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Protein

Inosine-5'-monophosphate dehydrogenase

Gene
N/A
Organism
Trypanosoma brucei brucei
Status
Reviewed-Annotation score: -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

K+UniRule annotation

Activity 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: XMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Inosine-5'-monophosphate dehydrogenase
This subpathway is part of the pathway XMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from IMP, the pathway XMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi320Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi322Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei323IMPUniRule annotation1
Active sitei325Thioimidate intermediateUniRule annotation1
Metal bindingi325Potassium; via carbonyl oxygenUniRule annotation1
Active sitei423Proton acceptorUniRule annotation1
Binding sitei435IMPUniRule annotation1
Metal bindingi494Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi495Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi268 – 270NADUniRule annotation3
Nucleotide bindingi318 – 320NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processGMP biosynthesis, Purine biosynthesis
LigandMetal-binding, NAD, Potassium

Enzyme and pathway databases

BRENDAi1.1.1.205 6519
UniPathwayi
UPA00601;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

GO - Cellular componenti

Keywords - Cellular componenti

Glycosome, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000936771 – 512Inosine-5'-monophosphate dehydrogenaseAdd BLAST512

Proteomic databases

PRIDEiP50098

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP50098
SMRiP50098
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini110 – 169CBS 1UniRule annotationAdd BLAST60
Domaini173 – 231CBS 2UniRule annotationAdd BLAST59

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni358 – 360IMP bindingUniRule annotation3
Regioni381 – 382IMP bindingUniRule annotation2
Regioni405 – 409IMP bindingUniRule annotation5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi510 – 512Microbody targeting signalUniRule annotation3

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation

Keywords - Domaini

CBS domain, Repeat

Family and domain databases

CDDicd00381 IMPDH, 1 hit
HAMAPiMF_01964 IMPDH, 1 hit
InterProiView protein in InterPro
IPR000644 CBS_dom
IPR005990 IMP_DH
IPR015875 IMP_DH/GMP_Rdtase_CS
IPR001093 IMP_DH_GMPRt
PfamiView protein in Pfam
PF00571 CBS, 2 hits
PF00478 IMPDH, 1 hit
PIRSFiPIRSF000130 IMPDH, 1 hit
SMARTiView protein in SMART
SM00116 CBS, 2 hits
TIGRFAMsiTIGR01302 IMP_dehydrog, 1 hit
PROSITEiView protein in PROSITE
PS51371 CBS, 2 hits
PS00487 IMP_DH_GMP_RED, 1 hit

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:
EMBLi
GenBanki
DDBJi
Links Updated
M97794 Genomic DNA Translation: AAB46420.1
PIRiA55407

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97794 Genomic DNA Translation: AAB46420.1
PIRiA55407

3D structure databases

ProteinModelPortaliP50098
SMRiP50098
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP50098

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayi
UPA00601;UER00295

BRENDAi1.1.1.205 6519

Family and domain databases

CDDicd00381 IMPDH, 1 hit
HAMAPiMF_01964 IMPDH, 1 hit
InterProiView protein in InterPro
IPR000644 CBS_dom
IPR005990 IMP_DH
IPR015875 IMP_DH/GMP_Rdtase_CS
IPR001093 IMP_DH_GMPRt
PfamiView protein in Pfam
PF00571 CBS, 2 hits
PF00478 IMPDH, 1 hit
PIRSFiPIRSF000130 IMPDH, 1 hit
SMARTiView protein in SMART
SM00116 CBS, 2 hits
TIGRFAMsiTIGR01302 IMP_dehydrog, 1 hit
PROSITEiView protein in PROSITE
PS51371 CBS, 2 hits
PS00487 IMP_DH_GMP_RED, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiIMDH_TRYBB
AccessioniPrimary (citable) accession number: P50098
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 10, 2018
This is version 107 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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