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P50096 (IMDH1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 112. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inosine-5'-monophosphate dehydrogenase 1
Short name=IMP dehydrogenase 1
Short name=IMPD 1
Short name=IMPDH 1
EC=1.1.1.205
Alternative name(s):
IMPDH-I
Gene names
Name:Impdh1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length514 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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. 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 By similarity. HAMAP-Rule MF_03156

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.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity HAMAP-Rule MF_03156.

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 2 CBS domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 514513Inosine-5'-monophosphate dehydrogenase 1 HAMAP-Rule MF_03156
PRO_0000093671

Regions

Domain114 – 17360CBS 1
Domain179 – 23759CBS 2
Nucleotide binding274 – 2763NAD By similarity
Nucleotide binding324 – 3263NAD By similarity
Region364 – 3663IMP binding By similarity
Region387 – 3882IMP binding By similarity
Region411 – 4155IMP binding By similarity

Sites

Active site3311Thioimidate intermediate By similarity
Metal binding3261Potassium; via carbonyl oxygen By similarity
Metal binding3281Potassium; via carbonyl oxygen By similarity
Metal binding3311Potassium; via carbonyl oxygen By similarity
Metal binding5001Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5011Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5021Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site3291IMP By similarity
Binding site4411IMP By similarity

Experimental info

Sequence conflict21 – 222QQ → HE in AAA18285. Ref.1
Sequence conflict2731L → H in AAA18285. Ref.1
Sequence conflict4141M → I in AAA18285. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P50096 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 69E2DD40F03701F2

FASTA51455,279
        10         20         30         40         50         60 
MADYLISGGT GYVPEDGLTA QQLFANADGL TYNDFLILPG FIDFIADEVD LTSALTRKIT 

        70         80         90        100        110        120 
LKTPLISSPM DTVTEADMAI AMALMGGIGF IHHNCTPEFQ ANEVRKVKKF EQGFITDPVV 

       130        140        150        160        170        180 
LSPSHTVGDV LEAKIQHGFS GIPITATGTM GSKLVGIVTS RDIDFLAEKD HTTLLSEVMT 

       190        200        210        220        230        240 
PRVELVVAPA GVTLKEANEI LQRSKKGKLP IVNDQDELVA IIARTDLKKN RDYPLASKDS 

       250        260        270        280        290        300 
HKQLLCGAAV GTREDDKYRL DLLTQAGADV IVLDSSQGNS VYQIAMVHYI KQKYPHLQVI 

       310        320        330        340        350        360 
GGNVVTAAQA KNLIDAGVDG LRVGMGCGSI CITQEVMACG RPQGTAVYKV AEYARRFGVP 

       370        380        390        400        410        420 
VIADGGIQTV GHVVKALALG ASTVMMGSLL AATTEAPGEY FFSDGVRLKK YRGMGSLDAM 

       430        440        450        460        470        480 
EKSSSSQKRY FSEGDKVKIA QGVSGSIQDK GSIQKFVPYL IAGIQHGCQD IGAQSLSVLR 

       490        500        510 
SMMYSGELKF EKRTMSAQIE GGVHGLHSYE KRLY

« Hide

References

« Hide 'large scale' references
[1]"Type I inosine monophosphate dehydrogenase: evidence for a single functional gene in mammalian species."
Dayton J.S., Mitchell B.S.
Biochem. Biophys. Res. Commun. 195:897-901(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leukemia.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U00978 mRNA. Translation: AAA18285.1.
AK171139 mRNA. Translation: BAE42272.1.
CH466533 Genomic DNA. Translation: EDL13790.1.
BC053416 mRNA. Translation: AAH53416.1.
IPIIPI00469835.
RefSeqNP_035959.2. NM_011829.2.
UniGeneMm.260707.

3D structure databases

ProteinModelPortalP50096.
SMRP50096. Positions 10-514.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-4098666.
STRING10090.ENSMUSP00000077289.

PTM databases

PhosphoSiteP50096.

Proteomic databases

PaxDbP50096.
PRIDEP50096.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000078155; ENSMUSP00000077289; ENSMUSG00000003500.
ENSMUST00000159124; ENSMUSP00000124931; ENSMUSG00000003500.
ENSMUST00000162099; ENSMUSP00000124541; ENSMUSG00000003500.
GeneID23917.
KEGGmmu:23917.
UCSCuc009bda.1. mouse.

Organism-specific databases

CTD3614.
MGIMGI:96567. Impdh1.

Phylogenomic databases

eggNOGCOG0517.
GeneTreeENSGT00530000062923.
HOGENOMHOG000165752.
HOVERGENHBG052122.
InParanoidQ7TSG7.
KOK00088.
OrthoDBEOG40VVP8.

Enzyme and pathway databases

UniPathwayUPA00601; UER00295.

Gene expression databases

ArrayExpressP50096.
BgeeP50096.
CleanExMM_IMPDH1.
GenevestigatorP50096.
GermOnlineENSMUSG00000003500. Mus musculus.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01964. IMPDH.
InterProIPR013785. Aldolase_TIM.
IPR000644. Cysta_beta_synth_core.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERPTHR11911:SF6. PTHR11911:SF6. 1 hit.
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

BindingDBP50096.
ChEMBLCHEMBL3302.
NextBio303685.
SOURCESearch...

Entry information

Entry nameIMDH1_MOUSE
AccessionPrimary (citable) accession number: P50096
Secondary accession number(s): Q7TSG7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: May 29, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents