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O67820 (IMDH_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Short name=IMP dehydrogenase
Short name=IMPD
Short name=IMPDH
EC=1.1.1.205
Gene names
Name:guaB
Ordered Locus Names:aq_2023
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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_01964

Catalytic activity

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH. HAMAP-Rule MF_01964

Cofactor

Potassium By similarity. HAMAP-Rule MF_01964

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_01964

Pathway

Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. HAMAP-Rule MF_01964

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01964

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 2 CBS domains.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionIMP dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

adenyl nucleotide binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 490490Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000093689

Regions

Domain96 – 15459CBS 1
Domain158 – 21861CBS 2
Nucleotide binding302 – 3043NAD By similarity
Region342 – 3443IMP binding By similarity
Region365 – 3662IMP binding By similarity
Region389 – 3935IMP binding By similarity

Sites

Active site3091Thioimidate intermediate By similarity
Metal binding3041Potassium; via carbonyl oxygen By similarity
Metal binding3061Potassium; via carbonyl oxygen By similarity
Metal binding3091Potassium; via carbonyl oxygen By similarity
Metal binding4721Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4731Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4741Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2521NAD By similarity
Binding site3071IMP By similarity
Binding site4181IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
O67820 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 66605CDDB8348CE4

FASTA49053,401
        10         20         30         40         50         60 
MVEVEKKIKE GLTFDDVLLV PQYSEVLPHE VDVSTYLTKR IKLNIPIVSA AMDTVTEARL 

        70         80         90        100        110        120 
AIALAREGGI GIIHRNLPIK KQAEEVEKVK KSESGMIINP VTVKPDTRVK EALDIMAKYK 

       130        140        150        160        170        180 
ISGVPVVDEE RKLIGILTNR DLRFIKPEDY SKPVSEFMTK ENLITAPEGI TLDEAEEIFR 

       190        200        210        220        230        240 
KYKIEKLPIV DKEGKIKGLI TIKDIVKRKK YPNACKDELG RLRVGAAVGT GEETLDRVAA 

       250        260        270        280        290        300 
LVEAGVDVIV VDTAHGHSKR VLETVEKIKA NFPEVDVIAG NVATAEGTKA LIEAGADAVK 

       310        320        330        340        350        360 
VGVGPGSICT TRIVAGVGVP QLTAIMEAAS AAREYDIPII ADGGIRYSGD IVKALAAGAS 

       370        380        390        400        410        420 
AVMLGNLLAG TEEAPGETIY YQGRAYKVYR GMGSLGAMSS RLSSDRYGQE KMEKFVPEGI 

       430        440        450        460        470        480 
EGRVPYKGKL ADVVYQLVGG LRSGMGYVGA RNIKELQEKA KFVRITWAGY RESHVHDVQI 

       490 
TREAPNYWVD 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07779.1.
PIRH70473.
RefSeqNP_214389.1. NC_000918.1.

3D structure databases

ProteinModelPortalO67820.
SMRO67820. Positions 6-487.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224324.aq_2023.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC07779; AAC07779; aq_2023.
GeneID1193717.
KEGGaae:aq_2023.
PATRIC20960942. VBIAquAeo85532_1566.

Phylogenomic databases

eggNOGCOG0517.
HOGENOMHOG000165754.
KOK00088.
OMAHGHSKNI.
OrthoDBEOG6GTZPV.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-1450-MONOMER.
RETL1328306-WGS:GSTH-803-MONOMER.
UniPathwayUPA00601; UER00295.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01964. IMPDH.
InterProIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
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...

Entry information

Entry nameIMDH_AQUAE
AccessionPrimary (citable) accession number: O67820
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways