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O58045 (IMDH_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:PH0307
OrganismPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]
Taxonomic identifier70601 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus ›

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
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_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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000093722

Regions

Domain99 – 15456CBS 1
Domain156 – 21560CBS 2
Nucleotide binding294 – 2963NAD By similarity
Region334 – 3363IMP binding HAMAP-Rule MF_01964
Region357 – 3582IMP binding HAMAP-Rule MF_01964
Region381 – 3855IMP binding HAMAP-Rule MF_01964

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
Binding site4121IMP

Secondary structure

1 ............................................................. 486
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O58045 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 6B21E9B7B3AA7C3C

FASTA48652,933
        10         20         30         40         50         60 
MGKFVEKLEK AIKGYTFDDV LLIPQATEVE PKDVDVSTRI TPNVKLNIPI LSAAMDTVTE 

        70         80         90        100        110        120 
WEMAVAMARE GGLGVIHRNM GIEEQVEQVK RVKRAERLIV EDVITIAPDE TVDFALFLME 

       130        140        150        160        170        180 
KHGIDGLPVV EDEKVVGIIT KKDIAAREGK LVKELMTKEV ITVPESIEVE EALKIMIENR 

       190        200        210        220        230        240 
IDRLPVVDER GKLVGLITMS DLVARKKYKN AVRDENGELL VAAAVSPFDI KRAIELDKAG 

       250        260        270        280        290        300 
VDVIVVDTAH AHNLKAIKSM KEMRQKVDAD FIVGNIANPK AVDDLTFADA VKVGIGPGSI 

       310        320        330        340        350        360 
CTTRIVAGVG VPQITAVAMV ADRAQEYGLY VIADGGIRYS GDIVKAIAAG ADAVMLGNLL 

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

       430        440        450        460        470        480 
RGTVSEVLYQ LVGGLKAGMG YVGARNIREL KEKGEFVIIT HAGIKESHPH DIIITNEAPN 


YPLEKF

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3."
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. expand/collapse author list , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.
DNA Res. 5:55-76(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
[2]"Crystal structure of inosine-5'-monophosphate dehydrogenase from Pyrococcus horikoshii OT3."
RIKEN structural genomics initiative (RSGI)
Submitted (JUL-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH XMP.
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000001 Genomic DNA. Translation: BAA29380.1.
PIRE71456.
RefSeqNP_142293.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CU0X-ray2.10A/B1-486[»]
ProteinModelPortalO58045.
SMRO58045. Positions 3-480.
ModBaseSearch...

Protein-protein interaction databases

STRING70601.PH0307.

Proteomic databases

PRIDEO58045.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA29380; BAA29380; BAA29380.
GeneID1444188.
KEGGpho:PH0307.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0517.
HOGENOMHOG000165755.
KOK00088.
OMASAGLKES.
ProtClustDBPRK05567.

Enzyme and pathway databases

BioCycPHOR70601:GJWR-289-MONOMER.
UniPathwayUPA00601; UER00295.

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

EvolutionaryTraceO58045.

Entry information

Entry nameIMDH_PYRHO
AccessionPrimary (citable) accession number: O58045
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: May 1, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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