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Q8F4Q4 (IMDH_LEPIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 82. 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:LA_1986
OrganismLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) [Reference proteome] [HAMAP]
Taxonomic identifier189518 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length508 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 – 508508Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000415689

Regions

Domain111 – 17060CBS 1
Domain174 – 23057CBS 2
Nucleotide binding317 – 3193NAD By similarity
Region357 – 3593IMP binding By similarity
Region380 – 3812IMP binding By similarity
Region404 – 4085IMP binding By similarity

Sites

Active site3241Thioimidate intermediate By similarity
Metal binding3191Potassium; via carbonyl oxygen By similarity
Metal binding3211Potassium; via carbonyl oxygen By similarity
Metal binding3241Potassium; via carbonyl oxygen By similarity
Metal binding4921Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2671NAD By similarity
Binding site3221IMP By similarity
Binding site4321IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8F4Q4 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 5D24AEC8D93512FA

FASTA50855,881
        10         20         30         40         50         60 
MSNQTYRDSE YLDGLSGEEL FNLQIGLTYR DFLVLPGFID FHPSEVELET RLTRNIKLKR 

        70         80         90        100        110        120 
PFISSPMDTV TESQMAIAQA LMGGIGIIHY NNTIEEQVAL VEKVKRFENG FITDPVILGP 

       130        140        150        160        170        180 
KNVIRDLDAI KERKGFTGIP VTEDGTRNSK LIGIVTNRDI DFEKNREITL DKVMTTNLIT 

       190        200        210        220        230        240 
GKEGITLQDA NEIIKKSKIG KLPIVDSQGK LVSLVSRSDL KKNKEFPDAS KDERKRLRCG 

       250        260        270        280        290        300 
AAVSTLLESR DRVAALYEAG VDVIIIDSAQ GNSNYQIEMI QFIKKEFKNL DIVAGNVVTR 

       310        320        330        340        350        360 
AQAENLIRAG ADGLRIGMGP GSICITQDTM AVGRAQATAI YQTAKHSAKY DVPVIADGGI 

       370        380        390        400        410        420 
SNIGDIANSL AIGASTCMMG FMFAGTTEAP GEYFYENGIR LKKYRGMASI EAMKAGGDKR 

       430        440        450        460        470        480 
YFNEGQKVKV AQGVSGSVVD RGSILNFIPY LSQGLRLSFQ DMGYKSIPEI HKALRDGKLR 

       490        500 
FERRSESAQA QGSVHGLYSF SAPTMRAE 

« Hide

References

[1]"Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing."
Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H. expand/collapse author list , Yin H.-F., Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.
Nature 422:888-893(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 56601.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE010300 Genomic DNA. Translation: AAN49185.1.
RefSeqNP_712167.1. NC_004342.2.

3D structure databases

ProteinModelPortalQ8F4Q4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING189518.LA1986.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN49185; AAN49185; LA_1986.
GeneID1151329.
KEGGlil:LA_1986.
PATRIC22384813. VBILepInt91350_1979.

Phylogenomic databases

HOGENOMHOG000165752.
KOK00088.
OMAHGHSKNI.
OrthoDBEOG6GTZPV.

Enzyme and pathway databases

BioCycLINT189518:GJBB-1599-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. 1 hit.
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_LEPIN
AccessionPrimary (citable) accession number: Q8F4Q4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 82 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