Inosine-5'-monophosphate dehydrogenase 3 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P50095 (IMDH3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 126. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	523 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity. 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.
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. HAMAP-Rule MF_03156
Sequence similarities	Belongs to the IMPDH/GMPR family. Contains 2 CBS domains.
Biophysicochemical properties	Kinetic parameters: K_M=100 µM for Inosine 5'-phosphate Ref.6 K_M=314 µM for NAD⁺

Ontologies

Keywords
Biological process	GMP biosynthesis Purine biosynthesis
Cellular component	Cytoplasm
Domain	CBS domain Repeat
Ligand	Metal-binding NAD Potassium
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GMP biosynthetic process Inferred from electronic annotation. Source: HAMAP GTP biosynthetic process Traceable author statement PubMed 11441018. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 11914276 Ref.3. Source: SGD plasma membrane Inferred from direct assay PubMed 16622836. Source: SGD
Molecular_function	IMP dehydrogenase activity Traceable author statement PubMed 11441018. Source: SGD metal ion binding Inferred from electronic annotation. Source: HAMAP nucleotide binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
IMD4	P50094	6	EBI-9190,EBI-9195

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 523

523

Inosine-5'-monophosphate dehydrogenase 3 HAMAP-Rule MF_03156

PRO_0000093683

Regions

Domain

121 – 183

CBS 1

Domain

184 – 240

CBS 2

Nucleotide binding

278 – 280

NAD By similarity

Nucleotide binding

328 – 330

NAD By similarity

Region

368 – 370

IMP binding By similarity

Region

391 – 392

IMP binding By similarity

Region

415 – 419

IMP binding By similarity

Sites

Active site

335

Thioimidate intermediate By similarity

Metal binding

330

Potassium; via carbonyl oxygen By similarity

Metal binding

332

Potassium; via carbonyl oxygen By similarity

Metal binding

335

Potassium; via carbonyl oxygen By similarity

Metal binding

508

Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Metal binding

509

Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Metal binding

510

Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Binding site

333

IMP By similarity

Binding site

449

IMP By similarity

Experimental info

Mutagenesis

253

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

Sequences

Sequence

Length

Mass (Da)

Tools

P50095 [UniParc].

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

FASTA

523

56,585

        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' referencesShow '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. Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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.
PIR	S59402.
RefSeq	NP_013536.3. NM_001182320.3.
3D structure databases
ProteinModelPortal	P50095.
SMR	P50095. Positions 3-521.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1947N.
IntAct	P50095. 198 interactions.
MINT	MINT-385605.
STRING	4932.YLR432W.
Proteomic databases
PaxDb	P50095.
PeptideAtlas	P50095.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR432W; YLR432W; YLR432W.
GeneID	851152.
KEGG	sce:YLR432W. sce:YLR435W.
Organism-specific databases
CYGD	YLR432w.
SGD	S000004424. IMD3.
Phylogenomic databases
eggNOG	COG0517.
GeneTree	ENSGT00530000062923.
HOGENOM	HOG000165752.
KO	K00088. K14800.
OMA	KRYEQGF.
OrthoDB	EOG41NXV9.
Enzyme and pathway databases
SABIO-RK	P50095.
UniPathway	UPA00601; UER00295.
Gene expression databases
Genevestigator	P50095.
GermOnline	YLR432W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_01964. IMPDH.
InterPro	IPR013785. Aldolase_TIM. IPR000644. Cysta_beta_synth_core. IPR005990. IMP_DH. IPR015875. IMP_DH/GMP_Rdtase_CS. IPR001093. IMP_DH_GMPRt. [Graphical view]
PANTHER	PTHR11911:SF6. PTHR11911:SF6. 1 hit.
Pfam	PF00571. CBS. 2 hits. PF00478. IMPDH. 1 hit. [Graphical view]
PIRSF	PIRSF000130. IMPDH. 1 hit.
SMART	SM00116. CBS. 2 hits. [Graphical view]
TIGRFAMs	TIGR01302. IMP_dehydrog. 1 hit.
PROSITE	PS51371. CBS. 2 hits. PS00487. IMP_DH_GMP_RED. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	967930.

Entry information

Entry name

IMDH3_YEAST

Accession

Primary (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:	May 1, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XII

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents