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P50098

- IMDH_TRYBB

UniProt

P50098 - IMDH_TRYBB

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Protein

Inosine-5'-monophosphate dehydrogenase

Gene
N/A
Organism
Trypanosoma brucei brucei
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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 annotation

Catalytic activityi

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

Cofactori

Potassium.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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi320 – 3201Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi322 – 3221Potassium; via carbonyl oxygenUniRule annotation
Binding sitei323 – 3231IMPUniRule annotation
Active sitei325 – 3251Thioimidate intermediateUniRule annotation
Metal bindingi325 – 3251Potassium; via carbonyl oxygenUniRule annotation
Binding sitei435 – 4351IMPUniRule annotation
Metal bindingi494 – 4941Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi495 – 4951Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi268 – 2703NADUniRule annotation
Nucleotide bindingi318 – 3203NADUniRule annotation

GO - Molecular functioni

  1. adenyl nucleotide binding Source: InterPro
  2. IMP dehydrogenase activity Source: UniProtKB-HAMAP
  3. metal ion 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
OrganismiTrypanosoma brucei brucei
Taxonomic identifieri5702 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Subcellular locationi

Glycosome UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Glycosome, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 512512Inosine-5'-monophosphate dehydrogenasePRO_0000093677Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP50098.
SMRiP50098. Positions 13-106.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini110 – 16960CBS 1UniRule annotationAdd
BLAST
Domaini173 – 23159CBS 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni358 – 3603IMP bindingUniRule annotation
Regioni381 – 3822IMP bindingUniRule annotation
Regioni405 – 4095IMP bindingUniRule annotation

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi510 – 5123Microbody targeting signalUniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

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.

P50098-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MENTNLRTKT LRDGTTAEEL FSQDGLSFND FIILPGFIDF DSSKVNVSGQ
60 70 80 90 100
FTKNILLHLP LVSSPMDTVT ESSMARAMAL MGGIGVIHNN CTVEQQARMV
110 120 130 140 150
RSVKLYRNGF IMKPKSVSPD VPVSTIRNIK SEKGISGILV TEGGKYDGKL
160 170 180 190 200
LGIVCTKDID FVKDASAPVS QYMTRRENMT VERYPIKLEE AMDVLNRSRH
210 220 230 240 250
GYLPVLNDKD EVVCLCSRRD AVRARDYPNS SLDRNGHLLC AAATSTREAD
260 270 280 290 300
KGRVAALSEA GIDVLVLDSS QGNTIYQVSF IRWVKKTYPH LEVVAGNVVT
310 320 330 340 350
QDQAKNLIDA GADSLRIGMG SGSICITQEV LACGRPQATA IYKVARYAAS
360 370 380 390 400
RGVPCVADGG LRNVGDVCKA LAVGANVAML GSMIAGTSET PGEYFFKDGM
410 420 430 440 450
RLKGYRGMGS IDAMLQGRES GKRYLSENET LQVAQGVAGA VLDKGSVLKL
460 470 480 490 500
LAYIHKGLQQ SAQDIGEVSF DAIREKVYEG QVLFNRRTLT AQSEGAVHSL
510
HHYERKLFAS KL
Length:512
Mass (Da):55,709
Last modified:October 1, 1996 - v1
Checksum:i1A86C46AE6445045
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M97794 Genomic DNA. Translation: AAB46420.1.
PIRiA55407.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M97794 Genomic DNA. Translation: AAB46420.1 .
PIRi A55407.

3D structure databases

ProteinModelPortali P50098.
SMRi P50098. Positions 13-106.
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.
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 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.

Entry informationi

Entry nameiIMDH_TRYBB
AccessioniPrimary (citable) accession number: P50098
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 89 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