UniProtKB - Q6P9U9 (Q6P9U9_RAT)
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Protein
Inosine-5'-monophosphate dehydrogenase
Gene
Impdh2
Organism
Rattus norvegicus (Rat)
Status
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
: XMP biosynthesis via de novo pathway Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.UniRule annotationProteins known to be involved in this subpathway in this organism are:
- Inosine-5'-monophosphate dehydrogenase (Impdh1), Inosine-5'-monophosphate dehydrogenase (Impdh2), Inosine-5'-monophosphate dehydrogenase 2 (Impdh2), Inosine-5'-monophosphate dehydrogenase 1 (Impdh1)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 326 | Potassium; via carbonyl oxygenUniRule annotation | 1 | |
Metal bindingi | 328 | Potassium; via carbonyl oxygenUniRule annotation | 1 | |
Binding sitei | 329 | IMPUniRule annotation | 1 | |
Active sitei | 331 | Thioimidate intermediateUniRule annotation | 1 | |
Metal bindingi | 331 | Potassium; via carbonyl oxygenUniRule annotation | 1 | |
Active sitei | 429 | Proton acceptorUniRule annotation | 1 | |
Binding sitei | 441 | IMPUniRule annotation | 1 | |
Metal bindingi | 496 | Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 274 – 276 | NADUniRule annotation | 3 | |
Nucleotide bindingi | 324 – 326 | NADUniRule annotation | 3 |
GO - Molecular functioni
- IMP dehydrogenase activity Source: UniProtKB-UniRule
- metal ion binding Source: UniProtKB-UniRule
- nucleotide binding Source: UniProtKB-UniRule
GO - Biological processi
- GMP biosynthetic process Source: UniProtKB-UniRule
Keywordsi
Molecular function | OxidoreductaseUniRule annotation |
Biological process | GMP biosynthesisUniRule annotation, Purine biosynthesis |
Ligand | Metal-bindingUniRule annotation, NADUniRule annotation, PotassiumUniRule annotation |
Enzyme and pathway databases
BRENDAi | 1.1.1.205. 5301. |
SABIO-RKi | Q6P9U9. |
UniPathwayi | UPA00601; 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 | |
Organismi | Rattus norvegicus (Rat)Imported |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Organism-specific databases
RGDi | 735092. Impdh2. |
Subcellular locationi
Keywords - Cellular componenti
CytoplasmUniRule annotation, NucleusUniRule annotationInteractioni
Subunit structurei
Homotetramer.UniRule annotation
Protein-protein interaction databases
IntActi | Q6P9U9. 1 interactor. |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 114 – 173 | CBSInterPro annotationAdd BLAST | 60 | |
Domaini | 179 – 237 | CBSInterPro annotationAdd BLAST | 59 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 364 – 366 | IMP bindingUniRule annotation | 3 | |
Regioni | 387 – 388 | IMP bindingUniRule annotation | 2 | |
Regioni | 411 – 415 | IMP bindingUniRule annotation | 5 |
Sequence similaritiesi
Belongs to the IMPDH/GMPR family.UniRule annotation
Keywords - Domaini
CBS domainPROSITE-ProRule annotationPhylogenomic databases
eggNOGi | KOG2550. Eukaryota. COG0516. LUCA. COG0517. LUCA. |
HOGENOMi | HOG000165752. |
HOVERGENi | HBG052122. |
KOi | K00088. |
PhylomeDBi | Q6P9U9. |
Family and domain databases
CDDi | cd00381. IMPDH. 1 hit. |
Gene3Di | 3.20.20.70. 2 hits. |
HAMAPi | MF_01964. IMPDH. 1 hit. |
InterProi | View protein in InterPro IPR013785. Aldolase_TIM. IPR000644. CBS_dom. IPR005990. IMP_DH. IPR015875. IMP_DH/GMP_Rdtase_CS. IPR001093. IMP_DH_GMPRt. |
Pfami | View protein in Pfam PF00571. CBS. 2 hits. PF00478. IMPDH. 1 hit. |
PIRSFi | PIRSF000130. IMPDH. 1 hit. |
SMARTi | View protein in SMART SM00116. CBS. 2 hits. |
TIGRFAMsi | TIGR01302. IMP_dehydrog. 1 hit. |
PROSITEi | View protein in PROSITE PS51371. CBS. 2 hits. PS00487. IMP_DH_GMP_RED. 1 hit. |
i Sequence
Sequence statusi: Complete.
Q6P9U9-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC060585 mRNA. Translation: AAH60585.1. |
RefSeqi | NP_954530.1. NM_199099.2. |
UniGenei | Rn.8093. |
Genome annotation databases
GeneIDi | 301005. |
KEGGi | rno:301005. |
UCSCi | RGD:735092. rat. |
Similar proteinsi
Entry informationi
Entry namei | Q6P9U9_RAT | |
Accessioni | Q6P9U9Primary (citable) accession number: Q6P9U9 | |
Entry historyi | Integrated into UniProtKB/TrEMBL: | July 5, 2004 |
Last sequence update: | July 5, 2004 | |
Last modified: | March 28, 2018 | |
This is version 114 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Unreviewed (UniProtKB/TrEMBL) |
Miscellaneousi
Caution
Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation