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P49058

- IMDH_BORBU

UniProt

P49058 - IMDH_BORBU

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Protein

Inosine-5'-monophosphate dehydrogenase

Gene
guaB, BB_B17
Organism
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Status
Reviewed - 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 Publications

Catalytic activityi

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

Cofactori

Potassium By similarity.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 By similarity.UniRule annotation

Kineticsi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei172 – 1721NAD By similarity
Metal bindingi224 – 2241Potassium; via carbonyl oxygen By similarity
Metal bindingi226 – 2261Potassium; via carbonyl oxygen By similarity
Binding sitei227 – 2271IMP By similarity
Active sitei229 – 2291Thioimidate intermediate By similarity
Metal bindingi229 – 2291Potassium; via carbonyl oxygen By similarity
Binding sitei340 – 3401IMP By similarity
Metal bindingi394 – 3941Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi395 – 3951Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi396 – 3961Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi222 – 2243NAD By similarity

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 dehydrogenase (EC:1.1.1.205)
Short name:
IMP dehydrogenase
Short name:
IMPD
Short name:
IMPDH
Gene namesi
Name:guaB
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 dehydrogenaseUniRule annotationPRO_0000093692Add
BLAST

Proteomic databases

PRIDEiP49058.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi224326.BBB17.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EEPX-ray2.40A/B1-404[»]
ProteinModelPortaliP49058.
SMRiP49058. Positions 3-389.

Miscellaneous databases

EvolutionaryTraceiP49058.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni262 – 2643IMP binding By similarity
Regioni285 – 2862IMP binding By similarity
Regioni309 – 3135IMP binding By similarity

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.

Phylogenomic databases

eggNOGiCOG0517.
KOiK00088.
OMAiHGHSKNI.
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

MPNKITKEAL TFDDVSLIPR KSSVLPSEVS LKTQLTKNIS LNIPFLSSAM    50
DTVTESQMAI AIAKEGGIGI IHKNMSIEAQ RKEIEKVKTY KFQKTINTNG 100
DTNEQKPEIF TAKQHLEKSD AYKNAEHKED FPNACKDLNN KLRVGAAVSI 150
DIDTIERVEE LVKAHVDILV IDSAHGHSTR IIELIKKIKT KYPNLDLIAG 200
NIVTKEAALD LISVGADCLK VGIGPGSICT TRIVAGVGVP QITAICDVYE 250
ACNNTNICII ADGGIRFSGD VVKAIAAGAD SVMIGNLFAG TKESPSEEII 300
YNGKKFKSYV GMGSISAMKR GSKSRYFQLE NNEPKKLVPE GIEGMVPYSG 350
KLKDILTQLK GGLMSGMGYL GAATISDLKI NSKFVKISHS SLKESHPHDV 400
FSIT 404
Length:404
Mass (Da):43,768
Last modified:February 1, 1996 - v1
Checksum:iA91D6D6C5CE522F1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U13372 Genomic DNA. Translation: AAA53247.1 .
AE000792 Genomic DNA. Translation: AAC66314.1 .
PIRi E70218.
RefSeqi NP_047003.1. NC_001903.1.
WP_010890582.1. NC_001903.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EEP X-ray 2.40 A/B 1-404 [» ]
ProteinModelPortali P49058.
SMRi P49058. Positions 3-389.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224326.BBB17.

Chemistry

BindingDBi P49058.

Proteomic databases

PRIDEi P49058.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC66314 ; AAC66314 ; BB_B17 .
GeneIDi 1194400.
KEGGi bbu:BB_B17.
PATRICi 20559101. VBIBorBur75917_1605.

Phylogenomic databases

eggNOGi COG0517.
KOi K00088.
OMAi HGHSKNI.
OrthoDBi EOG6GTZPV.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .
BioCyci BBUR224326:G9SO-1498-MONOMER.

Miscellaneous databases

EvolutionaryTracei P49058.

Family and domain databases

Gene3Di 3.20.20.70. 2 hits.
HAMAPi MF_01964. IMPDH.
InterProi IPR013785. Aldolase_TIM.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view ]
PANTHERi PTHR11911:SF6. PTHR11911:SF6. 1 hit.
Pfami PF00478. IMPDH. 1 hit.
[Graphical view ]
PROSITEi PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 109 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

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