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P0ADG8 (IMDH_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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:Z3772, ECs3370
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length488 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
   PTMAcetylation
   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 – 488488Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000093696

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

Amino acid modifications

Modified residue2671N6-acetyllysine By similarity
Modified residue4281N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P0ADG8 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: B0FD0A786779C98E

FASTA48852,022
        10         20         30         40         50         60 
MLRIAKEALT FDDVLLVPAH STVLPNTADL STQLTKTIRL NIPMLSAAMD TVTEARLAIA 

        70         80         90        100        110        120 
LAQEGGIGFI HKNMSIERQA EEVRRVKKHE SGVVTDPQTV LPTTTLREVK ELTERNGFAG 

       130        140        150        160        170        180 
YPVVTEENEL VGIITGRDVR FVTDLNQPVS VYMTPKERLV TVREGEAREV VLAKMHEKRV 

       190        200        210        220        230        240 
EKALVVDDEF HLIGMITVKD FQKAERKPNA CKDEQGRLRV GAAVGAGAGN EERVDALVAA 

       250        260        270        280        290        300 
GVDVLLIDSS HGHSEGVLQR IRETRAKYPD LQIIGGNVAT AAGARALAEA GCSAVKVGIG 

       310        320        330        340        350        360 
PGSICTTRIV TGVGVPQITA VADAVEALEG TGIPVIADGG IRFSGDIAKA IAAGASAVMV 

       370        380        390        400        410        420 
GSMLAGTEES PGEIELYQGR SYKSYRGMGS LGAMSKGSSD RYFQSDNAAD KLVPEGIEGR 

       430        440        450        460        470        480 
VAYKGRLKEI IHQQMGGLRS CMGLTGCGTI DELRTKAEFV RISGAGIQES HVHDVTITKE 


SPNYRLGS 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG57619.1.
BA000007 Genomic DNA. Translation: BAB36793.1.
PIRB91050.
G85894.
RefSeqNP_289062.1. NC_002655.2.
NP_311397.1. NC_002695.1.

3D structure databases

ProteinModelPortalP0ADG8.
SMRP0ADG8. Positions 1-487.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z3772.

Chemistry

BindingDBP0ADG8.

Proteomic databases

PRIDEP0ADG8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG57619; AAG57619; Z3772.
BAB36793; BAB36793; BAB36793.
GeneID917779.
957789.
KEGGece:Z3772.
ecs:ECs3370.
PATRIC18356164. VBIEscCol44059_3277.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycECOL386585:GJFA-3333-MONOMER.
ECOO157:GUAB-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_ECO57
AccessionPrimary (citable) accession number: P0ADG8
Secondary accession number(s): P06981, P76574, P78202
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: December 6, 2005
Last modified: February 19, 2014
This is version 65 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