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A9A5Y7 (IMDH_NITMS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. 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:Nmar_1569
OrganismNitrosopumilus maritimus (strain SCM1) [Reference proteome] [HAMAP]
Taxonomic identifier436308 [NCBI]
Taxonomic lineageArchaeaThaumarchaeotaNitrosopumilalesNitrosopumilaceaeNitrosopumilus

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_0000415694

Regions

Domain92 – 15059CBS 1
Domain151 – 20757CBS 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 binding4671Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4681Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2441NAD By similarity
Binding site2991IMP By similarity
Binding site4131IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9A5Y7 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 19BE67B0C7883900

FASTA47650,130
        10         20         30         40         50         60 
MEFKEGLTFD DVLLVPKYSD ITSRSQTDLT TKLSRNITIN IPFVSANMDT VTESSMAVAM 

        70         80         90        100        110        120 
ARAGGIGIIH RFLTIQEQAN EVLKVKRSGS VMIENPYSIS SDKSIQDALD YAEDKEISGL 

       130        140        150        160        170        180 
LVVDSNSKLV GIVTERDLLF AGSNGTIADV MTKDVVTAKP GVSLDEAKDI LHKHRIEKLP 

       190        200        210        220        230        240 
IVDDSGIIQG LITSKDITNN TDYPNASKDK KGRPLVGAAV GVKGDFLERS ESLLNAGADV 

       250        260        270        280        290        300 
LVVDIAHGHS ENAISTVRNI KKAFPDCELI AGNIATAQGA EDLIKAGVDA VKVGVGSGSI 

       310        320        330        340        350        360 
CITRVITGSG VPQLTAVMDC AKIGNDHGIP IISDGGTRTS GDATKALAAG ASSVMVGSML 

       370        380        390        400        410        420 
GGTDESPGTV LTKNGKRFKV YRGMASLAAS IGRKSKETGS ISLEDDLNDY VAEGVEAMVP 

       430        440        450        460        470 
YKGTVTDILK QLAGGVRSGL SYCGAHTIPQ MQQNAEFIKM SRAGFAESQP HDVLLM 

« Hide

References

[1]"Complete sequence of Nitrosopumilus maritimus SCM1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Stahl D., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SCM1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000866 Genomic DNA. Translation: ABX13465.1.
RefSeqYP_001582903.1. NC_010085.1.

3D structure databases

ProteinModelPortalA9A5Y7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING436308.Nmar_1569.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX13465; ABX13465; Nmar_1569.
GeneID5772999.
KEGGnmr:Nmar_1569.

Phylogenomic databases

eggNOGCOG0517.
HOGENOMHOG000165755.
KOK00088.
OMASSMGYCG.

Enzyme and pathway databases

BioCycNMAR436308:GI3J-1613-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_NITMS
AccessionPrimary (citable) accession number: A9A5Y7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: January 15, 2008
Last modified: February 19, 2014
This is version 42 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