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Q84XA3 (IMDH_VIGUN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. 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
Name:impdh
OrganismVigna unguiculata (Cowpea)
Taxonomic identifier3917 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

Protein attributes

Sequence length502 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.2

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. Ref.2

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03156.

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 1 CBS domain.

Biophysicochemical properties

Kinetic parameters:

KM=9.1 µM for Inosine 5'-phosphate Ref.2

KM=18 µM for NAD+

KM=1.6 mM for K+

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionIMP dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 502502Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_03156
PRO_0000415681

Regions

Domain168 – 22457CBS
Nucleotide binding264 – 2663NAD By similarity
Nucleotide binding314 – 3163NAD By similarity
Region354 – 3563IMP binding By similarity
Region377 – 3782IMP binding By similarity
Region401 – 4055IMP binding By similarity

Sites

Active site3211Thioimidate intermediate By similarity
Metal binding3161Potassium; via carbonyl oxygen By similarity
Metal binding3181Potassium; via carbonyl oxygen By similarity
Metal binding3211Potassium; via carbonyl oxygen By similarity
Metal binding4881Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4891Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4901Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site3191IMP By similarity
Binding site4291IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q84XA3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 61773EBE986FFD30

FASTA50253,450
        10         20         30         40         50         60 
MDFTPPPIED GFTAEKLFSQ GFSYTYDDVI FLPHYIDFAA DAVDLSTRLT RRLPLAVPLV 

        70         80         90        100        110        120 
ASPMDTVSES AMASAMASLG GIAIVHSNVP AAAQASLVRA AKSRRVPILS EPAFAAPSAV 

       130        140        150        160        170        180 
IEHEDDFAAS PFLLVTDIGA AGGKLLGYVA KRDWTNQKDK SLRVGDYMAP PPRRAPWNAD 

       190        200        210        220        230        240 
LNKIHEIMEN EKSGAVALER DGEVVDLVVR EEVERVKGYP KLAAPATVGP DGEFMVGAAM 

       250        260        270        280        290        300 
GTREDDKERL KHLVKAGVNV VVLDSSQGNS IYQLEMVKYV KSVYPELDVI GGNVVTMYQA 

       310        320        330        340        350        360 
ENLIQAGVDG LRVGMGSGSI CTTQEVCAVG RGQATAVYKV SSIAYKSGVP VIADGGISNS 

       370        380        390        400        410        420 
GHIVKALSLG ASTAMMGSFL AGSHEAPGAY VYQNGQRVKK YRGMGSLEAM TKGSDARYLG 

       430        440        450        460        470        480 
DTAKLKIAQG VVGAVKDKGS VLNFIPYTLQ AVRQGFQDIG ASSLQSAHDL LRSRVLRLEV 

       490        500 
RTGAAQVEGG VHGLVSYEKK YY 

« Hide

References

[1]"Vuimpdh mRNA from cowpea encoding inosine monophosphate dehydrogenase."
Mann A.J., Smith P.M.C., Bussell J.D.
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Root nodule.
[2]"Purification and properties of inosine monophosphate oxidoreductase from nitrogen-fixing nodules of cowpea (Vigna unguiculata L. Walp)."
Atkins C.A., Shelp B.J., Storer P.J.
Arch. Biochem. Biophys. 236:807-814(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY193837 mRNA. Translation: AAO40253.1.

3D structure databases

ProteinModelPortalQ84XA3.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

ProMEXQ84XA3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00601; UER00295.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01964. IMPDH.
InterProIPR013785. Aldolase_TIM.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERPTHR11911:SF6. PTHR11911:SF6. 1 hit.
PfamPF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFPIRSF000130. IMPDH. 1 hit.
TIGRFAMsTIGR01302. IMP_dehydrog. 1 hit.
PROSITEPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIMDH_VIGUN
AccessionPrimary (citable) accession number: Q84XA3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways