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P0ADG9

- IMDH_SHIFL

UniProt

P0ADG9 - IMDH_SHIFL

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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Shigella flexneri
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

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.UniRule 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

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. IMP dehydrogenase activity Source: UniProtKB-HAMAP
  3. 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

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:SF2554, S2726
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000001006: Chromosome, UP000002673: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 488488Inosine-5'-monophosphate dehydrogenasePRO_0000093705Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0ADG9.
PRIDEiP0ADG9.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi198214.SF2554.

Structurei

3D structure databases

ProteinModelPortaliP0ADG9.
SMRiP0ADG9. 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

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.
KOiK00088.
OrthoDBiEOG6GTZPV.

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.

P0ADG9-1 [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 databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN44054.2.
AE014073 Genomic DNA. Translation: AAP17881.1.
RefSeqiNP_708347.2. NC_004337.2.
NP_838071.1. NC_004741.1.

Genome annotation databases

EnsemblBacteriaiAAN44054; AAN44054; SF2554.
AAP17881; AAP17881; S2726.
GeneIDi1027589.
1078993.
KEGGisfl:SF2554.
sfx:S2726.
PATRICi18707082. VBIShiFle31049_3009.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN44054.2 .
AE014073 Genomic DNA. Translation: AAP17881.1 .
RefSeqi NP_708347.2. NC_004337.2.
NP_838071.1. NC_004741.1.

3D structure databases

ProteinModelPortali P0ADG9.
SMRi P0ADG9. Positions 1-487.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 198214.SF2554.

Chemistry

BindingDBi P0ADG9.

Proteomic databases

PaxDbi P0ADG9.
PRIDEi P0ADG9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN44054 ; AAN44054 ; SF2554 .
AAP17881 ; AAP17881 ; S2726 .
GeneIDi 1027589.
1078993.
KEGGi sfl:SF2554.
sfx:S2726.
PATRICi 18707082. VBIShiFle31049_3009.

Phylogenomic databases

eggNOGi COG0517.
HOGENOMi HOG000165755.
KOi K00088.
OrthoDBi EOG6GTZPV.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .

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

  1. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiIMDH_SHIFL
AccessioniPrimary (citable) accession number: P0ADG9
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: November 26, 2014
This is version 74 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3