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Q2G0Y7 (IMDH_STAA8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:SAOUHSC_00374
OrganismStaphylococcus aureus (strain NCTC 8325) [Reference proteome] [HAMAP]
Taxonomic identifier93061 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

Protein attributes

Sequence length488 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.

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.

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 2 CBS domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 488488Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000287360

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
Q2G0Y7 [UniParc].

Last modified March 21, 2006. 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

« Hide

References

[1]"The Staphylococcus aureus NCTC8325 genome."
Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 8325.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000253 Genomic DNA. Translation: ABD29540.1.
RefSeqYP_498963.1. NC_007795.1.

3D structure databases

ProteinModelPortalQ2G0Y7.
SMRQ2G0Y7. Positions 1-487.
ModBaseSearch...

Protein-protein interaction databases

STRING93061.SAOUHSC_00374.

Proteomic databases

PRIDEQ2G0Y7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD29540; ABD29540; SAOUHSC_00374.
GeneID3919793.
KEGGsao:SAOUHSC_00374.
PATRIC19578336. VBIStaAur99865_0344.

Phylogenomic databases

eggNOGCOG0517.
HOGENOMHOG000165754.
KOK00088.
OMASAGLKES.
ProtClustDBCLSK884611.

Enzyme and pathway databases

BioCycSAUR93061:GIWJ-357-MONOMER.
UniPathwayUPA00601; UER00295.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01964. IMPDH.
InterProIPR013785. Aldolase_TIM.
IPR000644. Cysta_beta_synth_core.
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_STAA8
AccessionPrimary (citable) accession number: Q2G0Y7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: March 21, 2006
Last modified: May 1, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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