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P96965 (P96965_PSEFL) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 59. Feed History...

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

Names and origin

Protein names
Gene names
Name:cumD EMBL BAA12150.1
OrganismPseudomonas fluorescens EMBL BAA12150.1
Taxonomic identifier294 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Ontologies

Keywords
   LigandChloride PDB 2D0D
   Molecular functionHydrolase EMBL BAA12150.1
   Technical term3D-structure PDB 1UKA PDB 1UKB PDB 1UK6 PDB 1UK7 PDB 1UK9 PDB 2D0D PDB 1IUP PDB 1UK8 PDB 1IUO PDB 1IUN
Gene Ontology (GO)
   Molecular_functionhydrolase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region121 – 1222Phosphate 1 binding PDB 2D0D
Region258 – 2614Phosphate 2 binding PDB 2D0D

Sites

Binding site341Acetate 1
Binding site341Chloride PDB 2D0D
Binding site1031Chloride PDB 2D0D
Binding site2151Phosphate 2 PDB 2D0D
Binding site2431Acetate 3 PDB 1IUN
Binding site2521Acetate 1
Binding site2721Acetate 3 PDB 1IUN
Site1031Important for catalytic activity PDB 1UK7
Site2241Important for catalytic activity PDB 1UK7
Site2521Important for catalytic activity PDB 1UK7

Sequences

Sequence LengthMass (Da)Tools
P96965 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 2FA69148F390DED9

FASTA28231,490
        10         20         30         40         50         60 
MANLEIGKSI LAAGVLTNYH DVGEGQPVIL IHGSGPGVSA YANWRLTIPA LSKFYRVIAP 

        70         80         90        100        110        120 
DMVGFGFTDR PENYNYSKDS WVDHIIGIMD ALEIEKAHIV GNSFGGGLAI ATALRYSERV 

       130        140        150        160        170        180 
DRMVLMGAAG TRFDVTEGLN AVWGYTPSIE NMRNLLDIFA YDRSLVTDEL ARLRYEASIQ 

       190        200        210        220        230        240 
PGFQESFSSM FPEPRQRWID ALASSDEDIK TLPNETLIIH GREDQVVPLS SSLRLGELID 

       250        260        270        280 
RAQLHVFGRC GHWTQIEQTD RFNRLVVEFF NEANTPKLVG RP 

« Hide

References

[1]"Analysis of cumene (isopropylbenzene) degradation genes from Pseudomonas fluorescens IP01."
Habe H., Kasuga K., Nojiri H., Yamane H., Omori T.
Appl. Environ. Microbiol. 62:4471-4477(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: IP01 EMBL BAA12150.1.
[2]"Crystal structures of a meta-cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) complexed with cleavage products."
Fushinobu S., Saku T., Hidaka M., Jun S.Y., Nojiri H., Yamane H., Shoun H., Omori T., Wakagi T.
Protein Sci. 11:2184-2195(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH ACETATE.
[3]"A series of crystal structures of a meta-cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) complexed with various cleavage products."
Fushinobu S., Jun S.Y., Hidaka M., Nojiri H., Yamane H., Shoun H., Omori T., Wakagi T.
Biosci. Biotechnol. Biochem. 69:491-498(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), ACTIVE SITE.
[4]"Improving the catalytic efficiency of a meta-cleavage product hydrolase (CumD) from Pseudomonas fluorescens IP01."
Jun S.Y., Fushinobu S., Nojiri H., Omori T., Shoun H., Wakagi T.
Biochim. Biophys. Acta 1764:1159-1166(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH CHLORIDE AND PHOSPHATE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D83955 Genomic DNA. Translation: BAA12150.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IUNX-ray2.80A/B1-282[»]
1IUOX-ray2.00A1-282[»]
1IUPX-ray1.60A1-282[»]
1UK6X-ray1.95A1-282[»]
1UK7X-ray1.70A1-282[»]
1UK8X-ray1.60A1-282[»]
1UK9X-ray1.80A1-282[»]
1UKAX-ray1.70A1-282[»]
1UKBX-ray1.80A1-282[»]
2D0DX-ray1.65A1-282[»]
ProteinModelPortalP96965.
SMRP96965. Positions 2-277.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PfamPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP96965.

Entry information

Entry nameP96965_PSEFL
AccessionPrimary (citable) accession number: P96965
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 1997
Last sequence update: May 1, 1997
Last modified: June 11, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)