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

P50094 (IMDH4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. 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 4

Short name=IMP dehydrogenase 4
Short name=IMPD 4
Short name=IMPDH 4
EC=1.1.1.205
Gene names
Name:IMD4
Ordered Locus Names:YML056C
ORF Names:YM9958.06C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length524 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.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.7

Subcellular location

Cytoplasm Ref.4.

Miscellaneous

Present with 2970 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 2 CBS domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IMD3P500956EBI-9195,EBI-9190

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 524524Inosine-5'-monophosphate dehydrogenase 4 HAMAP-Rule MF_03156
PRO_0000093684

Regions

Domain122 – 18362CBS 1
Domain185 – 24157CBS 2
Nucleotide binding279 – 2813NAD By similarity
Nucleotide binding329 – 3313NAD By similarity
Region369 – 3713IMP binding By similarity
Region392 – 3932IMP binding By similarity
Region416 – 4205IMP binding By similarity

Sites

Active site3361Thioimidate intermediate By similarity
Metal binding3311Potassium; via carbonyl oxygen By similarity
Metal binding3331Potassium; via carbonyl oxygen By similarity
Metal binding3361Potassium; via carbonyl oxygen By similarity
Metal binding5091Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5101Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5111Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site3341IMP By similarity
Binding site4501IMP By similarity

Amino acid modifications

Modified residue1251Phosphoserine Ref.8

Sequences

Sequence LengthMass (Da)Tools
P50094 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: A73D1E4EFE8AEAD9

FASTA52456,394
        10         20         30         40         50         60 
MSAAPLDYKK ALEHLKTYSS KDGLSVQELM DSTTRGGLTY NDFLVLPGLV NFPSSAVSLQ 

        70         80         90        100        110        120 
TKLTKKITLN TPFVSSPMDT VTEADMAIYM ALLGGIGFIH HNCTPKEQAS MVKKVKMFEN 

       130        140        150        160        170        180 
GFINSPIVIS PTTTVGEVKV MKRKFGFSGF PVTEDGKCPG KLVGLVTSRD IQFLEDDSLV 

       190        200        210        220        230        240 
VSEVMTKNPV TGIKGITLKE GNEILKQTKK GKLLIVDDNG NLVSMLSRAD LMKNQNYPLA 

       250        260        270        280        290        300 
SKSATTKQLL CGAAIGTIEA DKERLRLLVE AGLDVVILDS SQGNSVFQLN MIKWIKETFP 

       310        320        330        340        350        360 
DLEIIAGNVA TREQAANLIA AGADGLRIGM GSGSICITQE VMACGRPQGT AVYNVCQFAN 

       370        380        390        400        410        420 
QFGVPCMADG GVQNIGHITK ALALGSSTVM MGGMLAGTTE SPGEYFYKDG KRLKAYRGMG 

       430        440        450        460        470        480 
SIDAMQKTGN KGNASTSRYF SESDSVLVAQ GVSGAVVDKG SIKKFIPYLY NGLQHSCQDI 

       490        500        510        520 
GCESLTSLKE NVQNGEVRFE FRTASAQLEG GVHNLHSYEK RLYN 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(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]"Mapping of transcription start sites in Saccharomyces cerevisiae using 5' SAGE."
Zhang Z., Dietrich F.S.
Nucleic Acids Res. 33:2838-2851(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-83.
Strain: ATCC 208353 / W303-1A.
[4]"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].
[5]"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].
[6]"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.
[7]"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.
[8]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z46729 Genomic DNA. Translation: CAA86719.1.
AY899250 mRNA. Translation: AAX83935.1.
BK006946 Genomic DNA. Translation: DAA09842.1.
PIRS50890.
RefSeqNP_013656.1. NM_001182414.1.

3D structure databases

ProteinModelPortalP50094.
SMRP50094. Positions 2-523.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35111. 85 interactions.
DIPDIP-6458N.
IntActP50094. 60 interactions.
MINTMINT-675699.
STRING4932.YML056C.

Proteomic databases

MaxQBP50094.
PaxDbP50094.
PeptideAtlasP50094.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYML056C; YML056C; YML056C.
GeneID854948.
KEGGsce:YML056C.

Organism-specific databases

CYGDYML056c.
SGDS000004520. IMD4.

Phylogenomic databases

eggNOGCOG0517.
GeneTreeENSGT00530000062923.
HOGENOMHOG000165752.
KOK00088.
OMAYLIFLET.
OrthoDBEOG793BHK.

Enzyme and pathway databases

BioCycYEAST:YML056C-MONOMER.
UniPathwayUPA00601; UER00295.

Gene expression databases

GenevestigatorP50094.

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

NextBio978010.

Entry information

Entry nameIMDH4_YEAST
AccessionPrimary (citable) accession number: P50094
Secondary accession number(s): D6VZB8, Q2VQW8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 133 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 XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: 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