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P49058 (IMDH_BORBU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BB_B17
Encoded onPlasmid cp26 (circular 26 kb)
OrganismBorrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680) [Reference proteome] [HAMAP]
Taxonomic identifier224326 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group

Protein attributes

Sequence length404 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. Essential for mouse infection by tick bite and critical for the survival in environments that appear to lack sufficient amounts of guanine, guanosine, and/or deoxyguanosine to support spirochete growth, such as mammalian host tissues. Ref.3 Ref.4

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. Ref.3

Sequence similarities

Belongs to the IMPDH/GMPR family.

Biophysicochemical properties

Kinetic parameters:

KM=29 µM for Inosine 5'-phosphate Ref.3

KM=1100 µM for NAD+

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 404403Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000093692

Regions

Nucleotide binding222 – 2243NAD By similarity
Region262 – 2643IMP binding By similarity
Region285 – 2862IMP binding By similarity
Region309 – 3135IMP binding By similarity

Sites

Active site2291Thioimidate intermediate By similarity
Metal binding2241Potassium; via carbonyl oxygen By similarity
Metal binding2261Potassium; via carbonyl oxygen By similarity
Metal binding2291Potassium; via carbonyl oxygen By similarity
Metal binding3941Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding3951Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding3961Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site1721NAD By similarity
Binding site2271IMP By similarity
Binding site3401IMP By similarity

Secondary structure

........................................................... 404
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P49058 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: A91D6D6C5CE522F1

FASTA40443,768
        10         20         30         40         50         60 
MPNKITKEAL TFDDVSLIPR KSSVLPSEVS LKTQLTKNIS LNIPFLSSAM DTVTESQMAI 

        70         80         90        100        110        120 
AIAKEGGIGI IHKNMSIEAQ RKEIEKVKTY KFQKTINTNG DTNEQKPEIF TAKQHLEKSD 

       130        140        150        160        170        180 
AYKNAEHKED FPNACKDLNN KLRVGAAVSI DIDTIERVEE LVKAHVDILV IDSAHGHSTR 

       190        200        210        220        230        240 
IIELIKKIKT KYPNLDLIAG NIVTKEAALD LISVGADCLK VGIGPGSICT TRIVAGVGVP 

       250        260        270        280        290        300 
QITAICDVYE ACNNTNICII ADGGIRFSGD VVKAIAAGAD SVMIGNLFAG TKESPSEEII 

       310        320        330        340        350        360 
YNGKKFKSYV GMGSISAMKR GSKSRYFQLE NNEPKKLVPE GIEGMVPYSG KLKDILTQLK 

       370        380        390        400 
GGLMSGMGYL GAATISDLKI NSKFVKISHS SLKESHPHDV FSIT 

« Hide

References

« Hide 'large scale' references
[1]"Plasmid location of Borrelia purine biosynthesis gene homologs."
Margolis N., Hogan D., Tilly K., Rosa P.
J. Bacteriol. 176:6427-6432(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
[2]"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi."
Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. expand/collapse author list , Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., Smith H.O., Venter J.C.
Nature 390:580-586(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
[3]"Expression, purification, and characterization of inosine 5'-monophosphate dehydrogenase from Borrelia burgdorferi."
Zhou X., Cahoon M., Rosa P., Hedstrom L.
J. Biol. Chem. 272:21977-21981(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-7, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
[4]"GuaA and GuaB are essential for Borrelia burgdorferi survival in the tick-mouse infection cycle."
Jewett M.W., Lawrence K.A., Bestor A., Byram R., Gherardini F., Rosa P.A.
J. Bacteriol. 191:6231-6241(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
[5]"Crystal structure at 2.4-A resolution of Borrelia burgdorferi inosine 5'-monophosphate dehydrogenase: evidence of a substrate-induced hinged-lid motion by loop 6."
McMillan F.M., Cahoon M., White A., Hedstrom L., Petsko G.A., Ringe D.
Biochemistry 39:4533-4542(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U13372 Genomic DNA. Translation: AAA53247.1.
AE000792 Genomic DNA. Translation: AAC66314.1.
PIRE70218.
RefSeqNP_047003.1. NC_001903.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EEPX-ray2.40A/B1-404[»]
ProteinModelPortalP49058.
SMRP49058. Positions 3-389.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224326.BBB17.

Chemistry

BindingDBP49058.

Proteomic databases

PRIDEP49058.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC66314; AAC66314; BB_B17.
GeneID1194400.
KEGGbbu:BB_B17.
PATRIC20559101. VBIBorBur75917_1605.

Phylogenomic databases

eggNOGCOG0517.
KOK00088.
OMASSMGYCG.
OrthoDBEOG6GTZPV.
ProtClustDBPRK06843.

Enzyme and pathway databases

BioCycBBUR224326:G9SO-1498-MONOMER.
UniPathwayUPA00601; UER00295.

Family and domain databases

Gene3D3.20.20.70. 2 hits.
HAMAPMF_01964. IMPDH.
InterProIPR013785. Aldolase_TIM.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERPTHR11911:SF6. PTHR11911:SF6. 1 hit.
PfamPF00478. IMPDH. 1 hit.
[Graphical view]
PROSITEPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP49058.

Entry information

Entry nameIMDH_BORBU
AccessionPrimary (citable) accession number: P49058
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: February 19, 2014
This is version 107 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways