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P21620

- IMDH_LEIDO

UniProt

P21620 - IMDH_LEIDO

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Protein
Inosine-5'-monophosphate dehydrogenase
Gene
N/A
Organism
Leishmania donovani
Status
Reviewed - 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.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. Potently inhibited by MPA. Inhibited by XMP and GMP.1 Publication

Kineticsi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi322 – 3221Potassium; via carbonyl oxygen By similarity
Metal bindingi324 – 3241Potassium; via carbonyl oxygen By similarity
Binding sitei325 – 3251IMP By similarity
Active sitei327 – 3271Thioimidate intermediate By similarity
Metal bindingi327 – 3271Potassium; via carbonyl oxygen By similarity
Binding sitei437 – 4371IMP By similarity
Metal bindingi496 – 4961Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi497 – 4971Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi498 – 4981Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi270 – 2723NAD By similarity
Nucleotide bindingi320 – 3223NAD By similarity

GO - Molecular functioni

  1. IMP dehydrogenase activity Source: UniProtKB-HAMAP
  2. adenyl nucleotide binding Source: InterPro
  3. metal ion 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
OrganismiLeishmania donovani
Taxonomic identifieri5661 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Subcellular locationi

Glycosome 1 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 dehydrogenaseUniRule annotation
PRO_0000093675Add
BLAST

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP21620.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni360 – 3623IMP binding By similarity
Regioni383 – 3842IMP binding By similarity
Regioni407 – 4115IMP binding By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi512 – 5143Microbody targeting signal Reviewed prediction

Sequence similaritiesi

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

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

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MATNNANYRI KTIKDGCTAE ELFRGDGLTY NDFIILPGFI DFGAADVNIS    50
GQFTKRIRLH IPIVSSPMDT ITENEMAKTM ALMGGVGVLH NNCTVERQVE 100
MVKSVKAYRN GFISKPKSVP PNTPISNIIR IKEEKGISGI LVTENGDPHG 150
KLLGIVCTKD IDYVKNKDTP VSAVMTRREK MTVERAPIQL EEAMDVLNRS 200
RYGYLPIVNE NDEVVNLCSR RDAVRARDYP HSTLDKSGRL ICAAATSTRP 250
EDKRRVAALA DVGVDVLVLD SSQGNTIYQI AFIKWVKSTY PHLEVVAGNV 300
VTQDQAKNLI DAGADGIRIG MGSGSICITQ EVLACGRPQG TAVYKVAQYC 350
ASRGVPCTAD GGLRQVGDIC KALAIGANCA MLGGMLSGTT ETPGEYFFKG 400
GVRLKVYRGM GSLEAMSQGK ESGKRYLSEN EAVQVAQGVS GNVVDKGSAA 450
KLIAYVSKGL QQSAQDIGEI SFDAIREKMY AGQVLFSRRS PTAQGEGGVH 500
SLHSYEKKLF AAKM 514
Length:514
Mass (Da):55,552
Last modified:May 1, 1991 - v1
Checksum:iE251FCC1362D60E5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M55667 Genomic DNA. Translation: AAA29253.1 .
PIRi A38668.
RefSeqi XP_003860332.1. XM_003860284.1.

3D structure databases

ProteinModelPortali P21620.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 13386143.
KEGGi ldo:LDBPK_191590.

Phylogenomic databases

KOi K00088.

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.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view ]
PANTHERi PTHR11911:SF6. PTHR11911:SF6. 1 hit.
Pfami PF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000130. IMPDH. 1 hit.
SMARTi SM00116. CBS. 2 hits.
[Graphical view ]
TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
PROSITEi PS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1991) [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(2007) [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: June 11, 2014
This is version 95 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

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