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Q8G3N6 (IMDH_BIFLO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. 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:BL1722
OrganismBifidobacterium longum (strain NCC 2705) [Reference proteome] [HAMAP]
Taxonomic identifier206672 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length545 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 – 545545Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000415688

Regions

Domain138 – 19457CBS 1
Domain201 – 25858CBS 2
Nucleotide binding347 – 3493NAD By similarity
Region387 – 3893IMP binding By similarity
Region410 – 4112IMP binding By similarity
Region434 – 4385IMP binding By similarity

Sites

Active site3541Thioimidate intermediate By similarity
Metal binding3491Potassium; via carbonyl oxygen By similarity
Metal binding3511Potassium; via carbonyl oxygen By similarity
Metal binding3541Potassium; via carbonyl oxygen By similarity
Metal binding5241Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5251Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5261Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2951NAD By similarity
Binding site3521IMP By similarity
Binding site4701IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8G3N6 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E56CD074DAF63CD3

FASTA54558,263
        10         20         30         40         50         60 
MRCRTRQRIS ERSQACVVKV SACSYSVCMA TNLDELNAQS AYAPLPPIFA KLGLAYDDVL 

        70         80         90        100        110        120 
LLPNETDVIP SEVDTSTHLT RKIVMKAPVL SAAMDTVTES EMAIAMARNG GIGVLHRNLS 

       130        140        150        160        170        180 
IDDQAAQVDV VKRSESGMIT DPLTVNPEVT LADLDKLCGK FHISGLPVVD KENKLVGIIT 

       190        200        210        220        230        240 
NRDMRFIASE DYDTLKVKDV MTKENLVTGP SNISKDDAHR LLAQHKVEKL PLVDEEGHLT 

       250        260        270        280        290        300 
GLITVKDFVK TEQYPDATKD EQGRLRVAAG VGFLGDAWQR ASALMEAGVD VLVVDTANGE 

       310        320        330        340        350        360 
ARLALDMISR LKHDSAFDGV QIIGGNVGTR SGAQAMIEAG ADAVKVGIGP GSICTTRIVA 

       370        380        390        400        410        420 
GVGVPQLTAV YEAAQACRAA GVPCIADGGI HYSGDIAKAL VAGASSVMLG GTLAGCEEAP 

       430        440        450        460        470        480 
GEKVLLHGKQ YKLYRGMGSL GAMAPRGKKS YSKDRYFQAD VTSSDKVVPE GVEGEVPYRG 

       490        500        510        520        530        540 
PLNAVLYQML GGLHQSMFYI GAHNIAEMPE RGKFIRITDA GLRESHPHDI VMTTEAPNYS 


GFHNN 

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References

[1]"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract."
Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.
Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCC 2705.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014295 Genomic DNA. Translation: AAN25506.1.
RefSeqNP_696870.1. NC_004307.2.

3D structure databases

ProteinModelPortalQ8G3N6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING206672.BL1722.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN25506; AAN25506; BL1722.
GeneID1021976.
KEGGblo:BL1722.
PATRIC21120714. VBIBifLon107831_1776.

Phylogenomic databases

HOGENOMHOG000165755.
KOK00088.
OMAFQADVRS.
OrthoDBEOG6GTZPV.
PhylomeDBQ8G3N6.

Enzyme and pathway databases

BioCycBLON206672:GI1E-1707-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_BIFLO
AccessionPrimary (citable) accession number: Q8G3N6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 83 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