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Q7UJL3 (IMDH_RHOBA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 78. 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:RB11822
OrganismRhodopirellula baltica (strain SH1) [Reference proteome] [HAMAP]
Taxonomic identifier243090 [NCBI]
Taxonomic lineageBacteriaPlanctomycetesPlanctomycetiaPlanctomycetalesPlanctomycetaceaeRhodopirellula

Protein attributes

Sequence length539 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 – 539539Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000415690

Regions

Domain140 – 19657CBS 1
Domain200 – 25758CBS 2
Nucleotide binding343 – 3453NAD By similarity
Region383 – 3853IMP binding By similarity
Region406 – 4072IMP binding By similarity
Region430 – 4345IMP binding By similarity

Sites

Active site3501Thioimidate intermediate By similarity
Metal binding3451Potassium; via carbonyl oxygen By similarity
Metal binding3471Potassium; via carbonyl oxygen By similarity
Metal binding3501Potassium; via carbonyl oxygen By similarity
Metal binding5141Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5161Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2921NAD By similarity
Binding site3481IMP By similarity
Binding site4601IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7UJL3 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 7090A0C1A9075141

FASTA53957,876
        10         20         30         40         50         60 
MGASTRFRRQ SGKVPYNSTA ASVIIARFPH RITFGCPRPR GNENGMFDDK IGDLGVTFDD 

        70         80         90        100        110        120 
VLLQPRYSEV VPSEVDVSSQ MTQRIRLQIP LISSPMDTVT ESEMAIALAK EGGLGIVHKN 

       130        140        150        160        170        180 
LSVRRQTEEV LKVKRSANGI IVNPVTLNPA QKVSAAAELM DRANVSGIPI VEDDRTLAGI 

       190        200        210        220        230        240 
LTRRDLRFLE DPDMPISQVM TRENLVTAVG NVTLAQAEKI LTEKRVEKLL LIDEERKLTG 

       250        260        270        280        290        300 
LITIRDIDMM KRYPRACKDP QGRLRVGAAI GVGDYERAES LIGKGVDVLV VDSAHGHSRN 

       310        320        330        340        350        360 
VIETVREIKQ NKSWDIDVVA GNVATAEGAA DLIAAGADAV KVGIGPGSIC TTRVISGIGV 

       370        380        390        400        410        420 
PQVTAILSAV KVAQEKNIPV IADGGIRFSG DITKAIAAGA STVMIGSLFA GLAESPGKMI 

       430        440        450        460        470        480 
LYQGRTFKAY RGMGSMGAMV KGSSDRYRQK GTEAGKLVPE GVEGRVPFKG PLSDYAYQLV 

       490        500        510        520        530 
GGLRAGMGYV GTRTIEELRR DAKFIRVSAA TVRENHPHDI AITQEAPNYS PDVHSGDAG 

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References

[1]"Complete genome sequence of the marine planctomycete Pirellula sp. strain 1."
Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., Reinhardt R.
Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX294154 Genomic DNA. Translation: CAD77245.1.
RefSeqNP_870170.1. NC_005027.1.

3D structure databases

ProteinModelPortalQ7UJL3.
SMRQ7UJL3. Positions 46-530.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243090.RB11822.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD77245; CAD77245; RB11822.
GeneID1795246.
KEGGrba:RB11822.
PATRIC23252947. VBIRhoBal59814_5703.

Phylogenomic databases

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]
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_RHOBA
AccessionPrimary (citable) accession number: Q7UJL3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 78 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