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Q9HLK8 (IMDH_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. 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:Ta0219
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP]
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

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
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 – 485485Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000415695

Regions

Domain97 – 15458CBS 1
Domain155 – 21157CBS 2
Nucleotide binding295 – 2973NAD By similarity
Region335 – 3373IMP binding By similarity
Region358 – 3592IMP binding By similarity
Region382 – 3865IMP binding By similarity

Sites

Active site3021Thioimidate intermediate By similarity
Metal binding2971Potassium; via carbonyl oxygen By similarity
Metal binding2991Potassium; via carbonyl oxygen By similarity
Metal binding3021Potassium; via carbonyl oxygen By similarity
Metal binding4631Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4641Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4651Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2461NAD By similarity
Binding site3001IMP By similarity
Binding site4091IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HLK8 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 4450C3DC8FA68673

FASTA48552,225
        10         20         30         40         50         60 
MYREKFTKIT EGFTFDDVLL IPMRTAVEPK NVVVSSRISR HIQVKVPIVS SPMDTVTEDA 

        70         80         90        100        110        120 
MAIAMARYGA IGVIHRNQPR EKEVEMVKRV KREETIIIRD VYTISPETPI EVARTLMATR 

       130        140        150        160        170        180 
NIAGLPVVKD DKLVGIVTKR DLEFVKKGSS VSDVMVRDVI TAPENVDIDE AIEILHKNRI 

       190        200        210        220        230        240 
EKLPLVDSSG HLVGLITAKD IITRQKFPDA SRDSEGQLMV GAAVGPFDLD RAVEVEKAGA 

       250        260        270        280        290        300 
DFIVVDTAHA DNENVLSSLK KMRKQISVDI VAGNIATAQA AEDLISCDVD GLRVGIGPGS 

       310        320        330        340        350        360 
ICTTRIVAGV GVPQLTAISD VAEAAKDSGI PVIADGGIRY SGDIVKAIAA GADAVMLGSM 

       370        380        390        400        410        420 
LAGTEESPGQ EMIINGRKYK AYRGMGSIGA LTTGLSDRYS KLGNGFIAEG VEGAVPYRGR 

       430        440        450        460        470        480 
VDEVLFQLVG GLRTGMGYVG AATIEDLKRN GKFVRITNNG LRESHPHDIR LISEPPNYQI 


SNISP 

« Hide

References

[1]"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL445063 Genomic DNA. Translation: CAC11365.1.
RefSeqNP_393697.1. NC_002578.1.

3D structure databases

ProteinModelPortalQ9HLK8.
SMRQ9HLK8. Positions 199-477.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273075.Ta0219.

Proteomic databases

PRIDEQ9HLK8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC11365; CAC11365; CAC11365.
GeneID1455855.
KEGGtac:Ta0219.

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_THEAC
AccessionPrimary (citable) accession number: Q9HLK8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: March 1, 2001
Last modified: February 19, 2014
This is version 84 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