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Q9L6B7 (IMDH_PASMU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 97. 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:PM0295
OrganismPasteurella multocida (strain Pm70) [Complete proteome] [HAMAP]
Taxonomic identifier272843 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella

Protein attributes

Sequence length487 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
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 – 487487Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000093703

Regions

Domain93 – 14957CBS 1
Domain153 – 21462CBS 2
Nucleotide binding248 – 2503NAD By similarity
Nucleotide binding298 – 3003NAD By similarity
Region338 – 3403IMP binding By similarity
Region361 – 3622IMP binding By similarity
Region385 – 3895IMP binding By similarity

Sites

Active site3051Thioimidate intermediate By similarity
Metal binding3001Potassium; via carbonyl oxygen By similarity
Metal binding3021Potassium; via carbonyl oxygen By similarity
Metal binding3051Potassium; via carbonyl oxygen By similarity
Metal binding4691Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4701Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4711Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2481NAD By similarity
Binding site3031IMP By similarity
Binding site4151IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9L6B7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 0871DB08893B8FCA

FASTA48752,008
        10         20         30         40         50         60 
MLRVIKEALT FDDVLLVPAH STVLPNTADL STQLTKTIRL NIPMLSAAMD TVTETKLAIS 

        70         80         90        100        110        120 
LAQEGGIGFI HKNMSIERQA ERVRKVKKFE SGIVSDPVTV SPTLSLAELS ELVKKNGFAS 

       130        140        150        160        170        180 
FPVVDDEKNL VGIITGRDTR FVTDLNKTVA DFMTPKARLV TVKRNASRDE IFGLMHTHRV 

       190        200        210        220        230        240 
EKVLVVSDDF KLKGMITLKD YQKSEQKPQA CKDEFGRLRV GAAVGAGPGN EERIDALVKA 

       250        260        270        280        290        300 
GVDVLLIDSS HGHSEGVLQR VRETRAKYPD LPIVAGNVAT AEGAIALADA GASAVKVGIG 

       310        320        330        340        350        360 
PGSICTTRIV TGVGVPQITA IADAAEALKD RGIPVIADGG IRFSGDISKA IAAGASCVMV 

       370        380        390        400        410        420 
GSMFAGTEEA PGEIELYQGR AFKSYRGMGS LGAMSKGSSD RYFQSDNAAD KLVPEGIEGR 

       430        440        450        460        470        480 
IPYKGFLKEI IHQQMGGLRS CMGLTGCATI DELRTKAQFV RISGAGIQES HVHDVTITKE 


APNYRMG 

« Hide

References

« Hide 'large scale' references
[1]"Identification of Pasteurella multocida virulence genes in a septicemic mouse model using signature-tagged mutagenesis."
Fuller T.E., Kennedy M.J., Lowery D.E.
Microb. Pathog. 29:25-38(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genomic sequence of Pasteurella multocida Pm70."
May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pm70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF237921 Genomic DNA. Translation: AAF68407.1.
AE004439 Genomic DNA. Translation: AAK02379.1.
RefSeqNP_245232.1. NC_002663.1.

3D structure databases

ProteinModelPortalQ9L6B7.
SMRQ9L6B7. Positions 3-485.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272843.PM0295.

Proteomic databases

PRIDEQ9L6B7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK02379; AAK02379; PM0295.
GeneID1243642.
KEGGpmu:PM0295.
PATRIC22869746. VBIPasMul88067_0305.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0517.
HOGENOMHOG000165755.
KOK00088.
OMASSMGYCG.
OrthoDBEOG6GTZPV.
ProtClustDBPRK05567.

Enzyme and pathway databases

BioCycPMUL272843:GC8W-299-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_PASMU
AccessionPrimary (citable) accession number: Q9L6B7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 97 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