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Q49729 (IMDH_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 106. 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:ML0387
ORF Names:B1620_C3_238
OrganismMycobacterium leprae (strain TN) [Complete proteome] [HAMAP]
Taxonomic identifier272631 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length529 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 – 529529Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000093701

Regions

Domain129 – 18557CBS 1
Domain189 – 24658CBS 2
Nucleotide binding334 – 3363NAD By similarity
Region374 – 3763IMP binding By similarity
Region397 – 3982IMP binding By similarity
Region421 – 4255IMP binding By similarity

Sites

Active site3411Thioimidate intermediate By similarity
Metal binding3361Potassium; via carbonyl oxygen By similarity
Metal binding3381Potassium; via carbonyl oxygen By similarity
Metal binding3411Potassium; via carbonyl oxygen By similarity
Metal binding5111Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5121Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5131Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2831NAD By similarity
Binding site3391IMP By similarity
Binding site4581IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q49729 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 1565C62EC9529870

FASTA52954,814
        10         20         30         40         50         60 
MIRGMSNLKE SSDFVASSYV RLGGLMDDPA ATGGDNPHKV AMLGLTFDDV LLLPAASDVV 

        70         80         90        100        110        120 
PATADISSQL TKKIRLKVPL VSSAMDTVTE ARMAIAMARA GGMGVLHRNL PVGEQAGQVE 

       130        140        150        160        170        180 
TVKRSEAGMV TDPVTCRPDN TLAQVGALCA RFRISGLPVV DDSGALAGII TNRDMRFEVD 

       190        200        210        220        230        240 
QSKQVAEVMT KTPLITAAEG VSADAALGLL RRNKIEKLPV VDGHGRLTGL ITVKDFVKTE 

       250        260        270        280        290        300 
QHPLATKDND GRLLVGAAVG VGGDAWVRAM MLVDAGVDVL IVDTAHAHNR LVLDMVGKLK 

       310        320        330        340        350        360 
VEIGDRVQVI GGNVATRSAA AALVEAGADA VKVGVGPGST CTTRVVAGVG APQITAILEA 

       370        380        390        400        410        420 
VAACGPAGVP VIADGGLQYS GDIAKALAAG ASTTMLGSLL AGTAEAPGEL IFVNGKQFKS 

       430        440        450        460        470        480 
YRGMGSLGAM QGRGGDKSYS KDRYFADDAL SEDKLVPEGI EGRVPFRGPL SSVIHQLVGG 

       490        500        510        520 
LRAAMGYTGS PTIEVLQQAQ FVRITPAGLK ESHPHDVAMT VEAPNYYPR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00015 Genomic DNA. Translation: AAC43232.1.
AL583918 Genomic DNA. Translation: CAC29895.1.
PIRS72823.
RefSeqNP_301377.1. NC_002677.1.

3D structure databases

ProteinModelPortalQ49729.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272631.ML0387.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC29895; CAC29895; CAC29895.
GeneID909092.
KEGGmle:ML0387.
PATRIC18051408. VBIMycLep78757_0653.

Organism-specific databases

LepromaML0387.
CMRSearch...

Phylogenomic databases

eggNOGCOG0517.
HOGENOMHOG000165755.
KOK00088.
OMAHGHSKNI.
OrthoDBEOG6GTZPV.

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_MYCLE
AccessionPrimary (citable) accession number: Q49729
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 11, 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