Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9ZL14 (IMDH_HELPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 101. 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:jhp_0768
OrganismHelicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99) [Complete proteome] [HAMAP]
Taxonomic identifier85963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length481 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 – 481481Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000093699

Regions

Domain92 – 14857CBS 1
Domain152 – 20958CBS 2
Nucleotide binding293 – 2953NAD By similarity
Region333 – 3353IMP binding By similarity
Region356 – 3572IMP binding By similarity
Region380 – 3845IMP binding By similarity

Sites

Active site3001Thioimidate intermediate By similarity
Metal binding2951Potassium; via carbonyl oxygen By similarity
Metal binding2971Potassium; via carbonyl oxygen By similarity
Metal binding3001Potassium; via carbonyl oxygen By similarity
Metal binding4641Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4651Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4661Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2441NAD By similarity
Binding site2981IMP By similarity
Binding site4101IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZL14 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 688262DCD14EFDAB

FASTA48151,689
        10         20         30         40         50         60 
MRILQRALTF EDVLMVPRKS SVLPKDVSLK SRLTKNIGLN IPFISAAMDT VTEHKTAIAM 

        70         80         90        100        110        120 
ARLGGIGIVH KNMDIQTQVK EITKVKKSES GVINDPIFIH AHRTLADAKV ITDNYKISGV 

       130        140        150        160        170        180 
PVVDDKGLLI GILTNRDVRF ETDLSKKVGD VMTKMPLVTA HVGISLDEAS DLMHKHKIEK 

       190        200        210        220        230        240 
LPIVDKDNVL KGLITIKDIQ KRIEYPEANK DDFGRLRVGA AIGVGQLDRA EMLVKAGVDA 

       250        260        270        280        290        300 
LVLDSAHGHS ANILHTLEEI KKSLVVDVIV GNVVTKEATS DLISAGADAV KVGIGPGSIC 

       310        320        330        340        350        360 
TTRIVAGVGM PQVSAIDNCV EVASKFDIPV IADGGIRYSG DVAKALALGA SSVMIGSLLA 

       370        380        390        400        410        420 
GTEESPGDFM IYQGRQYKSY RGMGSIGAMT KGSSDRYFQE GVASEKLVPE GIEGRVPYRG 

       430        440        450        460        470        480 
KVSDMIFQLV GGVRSSMGYQ GAKNILELYQ NAEFVEITSA GLKESHVHGV DITKEAPNYY 


G 

« Hide

References

[1]"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori."
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. expand/collapse author list , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.
Nature 397:176-180(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J99 / ATCC 700824.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001439 Genomic DNA. Translation: AAD06347.1.
PIRH71890.
RefSeqNP_223486.1. NC_000921.1.

3D structure databases

ProteinModelPortalQ9ZL14.
SMRQ9ZL14. Positions 2-480.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9ZL14. 1 interaction.
STRING85963.jhp0768.

Proteomic databases

PRIDEQ9ZL14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD06347; AAD06347; jhp_0768.
GeneID890128.
KEGGhpj:jhp0768.
PATRIC20606261. VBIHelPyl98156_0836.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0517.
KOK00088.
OMASSMGYCG.
OrthoDBEOG6GTZPV.
ProtClustDBPRK05567.

Enzyme and pathway databases

BioCycHPYL85963:GJB9-780-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_HELPJ
AccessionPrimary (citable) accession number: Q9ZL14
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 1999
Last modified: February 19, 2014
This is version 101 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