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Protein
Submitted name:

2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase

Gene

etbD

Organism
Rhodococcus sp.
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Protein predictedi

Functioni

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

HydrolaseImported

Protein family/group databases

ESTHERirhosp-bphd. Carbon-carbon_bond_hydrolase.

Names & Taxonomyi

Protein namesi
Submitted name:
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolaseImported
Gene namesi
Name:etbDImported
OrganismiRhodococcus sp.Imported
Taxonomic identifieri1831 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesNocardiaceaeRhodococcus

Structurei

3D structure databases

ProteinModelPortaliO05149.
SMRiO05149. Positions 4-284.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO05149.

Family & Domainsi

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

O05149-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKTVEIIEK RFPSGTLASH ALVAGDPQSP AVVLLHGAGP GAHAASNWRP
60 70 80 90 100
IIPDLAENFF VVAPDLIGFG QSEYPETYPG HIMSWVGMRV EQILGLMNHF
110 120 130 140 150
GIEKSHIVGN SMGGAVTLQL VVEAPERFDK VALMGSVGAP MNARPPELAR
160 170 180 190 200
LLAFYADPRL TPYRELIHSF VYDPENFPGM EEIVKSRFEV ANDPEVRRIQ
210 220 230 240 250
EVMFESMKAG MESLVIPPAT LGRLPHDVLV FHGRQDRIVP LDTSLYLTKH
260 270 280
LKHAELVVLD RCGHWAQLER WDAMGPMLME HFRAA
Length:285
Mass (Da):31,643
Last modified:July 1, 1997 - v1
Checksum:i677F831D2CDEC6DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78322 Genomic DNA. Translation: BAA18939.1.
PIRiJC6325.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78322 Genomic DNA. Translation: BAA18939.1.
PIRiJC6325.

3D structure databases

ProteinModelPortaliO05149.
SMRiO05149. Positions 4-284.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERirhosp-bphd. Carbon-carbon_bond_hydrolase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO05149.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Identification and Cloning of an Alternative 2,3-Dihydroxybiphenyl 1,2-Dioxygenase in Rhodococcus sp. RHA1."
    Hauschild J.E., Masai E., Sugiyama K., Hatta T., Kimbara K., Fukuda M., Yano K.
    Appl. Environ. Microbiol. 62:2940-2946(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: RHA1Imported.
  2. "The bphDEF meta-cleavage pathway genes involved in biphenyl/polychlorinated biphenyl degradation are located on a linear plasmid and separated from the initial bphACB genes in Rhodococcus sp. strain RHA1."
    Masai E., Sugiyama K., Iwashita N., Shimizu S., Hauschild J.E., Hatta T., Kimbara K., Yano K., Fukuda M.
    Gene 187:141-149(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: RHA1Imported.

Entry informationi

Entry nameiO05149_RHOSO
AccessioniPrimary (citable) accession number: O05149
Entry historyi
Integrated into UniProtKB/TrEMBL: July 1, 1997
Last sequence update: July 1, 1997
Last modified: June 24, 2015
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.