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Q8KCW4 (IMDH_CHLTE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 88. 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:CT1293
OrganismChlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS) [Reference proteome] [HAMAP]
Taxonomic identifier194439 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum

Protein attributes

Sequence length494 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 – 494494Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000093693

Regions

Domain93 – 15462CBS 1
Domain158 – 21760CBS 2
Nucleotide binding301 – 3033NAD By similarity
Region341 – 3433IMP binding By similarity
Region364 – 3652IMP binding By similarity
Region388 – 3925IMP binding By similarity

Sites

Active site3081Thioimidate intermediate By similarity
Metal binding3031Potassium; via carbonyl oxygen By similarity
Metal binding3051Potassium; via carbonyl oxygen By similarity
Metal binding3081Potassium; via carbonyl oxygen By similarity
Metal binding4751Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4761Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4771Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2511NAD By similarity
Binding site3061IMP By similarity
Binding site4211IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8KCW4 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: CD4C06DBBCB724DE

FASTA49453,019
        10         20         30         40         50         60 
MDKILYDALT FDDVLLVPAY SNVLPKETVV KSRLTRQIEV NIPLVSAAMD TVTEAELAIA 

        70         80         90        100        110        120 
LARAGGIGII HKNLSIDEQA RQVAKVKRFE SGIIRNPIHL FEDATIQDAI DLMIRHSISG 

       130        140        150        160        170        180 
IPVVEHPTPE GCLLLKGIVT NRDLRMTASS DEKITTIMTT NLVTAKEGID LLTAEDILMR 

       190        200        210        220        230        240 
NKIEKLLIID DNGYLKGLIT FKDIQKRKQC PDACKDSQGR LRAGAAVGIR ANTMSRVDAL 

       250        260        270        280        290        300 
VAAGVDVVAV DTAHGHSQAV LDMVATIKQK YPELQVIAGN VATPEAVRDL VKAGADAVKV 

       310        320        330        340        350        360 
GIGPGSICTT RIVAGVGMPQ LTAIMKCAEE AKKTDIPLIA DGGIKYSGDI AKALAAGADS 

       370        380        390        400        410        420 
VMMGSVFAGT DESPGETILY EGRRFKAYRG MGSLGAMSEP EGSSDRYFQD VSAETKKYVP 

       430        440        450        460        470        480 
EGIEGRIPAK GKLDEVVYQL IGGLKSAMGY CGVRTITELK ENTRFVRITS AGLRESHPHD 

       490 
VMITKEAPNY STSA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006470 Genomic DNA. Translation: AAM72523.1.
RefSeqNP_662181.1. NC_002932.3.

3D structure databases

ProteinModelPortalQ8KCW4.
SMRQ8KCW4. Positions 2-491.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING194439.CT1293.

Proteomic databases

PRIDEQ8KCW4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM72523; AAM72523; CT1293.
GeneID1006653.
KEGGcte:CT1293.
PATRIC21400541. VBIChlTep116050_1178.

Phylogenomic databases

eggNOGCOG0517.
HOGENOMHOG000165755.
KOK00088.
OMAHGHSKNI.
OrthoDBEOG6GTZPV.

Enzyme and pathway databases

BioCycCTEP194439:GHN0-1329-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]
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_CHLTE
AccessionPrimary (citable) accession number: Q8KCW4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: October 1, 2002
Last modified: June 11, 2014
This is version 88 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