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Protein

Inosine-5'-monophosphate dehydrogenase

Gene
N/A
Organism
Leishmania donovani
Status
Reviewed-Annotation score: Annotation score: 5 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.UniRule annotation1 Publication

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. Potently inhibited by MPA. Inhibited by XMP and GMP.UniRule annotation1 Publication

Kineticsi

  1. KM=33 µM for Inosine 5'-phosphate1 Publication
  2. KM=390 µM for NAD+1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi322 – 3221Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi324 – 3241Potassium; via carbonyl oxygenUniRule annotation
Binding sitei325 – 3251IMPUniRule annotation
Active sitei327 – 3271Thioimidate intermediateUniRule annotation
Metal bindingi327 – 3271Potassium; via carbonyl oxygenUniRule annotation
Binding sitei437 – 4371IMPUniRule annotation
Metal bindingi496 – 4961Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi497 – 4971Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi498 – 4981Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi270 – 2723NADUniRule annotation
Nucleotide bindingi320 – 3223NADUniRule 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

BRENDAi1.1.1.205. 2947.
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
OrganismiLeishmania donovani
Taxonomic identifieri5661 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Subcellular locationi

Glycosome UniRule annotation1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Glycosome, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 514514Inosine-5'-monophosphate dehydrogenasePRO_0000093675Add
BLAST

Interactioni

Subunit structurei

Heterotetramer. Interacts with glycosomal protein sorting receptor PEX5.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP21620.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini112 – 17160CBS 1UniRule annotationAdd
BLAST
Domaini175 – 23359CBS 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni360 – 3623IMP bindingUniRule annotation
Regioni383 – 3842IMP bindingUniRule annotation
Regioni407 – 4115IMP bindingUniRule annotation

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi512 – 5143Microbody targeting signalUniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

KOiK00088.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH.
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. 1 hit.
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.

P21620-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATNNANYRI KTIKDGCTAE ELFRGDGLTY NDFIILPGFI DFGAADVNIS
60 70 80 90 100
GQFTKRIRLH IPIVSSPMDT ITENEMAKTM ALMGGVGVLH NNCTVERQVE
110 120 130 140 150
MVKSVKAYRN GFISKPKSVP PNTPISNIIR IKEEKGISGI LVTENGDPHG
160 170 180 190 200
KLLGIVCTKD IDYVKNKDTP VSAVMTRREK MTVERAPIQL EEAMDVLNRS
210 220 230 240 250
RYGYLPIVNE NDEVVNLCSR RDAVRARDYP HSTLDKSGRL ICAAATSTRP
260 270 280 290 300
EDKRRVAALA DVGVDVLVLD SSQGNTIYQI AFIKWVKSTY PHLEVVAGNV
310 320 330 340 350
VTQDQAKNLI DAGADGIRIG MGSGSICITQ EVLACGRPQG TAVYKVAQYC
360 370 380 390 400
ASRGVPCTAD GGLRQVGDIC KALAIGANCA MLGGMLSGTT ETPGEYFFKG
410 420 430 440 450
GVRLKVYRGM GSLEAMSQGK ESGKRYLSEN EAVQVAQGVS GNVVDKGSAA
460 470 480 490 500
KLIAYVSKGL QQSAQDIGEI SFDAIREKMY AGQVLFSRRS PTAQGEGGVH
510
SLHSYEKKLF AAKM
Length:514
Mass (Da):55,552
Last modified:May 1, 1991 - v1
Checksum:iE251FCC1362D60E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55667 Genomic DNA. Translation: AAA29253.1.
PIRiA38668.
RefSeqiXP_003860332.1. XM_003860284.1.

Genome annotation databases

GeneIDi13386143.
KEGGildo:LDBPK_191590.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55667 Genomic DNA. Translation: AAA29253.1.
PIRiA38668.
RefSeqiXP_003860332.1. XM_003860284.1.

3D structure databases

ProteinModelPortaliP21620.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi13386143.
KEGGildo:LDBPK_191590.

Phylogenomic databases

KOiK00088.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.
BRENDAi1.1.1.205. 2947.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH.
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. 1 hit.
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...

Publicationsi

  1. "Amplification and molecular cloning of the IMP dehydrogenase gene of Leishmania donovani."
    Wilson K.E., Collart F.R., Huberman E., Stringer J.R., Ullman B.
    J. Biol. Chem. 266:1665-1671(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Kinetic characterization of inosine monophosphate dehydrogenase of Leishmania donovani."
    Dobie F., Berg A., Boitz J.M., Jardim A.
    Mol. Biochem. Parasitol. 152:11-21(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH PEX5, SUBUNIT.

Entry informationi

Entry nameiIMDH_LEIDO
AccessioniPrimary (citable) accession number: P21620
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: April 1, 2015
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

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

External Data

Dasty 3

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 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.