Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Inosine-5'-monophosphate dehydrogenase

Gene

ras

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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.UniRule annotation2 Publications

Catalytic activityi

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

Cofactori

K(+)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.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi345 – 3451Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi347 – 3471Potassium; via carbonyl oxygenUniRule annotation
Binding sitei348 – 3481IMPUniRule annotation
Active sitei350 – 3501Thioimidate intermediateUniRule annotation
Metal bindingi350 – 3501Potassium; via carbonyl oxygenUniRule annotation
Binding sitei464 – 4641IMPUniRule annotation
Metal bindingi523 – 5231Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi524 – 5241Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi293 – 2953NADUniRule annotation
Nucleotide bindingi343 – 3453NADUniRule annotation

GO - Molecular functioni

  1. IMP dehydrogenase activity Source: UniProtKB-HAMAP
  2. metal ion binding Source: UniProtKB-HAMAP
  3. nucleotide binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. axon guidance Source: FlyBase
  2. GMP biosynthetic process Source: UniProtKB-HAMAP
  3. oogenesis Source: FlyBase
  4. phagocytosis Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Potassium

Enzyme and pathway databases

ReactomeiREACT_283178. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00601; UER00295.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-5'-monophosphate dehydrogenaseUniRule annotation (EC:1.1.1.205UniRule annotation)
Short name:
IMP dehydrogenaseUniRule annotation
Short name:
IMPDUniRule annotation
Short name:
IMPDHUniRule annotation
Alternative name(s):
Protein raspberry
Gene namesi
Name:ras
ORF Names:CG1799
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0003204. ras.

Subcellular locationi

  1. Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 537537Inosine-5'-monophosphate dehydrogenasePRO_0000093678Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ07152.
PRIDEiQ07152.

Expressioni

Tissue specificityi

Enriched in adult ovary and testis.1 Publication

Developmental stagei

Expressed both maternally and zygotically.1 Publication

Gene expression databases

BgeeiQ07152.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

BioGridi68684. 9 interactions.
DIPiDIP-21552N.
IntActiQ07152. 4 interactions.
MINTiMINT-910823.

Structurei

3D structure databases

ProteinModelPortaliQ07152.
SMRiQ07152. Positions 38-537.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini136 – 19560CBS 1UniRule annotationAdd
BLAST
Domaini200 – 25657CBS 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni383 – 3853IMP bindingUniRule annotation
Regioni406 – 4072IMP bindingUniRule annotation
Regioni430 – 4345IMP bindingUniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiCOG0517.
GeneTreeiENSGT00530000062923.
InParanoidiQ07152.
KOiK00088.
OMAiSSMGYCG.
OrthoDBiEOG7VTDMM.
PhylomeDBiQ07152.

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]
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: Q07152-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MESTTKVKVN GFVESTSSSA APAIQTKSTT GFDAELQDGL SCKELFQNGE
60 70 80 90 100
GLTYNDFLIL PGYIDFTAEE VDLSSPLTKS LTLRAPLVSS PMDTVTESEM
110 120 130 140 150
AIAMALCGGI GIIHHNCTPE YQALEVHKVK KYKHGFMRDP SVMSPTNTVG
160 170 180 190 200
DVLEARRKNG FTGYPVTENG KLGGKLLGMV TSRDIDFREN QPEVLLADIM
210 220 230 240 250
TTELVTAPNG INLPTANAIL EKSKKGKLPI VNQAGELVAM IARTDLKKAR
260 270 280 290 300
SYPNASKDSN KQLLVGAAIG TRSEDKARLA LLVANGVDVI ILDSSQGNSV
310 320 330 340 350
YQVEMIKYIK ETYPELQVIG GNVVTRAQAK NLIDAGVDGL RVGMGSGSIC
360 370 380 390 400
ITQEVMACGC PQATAVYQVS TYARQFGVPV IADGGIQSIG HIVKAIALGA
410 420 430 440 450
SAVMMGSLLA GTSEAPGEYF FSDGVRLKKY RGMGSLEAME RGDAKGAAMS
460 470 480 490 500
RYYHNEMDKM KVAQGVSGSI VDKGSVLRYL PYLECGLQHS CQDIGANSIN
510 520 530
KLRDMIYNGQ LRFMKRTHSA QLEGNVHGLF SYEKRLF
Length:537
Mass (Da):57,829
Last modified:November 1, 1995 - v1
Checksum:iA5EAB41AEAA64EBD
GO
Isoform B (identifier: Q07152-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-91: Missing.

Note: No experimental confirmation available.

Show »
Length:446
Mass (Da):48,139
Checksum:i15746E0A799702BB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381D → V in AAB35628 (PubMed:7476879).Curated
Sequence conflicti53 – 531T → P in AAB35628 (PubMed:7476879).Curated
Sequence conflicti99 – 1024EMAI → RCH in AAB35628 (PubMed:7476879).Curated
Sequence conflicti184 – 1841D → A in AAB35628 (PubMed:7476879).Curated
Sequence conflicti194 – 1941V → S in AAB35628 (PubMed:7476879).Curated
Sequence conflicti216 – 2172AN → EH in AAB35628 (PubMed:7476879).Curated
Sequence conflicti226 – 2294GKLP → ATA in AAB35628 (PubMed:7476879).Curated
Sequence conflicti244 – 2441T → A in AAB35628 (PubMed:7476879).Curated
Sequence conflicti261 – 2622KQ → TR in AAB35628 (PubMed:7476879).Curated
Sequence conflicti265 – 2662VG → CP in AAB35628 (PubMed:7476879).Curated
Sequence conflicti277 – 2782AR → GCRA in AAB35628 (PubMed:7476879).Curated
Sequence conflicti284 – 2841A → R in AAB35628 (PubMed:7476879).Curated
Sequence conflicti301 – 3011Y → I in AAB35628 (PubMed:7476879).Curated
Sequence conflicti387 – 3882QS → HA in AAB35628 (PubMed:7476879).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9191Missing in isoform B. 1 PublicationVSP_010299Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS41064.
S59508.
RefSeqiNP_001259427.1. NM_001272498.2. [Q07152-1]
NP_524646.5. NM_079907.7. [Q07152-1]
NP_727441.1. NM_167240.3. [Q07152-1]
NP_727442.1. NM_167241.3. [Q07152-1]
UniGeneiDm.6459.

Genome annotation databases

EnsemblMetazoaiFBtr0071494; FBpp0071423; FBgn0003204. [Q07152-1]
FBtr0071495; FBpp0071424; FBgn0003204. [Q07152-1]
FBtr0332294; FBpp0304573; FBgn0003204. [Q07152-1]
FBtr0343043; FBpp0309791; FBgn0003204. [Q07152-1]
GeneIDi43873.
KEGGidme:Dmel_CG1799.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS41064.
S59508.
RefSeqiNP_001259427.1. NM_001272498.2. [Q07152-1]
NP_524646.5. NM_079907.7. [Q07152-1]
NP_727441.1. NM_167240.3. [Q07152-1]
NP_727442.1. NM_167241.3. [Q07152-1]
UniGeneiDm.6459.

3D structure databases

ProteinModelPortaliQ07152.
SMRiQ07152. Positions 38-537.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68684. 9 interactions.
DIPiDIP-21552N.
IntActiQ07152. 4 interactions.
MINTiMINT-910823.

Proteomic databases

PaxDbiQ07152.
PRIDEiQ07152.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071494; FBpp0071423; FBgn0003204. [Q07152-1]
FBtr0071495; FBpp0071424; FBgn0003204. [Q07152-1]
FBtr0332294; FBpp0304573; FBgn0003204. [Q07152-1]
FBtr0343043; FBpp0309791; FBgn0003204. [Q07152-1]
GeneIDi43873.
KEGGidme:Dmel_CG1799.

Organism-specific databases

CTDi19412.
FlyBaseiFBgn0003204. ras.

Phylogenomic databases

eggNOGiCOG0517.
GeneTreeiENSGT00530000062923.
InParanoidiQ07152.
KOiK00088.
OMAiSSMGYCG.
OrthoDBiEOG7VTDMM.
PhylomeDBiQ07152.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.
ReactomeiREACT_283178. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

ChiTaRSiRas85D. fly.
GenomeRNAii43873.
NextBioi836266.
PROiQ07152.

Gene expression databases

BgeeiQ07152.

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]
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  7. 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.

Entry informationi

Entry nameiIMDH_DROME
AccessioniPrimary (citable) accession number: Q07152
Secondary accession number(s): Q26455, Q8SXM5, Q9W2R8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 1, 2015
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.