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UniProtKB/Swiss-Prot entry P38697


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IMDH2_YEAST
Primary accession number P38697
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on February 1, 1995 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 79)
Name and origin of the protein
Protein name Inosine-5'-monophosphate dehydrogenase IMD2
Synonyms IMP dehydrogenase
IMPDH
IMPD
EC 1.1.1.205
Gene name
Name: IMD2
Synonyms: PUR5
OrderedLocusNames: YHR216W
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=8091229 [NCBI, ExPASy, EBI, Israel, Japan]
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII.";
Science 265:2077-2082(1994).
[2]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U00029; AAB69728.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S48997; S48997.
RefSeq NP_012088.1; -.
3D structure databases
HSSP P12268; 1B3O. [HSSP ENTRY / PDB]
ModBase P38697.
Protein-protein interaction databases
DIP DIP:2840N; -.
IntAct P38697; 52.
Organism-specific databases
CYGD YHR216w; -.
SGD S000001259; IMD2.
Yeast-GFP YHR216W.
Gene expression databases
GermOnline YHR216W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0003938; Molecular function: IMP dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0030955; Molecular function: potassium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006177; Biological process: GMP biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006183; Biological process: GTP biosynthetic process (traceable author statement from SGD).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013785; Aldolase_TIM.
IPR000644; Cysta_beta_synth_core.
IPR015875; IMP_DH/GMP_Rdtase_CS.
IPR005990; IMP_DHase.
IPR001093; IMP_DHase_GMPRtase.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
PANTHER PTHR11911:SF6; IMP_DH_GMPRtase; 1.
Pfam PF00571; CBS; 1.
PF00478; IMPDH; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000130; IMPDH; 1.
SMART SM00116; CBS; 2.
SMART graphical view of domain structure.
TIGRFAMs TIGR01302; IMP_dehydrog; 1.
PROSITE PS51371; CBS; 2.
PS00487; IMP_DH_GMP_RED; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE P38697; -.
Genome annotation databases
Ensembl YHR216W; Saccharomyces cerevisiae. [Contig view]
GeneID 856626; -.
GenomeReviews U00093_GR; YHR216W.
KEGG sce:YHR216W; -.
NMPDR fig|4932.3.peg.3265; -.
Phylogenomic databases
HOGENOM P38697; -.
Other
LinkHub P38697; -.
NextBio 982568; -.
ProtoNet P38697.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
CBS domain; Complete proteome; GMP biosynthesis; Metal-binding; NAD; Oxidoreductase; Potassium; Purine biosynthesis; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   523  523     Inosine-5'-monophosphate dehydrogenase IMD2. PRO_0000093682
DOMAIN   121   183  63     CBS 1. 
DOMAIN   184   240  57     CBS 2. 
NP_BIND   257   280  24     NAD (By similarity). 
ACT_SITE   335   335        Thioimidate intermediate (By similarity). 
METAL   330   330        Potassium; via carbonyl oxygen (By similarity). 
METAL   332   332        Potassium; via carbonyl oxygen (By similarity). 
BINDING   280   280        Inhibitor (By similarity). 
BINDING   337   337        Inhibitor (By similarity). 
BINDING   368   368        IMP (By similarity). 
BINDING   415   415        IMP (By similarity). 
Sequence information
Length: 523 AA [This is the length of the unprocessed precursor] Molecular weight: 56530 Da [This is the MW of the unprocessed precursor] CRC64: 7CA3EC11238906B9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAIRDYKTA LDFTKSLPRP DGLSVQELMD SKIRGGLTYN DFLILPGLVD FASSEVSLQT 

        70         80         90        100        110        120 
KLTRNITLNI PLVSSPMDTV TESEMATFMA LLGGIGFIHH NCTPEDQADM VRRVKNYENG 

       130        140        150        160        170        180 
FINNPIVISP TTTVGEAKSM KEKYGFAGFP VTTDGKRNAK LVGVITSRDI QFVEDNSLLV 

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

       250        260        270        280        290        300 
KSANTKQLLC GASIGTMDAD KERLRLLVKA GLDVVILDSS QGNSIFELNM LKWVKESFPG 

       310        320        330        340        350        360 
LEVIAGNVVT REQAANLIAA GADGLRIGMG TGSICITQEV MACGRPQGTA VYNVCEFANQ 

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

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

       490        500        510        520 
CRSLTLLKNN VQRGKVRFEF RTASAQLEGG VHNLHSYEKR LHN 

P38697 in FASTA format

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