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P50098 (IMDH_TRYBB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. 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
OrganismTrypanosoma brucei brucei
Taxonomic identifier5702 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Protein attributes

Sequence length512 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_03156

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 By similarity. HAMAP-Rule MF_03156

Subcellular location

Glycosome By similarity HAMAP-Rule MF_03156.

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 2 CBS domains.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentglycosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionIMP dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

adenyl nucleotide binding

Inferred from electronic annotation. Source: InterPro

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 – 512512Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_03156
PRO_0000093677

Regions

Domain110 – 16960CBS 1
Domain173 – 23159CBS 2
Nucleotide binding268 – 2703NAD By similarity
Nucleotide binding318 – 3203NAD By similarity
Region358 – 3603IMP binding By similarity
Region381 – 3822IMP binding By similarity
Region405 – 4095IMP binding By similarity
Motif510 – 5123Microbody targeting signal Potential

Sites

Active site3251Thioimidate intermediate By similarity
Metal binding3201Potassium; via carbonyl oxygen By similarity
Metal binding3221Potassium; via carbonyl oxygen By similarity
Metal binding3251Potassium; via carbonyl oxygen By similarity
Metal binding4941Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4951Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site3231IMP By similarity
Binding site4351IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
P50098 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 1A86C46AE6445045

FASTA51255,709
        10         20         30         40         50         60 
MENTNLRTKT LRDGTTAEEL FSQDGLSFND FIILPGFIDF DSSKVNVSGQ FTKNILLHLP 

        70         80         90        100        110        120 
LVSSPMDTVT ESSMARAMAL MGGIGVIHNN CTVEQQARMV RSVKLYRNGF IMKPKSVSPD 

       130        140        150        160        170        180 
VPVSTIRNIK SEKGISGILV TEGGKYDGKL LGIVCTKDID FVKDASAPVS QYMTRRENMT 

       190        200        210        220        230        240 
VERYPIKLEE AMDVLNRSRH GYLPVLNDKD EVVCLCSRRD AVRARDYPNS SLDRNGHLLC 

       250        260        270        280        290        300 
AAATSTREAD KGRVAALSEA GIDVLVLDSS QGNTIYQVSF IRWVKKTYPH LEVVAGNVVT 

       310        320        330        340        350        360 
QDQAKNLIDA GADSLRIGMG SGSICITQEV LACGRPQATA IYKVARYAAS RGVPCVADGG 

       370        380        390        400        410        420 
LRNVGDVCKA LAVGANVAML GSMIAGTSET PGEYFFKDGM RLKGYRGMGS IDAMLQGRES 

       430        440        450        460        470        480 
GKRYLSENET LQVAQGVAGA VLDKGSVLKL LAYIHKGLQQ SAQDIGEVSF DAIREKVYEG 

       490        500        510 
QVLFNRRTLT AQSEGAVHSL HHYERKLFAS KL 

« Hide

References

[1]"Amplification of the inosinate dehydrogenase gene in Trypanosoma brucei gambiense due to an increase in chromosome copy number."
Wilson K., Berens R.L., Sifri C.D., Ullman B.
J. Biol. Chem. 269:28979-28987(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Eatro 164 / ISTat 1.7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97794 Genomic DNA. Translation: AAB46420.1.
PIRA55407.

3D structure databases

ProteinModelPortalP50098.
SMRP50098. Positions 13-106.
ModBaseSearch...
MobiDBSearch...

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.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERPTHR11911:SF6. PTHR11911:SF6. 1 hit.
PfamPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFPIRSF000130. IMPDH. 1 hit.
SMARTSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsTIGR01302. IMP_dehydrog. 1 hit.
PROSITEPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIMDH_TRYBB
AccessionPrimary (citable) accession number: P50098
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 19, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways