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Q9SA34 (IMDH2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. 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 2

Short name=IMP dehydrogenase 2
Short name=IMPD 2
Short name=IMPDH 2
EC=1.1.1.205
Gene names
Ordered Locus Names:At1g16350
ORF Names:F3O9.15
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length502 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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-KW

   Cellular_componentcytosol

Inferred from direct assay PubMed 21166475. Source: TAIR

   Molecular_functionIMP dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 502501Inosine-5'-monophosphate dehydrogenase 2 HAMAP-Rule MF_03156
PRO_0000093687

Regions

Domain166 – 22560CBS
Nucleotide binding264 – 2663NAD By similarity
Nucleotide binding314 – 3163NAD By similarity
Region354 – 3563IMP binding By similarity
Region377 – 3782IMP binding By similarity
Region401 – 4055IMP binding By similarity

Sites

Active site3211Thioimidate intermediate By similarity
Metal binding3161Potassium; via carbonyl oxygen By similarity
Metal binding3181Potassium; via carbonyl oxygen By similarity
Metal binding3211Potassium; via carbonyl oxygen By similarity
Metal binding4881Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4891Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4901Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site3191IMP By similarity
Binding site4291IMP By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9SA34 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: FB87D84160818310

FASTA50254,051
        10         20         30         40         50         60 
MSGFEDGFSA EKLFSQGYSY TYDDVIFLPH FIDFSTDAVS LSTRLSKRVP LSIPCVASPM 

        70         80         90        100        110        120 
DTVSESHMAA AMAALGGIGI VHYNCDIDTQ ASVIRHAKSL QVPIASDAVF KCPEHQIGSV 

       130        140        150        160        170        180 
DDFGPSSFVF VSQTGTLTPK LLGYVSKSEW SSMKDDQKEV KIYDYMKSCE NKDYYVPWDI 

       190        200        210        220        230        240 
DLDKIEAVLE DKQKGFVVLE KEGETVNVVT KDDVERVKGY PKLGSGTVGA DKKWMVGAAI 

       250        260        270        280        290        300 
GTRESDKERL EHLVKAGANV VVLDSSQGNS IYQLEMIKYV KNTYPELDVV GGNVVTMYQA 

       310        320        330        340        350        360 
ENLIKAGVDG LRVGMGSGSI CTTQEVCAVG RGQATAVYKV STLAAQHGVP VIADGGISNS 

       370        380        390        400        410        420 
GHIVKALVLG ASTVMMGSFL AGSTEAPGAY EYRNGRRVKK YRGMGSLEAM TKGSDQRYLG 

       430        440        450        460        470        480 
DTAKLKIAQG VVGAVADKGS VLKFIPYTMH AVKQGFQDLG ASSLQSAHEL LRDNTLRLEA 

       490        500 
RTGAAQIEGG IHGLVSYEKK SF 

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC006341 Genomic DNA. Translation: AAD34687.1.
CP002684 Genomic DNA. Translation: AEE29441.1.
PIRF86298.
RefSeqNP_173085.1. NM_101501.2.
UniGeneAt.41887.

3D structure databases

ProteinModelPortalQ9SA34.
SMRQ9SA34. Positions 5-502.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid23444. 1 interaction.

Proteomic databases

PaxDbQ9SA34.
PRIDEQ9SA34.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G16350.1; AT1G16350.1; AT1G16350.
GeneID838204.
KEGGath:AT1G16350.

Organism-specific databases

TAIRAT1G16350.

Phylogenomic databases

eggNOGCOG0516.
HOGENOMHOG000165752.
InParanoidQ9SA34.
KOK00088.
OMATEGAMAI.
PhylomeDBQ9SA34.
ProtClustDBPLN02274.

Enzyme and pathway databases

BioCycARA:AT1G16350-MONOMER.
UniPathwayUPA00601; UER00295.

Gene expression databases

GenevestigatorQ9SA34.

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 nameIMDH2_ARATH
AccessionPrimary (citable) accession number: Q9SA34
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 110 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