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P65168 (IMDH_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 73. 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:Mb3445c
OrganismMycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]
Taxonomic identifier233413 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

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_0000093700

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
P65168 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 689A7C7C53993C0A

FASTA52954,867
        10         20         30         40         50         60 
MSRGMSGLED SSDLVVSPYV RMGGLTTDPV PTGGDDPHKV AMLGLTFDDV LLLPAASDVV 

        70         80         90        100        110        120 
PATADTSSQL TKKIRLKVPL VSSAMDTVTE SRMAIAMARA GGMGVLHRNL PVAEQAGQVE 

       130        140        150        160        170        180 
MVKRSEAGMV TDPVTCRPDN TLAQVDALCA RFRISGLPVV DDDGALVGII TNRDMRFEVD 

       190        200        210        220        230        240 
QSKQVAEVMT KAPLITAQEG VSASAALGLL RRNKIEKLPV VDGRGRLTGL ITVKDFVKTE 

       250        260        270        280        290        300 
QHPLATKDSD GRLLVGAAVG VGGDAWVRAM MLVDAGVDVL VVDTAHAHNR LVLDMVGKLK 

       310        320        330        340        350        360 
SEVGDRVEVV GGNVATRSAA AALVDAGADA VKVGVGPGSI CTTRVVAGVG APQITAILEA 

       370        380        390        400        410        420 
VAACRPAGVP VIADGGLQYS GDIAKALAAG ASTAMLGSLL AGTAEAPGEL IFVNGKQYKS 

       430        440        450        460        470        480 
YRGMGSLGAM RGRGGATSYS KDRYFADDAL SEDKLVPEGI EGRVPFRGPL SSVIHQLTGG 

       490        500        510        520 
LRAAMGYTGS PTIEVLQQAQ FVRITPAGLK ESHPHDVAMT VEAPNYYAR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248333 Genomic DNA. Translation: CDO44716.1.
RefSeqNP_857085.1. NC_002945.3.

3D structure databases

ProteinModelPortalP65168.
SMRP65168. Positions 6-526.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233413.Mb3445c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD95632; CAD95632; Mb3445c.
GeneID1091016.
KEGGmbo:Mb3445c.
PATRIC18009304. VBIMycBov88188_3780.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0517.
HOGENOMHOG000165755.
KOK00088.
OMAFQADVRS.
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_MYCBO
AccessionPrimary (citable) accession number: P65168
Secondary accession number(s): Q50715, X2BPI0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: June 11, 2014
This is version 73 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