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P47996 (IMDH1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 120. 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

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
Gene names
Name:IMPDH
Ordered Locus Names:At1g79470
ORF Names:T8K14.11
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length503 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 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 By similarity. HAMAP-Rule MF_03156

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03156.

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 1 CBS domain.

Ontologies

Keywords
   Biological processGMP biosynthesis
Purine biosynthesis
   Cellular componentCytoplasm
   DomainCBS domain
   LigandMetal-binding
NAD
Potassium
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytosol

Inferred from direct assay PubMed 21166475. Source: TAIR

   Molecular_functionIMP dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 503502Inosine-5'-monophosphate dehydrogenase 1 HAMAP-Rule MF_03156
PRO_0000093686

Regions

Domain167 – 22559CBS
Nucleotide binding265 – 2673NAD By similarity
Nucleotide binding315 – 3173NAD By similarity
Region355 – 3573IMP binding By similarity
Region378 – 3792IMP binding By similarity
Region402 – 4065IMP binding By similarity

Sites

Active site3221Thioimidate intermediate By similarity
Metal binding3171Potassium; via carbonyl oxygen By similarity
Metal binding3191Potassium; via carbonyl oxygen By similarity
Metal binding3221Potassium; via carbonyl oxygen By similarity
Metal binding4891Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4901Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4911Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site3201IMP By similarity
Binding site4301IMP By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P47996 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: ADDDAF9C3A697A9A

FASTA50354,194
        10         20         30         40         50         60 
MSTLEDGFPA DKLFAQGYSY TYDDVIFLPH FIDFSTDAVS LSTRLSRRVP LSIPCVSSPM 

        70         80         90        100        110        120 
DTVSESHMAA AMASLGGIGI VHYNCGIAAQ ASIIRQAKSL KHPIASDAGV KFPEYEITSL 

       130        140        150        160        170        180 
DAFGPSSFVF VEQTGTMTTP KLLGYVTKSQ WKRMNYEQRE MKIYDYMKSC DSSDYCVPWE 

       190        200        210        220        230        240 
IDFEKLEFVL EDKQKGFVVL ERDGETVNVV TKDDIQRVKG YPKSGPGTVG PDGEWMVGAA 

       250        260        270        280        290        300 
IGTRESDKER LEHLVNVGVN AVVLDSSQGN SIYQLEMIKY VKKTYPELDV IGGNVVTMYQ 

       310        320        330        340        350        360 
AQNLIQAGVD GLRVGMGSGS ICTTQEVCAV GRGQATAVYK VCSIAAQSGI PVIADGGISN 

       370        380        390        400        410        420 
SGHIVKALVL GASTVMMGSF LAGSTEAPGG YEYTNGKRIK KYRGMGSLEA MTKGSDQRYL 

       430        440        450        460        470        480 
GDQTKLKIAQ GVVGAVADKG SVLKLIPYTM HAVKQGFQDL GASSLQSAHG LLRSNILRLE 

       490        500 
ARTGAAQVEG GVHGLVSYEK KSF 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the gene encoding IMP dehydrogenase from Arabidopsis thaliana."
Collart F.R., Osipiuk J., Trent J., Olsen G.J., Huberman E.
Gene 174:217-220(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L34684 Genomic DNA. Translation: AAB41940.1.
AC007202 Genomic DNA. Translation: AAD30229.1.
CP002684 Genomic DNA. Translation: AEE36247.1.
AF462859 mRNA. Translation: AAL58945.1.
BT000820 mRNA. Translation: AAN33195.1.
PIRJC4999.
RefSeqNP_178065.1. NM_106595.3.
UniGeneAt.28603.

3D structure databases

ProteinModelPortalP47996.
SMRP47996. Positions 5-503.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid29504. 2 interactions.
IntActP47996. 2 interactions.
STRING3702.AT1G79470.1-P.

Proteomic databases

PaxDbP47996.
PRIDEP47996.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G79470.1; AT1G79470.1; AT1G79470.
GeneID844285.
KEGGath:AT1G79470.

Organism-specific databases

TAIRAT1G79470.

Phylogenomic databases

eggNOGCOG0516.
HOGENOMHOG000165752.
InParanoidP47996.
KOK00088.
OMAFPEYEIT.
PhylomeDBP47996.

Enzyme and pathway databases

BioCycARA:AT1G79470-MONOMER.
UniPathwayUPA00601; UER00295.

Gene expression databases

ArrayExpressP47996.
GenevestigatorP47996.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01964. IMPDH.
InterProIPR013785. Aldolase_TIM.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERPTHR11911:SF6. PTHR11911:SF6. 1 hit.
PfamPF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFPIRSF000130. IMPDH. 1 hit.
TIGRFAMsTIGR01302. IMP_dehydrog. 1 hit.
PROSITEPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIMDH1_ARATH
AccessionPrimary (citable) accession number: P47996
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names