Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 PublicationsUniRule annotation

Catalytic activityi

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

Cofactori

K(+)UniRule annotation

Enzyme regulationi

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.UniRule annotation

Kineticsi

  1. KM=29 µM for Inosine 5'-phosphate1 Publication
  2. KM=1100 µM for NAD+1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei172 – 1721NADUniRule annotation
Metal bindingi224 – 2241Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi226 – 2261Potassium; via carbonyl oxygenUniRule annotation
Binding sitei227 – 2271IMPUniRule annotation
Active sitei229 – 2291Thioimidate intermediateUniRule annotation
Metal bindingi229 – 2291Potassium; via carbonyl oxygenUniRule annotation
Binding sitei340 – 3401IMPUniRule annotation
Metal bindingi394 – 3941Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi395 – 3951Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi396 – 3961Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi222 – 2243NADUniRule annotation

GO - Molecular functioni

  1. IMP dehydrogenase activity Source: UniProtKB-HAMAP
  2. metal ion binding Source: UniProtKB-HAMAP
  3. nucleotide binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. GMP biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Potassium

Enzyme and pathway databases

BioCyciBBUR224326:G9SO-1498-MONOMER.
UniPathwayiUPA00601; UER00295.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-5'-monophosphate dehydrogenaseUniRule annotation (EC:1.1.1.205UniRule annotation)
Short name:
IMP dehydrogenaseUniRule annotation
Short name:
IMPDUniRule annotation
Short name:
IMPDHUniRule annotation
Gene namesi
Name:guaBUniRule annotation
Ordered Locus Names:BB_B17
Encoded oniPlasmid cp26 (circular 26 kb)0 Publication
OrganismiBorrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Taxonomic identifieri224326 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group
ProteomesiUP000001807: Plasmid cp26

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 404403Inosine-5'-monophosphate dehydrogenasePRO_0000093692Add
BLAST

Proteomic databases

PRIDEiP49058.

Interactioni

Subunit structurei

Homotetramer.1 PublicationUniRule annotation

Protein-protein interaction databases

STRINGi224326.BBB17.

Structurei

Secondary structure

1
404
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 143Combined sources
Beta strandi15 – 173Combined sources
Helixi26 – 283Combined sources
Beta strandi33 – 386Combined sources
Beta strandi40 – 478Combined sources
Turni51 – 533Combined sources
Helixi56 – 6510Combined sources
Beta strandi67 – 715Combined sources
Beta strandi73 – 753Combined sources
Helixi77 – 8812Combined sources
Beta strandi145 – 1484Combined sources
Helixi154 – 16310Combined sources
Beta strandi167 – 1715Combined sources
Helixi179 – 19113Combined sources
Beta strandi196 – 2027Combined sources
Helixi205 – 2128Combined sources
Turni213 – 2153Combined sources
Beta strandi217 – 2215Combined sources
Helixi230 – 2356Combined sources
Helixi241 – 25212Combined sources
Beta strandi258 – 2636Combined sources
Helixi268 – 27710Combined sources
Beta strandi280 – 2845Combined sources
Helixi286 – 2894Combined sources
Beta strandi294 – 2963Combined sources
Beta strandi298 – 3014Combined sources
Beta strandi304 – 3074Combined sources
Helixi352 – 37019Combined sources
Helixi375 – 3806Combined sources
Beta strandi384 – 3863Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EEPX-ray2.40A/B1-404[»]
ProteinModelPortaliP49058.
SMRiP49058. Positions 3-389.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49058.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni262 – 2643IMP bindingUniRule annotation
Regioni285 – 2862IMP bindingUniRule annotation
Regioni309 – 3135IMP bindingUniRule annotation

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0517.
KOiK00088.
OMAiSSMGYCG.
OrthoDBiEOG6GTZPV.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
HAMAPiMF_01964. IMPDH.
InterProiIPR013785. Aldolase_TIM.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERiPTHR11911:SF6. PTHR11911:SF6. 1 hit.
PfamiPF00478. IMPDH. 1 hit.
[Graphical view]
PROSITEiPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P49058-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPNKITKEAL TFDDVSLIPR KSSVLPSEVS LKTQLTKNIS LNIPFLSSAM
60 70 80 90 100
DTVTESQMAI AIAKEGGIGI IHKNMSIEAQ RKEIEKVKTY KFQKTINTNG
110 120 130 140 150
DTNEQKPEIF TAKQHLEKSD AYKNAEHKED FPNACKDLNN KLRVGAAVSI
160 170 180 190 200
DIDTIERVEE LVKAHVDILV IDSAHGHSTR IIELIKKIKT KYPNLDLIAG
210 220 230 240 250
NIVTKEAALD LISVGADCLK VGIGPGSICT TRIVAGVGVP QITAICDVYE
260 270 280 290 300
ACNNTNICII ADGGIRFSGD VVKAIAAGAD SVMIGNLFAG TKESPSEEII
310 320 330 340 350
YNGKKFKSYV GMGSISAMKR GSKSRYFQLE NNEPKKLVPE GIEGMVPYSG
360 370 380 390 400
KLKDILTQLK GGLMSGMGYL GAATISDLKI NSKFVKISHS SLKESHPHDV

FSIT
Length:404
Mass (Da):43,768
Last modified:February 1, 1996 - v1
Checksum:iA91D6D6C5CE522F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13372 Genomic DNA. Translation: AAA53247.1.
AE000792 Genomic DNA. Translation: AAC66314.1.
PIRiE70218.
RefSeqiNP_047003.1. NC_001903.1.
WP_010890582.1. NC_001903.1.

Genome annotation databases

EnsemblBacteriaiAAC66314; AAC66314; BB_B17.
GeneIDi1194400.
KEGGibbu:BB_B17.
PATRICi20559101. VBIBorBur75917_1605.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13372 Genomic DNA. Translation: AAA53247.1.
AE000792 Genomic DNA. Translation: AAC66314.1.
PIRiE70218.
RefSeqiNP_047003.1. NC_001903.1.
WP_010890582.1. NC_001903.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EEPX-ray2.40A/B1-404[»]
ProteinModelPortaliP49058.
SMRiP49058. Positions 3-389.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224326.BBB17.

Chemistry

BindingDBiP49058.

Proteomic databases

PRIDEiP49058.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC66314; AAC66314; BB_B17.
GeneIDi1194400.
KEGGibbu:BB_B17.
PATRICi20559101. VBIBorBur75917_1605.

Phylogenomic databases

eggNOGiCOG0517.
KOiK00088.
OMAiSSMGYCG.
OrthoDBiEOG6GTZPV.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.
BioCyciBBUR224326:G9SO-1498-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP49058.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
HAMAPiMF_01964. IMPDH.
InterProiIPR013785. Aldolase_TIM.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERiPTHR11911:SF6. PTHR11911:SF6. 1 hit.
PfamiPF00478. IMPDH. 1 hit.
[Graphical view]
PROSITEiPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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).

Entry informationi

Entry nameiIMDH_BORBU
AccessioniPrimary (citable) accession number: P49058
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: January 7, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Plasmid, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.