Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9HXM5 (Q9HXM5_PSEAE) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein attributes

Sequence length489 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_01964

Catalytic activity

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH. RuleBase RU003928 HAMAP-Rule MF_01964

Cofactor

Potassium By similarity. HAMAP-Rule MF_01964

Enzyme regulation

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. HAMAP-Rule MF_01964

Pathway

Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. RuleBase RU003928 HAMAP-Rule MF_01964

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01964

Sequence similarities

Belongs to the IMPDH/GMPR family. HAMAP-Rule MF_01964

Contains 2 CBS domains. HAMAP-Rule MF_01964

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain93 – 14856CBS 1 By similarity HAMAP-Rule MF_01964
Domain152 – 21059CBS 2 By similarity HAMAP-Rule MF_01964
Nucleotide binding118 – 1203ATP PDB 4DQW
Nucleotide binding134 – 1374ATP PDB 4DQW
Nucleotide binding180 – 1812ATP PDB 4DQW
Nucleotide binding198 – 1992ATP PDB 4DQW
Nucleotide binding297 – 2993NAD By similarity HAMAP-Rule MF_01964
Region337 – 3393IMP binding By similarity HAMAP-Rule MF_01964
Region360 – 3612IMP binding By similarity HAMAP-Rule MF_01964
Region384 – 3885IMP binding By similarity HAMAP-Rule MF_01964

Sites

Active site3041Thioimidate intermediate By similarity PIRSR PIRSR000130-1 HAMAP-Rule MF_01964
Metal binding2991Potassium; via carbonyl oxygen By similarity HAMAP-Rule MF_01964
Metal binding3011Potassium; via carbonyl oxygen By similarity HAMAP-Rule MF_01964
Metal binding3041Potassium; via carbonyl oxygen By similarity HAMAP-Rule MF_01964
Metal binding4711Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity HAMAP-Rule MF_01964
Metal binding4721Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity HAMAP-Rule MF_01964
Metal binding4731Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity HAMAP-Rule MF_01964
Binding site981ATP; via amide nitrogen and carbonyl oxygen PDB 4DQW
Binding site1531ATP PDB 4DQW
Binding site1591ATP; via amide nitrogen and carbonyl oxygen PDB 4DQW
Binding site2471NAD By similarity HAMAP-Rule MF_01964
Binding site3021IMP By similarity HAMAP-Rule MF_01964
Binding site3391Phosphate; via amide nitrogen PDB 4DQW
Binding site4171IMP By similarity HAMAP-Rule MF_01964

Sequences

Sequence LengthMass (Da)Tools
Q9HXM5 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 6D2320AFD52C888B

FASTA48951,707
        10         20         30         40         50         60 
MLRISQEALT FDDVLLIPGY SEVLPKDVSL KTRLTRGIEL NIPLVSAAMD TVTEARLAIA 

        70         80         90        100        110        120 
MAQEGGIGII HKNMGIEQQA AEVRKVKKHE TAIVRDPVTV TPSTKIIELL QMAREYGFSG 

       130        140        150        160        170        180 
FPVVEQGELV GIVTGRDLRV KPNAGDTVAA IMTPKDKLVT AREGTPLEEM KAKLYENRIE 

       190        200        210        220        230        240 
KMLVVDENFY LRGLVTFRDI EKAKTYPLAS KDEQGRLRVG AAVGTGADTG ERVAALVAAG 

       250        260        270        280        290        300 
VDVVVVDTAH GHSKGVIERV RWVKQTFPDV QVIGGNIATA EAAKALAEAG ADAVKVGIGP 

       310        320        330        340        350        360 
GSICTTRIVA GVGVPQISAI ANVAAALEGT GVPLIADGGI RFSGDLAKAM VAGAYCVMMG 

       370        380        390        400        410        420 
SMFAGTEEAP GEIELFQGRS YKSYRGMGSL GAMSGSQGSS DRYFQDASAG AEKLVPEGIE 

       430        440        450        460        470        480 
GRVPYKGALS AIVHQLMGGL RAAMGYTGSA DIQQMRTQPQ FVRITGAGMA ESHVHDVQIT 


KEAPNYRVG 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004091 Genomic DNA. Translation: AAG07157.1.
PIRH83173.
RefSeqNP_252459.1. NC_002516.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZFHX-ray2.25A1-489[»]
4AVFX-ray2.23A/B/C/D1-489[»]
4DQWX-ray2.51A/B1-489[»]
ProteinModelPortalQ9HXM5.
SMRQ9HXM5. Positions 1-468.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-60162N.
STRING208964.PA3770.

Proteomic databases

PRIDEQ9HXM5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID880535.
KEGGpae:PA3770.
PATRIC19842179. VBIPseAer58763_3947.

Organism-specific databases

PseudoCAPPA3770.

Phylogenomic databases

HOGENOMHOG000165755.
KOK00088.
OMASSMGYCG.
OrthoDBEOG6GTZPV.
ProtClustDBPRK05567.

Enzyme and pathway databases

UniPathwayUPA00601; UER00295.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01964. IMPDH.
InterProIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERPTHR11911:SF6. PTHR11911:SF6. 1 hit.
PfamPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFPIRSF000130. IMPDH. 1 hit.
SMARTSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsTIGR01302. IMP_dehydrog. 1 hit.
PROSITEPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ9HXM5_PSEAE
AccessionPrimary (citable) accession number: Q9HXM5
Entry history
Integrated into UniProtKB/TrEMBL: March 1, 2001
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)