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

Preferred order of sections

Names and origin

Protein names

Submitted name:
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase EMBL BAA18939.1

Gene names

Name:

etbD EMBL BAA18939.1

Organism

Rhodococcus sp. EMBL BAA18939.1

Taxonomic identifier

1831 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length	285 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Molecular function	Hydrolase EMBL BAA18939.1
Technical term	3D-structure PDB 1C4X
Gene Ontology (GO)
Molecular_function	hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Site

111

1

Important for catalytic activity PDB 1C4X

Site

236

1

Important for catalytic activity PDB 1C4X

Site

264

1

Important for catalytic activity PDB 1C4X

Sequences

Sequence

Length

Mass (Da)

Tools

O05149 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 677F831D2CDEC6DD
Show »

FASTA

285

31,643

        10         20         30         40         50         60 
MAKTVEIIEK RFPSGTLASH ALVAGDPQSP AVVLLHGAGP GAHAASNWRP IIPDLAENFF 

        70         80         90        100        110        120 
VVAPDLIGFG QSEYPETYPG HIMSWVGMRV EQILGLMNHF GIEKSHIVGN SMGGAVTLQL 

       130        140        150        160        170        180 
VVEAPERFDK VALMGSVGAP MNARPPELAR LLAFYADPRL TPYRELIHSF VYDPENFPGM 

       190        200        210        220        230        240 
EEIVKSRFEV ANDPEVRRIQ EVMFESMKAG MESLVIPPAT LGRLPHDVLV FHGRQDRIVP 

       250        260        270        280 
LDTSLYLTKH LKHAELVVLD RCGHWAQLER WDAMGPMLME HFRAA

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References

[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: RHA1 EMBL BAA18939.1.

[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: RHA1 EMBL BAA18939.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D78322 Genomic DNA. Translation: BAA18939.1.

PIR

JC6325.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C4X	X-ray	2.40	A	1-285	[»]

ProteinModelPortal

O05149.

SMR

O05149. Positions 4-284.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR000073. AB_hydrolase_1.
[Graphical view]

PRINTS

PR00111. ABHYDROLASE.

ProtoNet

Search...

Other

EvolutionaryTrace

O05149.

Entry information

Entry name

O05149_RHOSO

Accession

Primary (citable) accession number: O05149

Entry history

Integrated into UniProtKB/TrEMBL:	July 1, 1997
Last sequence update:	July 1, 1997
Last modified:	April 3, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)