Biphenyl 2,3-dioxygenase beta subunit - Rhodococcus sp. (strain RHA1)

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Q53123 (Q53123_RHOSR) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 67. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

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Names·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Submitted name:
Biphenyl 2,3-dioxygenase beta subunit EMBL ABG99106.1
EC=1.14.12.18 EMBL ABG99106.1

Submitted name:
Biphenyl dioxygenase EMBL BAA06869.1

Gene names

Name:	bphA2 EMBL BAA06869.1
Synonyms:	bphAb EMBL ABG99106.1
Ordered Locus Names:	RHA1_ro08059

Encoded on

Plasmid pRHL1 Ref.3 EMBL ABG99106.1

Organism

Rhodococcus sp. (strain RHA1) [Complete proteome] [HAMAP] EMBL BAA06869.1

Taxonomic identifier

Taxonomic lineage

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

Protein attributes

Sequence length	187 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Iron PDB 1ULI Metal-binding PDB 1ULI
Molecular function	Dioxygenase EMBL BAA06869.1 Oxidoreductase
Technical term	3D-structure PDB 1ULI PDB 1ULJ Complete proteome Plasmid EMBL ABG99106.1
Gene Ontology (GO)
Biological process	cellular aromatic compound metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	biphenyl 2,3-dioxygenase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.2. Source: IntAct
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

1

Iron; via tele nitrogen PDB 1ULI

Sequences

Sequence

Length

Mass (Da)

Tools

Q53123 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 896AE86BC80F215C
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187

22,020

        10         20         30         40         50         60 
MIDAESPTTA FRTKPAPVDP SLQHEIEQFY YWEAKLLNDR RFQEWFDLLA EDIHYFMPIR 

        70         80         90        100        110        120 
TTRIMRETAQ EYSGAREYAH FDDNAQMMRG RLRKITSDVS WSENPASRTR HVISNVMIVD 

       130        140        150        160        170        180 
GEKPGEYHVS SVFIVYRNRL ERQLDIFAGE RKDILRRTGS EAGFELAKRT ILIDQSTILS 


NNLSFFF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of biphenyl catabolic genes of gram-positive polychlorinated biphenyl degrader Rhodococcus sp. strain RHA1." Masai E., Yamada A., Healy J.M., Hatta T., Kimbara K., Fukuda M., Yano K. Appl. Environ. Microbiol. 61:2079-2085(1995) [PubMed: 7793929] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: RHA1 EMBL BAA06869.1.
[2]	"Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1." Furusawa Y., Nagarajan V., Tanokura M., Masai E., Fukuda M., Senda T. J. Mol. Biol. 342:1041-1052(2004) [PubMed: 15342255] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH IRON.
[3]	"The complete genome of Rhodococcus sp. RHA1 provides insights into a catabolic powerhouse." McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H. Eltis L.D. Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006) [PubMed: 17030794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

CP000432 Genomic DNA. Translation: ABG99106.1.
D32142 Genomic DNA. Translation: BAA06869.1.

RefSeq

YP_707264.1. NC_008269.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ULI	X-ray	2.20	B/D/F	1-187	[»]
1ULJ	X-ray	2.60	B/D/F	1-187	[»]

ProteinModelPortal

SMR

Q53123. Positions 10-187.

ModBase

Protein-protein interaction databases

IntAct

Q53123. 1 interaction.

STRING

Protocols and materials databases

StructuralBiologyKnowledgebase

Genome annotation databases

GeneID

GenomeReviews

Gene locus RHA1_ro08059 in contig CP000432_GR.

KEGG

rha:RHA1_ro08059.

PATRIC

23213684. VBIRhoJos26306_7406.

Organism-specific databases

CMR

Phylogenomic databases

eggNOG

HOGENOM

OMA

ProtClustDB

Enzyme and pathway databases

BioCyc

RSP101510:RHA1_RO08059-MONOMER.

Family and domain databases

InterPro

IPR000391. Rng_hydr_dOase-bsu.
[Graphical view]

KO

Pfam

PF00866. Ring_hydroxyl_B. 1 hit.
[Graphical view]

ProtoNet

Entry information

Entry name

Q53123_RHOSR

Accession

Primary (citable) accession number: Q53123

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

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Names·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info