Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P50095 (IMDH3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inosine-5'-monophosphate dehydrogenase 3

Short name=IMP dehydrogenase 3
Short name=IMPD 3
Short name=IMPDH 3
EC=1.1.1.205
Gene names
Name:IMD3
Ordered Locus Names:YLR432W
ORF Names:L9753.4
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length523 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.5 Ref.6 Ref.7

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. Seems to be able to form heterotetramers composed from more than 1 of the 3 IMPDH gene products (IMD2-4). Ref.6

Subcellular location

Cytoplasm Ref.3.

Miscellaneous

Present with 26300 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 2 CBS domains.

Biophysicochemical properties

Kinetic parameters:

KM=100 µM for Inosine 5'-phosphate Ref.6

KM=314 µM for NAD+

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IMD4P500946EBI-9190,EBI-9195

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 523523Inosine-5'-monophosphate dehydrogenase 3 HAMAP-Rule MF_03156
PRO_0000093683

Regions

Domain121 – 18363CBS 1
Domain184 – 24057CBS 2
Nucleotide binding278 – 2803NAD By similarity
Nucleotide binding328 – 3303NAD By similarity
Region368 – 3703IMP binding By similarity
Region391 – 3922IMP binding By similarity
Region415 – 4195IMP binding By similarity

Sites

Active site3351Thioimidate intermediate By similarity
Metal binding3301Potassium; via carbonyl oxygen By similarity
Metal binding3321Potassium; via carbonyl oxygen By similarity
Metal binding3351Potassium; via carbonyl oxygen By similarity
Metal binding5081Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5091Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5101Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site3331IMP By similarity
Binding site4491IMP By similarity

Experimental info

Mutagenesis2531A → S: Increases drug-resistance to MPA. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P50095 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: A0C84C22527AAEA6

FASTA52356,585
        10         20         30         40         50         60 
MAAVRDYKTA LEFAKSLPRL DGLSVQELMD SKTRGGLTYN DFLVLPGLVD FPSSEVSLQT 

        70         80         90        100        110        120 
KLTRNITLNT PFVSSPMDTV TESEMAIFMA LLGGIGFIHH NCTPEDQADM VRRVKNYENG 

       130        140        150        160        170        180 
FINNPIVISP TTTVGEAKSM KERFGFSGFP VTEDGKRNGK LMGIVTSRDI QFVEDNSLLV 

       190        200        210        220        230        240 
QDVMTKNPVT GAQGITLSEG NEILKKIKKG KLLIVDDNGN LVSMLSRTDL MKNQNYPLAS 

       250        260        270        280        290        300 
KSATTKQLLC GAAIGTIDAD KERLRLLVEA GLDVVILDSS QGNSIFQLNM IKWIKETFPD 

       310        320        330        340        350        360 
LEIIAGNVAT REQAANLIAA GADGLRIGMG SGSICITQEV MACGRPQGTA VYNVCEFANQ 

       370        380        390        400        410        420 
FGIPCMADGG VQNIGHITKA LALGSSTVMM GGMLAGTTES PGEYFYQDGK RLKAYRGMGS 

       430        440        450        460        470        480 
IDAMQKTGTK GNASTSRYFS ESDSVLVAQG VSGAVVDKGS IKKFIPYLYN GLQHSCQDIG 

       490        500        510        520 
YKSLTLLKEN VQSGKVRFEF RTASAQLEGG VHNLHSYEKR LHN 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"Functional distinctions between IMP dehydrogenase genes in providing mycophenolate resistance and guanine prototrophy to yeast."
Hyle J.W., Shaw R.J., Reines D.
J. Biol. Chem. 278:28470-28478(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Detection of the mycophenolate-inhibited form of IMP dehydrogenase in vivo."
McPhillips C.C., Hyle J.W., Reines D.
Proc. Natl. Acad. Sci. U.S.A. 101:12171-12176(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
[7]"Dissection of the molecular basis of mycophenolate resistance in Saccharomyces cerevisiae."
Jenks M.H., Reines D.
Yeast 22:1181-1190(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ALA-253.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U21094 Genomic DNA. Translation: AAB67516.1.
BK006945 Genomic DNA. Translation: DAA09733.1.
PIRS59402.
RefSeqNP_013536.3. NM_001182320.3.

3D structure databases

ProteinModelPortalP50095.
SMRP50095. Positions 3-521.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31691. 127 interactions.
DIPDIP-1947N.
IntActP50095. 191 interactions.
MINTMINT-385605.
STRING4932.YLR432W.

Proteomic databases

MaxQBP50095.
PaxDbP50095.
PeptideAtlasP50095.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR432W; YLR432W; YLR432W.
GeneID851152.
KEGGsce:YLR432W.

Organism-specific databases

CYGDYLR432w.
SGDS000004424. IMD3.

Phylogenomic databases

eggNOGCOG0517.
GeneTreeENSGT00530000062923.
HOGENOMHOG000165752.
KOK00088.
OMASEMAIFM.
OrthoDBEOG793BHK.

Enzyme and pathway databases

BioCycYEAST:YLR432W-MONOMER.
SABIO-RKP50095.
UniPathwayUPA00601; UER00295.

Gene expression databases

GenevestigatorP50095.

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...

Other

NextBio967930.

Entry information

Entry nameIMDH3_YEAST
AccessionPrimary (citable) accession number: P50095
Secondary accession number(s): D6VZ67
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways