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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 PublicationUniRule 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

Kineticsi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi316 – 3161Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi318 – 3181Potassium; via carbonyl oxygenUniRule annotation
Binding sitei319 – 3191IMPUniRule annotation
Active sitei321 – 3211Thioimidate intermediateUniRule annotation
Metal bindingi321 – 3211Potassium; via carbonyl oxygenUniRule annotation
Binding sitei429 – 4291IMPUniRule annotation
Metal bindingi488 – 4881Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi489 – 4891Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi490 – 4901Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi264 – 2663NADUniRule annotation
Nucleotide bindingi314 – 3163NADUniRule annotation

GO - Molecular functioni

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

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 dehydrogenaseUniRule annotation (EC:1.1.1.205UniRule annotation)
Short name:
IMP dehydrogenaseUniRule annotation
Short name:
IMPDUniRule annotation
Short name:
IMPDHUniRule annotation
Gene namesi
Name:impdh
OrganismiVigna unguiculata (Cowpea)
Taxonomic identifieri3917 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 502502Inosine-5'-monophosphate dehydrogenasePRO_0000415681Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 PublicationUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ84XA3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini168 – 22457CBSUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni354 – 3563IMP bindingUniRule annotation
Regioni377 – 3782IMP bindingUniRule annotation
Regioni401 – 4055IMP bindingUniRule annotation

Sequence similaritiesi

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

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

        10         20         30         40         50
MDFTPPPIED GFTAEKLFSQ GFSYTYDDVI FLPHYIDFAA DAVDLSTRLT
60 70 80 90 100
RRLPLAVPLV ASPMDTVSES AMASAMASLG GIAIVHSNVP AAAQASLVRA
110 120 130 140 150
AKSRRVPILS EPAFAAPSAV IEHEDDFAAS PFLLVTDIGA AGGKLLGYVA
160 170 180 190 200
KRDWTNQKDK SLRVGDYMAP PPRRAPWNAD LNKIHEIMEN EKSGAVALER
210 220 230 240 250
DGEVVDLVVR EEVERVKGYP KLAAPATVGP DGEFMVGAAM GTREDDKERL
260 270 280 290 300
KHLVKAGVNV VVLDSSQGNS IYQLEMVKYV KSVYPELDVI GGNVVTMYQA
310 320 330 340 350
ENLIQAGVDG LRVGMGSGSI CTTQEVCAVG RGQATAVYKV SSIAYKSGVP
360 370 380 390 400
VIADGGISNS GHIVKALSLG ASTAMMGSFL AGSHEAPGAY VYQNGQRVKK
410 420 430 440 450
YRGMGSLEAM TKGSDARYLG DTAKLKIAQG VVGAVKDKGS VLNFIPYTLQ
460 470 480 490 500
AVRQGFQDIG ASSLQSAHDL LRSRVLRLEV RTGAAQVEGG VHGLVSYEKK

YY
Length:502
Mass (Da):53,450
Last modified:June 1, 2003 - v1
Checksum:i61773EBE986FFD30
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY193837 mRNA. Translation: AAO40253.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY193837 mRNA. Translation: AAO40253.1 .

3D structure databases

ProteinModelPortali Q84XA3.
ModBasei Search...
MobiDBi Search...

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: November 26, 2014
This is version 68 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