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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

Impdh2

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.UniRule annotation

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: XMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Inosine-5'-monophosphate dehydrogenase (Impdh1), Inosine-5'-monophosphate dehydrogenase (Impdh2), Inosine-5'-monophosphate dehydrogenase 2 (Impdh2), Inosine-5'-monophosphate dehydrogenase 1 (Impdh1)
This subpathway is part of the pathway XMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from IMP, the pathway XMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi326 – 3261Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi328 – 3281Potassium; via carbonyl oxygenUniRule annotation
Binding sitei329 – 3291IMPUniRule annotation
Active sitei331 – 3311Thioimidate intermediateUniRule annotation
Metal bindingi331 – 3311Potassium; via carbonyl oxygenUniRule annotation
Active sitei429 – 4291Proton acceptorUniRule annotation
Binding sitei441 – 4411IMPUniRule annotation
Metal bindingi496 – 4961Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi274 – 2763NADUniRule annotation
Nucleotide bindingi324 – 3263NADUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Biological processi

GMP biosynthesisUniRule annotation, Purine biosynthesis

Keywords - Ligandi

Metal-bindingUniRule annotation, NADUniRule annotation, PotassiumUniRule annotation

Enzyme and pathway databases

BRENDAi1.1.1.205. 5301.
SABIO-RKQ6P9U9.
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
Gene namesi
Name:Impdh2Imported
Synonyms:ImpdhUniRule annotation
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Organism-specific databases

RGDi735092. Impdh2.

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Nucleus UniRule annotation

Keywords - Cellular componenti

CytoplasmUniRule annotation, NucleusUniRule annotation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedUniRule annotation

Proteomic databases

PaxDbiQ6P9U9.
PRIDEiQ6P9U9.

Expressioni

Gene expression databases

GenevisibleiQ6P9U9. RN.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

IntActiQ6P9U9. 1 interaction.
STRINGi10116.ENSRNOP00000040635.

Structurei

3D structure databases

ProteinModelPortaliQ6P9U9.
SMRiQ6P9U9. Positions 10-514.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini114 – 17360CBSInterPro annotationAdd
BLAST
Domaini179 – 23759CBSInterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni364 – 3663IMP bindingUniRule annotation
Regioni387 – 3882IMP bindingUniRule annotation
Regioni411 – 4155IMP bindingUniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

CBS domainUniRule annotation, RepeatUniRule annotation

Phylogenomic databases

eggNOGiKOG2550. Eukaryota.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165752.
HOVERGENiHBG052122.
KOiK00088.
PhylomeDBiQ6P9U9.

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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6P9U9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADYLISGGT SYVPDDGLTA QQLFNCGDGL TYNDFLILPG YIDFTADQVD
60 70 80 90 100
LTSALTKKIT LKTPLVSSPM DTVTEAGMAI AMALTGGIGF IHHNCTPEFQ
110 120 130 140 150
ANEVRKVKKY EQGFITDPVV LSPKDRVRDV FEAKARHGFC GIPITDTGRM
160 170 180 190 200
GSRLVGIISS RDIDFLKEEE HDRFLEEIMT KREDLVVAPA GVTLKEANEI
210 220 230 240 250
LQRSKKGKLP IVNESDELVA IIARTDLKKN RDYPLASKDT KKQLLCGAAI
260 270 280 290 300
GTHEDDKYRL DLLALAGVDV VVLDSSQGNS IFQINMIKYI KEKYPNLQVI
310 320 330 340 350
GGNVVTAAQA KNLIDAGVDA LRVGMGSGSI CITQEVLASG RPQATAVYKV
360 370 380 390 400
SEYARRFGVP VIADGGIQNV GHIAKALALG ASTVMMGSLL AATTEAPGEY
410 420 430 440 450
FFSDGIRLKK YRGMGSLDAM DKHLSSQNRY FSEADKIKVA QGVSGAVQDK
460 470 480 490 500
GSIHKFVPYL IAGIQHSCQD IGAKSLTQVR AMMYSGELKF EKRTSSAQVE
510
GGVHGLHSYE KRLF
Length:514
Mass (Da):55,799
Last modified:July 5, 2004 - v1
Checksum:iFE85D44B8BEA2319
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC060585 mRNA. Translation: AAH60585.1.
RefSeqiNP_954530.1. NM_199099.2.
UniGeneiRn.8093.

Genome annotation databases

GeneIDi301005.
KEGGirno:301005.
UCSCiRGD:735092. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC060585 mRNA. Translation: AAH60585.1.
RefSeqiNP_954530.1. NM_199099.2.
UniGeneiRn.8093.

3D structure databases

ProteinModelPortaliQ6P9U9.
SMRiQ6P9U9. Positions 10-514.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ6P9U9. 1 interaction.
STRINGi10116.ENSRNOP00000040635.

Proteomic databases

PaxDbiQ6P9U9.
PRIDEiQ6P9U9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi301005.
KEGGirno:301005.
UCSCiRGD:735092. rat.

Organism-specific databases

CTDi3615.
RGDi735092. Impdh2.

Phylogenomic databases

eggNOGiKOG2550. Eukaryota.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165752.
HOVERGENiHBG052122.
KOiK00088.
PhylomeDBiQ6P9U9.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.
BRENDAi1.1.1.205. 5301.
SABIO-RKQ6P9U9.

Gene expression databases

GenevisibleiQ6P9U9. RN.

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

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary glandImported.

Entry informationi

Entry nameiQ6P9U9_RAT
AccessioniPrimary (citable) accession number: Q6P9U9
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: June 8, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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 one 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.