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Q07152

- IMDH_DROME

UniProt

Q07152 - IMDH_DROME

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Protein
Inosine-5'-monophosphate dehydrogenase
Gene
ras, CG1799
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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.2 Publications

Catalytic activityi

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

Cofactori

Potassium By similarity.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 By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi345 – 3451Potassium; via carbonyl oxygen By similarity
Metal bindingi347 – 3471Potassium; via carbonyl oxygen By similarity
Binding sitei348 – 3481IMP By similarity
Active sitei350 – 3501Thioimidate intermediate By similarity
Metal bindingi350 – 3501Potassium; via carbonyl oxygen By similarity
Binding sitei464 – 4641IMP By similarity
Metal bindingi523 – 5231Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi524 – 5241Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi293 – 2953NAD By similarity
Nucleotide bindingi343 – 3453NAD By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. GMP biosynthetic process Source: UniProtKB-HAMAP
  2. axon guidance Source: FlyBase
  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_208157. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00601; UER00295.

Names & Taxonomyi

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

Organism-specific databases

FlyBaseiFBgn0003204. ras.

Subcellular locationi

Cytoplasm By similarity 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 dehydrogenaseUniRule annotation
PRO_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 By similarity.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.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni383 – 3853IMP binding By similarity
Regioni406 – 4072IMP binding By similarity
Regioni430 – 4345IMP binding By similarity

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiCOG0517.
GeneTreeiENSGT00530000062923.
InParanoidiQ07152.
KOiK00088.
OMAiFQAKARH.
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. Align

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

MESTTKVKVN GFVESTSSSA APAIQTKSTT GFDAELQDGL SCKELFQNGE    50
GLTYNDFLIL PGYIDFTAEE VDLSSPLTKS LTLRAPLVSS PMDTVTESEM 100
AIAMALCGGI GIIHHNCTPE YQALEVHKVK KYKHGFMRDP SVMSPTNTVG 150
DVLEARRKNG FTGYPVTENG KLGGKLLGMV TSRDIDFREN QPEVLLADIM 200
TTELVTAPNG INLPTANAIL EKSKKGKLPI VNQAGELVAM IARTDLKKAR 250
SYPNASKDSN KQLLVGAAIG TRSEDKARLA LLVANGVDVI ILDSSQGNSV 300
YQVEMIKYIK ETYPELQVIG GNVVTRAQAK NLIDAGVDGL RVGMGSGSIC 350
ITQEVMACGC PQATAVYQVS TYARQFGVPV IADGGIQSIG HIVKAIALGA 400
SAVMMGSLLA GTSEAPGEYF FSDGVRLKKY RGMGSLEAME RGDAKGAAMS 450
RYYHNEMDKM KVAQGVSGSI VDKGSVLRYL PYLECGLQHS CQDIGANSIN 500
KLRDMIYNGQ LRFMKRTHSA QLEGNVHGLF SYEKRLF 537
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9191Missing in isoform B.
VSP_010299Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381D → V in AAB35628. 1 Publication
Sequence conflicti53 – 531T → P in AAB35628. 1 Publication
Sequence conflicti99 – 1024EMAI → RCH in AAB35628. 1 Publication
Sequence conflicti184 – 1841D → A in AAB35628. 1 Publication
Sequence conflicti194 – 1941V → S in AAB35628. 1 Publication
Sequence conflicti216 – 2172AN → EH in AAB35628. 1 Publication
Sequence conflicti226 – 2294GKLP → ATA in AAB35628. 1 Publication
Sequence conflicti244 – 2441T → A in AAB35628. 1 Publication
Sequence conflicti261 – 2622KQ → TR in AAB35628. 1 Publication
Sequence conflicti265 – 2662VG → CP in AAB35628. 1 Publication
Sequence conflicti277 – 2782AR → GCRA in AAB35628. 1 Publication
Sequence conflicti284 – 2841A → R in AAB35628. 1 Publication
Sequence conflicti301 – 3011Y → I in AAB35628. 1 Publication
Sequence conflicti387 – 3882QS → HA in AAB35628. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_001272498.1. [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]
UniGeneiDm.6459.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi S41064.
S59508.
RefSeqi NP_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 ]
UniGenei Dm.6459.

3D structure databases

ProteinModelPortali Q07152.
SMRi Q07152. Positions 38-537.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 68684. 9 interactions.
DIPi DIP-21552N.
IntActi Q07152. 4 interactions.
MINTi MINT-910823.

Proteomic databases

PaxDbi Q07152.
PRIDEi Q07152.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0071494 ; FBpp0071423 ; FBgn0003204 . [Q07152-1 ]
FBtr0071495 ; FBpp0071424 ; FBgn0003204 . [Q07152-1 ]
FBtr0332294 ; FBpp0304573 ; FBgn0003204 . [Q07152-1 ]
GeneIDi 43873.
KEGGi dme:Dmel_CG1799.

Organism-specific databases

CTDi 19412.
FlyBasei FBgn0003204. ras.

Phylogenomic databases

eggNOGi COG0517.
GeneTreei ENSGT00530000062923.
InParanoidi Q07152.
KOi K00088.
OMAi FQAKARH.
OrthoDBi EOG7VTDMM.
PhylomeDBi Q07152.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .
Reactomei REACT_208157. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

ChiTaRSi Ras85D. drosophila.
GenomeRNAii 43873.
NextBioi 836266.
PROi Q07152.

Gene expression databases

Bgeei Q07152.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01964. IMPDH.
InterProi IPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view ]
Pfami PF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000130. IMPDH. 1 hit.
SMARTi SM00116. CBS. 2 hits.
[Graphical view ]
TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
PROSITEi PS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 134 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

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