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Q07152 (IMDH_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inosine-5'-monophosphate dehydrogenase

Short name=IMP dehydrogenase
Short name=IMPD
Short name=IMPDH
EC=1.1.1.205
Alternative name(s):
Protein raspberry
Gene names
Name:ras
ORF Names:CG1799
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length537 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.2 Ref.4

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 By similarity. HAMAP-Rule MF_03156

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03156.

Tissue specificity

Enriched in adult ovary and testis. Ref.4

Developmental stage

Expressed both maternally and zygotically. Ref.4

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 2 CBS domains.

Ontologies

Keywords
   Biological processGMP biosynthesis
Purine biosynthesis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainCBS domain
Repeat
   LigandMetal-binding
NAD
Potassium
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

axon guidance

Inferred from mutant phenotype PubMed 16322525. Source: FlyBase

oogenesis

Traceable author statement PubMed 3089870. Source: FlyBase

phagocytosis

Inferred from mutant phenotype PubMed 16336044. Source: FlyBase

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionIMP dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

adenyl nucleotide binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q07152-1)

Also known as: C;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: Q07152-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-91: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 537537Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_03156
PRO_0000093678

Regions

Domain136 – 19560CBS 1
Domain200 – 25657CBS 2
Nucleotide binding293 – 2953NAD By similarity
Nucleotide binding343 – 3453NAD By similarity
Region383 – 3853IMP binding By similarity
Region406 – 4072IMP binding By similarity
Region430 – 4345IMP binding By similarity

Sites

Active site3501Thioimidate intermediate By similarity
Metal binding3451Potassium; via carbonyl oxygen By similarity
Metal binding3471Potassium; via carbonyl oxygen By similarity
Metal binding3501Potassium; via carbonyl oxygen By similarity
Metal binding5231Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5241Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site3481IMP By similarity
Binding site4641IMP By similarity

Amino acid modifications

Modified residue281Phosphoserine Ref.8

Natural variations

Alternative sequence1 – 9191Missing in isoform B.
VSP_010299

Experimental info

Sequence conflict381D → V in AAB35628. Ref.4
Sequence conflict531T → P in AAB35628. Ref.4
Sequence conflict99 – 1024EMAI → RCH in AAB35628. Ref.4
Sequence conflict1841D → A in AAB35628. Ref.4
Sequence conflict1941V → S in AAB35628. Ref.4
Sequence conflict216 – 2172AN → EH in AAB35628. Ref.4
Sequence conflict226 – 2294GKLP → ATA in AAB35628. Ref.4
Sequence conflict2441T → A in AAB35628. Ref.4
Sequence conflict261 – 2622KQ → TR in AAB35628. Ref.4
Sequence conflict265 – 2662VG → CP in AAB35628. Ref.4
Sequence conflict277 – 2782AR → GCRA in AAB35628. Ref.4
Sequence conflict2841A → R in AAB35628. Ref.4
Sequence conflict3011Y → I in AAB35628. Ref.4
Sequence conflict387 – 3882QS → HA in AAB35628. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform A (C) [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: A5EAB41AEAA64EBD

FASTA53757,829
        10         20         30         40         50         60 
MESTTKVKVN GFVESTSSSA APAIQTKSTT GFDAELQDGL SCKELFQNGE GLTYNDFLIL 

        70         80         90        100        110        120 
PGYIDFTAEE VDLSSPLTKS LTLRAPLVSS PMDTVTESEM AIAMALCGGI GIIHHNCTPE 

       130        140        150        160        170        180 
YQALEVHKVK KYKHGFMRDP SVMSPTNTVG DVLEARRKNG FTGYPVTENG KLGGKLLGMV 

       190        200        210        220        230        240 
TSRDIDFREN QPEVLLADIM TTELVTAPNG INLPTANAIL EKSKKGKLPI VNQAGELVAM 

       250        260        270        280        290        300 
IARTDLKKAR SYPNASKDSN KQLLVGAAIG TRSEDKARLA LLVANGVDVI ILDSSQGNSV 

       310        320        330        340        350        360 
YQVEMIKYIK ETYPELQVIG GNVVTRAQAK NLIDAGVDGL RVGMGSGSIC ITQEVMACGC 

       370        380        390        400        410        420 
PQATAVYQVS TYARQFGVPV IADGGIQSIG HIVKAIALGA SAVMMGSLLA GTSEAPGEYF 

       430        440        450        460        470        480 
FSDGVRLKKY RGMGSLEAME RGDAKGAAMS RYYHNEMDKM KVAQGVSGSI VDKGSVLRYL 

       490        500        510        520        530 
PYLECGLQHS CQDIGANSIN KLRDMIYNGQ LRFMKRTHSA QLEGNVHGLF SYEKRLF 

« Hide

Isoform B [UniParc].

Checksum: 15746E0A799702BB
Show »

FASTA44648,139

References

« Hide 'large scale' references
[1]"Drosophila inosine monophosphate dehydrogenase is encoded at the raspberry locus."
Nash D., Hu S.
(In) Proceedings of the 35th meeting of the Canadian Federation of Biological Societies, pp.72-72, Victoria (1992)
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM A).
Strain: Oregon-R.
Tissue: Embryo.
[2]"The raspberry locus of Drosophila melanogaster includes an inosine monophosphate dehydrogenase like coding sequence."
Nash D., Hu S., Leonard N.J., Tiong S.Y., Fillips D.
Genome 37:333-344(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), FUNCTION.
Strain: Oregon-R.
Tissue: Embryo.
[3]"Cloning and sequence analysis of a Drosophila melanogaster cDNA encoding IMP dehydrogenase."
Sifri C.D., Wilson K., Smolik S., Forte M.A., Ullman B.
Biochim. Biophys. Acta 1217:103-106(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
Strain: Canton-S.
[4]"The raspberry locus encodes Drosophila inosine monophosphate dehydrogenase."
Slee R., Bownes M.
Mol. Gen. Genet. 248:755-766(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[5]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[6]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[7]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Strain: Berkeley.
Tissue: Embryo.
[8]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L14847 Genomic DNA. Translation: AAA21831.1.
L22608 mRNA. Translation: AAA16839.1.
S80430 mRNA. Translation: AAB35628.1.
AE014298 Genomic DNA. Translation: AAF46621.2.
AE014298 Genomic DNA. Translation: AAF46622.1.
AY089553 mRNA. Translation: AAL90291.1.
PIRS41064.
S59508.
RefSeqNP_001259427.1. NM_001272498.1. [Q07152-1]
NP_524646.4. NM_079907.6. [Q07152-2]
NP_727441.1. NM_167240.2. [Q07152-1]
NP_727442.1. NM_167241.2. [Q07152-1]
UniGeneDm.6459.

3D structure databases

ProteinModelPortalQ07152.
SMRQ07152. Positions 38-537.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid68684. 9 interactions.
DIPDIP-21552N.
IntActQ07152. 4 interactions.
MINTMINT-910823.

Proteomic databases

PaxDbQ07152.
PRIDEQ07152.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0071494; FBpp0071423; FBgn0003204. [Q07152-1]
FBtr0071495; FBpp0071424; FBgn0003204. [Q07152-1]
FBtr0332294; FBpp0304573; FBgn0003204. [Q07152-1]
GeneID43873.
KEGGdme:Dmel_CG1799.

Organism-specific databases

CTD19412.
FlyBaseFBgn0003204. ras.

Phylogenomic databases

eggNOGCOG0517.
GeneTreeENSGT00530000062923.
InParanoidQ07152.
KOK00088.
OMAFQAKARH.
OrthoDBEOG7VTDMM.
PhylomeDBQ07152.

Enzyme and pathway databases

UniPathwayUPA00601; UER00295.

Gene expression databases

BgeeQ07152.

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]
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

ChiTaRSRas85D. drosophila.
GenomeRNAi43873.
NextBio836266.
PROQ07152.

Entry information

Entry nameIMDH_DROME
AccessionPrimary (citable) accession number: Q07152
Secondary accession number(s): Q26455, Q8SXM5, Q9W2R8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
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 programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase