH3.

Entry information

Entry nameIMDH_CAEEL
AccessionPrimary (citable) accession number: Q9GZH3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: March 1, 2002
Last modified: June 11, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase