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P50095

- IMDH3_YEAST

UniProt

P50095 - IMDH3_YEAST

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Protein

Inosine-5'-monophosphate dehydrogenase 3

Gene
IMD3, YLR432W, L9753.4
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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.3 Publications

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 By similarity.UniRule annotation

Kineticsi

  1. KM=100 µM for Inosine 5'-phosphate1 Publication
  2. KM=314 µM for NAD+

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi330 – 3301Potassium; via carbonyl oxygen By similarity
Metal bindingi332 – 3321Potassium; via carbonyl oxygen By similarity
Binding sitei333 – 3331IMP By similarity
Active sitei335 – 3351Thioimidate intermediate By similarity
Metal bindingi335 – 3351Potassium; via carbonyl oxygen By similarity
Binding sitei449 – 4491IMP By similarity
Metal bindingi508 – 5081Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi509 – 5091Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi510 – 5101Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi278 – 2803NAD By similarity
Nucleotide bindingi328 – 3303NAD By similarity

GO - Molecular functioni

  1. adenyl nucleotide binding Source: InterPro
  2. IMP dehydrogenase activity Source: SGD
  3. metal ion binding Source: UniProtKB-HAMAP
  4. protein binding Source: IntAct

GO - Biological processi

  1. GMP biosynthetic process Source: UniProtKB-HAMAP
  2. GTP biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Potassium

Enzyme and pathway databases

BioCyciYEAST:YLR432W-MONOMER.
SABIO-RKP50095.
UniPathwayiUPA00601; UER00295.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-5'-monophosphate dehydrogenase 3 (EC:1.1.1.205)
Short name:
IMP dehydrogenase 3
Short name:
IMPD 3
Short name:
IMPDH 3
Gene namesi
Name:IMD3
Ordered Locus Names:YLR432W
ORF Names:L9753.4
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

CYGDiYLR432w.
SGDiS000004424. IMD3.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi253 – 2531A → S: Increases drug-resistance to MPA. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 523523Inosine-5'-monophosphate dehydrogenase 3UniRule annotationPRO_0000093683Add
BLAST

Proteomic databases

MaxQBiP50095.
PaxDbiP50095.
PeptideAtlasiP50095.

Expressioni

Gene expression databases

GenevestigatoriP50095.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
IMD4P500946EBI-9190,EBI-9195

Protein-protein interaction databases

BioGridi31691. 127 interactions.
DIPiDIP-1947N.
IntActiP50095. 191 interactions.
MINTiMINT-385605.
STRINGi4932.YLR432W.

Structurei

3D structure databases

ProteinModelPortaliP50095.
SMRiP50095. Positions 3-521.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini121 – 18363CBS 1Add
BLAST
Domaini184 – 24057CBS 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni368 – 3703IMP binding By similarity
Regioni391 – 3922IMP binding By similarity
Regioni415 – 4195IMP binding By similarity

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiCOG0517.
GeneTreeiENSGT00530000062923.
HOGENOMiHOG000165752.
KOiK00088.
OMAiSEMAIFM.
OrthoDBiEOG793BHK.

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.

P50095-1 [UniParc]FASTAAdd to Basket

« Hide

MAAVRDYKTA LEFAKSLPRL DGLSVQELMD SKTRGGLTYN DFLVLPGLVD    50
FPSSEVSLQT KLTRNITLNT PFVSSPMDTV TESEMAIFMA LLGGIGFIHH 100
NCTPEDQADM VRRVKNYENG FINNPIVISP TTTVGEAKSM KERFGFSGFP 150
VTEDGKRNGK LMGIVTSRDI QFVEDNSLLV QDVMTKNPVT GAQGITLSEG 200
NEILKKIKKG KLLIVDDNGN LVSMLSRTDL MKNQNYPLAS KSATTKQLLC 250
GAAIGTIDAD KERLRLLVEA GLDVVILDSS QGNSIFQLNM IKWIKETFPD 300
LEIIAGNVAT REQAANLIAA GADGLRIGMG SGSICITQEV MACGRPQGTA 350
VYNVCEFANQ FGIPCMADGG VQNIGHITKA LALGSSTVMM GGMLAGTTES 400
PGEYFYQDGK RLKAYRGMGS IDAMQKTGTK GNASTSRYFS ESDSVLVAQG 450
VSGAVVDKGS IKKFIPYLYN GLQHSCQDIG YKSLTLLKEN VQSGKVRFEF 500
RTASAQLEGG VHNLHSYEKR LHN 523
Length:523
Mass (Da):56,585
Last modified:October 1, 1996 - v1
Checksum:iA0C84C22527AAEA6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U21094 Genomic DNA. Translation: AAB67516.1.
BK006945 Genomic DNA. Translation: DAA09733.1.
PIRiS59402.
RefSeqiNP_013536.3. NM_001182320.3.

Genome annotation databases

EnsemblFungiiYLR432W; YLR432W; YLR432W.
GeneIDi851152.
KEGGisce:YLR432W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U21094 Genomic DNA. Translation: AAB67516.1 .
BK006945 Genomic DNA. Translation: DAA09733.1 .
PIRi S59402.
RefSeqi NP_013536.3. NM_001182320.3.

3D structure databases

ProteinModelPortali P50095.
SMRi P50095. Positions 3-521.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31691. 127 interactions.
DIPi DIP-1947N.
IntActi P50095. 191 interactions.
MINTi MINT-385605.
STRINGi 4932.YLR432W.

Proteomic databases

MaxQBi P50095.
PaxDbi P50095.
PeptideAtlasi P50095.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YLR432W ; YLR432W ; YLR432W .
GeneIDi 851152.
KEGGi sce:YLR432W.

Organism-specific databases

CYGDi YLR432w.
SGDi S000004424. IMD3.

Phylogenomic databases

eggNOGi COG0517.
GeneTreei ENSGT00530000062923.
HOGENOMi HOG000165752.
KOi K00088.
OMAi SEMAIFM.
OrthoDBi EOG793BHK.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .
BioCyci YEAST:YLR432W-MONOMER.
SABIO-RK P50095.

Miscellaneous databases

NextBioi 967930.

Gene expression databases

Genevestigatori P50095.

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

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. 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.

Entry informationi

Entry nameiIMDH3_YEAST
AccessioniPrimary (citable) accession number: P50095
Secondary accession number(s): D6VZ67
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

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