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P49058 (IMDH_BORBU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BB_B17
Encoded onPlasmid cp26 (circular 26 kb)
OrganismBorrelia burgdorferi (Lyme disease spirochete)
Taxonomic identifier139 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length404 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.

Pathway

Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.

Sequence similarities

Belongs to the IMPDH/GMPR family.

Ontologies

Keywords
   Biological processGMP biosynthesis
Purine biosynthesis
   LigandMetal-binding
NAD
Potassium
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Plasmid
Reference proteome
Gene Ontology (GO)
   Biological processGMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionIMP dehydrogenase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 404404Inosine-5'-monophosphate dehydrogenase
PRO_0000093692

Regions

Nucleotide binding151 – 17424NAD By similarity

Sites

Active site2291Thioimidate intermediate By similarity
Metal binding2241Potassium; via carbonyl oxygen By similarity
Metal binding2261Potassium; via carbonyl oxygen By similarity
Binding site2621IMP By similarity
Binding site3091IMP By similarity

Secondary structure

1 ............................................................. 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: 7961392] [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: 9403685] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
[3]"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: 10758003] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+Additional computationally mapped references.

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...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBORT00000009586; EBBORP00000008873; EBBORG00000009585.
GeneID1194400.
GenomeReviewsGene locus BB_B17 in contig AE000792_GR.
KEGGbbu:BBB17.
NMPDRfig|224326.1.peg.1617.
PATRIC20559101. VBIBorBur75917_1605.
TIGRBB_B17.

Phylogenomic databases

GeneTreeEBGT00050000007045.
HOGENOMHBG298985.
OMAGIGIVHK.
PhylomeDBP49058.
ProtClustDBPRK06843.

Enzyme and pathway databases

BioCycBBUR224326:BB_B17-MONOMER.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR018529. IMP_DH-rel.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 2 hits.
KOK00088.
PANTHERPTHR11911:SF6. IMP_DH_GMPRtase. 1 hit.
PfamPF00478. IMPDH. 1 hit.
[Graphical view]
PROSITEPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

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: January 25, 2012
This is version 91 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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