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P0ADG7

- IMDH_ECOLI

UniProt

P0ADG7 - IMDH_ECOLI

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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Escherichia coli (strain K12)
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.1 PublicationUniRule annotation

Catalytic activityi

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

Cofactori

Potassium.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. IMP dehydrogenase subunit of E.coli contains a cysteine at the IMP binding site and is inhibited in a simple competitive manner by GMP. It does not exhibit allosteric properties as does IMP dehydrogenase from B.subtilis or S.typhimurium.1 PublicationUniRule annotation

Kineticsi

  1. KM=61 µM for Inosine 5'-phosphate1 Publication
  2. KM=2000 µM for NAD+1 Publication
  3. KM=2.8 mM for K+1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei248 – 2481NADUniRule annotation
Metal bindingi300 – 3001Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi302 – 3021Potassium; via carbonyl oxygenUniRule annotation
Binding sitei303 – 3031IMPUniRule annotation
Active sitei305 – 3051Thioimidate intermediateUniRule annotation
Metal bindingi305 – 3051Potassium; via carbonyl oxygenUniRule annotation
Binding sitei415 – 4151IMPUniRule annotation
Metal bindingi469 – 4691Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi470 – 4701Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi471 – 4711Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi248 – 2503NADUniRule annotation
Nucleotide bindingi298 – 3003NADUniRule annotation

GO - Molecular functioni

  1. adenyl nucleotide binding Source: InterPro
  2. identical protein binding Source: EcoCyc
  3. IMP dehydrogenase activity Source: EcoCyc
  4. metal ion 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

BioCyciEcoCyc:IMP-DEHYDROG-MONOMER.
ECOL316407:JW5401-MONOMER.
MetaCyc:IMP-DEHYDROG-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
Synonyms:guaR
Ordered Locus Names:b2508, JW5401
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10421. guaB.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 131D → A: Causes a 38-fold increase in the value of Km for K(+). No change is observed in the value of Km for IMP. 1 Publication
Mutagenesisi50 – 501D → A: Causes a 17-fold increase in the value of Km for K(+). 1 Publication
Mutagenesisi54 – 541E → A: No effect. 1 Publication
Mutagenesisi138 – 1381D → A: No effect. 1 Publication
Mutagenesisi200 – 2001D → A: No effect. 1 Publication
Mutagenesisi243 – 2431D → A: No effect. 1 Publication
Mutagenesisi248 – 2481D → A: Causes a 130-fold decrease in the value of kcat. 1 Publication
Mutagenesisi338 – 3381D → A: Decreases the value of kcat by 600-fold. Increases the value of Km for IMP by 12-fold. 1 Publication
Mutagenesisi369 – 3691E → A: No effect. 1 Publication
Mutagenesisi373 – 3731E → A: No effect. 1 Publication
Mutagenesisi469 – 4691E → A: Increases the value of Km for K(+) by 17-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 488488Inosine-5'-monophosphate dehydrogenasePRO_0000093695Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei267 – 2671N6-acetyllysine1 Publication
Modified residuei428 – 4281N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0ADG7.
PRIDEiP0ADG7.

2D gel databases

SWISS-2DPAGEP0ADG7.

Expressioni

Gene expression databases

GenevestigatoriP0ADG7.

Interactioni

Subunit structurei

Homotetramer.1 PublicationUniRule annotation

Protein-protein interaction databases

BioGridi851324. 1 interaction.
DIPiDIP-36207N.
IntActiP0ADG7. 1 interaction.
MINTiMINT-1235980.
STRINGi511145.b2508.

Structurei

3D structure databases

ProteinModelPortaliP0ADG7.
SMRiP0ADG7. Positions 1-487.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini93 – 14957CBS 1UniRule annotationAdd
BLAST
Domaini153 – 21462CBS 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni338 – 3403IMP bindingUniRule annotation
Regioni361 – 3622IMP bindingUniRule annotation
Regioni385 – 3895IMP bindingUniRule annotation

Domaini

The CBS domain of IMPDH is a negative trans-regulator of adenylate nucleotide synthesis, and this role is independent of the catalytic function of IMPDH in the de novo GMP biosynthesis. Deletion of the CBS domain derepresses the synthesis of AMP from IMP.2 Publications

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation
Contains 2 CBS domains.UniRule annotation

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiCOG0517.
HOGENOMiHOG000165755.
InParanoidiP0ADG7.
KOiK00088.
OMAiHGHSKNI.
OrthoDBiEOG6GTZPV.
PhylomeDBiP0ADG7.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH.
InterProiIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PfamiPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFiPIRSF000130. IMPDH. 1 hit.
SMARTiSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
PROSITEiPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ADG7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLRIAKEALT FDDVLLVPAH STVLPNTADL STQLTKTIRL NIPMLSAAMD
60 70 80 90 100
TVTEARLAIA LAQEGGIGFI HKNMSIERQA EEVRRVKKHE SGVVTDPQTV
110 120 130 140 150
LPTTTLREVK ELTERNGFAG YPVVTEENEL VGIITGRDVR FVTDLNQPVS
160 170 180 190 200
VYMTPKERLV TVREGEAREV VLAKMHEKRV EKALVVDDEF HLIGMITVKD
210 220 230 240 250
FQKAERKPNA CKDEQGRLRV GAAVGAGAGN EERVDALVAA GVDVLLIDSS
260 270 280 290 300
HGHSEGVLQR IRETRAKYPD LQIIGGNVAT AAGARALAEA GCSAVKVGIG
310 320 330 340 350
PGSICTTRIV TGVGVPQITA VADAVEALEG TGIPVIADGG IRFSGDIAKA
360 370 380 390 400
IAAGASAVMV GSMLAGTEES PGEIELYQGR SYKSYRGMGS LGAMSKGSSD
410 420 430 440 450
RYFQSDNAAD KLVPEGIEGR VAYKGRLKEI IHQQMGGLRS CMGLTGCGTI
460 470 480
DELRTKAEFV RISGAGIQES HVHDVTITKE SPNYRLGS
Length:488
Mass (Da):52,022
Last modified:December 6, 2005 - v1
Checksum:iB0FD0A786779C98E
GO

Sequence cautioni

The sequence CAA26133.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti206 – 2061R → A in CAA26133. (PubMed:2860637)Curated
Sequence conflicti206 – 2061R → A in AAB18618. (PubMed:2860637)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02209 Genomic DNA. Translation: CAA26133.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75561.1.
AP009048 Genomic DNA. Translation: BAA16395.2.
M10101 Genomic DNA. Translation: AAB18618.1.
PIRiC65027. DEECIP.
RefSeqiNP_417003.1. NC_000913.3.
YP_490736.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75561; AAC75561; b2508.
BAA16395; BAA16395; BAA16395.
GeneIDi12934227.
946985.
KEGGiecj:Y75_p2461.
eco:b2508.
PATRICi32120407. VBIEscCol129921_2606.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02209 Genomic DNA. Translation: CAA26133.1 . Different initiation.
U00096 Genomic DNA. Translation: AAC75561.1 .
AP009048 Genomic DNA. Translation: BAA16395.2 .
M10101 Genomic DNA. Translation: AAB18618.1 .
PIRi C65027. DEECIP.
RefSeqi NP_417003.1. NC_000913.3.
YP_490736.1. NC_007779.1.

3D structure databases

ProteinModelPortali P0ADG7.
SMRi P0ADG7. Positions 1-487.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 851324. 1 interaction.
DIPi DIP-36207N.
IntActi P0ADG7. 1 interaction.
MINTi MINT-1235980.
STRINGi 511145.b2508.

Chemistry

BindingDBi P0ADG7.
ChEMBLi CHEMBL3630.

2D gel databases

SWISS-2DPAGE P0ADG7.

Proteomic databases

PaxDbi P0ADG7.
PRIDEi P0ADG7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75561 ; AAC75561 ; b2508 .
BAA16395 ; BAA16395 ; BAA16395 .
GeneIDi 12934227.
946985.
KEGGi ecj:Y75_p2461.
eco:b2508.
PATRICi 32120407. VBIEscCol129921_2606.

Organism-specific databases

EchoBASEi EB0416.
EcoGenei EG10421. guaB.

Phylogenomic databases

eggNOGi COG0517.
HOGENOMi HOG000165755.
InParanoidi P0ADG7.
KOi K00088.
OMAi HGHSKNI.
OrthoDBi EOG6GTZPV.
PhylomeDBi P0ADG7.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .
BioCyci EcoCyc:IMP-DEHYDROG-MONOMER.
ECOL316407:JW5401-MONOMER.
MetaCyc:IMP-DEHYDROG-MONOMER.

Miscellaneous databases

PROi P0ADG7.

Gene expression databases

Genevestigatori P0ADG7.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01964. IMPDH.
InterProi IPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view ]
Pfami PF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000130. IMPDH. 1 hit.
SMARTi SM00116. CBS. 2 hits.
[Graphical view ]
TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
PROSITEi PS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the guaB locus encoding IMP dehydrogenase of Escherichia coli K12."
    Tiedeman A.A., Smith J.M.
    Nucleic Acids Res. 13:1303-1316(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Nucleotide sequence and organisation of the gua promoter region of Escherichia coli."
    Thomas M.S., Drabble W.T.
    Gene 36:45-53(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
  6. "Regulation of the gua operon of Escherichia coli by the DnaA protein."
    Tesfa-Selase F., Drabble W.T.
    Mol. Gen. Genet. 231:256-264(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90.
  7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / EMG2.
  8. Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
    Submitted (FEB-1996) to UniProtKB
    Cited for: PARTIAL PROTEIN SEQUENCE OF 1-11.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  9. "Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis."
    Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M., Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A.
    Electrophoresis 19:837-844(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-5.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  10. Cited for: PROTEIN SEQUENCE OF 1-4.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  11. "The roles of conserved carboxylate residues in IMP dehydrogenase and identification of a transition state analog."
    Kerr K.M., Hedstrom L.
    Biochemistry 36:13365-13373(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ENZYME REGULATION, MUTAGENESIS OF ASP-13; ASP-50; GLU-54; ASP-138; ASP-200; ASP-243; ASP-248; ASP-338; GLU-369; GLU-373 AND GLU-469.
    Strain: K12.
  12. "The CBS subdomain of inosine 5'-monophosphate dehydrogenase regulates purine nucleotide turnover."
    Pimkin M., Markham G.D.
    Mol. Microbiol. 68:342-359(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN CBS.
    Strain: K12 / BW25113.
  13. "A regulatory role of the Bateman domain of IMP dehydrogenase in adenylate nucleotide biosynthesis."
    Pimkin M., Pimkina J., Markham G.D.
    J. Biol. Chem. 284:7960-7969(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN CBS.
    Strain: K12 / BW25113.
  14. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267 AND LYS-428, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiIMDH_ECOLI
AccessioniPrimary (citable) accession number: P0ADG7
Secondary accession number(s): P06981, P76574, P78202
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: December 6, 2005
Last modified: October 29, 2014
This is version 86 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3