Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5X9A3 (IMDH_STRP6) 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:M6_Spy1875
OrganismStreptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394) [Complete proteome] [HAMAP]
Taxonomic identifier286636 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 493492Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000093717

Regions

Domain97 – 15559CBS 1
Domain159 – 21961CBS 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
Q5X9A3 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9C317AD598CB5740

FASTA49352,807
        10         20         30         40         50         60 
MSNWDTKFLK KGYTFDDVLL IPAESHVLPN EVDLKTKLAD NLTLNIPIIT AAMDTVTGSK 

        70         80         90        100        110        120 
MAIAIARAGG LGVIHKNMSI TEQAEEVRKV KRSENGVIID PFFLTPEHKV SEAEELMQRY 

       130        140        150        160        170        180 
RISGVPIVET LANRKLVGII TNRDMRFISD YNAPISEHMT SEHLVTAAVG TDLETAERIL 

       190        200        210        220        230        240 
HEHRIEKLPL VDNSGRLSGL ITIKDIEKVI EFPHAAKDEF GRLLVAAAVG VTSDTFERAE 

       250        260        270        280        290        300 
ALFEAGADAI VIDTAHGHSA GVLRKIAEIR AHFPNRTLIA GNIATAEGAR ALYDAGVDVV 

       310        320        330        340        350        360 
KVGIGPGSIC TTRVVAGVGV PQVTAIYDAA AVAREYGKTI IADGGIKYSG DIVKALAAGG 

       370        380        390        400        410        420 
NAVMLGSMFA GTDEAPGETE IYQGRKFKTY RGMGSIAAMK KGSSDRYFQG SVNEANKLVP 

       430        440        450        460        470        480 
EGIEGRVAYK GAASDIVFQM LGGIRSGMGY VGAGDIQELH ENAQFVEMSG AGLIESHPHD 

       490 
VQITNEAPNY SVH 

« Hide

References

« Hide 'large scale' references
[1]"Progress toward characterization of the group A Streptococcus metagenome: complete genome sequence of a macrolide-resistant serotype M6 strain."
Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E., Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.
J. Infect. Dis. 190:727-738(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-946 / MGAS10394.
[2]"Two-dimensional gel electrophoresis map of Streptococcus pyogenes proteins."
Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J., VanBogelen R.A.
Submitted (MAY-2000) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-35; 77-89; 110-119; 122-143; 185-264; 277-301; 407-426 AND 431-445.
Strain: JRS4 / Serotype M6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000003 Genomic DNA. Translation: AAT88010.1.
RefSeqYP_061193.1. NC_006086.1.

3D structure databases

ProteinModelPortalQ5X9A3.
SMRQ5X9A3. Positions 2-491.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING286636.M6_Spy1875.

Chemistry

BindingDBQ5X9A3.

Proteomic databases

PRIDEQ5X9A3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT88010; AAT88010; M6_Spy1875.
GeneID2941087.
KEGGspa:M6_Spy1875.
PATRIC19726057. VBIStrPyo30273_1950.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0517.
HOGENOMHOG000165755.
KOK00088.
OMAHAAKDEH.
OrthoDBEOG6GTZPV.

Enzyme and pathway databases

BioCycSPYO286636:GHNO-1957-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_STRP6
AccessionPrimary (citable) accession number: Q5X9A3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 78 of the entry and version 3 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