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Q0WD32 (IMDH_YERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. 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:YPO2871, y1362, YP_2737
OrganismYersinia pestis [Reference proteome] [HAMAP]
Taxonomic identifier632 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

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.

Sequence caution

The sequence AAM84935.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAS62925.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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 – 487487Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000415691

Regions

Domain93 – 15260CBS 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
Q0WD32 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 97A043EB8F1BA09A

FASTA48751,824
        10         20         30         40         50         60 
MLRIAKEALT FDDVLLVPAH STVLPNTAEL GTQLTATIRL NIPMLSAAMD TVTESRLAIA 

        70         80         90        100        110        120 
LAQEGGLGFI HKNMSIERQA EEVSRVKKHE SGVVTEPQTV TPTTTLRQVK ELTARNGFAG 

       130        140        150        160        170        180 
YPVVTEDYEL VGIITGRDVR FVTDLDQPVT AVMTPKERLV TVKEGETREV VLQKMHEKRV 

       190        200        210        220        230        240 
EKVLVVDDSF HLRGMITVKD FQKAERKPNA CKDEHGRLRV GAAVGAGAGN EERIDALVAA 

       250        260        270        280        290        300 
GVDVLLIDSS HGHSEGVLQR IRETRAKYPN LQIVGGNVAT GAGAKALADA GVSAVKVGIG 

       310        320        330        340        350        360 
PGSICTTRIV TGVGVPQITA IADAVEALEG TGIPVIADGG IRFSGDIAKA IAAGASCVMV 

       370        380        390        400        410        420 
GSMLAGTEES PGEIELYQGR SFKSYRGMGS LGAMSKGSSD RYFQTDNAAD KLVPEGIEGR 

       430        440        450        460        470        480 
VAYKGLLKEI VHQQMGGLRS CMGLTGCGTI NELRTKAEFV RISGAGIQES HVHDVTITKE 


SPNYRMM 

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References

[1]"Genome sequence of Yersinia pestis, the causative agent of plague."
Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. expand/collapse author list , Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:523-527(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CO-92 / Biovar Orientalis.
[2]"Genome sequence of Yersinia pestis KIM."
Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. expand/collapse author list , Matson J.S., Blattner F.R., Perry R.D.
J. Bacteriol. 184:4601-4611(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KIM10+ / Biovar Mediaevalis.
[3]"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."
Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. expand/collapse author list , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.
DNA Res. 11:179-197(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 91001 / Biovar Mediaevalis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL590842 Genomic DNA. Translation: CAL21482.1.
AE009952 Genomic DNA. Translation: AAM84935.1. Different initiation.
AE017042 Genomic DNA. Translation: AAS62925.1. Different initiation.
PIRAG0349.
RefSeqNP_668684.1. NC_004088.1.
NP_994048.1. NC_005810.1.
YP_002347806.1. NC_003143.1.

3D structure databases

ProteinModelPortalQ0WD32.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING214092.YPO2871.

Proteomic databases

PRIDEQ0WD32.

Protocols and materials databases

DNASU1146309.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM84935; AAM84935; y1362.
AAS62925; AAS62925; YP_2737.
GeneID1146309.
1175695.
2765560.
KEGGype:YPO2871.
ypk:y1362.
ypm:YP_2737.
PATRIC18595578. VBIYerPes7843_3491.
18624444. VBIYerPes99487_3147.

Phylogenomic databases

HOGENOMHOG000165755.
KOK00088.
OMASSMGYCG.
OrthoDBEOG6GTZPV.
ProtClustDBPRK05567.

Enzyme and pathway databases

BioCycYPES214092:GKDD-2833-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_YERPE
AccessionPrimary (citable) accession number: Q0WD32
Secondary accession number(s): Q74S88, Q8D0Z1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: September 5, 2006
Last modified: February 19, 2014
This is version 62 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