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Reviewed, UniProtKB/Swiss-Prot O58045 (IMDH_PYRHO)

Last modified June 16, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Inosine-5'-monophosphate dehydrogenase
      Short name=IMP dehydrogenase
      Short name=IMPDH
      Short name=IMPD
    EC=1.1.1.205
Gene names
Name: guaB
Ordered Locus Names: PH0307
OrganismPyrococcus horikoshii [Complete proteome] [HAMAP]
Taxonomic identifier53953 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

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Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

IMP is the rate limiting enzyme in the de novo synthesis of guanine nucleotides and therefore is involved in the regulation of cell growth By similarity.

Catalytic activity

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

Pathway

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

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 2 CBS domains.

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Ontologies

Keywords
   Biological processGMP biosynthesis
Purine biosynthesis
   DomainCBS domain
Repeat
   LigandMetal-binding
NAD
Potassium
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processGMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionIMP dehydrogenase activity

Inferred from electronic annotation. Source: EC

potassium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Inosine-5'-monophosphate dehydrogenase
PRO_0000093722

Regions

Domain99 – 15456CBS 1
Domain156 – 21560CBS 2
Nucleotide binding228 – 24922NAD By similarity

Sites

Active site3011Thioimidate intermediate By similarity
Metal binding2961Potassium; via carbonyl oxygen By similarity
Metal binding2981Potassium; via carbonyl oxygen By similarity
Binding site3341IMP By similarity
Binding site3811IMP By similarity

Secondary structure

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

Details...

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Sequences

Sequence LengthMass (Da)Tools
O58045-1 [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

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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: 9679194] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OT3.

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Cross-references

Sequence databases

BA000001 Genomic DNA. Translation: BAA29380.1.
PIRE71456.
RefSeqNP_142293.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2CU0X-ray2.10A/B1-486[»]
ModBaseSearch...

Genome annotation databases

GeneID1444188.
GenomeReviewsGene locus PH0307 in contig BA000001_GR.
KEGGpho:PH0307.
NMPDRfig|70601.1.peg.288.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO58045.
OMAO58045. INGRKYK.

Enzyme and pathway databases

BRENDA1.1.1.205. 74679.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR000644. Cysta_beta_synth_core.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
IPR018529. IMP_DH_rel.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PfamPF00571. CBS. 1 hit.
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...

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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: June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents