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P65169 (IMDH_STAAM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:SAV0390
OrganismStaphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]
Taxonomic identifier158878 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 – 488488Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000093707

Regions

Domain95 – 15359CBS 1
Domain157 – 21660CBS 2
Nucleotide binding300 – 3023NAD By similarity
Region340 – 3423IMP binding By similarity
Region363 – 3642IMP binding By similarity
Region387 – 3915IMP binding By similarity

Sites

Active site3071Thioimidate intermediate By similarity
Metal binding3021Potassium; via carbonyl oxygen By similarity
Metal binding3041Potassium; via carbonyl oxygen By similarity
Metal binding3071Potassium; via carbonyl oxygen By similarity
Metal binding4711Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4721Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4731Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2501NAD By similarity
Binding site3051IMP By similarity
Binding site4171IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
P65169 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: C4E945D25D41491D

FASTA48852,851
        10         20         30         40         50         60 
MWESKFAKES LTFDDVLLIP AQSDILPKDV DLSVQLSDKV KLNIPVISAG MDTVTESKMA 

        70         80         90        100        110        120 
IAMARQGGLG VIHKNMGVEE QADEVQKVKR SENGVISNPF FLTPEESVYE AEALMGKYRI 

       130        140        150        160        170        180 
SGVPIVDNKE DRNLVGILTN RDLRFIEDFS IKIVDVMTQE NLITAPVNTT LEEAEKILQK 

       190        200        210        220        230        240 
HKIEKLPLVK DGRLEGLITI KDIEKVIEFP NAAKDEHGRL LVAAAIGISK DTDIRAQKLV 

       250        260        270        280        290        300 
EAGVDVLVID TAHGHSKGVI DQVKHIKKTY PEITLVAGNV ATAEATKDLF EAGADIVKVG 

       310        320        330        340        350        360 
IGPGSICTTR VVAGVGVPQI TAIYDCATEA RKHGKAIIAD GGIKFSGDII KALAAGGHAV 

       370        380        390        400        410        420 
MLGSLLAGTE ESPGATEIFQ GRQYKVYRGM GSLGAMEKGS NDRYFQEDKA PKKFVPEGIE 

       430        440        450        460        470        480 
GRTAYKGALQ DTIYQLMGGV RAGMGYTGSH DLRELREEAQ FTRMGPAGLA ESHPHNIQIT 


KESPNYSF 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000017 Genomic DNA. Translation: BAB56552.1.
RefSeqNP_370914.1. NC_002758.2.

3D structure databases

ProteinModelPortalP65169.
SMRP65169. Positions 1-487.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING158878.SAV0390.

2D gel databases

World-2DPAGE0002:P65169.

Proteomic databases

PRIDEP65169.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB56552; BAB56552; SAV0390.
GeneID1120347.
KEGGsav:SAV0390.
PATRIC19561398. VBIStaAur52173_0396.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0517.
HOGENOMHOG000165754.
KOK00088.
OMASSMGYCG.
OrthoDBEOG6GTZPV.
ProtClustDBCLSK884611.

Enzyme and pathway databases

BioCycSAUR158878:GJJ5-391-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]
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_STAAM
AccessionPrimary (citable) accession number: P65169
Secondary accession number(s): Q99WI9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: February 19, 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