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Q59011 (IMDH_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:MJ1616
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length496 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 – 496496Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000093719

Regions

Domain96 – 15257CBS 1
Domain156 – 21257CBS 2
Nucleotide binding299 – 3013NAD By similarity
Region339 – 3413IMP binding By similarity
Region362 – 3632IMP binding By similarity
Region386 – 3905IMP binding By similarity

Sites

Active site3061Thioimidate intermediate By similarity
Metal binding3011Potassium; via carbonyl oxygen By similarity
Metal binding3031Potassium; via carbonyl oxygen By similarity
Metal binding3061Potassium; via carbonyl oxygen By similarity
Metal binding4771Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4781Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4791Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2471NAD By similarity
Binding site3041IMP By similarity
Binding site4231IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q59011 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: C3E03FDDF3898396

FASTA49653,317
        10         20         30         40         50         60 
MFLKKLIEAK KAYTFDDVLL VPNASWVEPK DTDVSTDLAG LKLNIPIVSA AMDTVTEKEM 

        70         80         90        100        110        120 
AIALARLGGL GVIHRNMSIE EQVHQVQAVK KADEVVIKDV ITVSPDDTVG EAINVMETYS 

       130        140        150        160        170        180 
ISGLPVVDNE DKLVGIITHR DVKAIEDKTK KVKDVMTKDV VCAKEDVEEE EALELMYANR 

       190        200        210        220        230        240 
VERLPIVDDE NRLIGIITLR DILKRRKYPQ AARDKKGRLL VAAACGPHDF ERAKALIEAE 

       250        260        270        280        290        300 
VDAIAIDCAH AHNMRVVENV KKFKEMLEGT DIKLIVGNIA TKEAAEDLIK AGADVLKVGI 

       310        320        330        340        350        360 
GPGSICTTRV VAGVGVPQLT AVAEVADVAK EHNVPIIADG GIRYSGDIAK AIAAGADAVM 

       370        380        390        400        410        420 
LGSLLAGTDE APGQLMVING RKYKQYRGMG SLGAMTGGVG AGADRYFQAP AKSHMKHVKL 

       430        440        450        460        470        480 
VPEGVEGAVP YKGPVSEVVF QLIGGLRASM GYCGAKNLKE MQEKARFVII TPSGQVESHP 

       490 
HDIIITNEAP NYPLGK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77117 Genomic DNA. Translation: AAB99638.1.
PIRG64501.
RefSeqNP_248626.1. NC_000909.1.

3D structure databases

ProteinModelPortalQ59011.
SMRQ59011. Positions 2-493.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243232.MJ1616.

Proteomic databases

PRIDEQ59011.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB99638; AAB99638; MJ_1616.
GeneID1452525.
KEGGmja:MJ_1616.

Phylogenomic databases

eggNOGCOG0517.
KOK00088.
OMAHGHSKNI.
PhylomeDBQ59011.

Enzyme and pathway databases

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]
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_METJA
AccessionPrimary (citable) accession number: Q59011
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 106 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

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names