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B1L5U5 (IMDH_KORCO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. 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:Kcr_1078
OrganismKorarchaeum cryptofilum (strain OPF8) [Reference proteome] [HAMAP]
Taxonomic identifier374847 [NCBI]
Taxonomic lineageArchaeaKorarchaeotaCandidatus Korarchaeum

Protein attributes

Sequence length476 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 – 476476Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000415693

Regions

Domain93 – 15159CBS 1
Domain152 – 21160CBS 2
Nucleotide binding292 – 2943NAD By similarity
Region334 – 3363IMP binding By similarity
Region357 – 3582IMP binding By similarity
Region381 – 3855IMP binding By similarity

Sites

Active site2991Thioimidate intermediate By similarity
Metal binding2941Potassium; via carbonyl oxygen By similarity
Metal binding2961Potassium; via carbonyl oxygen By similarity
Metal binding2991Potassium; via carbonyl oxygen By similarity
Metal binding4621Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2421NAD By similarity
Binding site2971IMP By similarity
Binding site4081IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
B1L5U5 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 6AAC31F930E62260

FASTA47651,195
        10         20         30         40         50         60 
MRIDRFEFAF TFNDVILLPG KTEIEPSNVD LTTRIGNIAL SIPILSSPMD TVTEEEMSIA 

        70         80         90        100        110        120 
MARMGGLGIL HRNCSVEEQV NMAKAVKRAE SFIIRDVITV SPEDSVEEAR RLMREHGISG 

       130        140        150        160        170        180 
LPVIVGRKLV GIVTRRDVYF AENGSLLVKD IMTKDPITVG PEITPQEARK IMARYKIEKL 

       190        200        210        220        230        240 
PVVSESGELI GLVTAKDVFY RESHPFATRD EEGRLRVGAA ISPFDIDRAK TLAPYVDVLV 

       250        260        270        280        290        300 
TDVAHFHNEN VISATKRIID EVGVPVIAGN IGTYEAAEEA ITRLDIIGLR VGIGSGSICT 

       310        320        330        340        350        360 
TGEVTGVAAP TLYAVASASE AVRKYSKDVA VIADGGIRGP GEAAKAFAMG ADAVMLGYAL 

       370        380        390        400        410        420 
AGTKEAPGST MMIGGKMYKI YRGMGSPSAR SKRFAMDRYS KPSKDIAEGI EGLVPYRGDV 

       430        440        450        460        470 
TTVVDRFVAG LKAAFGYVGA ANISEMKSKA RVALISHSGM SEIAPHDVKP LEKISD 

« Hide

References

[1]"A korarchaeal genome reveals new insights into the evolution of the Archaea."
Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L., Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A., Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G., Richardson P., Keller M., Stetter K.O.
Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OPF8.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000968 Genomic DNA. Translation: ACB07824.1.
RefSeqYP_001737507.1. NC_010482.1.

3D structure databases

ProteinModelPortalB1L5U5.
SMRB1L5U5. Positions 9-92.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING374847.Kcr_1078.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB07824; ACB07824; Kcr_1078.
GeneID6094355.
KEGGkcr:Kcr_1078.

Phylogenomic databases

eggNOGCOG0516.
HOGENOMHOG000165755.
KOK00088.
OMAHGHSKNI.

Enzyme and pathway databases

BioCycKCRY374847:GH12-1082-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]
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_KORCO
AccessionPrimary (citable) accession number: B1L5U5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: April 29, 2008
Last modified: May 14, 2014
This is version 41 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