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Q9HXM5

- Q9HXM5_PSEAE

UniProt

Q9HXM5 - Q9HXM5_PSEAE

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Protein

Inosine-5'-monophosphate dehydrogenase

Gene
guaB, PA3770
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Unreviewed - Annotation score: 4 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 By similarity.UniRule annotation

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei98 – 981ATP; via amide nitrogen and carbonyl oxygenImported
Binding sitei153 – 1531ATPImported
Binding sitei159 – 1591ATP; via amide nitrogen and carbonyl oxygenImported
Binding sitei247 – 2471NAD By similarityUniRule annotation
Metal bindingi299 – 2991Potassium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi301 – 3011Potassium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei302 – 3021IMP By similarityUniRule annotation
Active sitei304 – 3041Thioimidate intermediate By similarityUniRule annotation
Metal bindingi304 – 3041Potassium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei339 – 3391Phosphate; via amide nitrogenImported
Binding sitei417 – 4171IMP By similarityUniRule annotation
Metal bindingi471 – 4711Potassium; via carbonyl oxygen; shared with tetrameric partner By similarityUniRule annotation
Metal bindingi472 – 4721Potassium; via carbonyl oxygen; shared with tetrameric partner By similarityUniRule annotation
Metal bindingi473 – 4731Potassium; via carbonyl oxygen; shared with tetrameric partner By similarityUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi118 – 1203ATPImported
Nucleotide bindingi134 – 1374ATPImported
Nucleotide bindingi180 – 1812ATPImported
Nucleotide bindingi198 – 1992ATPImported
Nucleotide bindingi297 – 2993NAD By similarityUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  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

OxidoreductaseUniRule annotation

Keywords - Biological processi

GMP biosynthesisUniRule annotation, Purine biosynthesis

Keywords - Ligandi

ATP-bindingImported, Metal-bindingUniRule annotation, NADUniRule annotation, Nucleotide-binding, PotassiumUniRule annotation

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 annotationImported
Ordered Locus Names:PA3770Imported
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)Imported
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438: Chromosome

Organism-specific databases

PseudoCAPiPA3770.

PTM / Processingi

Proteomic databases

PRIDEiQ9HXM5.

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

DIPiDIP-60162N.
STRINGi208964.PA3770.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZFHX-ray2.25A1-489[»]
4AVFX-ray2.23A/B/C/D1-489[»]
4DQWX-ray2.51A/B1-489[»]
ProteinModelPortaliQ9HXM5.
SMRiQ9HXM5. Positions 1-468.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini93 – 14856CBS 1 By similarityUniRule annotationAdd
BLAST
Domaini152 – 21059CBS 2 By similarityUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni337 – 3393IMP binding By similarityUniRule annotation
Regioni360 – 3612IMP binding By similarityUniRule annotation
Regioni384 – 3885IMP binding By similarityUniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

CBS domainUniRule annotation, RepeatUniRule annotation

Phylogenomic databases

HOGENOMiHOG000165755.
KOiK00088.
OMAiNNSQKRY.
OrthoDBiEOG6GTZPV.
PhylomeDBiQ9HXM5.

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.

Q9HXM5-1 [UniParc]FASTAAdd to Basket

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MLRISQEALT FDDVLLIPGY SEVLPKDVSL KTRLTRGIEL NIPLVSAAMD    50
TVTEARLAIA MAQEGGIGII HKNMGIEQQA AEVRKVKKHE TAIVRDPVTV 100
TPSTKIIELL QMAREYGFSG FPVVEQGELV GIVTGRDLRV KPNAGDTVAA 150
IMTPKDKLVT AREGTPLEEM KAKLYENRIE KMLVVDENFY LRGLVTFRDI 200
EKAKTYPLAS KDEQGRLRVG AAVGTGADTG ERVAALVAAG VDVVVVDTAH 250
GHSKGVIERV RWVKQTFPDV QVIGGNIATA EAAKALAEAG ADAVKVGIGP 300
GSICTTRIVA GVGVPQISAI ANVAAALEGT GVPLIADGGI RFSGDLAKAM 350
VAGAYCVMMG SMFAGTEEAP GEIELFQGRS YKSYRGMGSL GAMSGSQGSS 400
DRYFQDASAG AEKLVPEGIE GRVPYKGALS AIVHQLMGGL RAAMGYTGSA 450
DIQQMRTQPQ FVRITGAGMA ESHVHDVQIT KEAPNYRVG 489
Length:489
Mass (Da):51,707
Last modified:March 1, 2001 - v1
Checksum:i6D2320AFD52C888B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004091 Genomic DNA. Translation: AAG07157.1.
PIRiH83173.
RefSeqiNP_252459.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG07157; AAG07157; PA3770.
GeneIDi880535.
KEGGipae:PA3770.
PATRICi19842179. VBIPseAer58763_3947.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004091 Genomic DNA. Translation: AAG07157.1 .
PIRi H83173.
RefSeqi NP_252459.1. NC_002516.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ZFH X-ray 2.25 A 1-489 [» ]
4AVF X-ray 2.23 A/B/C/D 1-489 [» ]
4DQW X-ray 2.51 A/B 1-489 [» ]
ProteinModelPortali Q9HXM5.
SMRi Q9HXM5. Positions 1-468.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-60162N.
STRINGi 208964.PA3770.

Proteomic databases

PRIDEi Q9HXM5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG07157 ; AAG07157 ; PA3770 .
GeneIDi 880535.
KEGGi pae:PA3770.
PATRICi 19842179. VBIPseAer58763_3947.

Organism-specific databases

PseudoCAPi PA3770.

Phylogenomic databases

HOGENOMi HOG000165755.
KOi K00088.
OMAi NNSQKRY.
OrthoDBi EOG6GTZPV.
PhylomeDBi Q9HXM5.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  2. "The AEROPATH project targeting Pseudomonas aeruginosa: crystallographic studies for assessment of potential targets in early-stage drug discovery."
    Moynie L., Schnell R., McMahon S.A., Sandalova T., Boulkerou W.A., Schmidberger J.W., Alphey M., Cukier C., Duthie F., Kopec J., Liu H., Jacewicz A., Hunter W.N., Naismith J.H., Schneider G.
    Acta Crystallogr. F 69:25-34(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS).
  3. "Structure of Pseudomonas aeruginosa inosine 5'-monophosphate dehydrogenase."
    Rao V.A., Shepherd S.M., Owen R., Hunter W.N.
    Acta Crystallogr. F 69:243-247(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
  4. "MgATP regulates allostery and fiber formation in IMPDHs."
    Labesse G., Alexandre T., Vaupre L., Salard-Arnaud I., Him J.L., Raynal B., Bron P., Munier-Lehmann H.
    Structure 21:975-985(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) IN COMPLEX WITH ATP AND PHOSPHATE.

Entry informationi

Entry nameiQ9HXM5_PSEAE
AccessioniPrimary (citable) accession number: Q9HXM5
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2001
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported, Complete proteome, Reference proteome

External Data

Dasty 3

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