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Q9UY49 (IMDH_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 102. 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:PYRAB16590
ORF Names:PAB1250
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length485 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
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 – 485485Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000093720

Regions

Domain99 – 15456CBS 1
Domain156 – 21560CBS 2
Nucleotide binding294 – 2963NAD By similarity
Region334 – 3363IMP binding By similarity
Region357 – 3582IMP binding By similarity
Region381 – 3855IMP binding By similarity

Sites

Active site3011Thioimidate intermediate By similarity
Metal binding2961Potassium; via carbonyl oxygen By similarity
Metal binding2981Potassium; via carbonyl oxygen By similarity
Metal binding3011Potassium; via carbonyl oxygen By similarity
Metal binding4661Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4671Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4681Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2471NAD By similarity
Binding site2991IMP By similarity
Binding site4121IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9UY49 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: FF3DDB8521FC7113

FASTA48552,868
        10         20         30         40         50         60 
MGKFAKKLER AIRGYTFDDV LLIPQATEVE PKDVDVSTQI TPNVKLNIPI LSAAMDTVTE 

        70         80         90        100        110        120 
WEMAVAMARE GGLGVIHRNM SIEEQVEQVK RVKKAERFIV EDVITISPEE TVDFALFLME 

       130        140        150        160        170        180 
KHDIDGLPVV ENEKVVGIIS KKDIAAREGK LVKELMTKDV ITVPENIEVE EALKIMIENR 

       190        200        210        220        230        240 
IDRLPVVDKE GRLIGLITMS DLVARKKYKN AVRDENGELL VAAAVSPFDI RRAIELDRAG 

       250        260        270        280        290        300 
ADVIVVDTAH AHNLKAIKAM KEMRQKVDAD FIVGNIANPK AVDDLTFADA VKVGIGPGSI 

       310        320        330        340        350        360 
CTTRIVAGVG VPQITAIAMV ADRAQEYGLY VIADGGIKYS GDIVKAIAAG ADAVMLGNLL 

       370        380        390        400        410        420 
AGTKEAPGKE VIINGRKYKQ YRGMGSLGAM MKGGAERYYQ GGYMKTRKFV PEGVEGVVPY 

       430        440        450        460        470        480 
RGTVSEVLYQ LVGGLKAGMG YVGARNIKEL KEKGEFVIIT SAGLRESHPH DIIITNEAPN 


YPLEK 

« Hide

References

« Hide 'large scale' references
[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.
[2]"Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
Gao J., Wang J.
Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ248288 Genomic DNA. Translation: CAB50563.1.
HE613800 Genomic DNA. Translation: CCE71127.1.
PIRE75015.
RefSeqNP_127333.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9UY49.
SMRQ9UY49. Positions 3-480.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272844.PAB1250.

Proteomic databases

PRIDEQ9UY49.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB50563; CAB50563; PAB1250.
GeneID1495956.
KEGGpab:PAB1250.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0517.
HOGENOMHOG000165755.
KOK00088.
OMASSMGYCG.
ProtClustDBPRK05567.

Enzyme and pathway databases

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]
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...

Entry information

Entry nameIMDH_PYRAB
AccessionPrimary (citable) accession number: Q9UY49
Secondary accession number(s): G8ZK20
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 102 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