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Q9KH33 (IMDH_RHITR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. 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
OrganismRhizobium tropici
Taxonomic identifier398 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length498 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
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 – 498498Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000093704

Regions

Domain98 – 15558CBS 1
Domain159 – 21658CBS 2
Nucleotide binding303 – 3053NAD By similarity
Region343 – 3453IMP binding By similarity
Region366 – 3672IMP binding By similarity
Region390 – 3945IMP binding By similarity

Sites

Active site3101Thioimidate intermediate By similarity
Metal binding3051Potassium; via carbonyl oxygen By similarity
Metal binding3071Potassium; via carbonyl oxygen By similarity
Metal binding3101Potassium; 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 site2531NAD By similarity
Binding site3081IMP By similarity
Binding site4211IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KH33 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 0A99E38B1078ED73

FASTA49852,838
        10         20         30         40         50         60 
MARIIETSTG LDALTFDDVL LQPGHSEVMP GQTNIATRIA QDIELNVPIL SAAMDTVTES 

        70         80         90        100        110        120 
RLAIAMAQAG GMGVIHRNLT PVQQAEEVRQ VKKFESGMVV NPVTIGPDAT LAEALSLDEG 

       130        140        150        160        170        180 
PRHFRASPVV EKSHRLVGIL TNRDVRFASD PEQKIYELMT RENLVTVKDG VQQHEAKRLL 

       190        200        210        220        230        240 
HTHRIEKXLV VDADSRFVGL ITVKDIEKSQ LNPHASKDAQ GRLRAAAAIS VGDDGYERAE 

       250        260        270        280        290        300 
RLIDAGVDLL VVDTAHGHSQ RVLDAVTRVK KLSNSVRIMA GNVATYDGTR ALIDAGADAV 

       310        320        330        340        350        360 
KVGIGPGSIC TTRIVAGVGV PQLAAIMSAV QAAQDQNIPI IADGGIKFSG DLAKAIAAGA 

       370        380        390        400        410        420 
SAAMIGSLLA GTDESPGEVY LYQGRSFKAY RGMGSVGAMA RGSADRYFQA EVRDTLKLVP 

       430        440        450        460        470        480 
EGIEGXVPYK GPVSGVLHQL AGGLKAAMGY VGGADLKDFQ ERATFVRISG AGLRESHAHD 

       490 
VTITPRKARI IPAQAADR 

« Hide

References

[1]"A guaB mutant strain of Rhizobium tropici CIAT899 pleiotropically defective in thermal tolerance and symbiosis."
Riccillo P.M., Collavino M.M., Grasso D.H., England R., de Bruijn F.J., Aguilar O.M.
Mol. Plant Microbe Interact. 13:1228-1236(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 899.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF272827 Genomic DNA. Translation: AAF85967.1.

3D structure databases

ProteinModelPortalQ9KH33.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9KH33.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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]
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_RHITR
AccessionPrimary (citable) accession number: Q9KH33
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 81 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