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Q84XA3

- IMDH_VIGUN

UniProt

Q84XA3 - IMDH_VIGUN

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Protein
Inosine-5'-monophosphate dehydrogenase
Gene
impdh
Organism
Vigna unguiculata (Cowpea)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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.1 Publication

Catalytic activityi

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

Cofactori

Potassium By similarity.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 By similarity.UniRule annotation

Kineticsi

  1. KM=9.1 µM for Inosine 5'-phosphate1 Publication
  2. KM=18 µM for NAD+
  3. KM=1.6 mM for K+

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi316 – 3161Potassium; via carbonyl oxygen By similarity
Metal bindingi318 – 3181Potassium; via carbonyl oxygen By similarity
Binding sitei319 – 3191IMP By similarity
Active sitei321 – 3211Thioimidate intermediate By similarity
Metal bindingi321 – 3211Potassium; via carbonyl oxygen By similarity
Binding sitei429 – 4291IMP By similarity
Metal bindingi488 – 4881Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi489 – 4891Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi490 – 4901Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi264 – 2663NAD By similarity
Nucleotide bindingi314 – 3163NAD By similarity

GO - Molecular functioni

  1. IMP dehydrogenase activity Source: UniProtKB-HAMAP
  2. metal ion binding Source: UniProtKB-HAMAP
  3. nucleotide binding Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

  1. GMP biosynthetic process Source: UniProtKB-HAMAP
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 dehydrogenase (EC:1.1.1.205)
Short name:
IMP dehydrogenase
Short name:
IMPD
Short name:
IMPDH
Gene namesi
Name:impdh
OrganismiVigna unguiculata (Cowpea)
Taxonomic identifieri3917 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 502502Inosine-5'-monophosphate dehydrogenaseUniRule annotation
PRO_0000415681Add
BLAST

Proteomic databases

ProMEXiQ84XA3.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ84XA3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini168 – 22457CBS
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni354 – 3563IMP binding By similarity
Regioni377 – 3782IMP binding By similarity
Regioni401 – 4055IMP binding By similarity

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.
Contains 1 CBS domain.

Keywords - Domaini

CBS domain

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH.
InterProiIPR013785. Aldolase_TIM.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERiPTHR11911:SF6. PTHR11911:SF6. 1 hit.
PfamiPF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFiPIRSF000130. IMPDH. 1 hit.
TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
PROSITEiPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q84XA3-1 [UniParc]FASTAAdd to Basket

« Hide

MDFTPPPIED GFTAEKLFSQ GFSYTYDDVI FLPHYIDFAA DAVDLSTRLT    50
RRLPLAVPLV ASPMDTVSES AMASAMASLG GIAIVHSNVP AAAQASLVRA 100
AKSRRVPILS EPAFAAPSAV IEHEDDFAAS PFLLVTDIGA AGGKLLGYVA 150
KRDWTNQKDK SLRVGDYMAP PPRRAPWNAD LNKIHEIMEN EKSGAVALER 200
DGEVVDLVVR EEVERVKGYP KLAAPATVGP DGEFMVGAAM GTREDDKERL 250
KHLVKAGVNV VVLDSSQGNS IYQLEMVKYV KSVYPELDVI GGNVVTMYQA 300
ENLIQAGVDG LRVGMGSGSI CTTQEVCAVG RGQATAVYKV SSIAYKSGVP 350
VIADGGISNS GHIVKALSLG ASTAMMGSFL AGSHEAPGAY VYQNGQRVKK 400
YRGMGSLEAM TKGSDARYLG DTAKLKIAQG VVGAVKDKGS VLNFIPYTLQ 450
AVRQGFQDIG ASSLQSAHDL LRSRVLRLEV RTGAAQVEGG VHGLVSYEKK 500
YY 502
Length:502
Mass (Da):53,450
Last modified:June 1, 2003 - v1
Checksum:i61773EBE986FFD30
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY193837 mRNA. Translation: AAO40253.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY193837 mRNA. Translation: AAO40253.1 .

3D structure databases

ProteinModelPortali Q84XA3.
ModBasei Search...

Proteomic databases

ProMEXi Q84XA3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01964. IMPDH.
InterProi IPR013785. Aldolase_TIM.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view ]
PANTHERi PTHR11911:SF6. PTHR11911:SF6. 1 hit.
Pfami PF00478. IMPDH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000130. IMPDH. 1 hit.
TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
PROSITEi PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiIMDH_VIGUN
AccessioniPrimary (citable) accession number: Q84XA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: June 1, 2003
Last modified: June 11, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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