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

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Q53122 (Q53122_RHOSR) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 76. History...

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

Third-party data

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

Names and origin

Protein names

Submitted name:
Biphenyl 2,3-dioxygenase alpha subunit EMBL ABG99107.1
EC=1.14.12.18 EMBL ABG99107.1

Submitted name:
Biphenyl dioxygenase EMBL BAA06868.1

Gene names

Name:	bphA1 EMBL BAA06868.1
Synonyms:	bphAa EMBL ABG99107.1
Ordered Locus Names:	RHA1_ro08060

Encoded on

Plasmid pRHL1 Ref.3 EMBL ABG99107.1

Organism

Rhodococcus sp. (strain RHA1) [Complete proteome] [HAMAP] EMBL BAA06868.1

Taxonomic identifier

101510 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	460 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Contains 1 Rieske domain. RuleBase RU004493

Ontologies

Keywords
Ligand	2Fe-2S RuleBase RU004492 PDB 1ULJ PDB 1ULI Iron Iron-sulfur Metal-binding
Molecular function	Dioxygenase EMBL BAA06868.1 Oxidoreductase
Technical term	3D-structure PDB 1ULJ PDB 1ULI Complete proteome Plasmid EMBL ABG99107.1
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW biphenyl 2,3-dioxygenase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: InterPro 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

Iron-sulfur (2Fe-2S) PDB 1ULJ PDB 1ULI

Metal binding

100

Iron-sulfur (2Fe-2S); via pros nitrogen PDB 1ULJ PDB 1ULI

Metal binding

118

Iron-sulfur (2Fe-2S) PDB 1ULJ PDB 1ULI

Metal binding

121

Iron-sulfur (2Fe-2S); via pros nitrogen PDB 1ULJ PDB 1ULI

Metal binding

123

Iron-sulfur (2Fe-2S) PDB 1ULI

Metal binding

217

Iron PDB 1ULJ

Metal binding

224

Iron; via tele nitrogen PDB 1ULJ PDB 1ULI

Metal binding

230

Iron; via tele nitrogen PDB 1ULJ PDB 1ULI

Metal binding

378

Iron PDB 1ULJ PDB 1ULI

Sequences

Sequence

Length

Mass (Da)

Tools

Q53122 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 28D86F926FA4E9A0
Show »

FASTA

460

51,592

        10         20         30         40         50         60 
MTDVQCEPAL AGRKPKWADA DIAELVDERT GRLDPRIYTD EALYEQELER IFGRSWLLMG 

        70         80         90        100        110        120 
HETQIPKAGD FMTNYMGEDP VMVVRQKNGE IRVFLNQCRH RGMRICRADG GNAKSFTCSY 

       130        140        150        160        170        180 
HGWAYDTGGN LVSVPFEEQA FPGLRKEDWG PLQARVETYK GLIFANWDAD APDLDTYLGE 

       190        200        210        220        230        240 
AKFYMDHMLD RTEAGTEAIP GIQKWVIPCN WKFAAEQFCS DMYHAGTTSH LSGILAGLPD 

       250        260        270        280        290        300 
GVDLSELAPP TEGIQYRATW GGHGSGFYIG DPNLLLAIMG PKVTEYWTQG PAAEKASERL 

       310        320        330        340        350        360 
GSTERGQQLM AQHMTIFPTC SFLPGINTIR AWHPRGPNEI EVWAFTVVDA DAPEEMKEEY 

       370        380        390        400        410        420 
RQQTLRTFSA GGVFEQDDGE NWVEIQQVLR GHKARSRPFN AEMGLGQTDS DNPDYPGTIS 

       430        440        450        460 
YVYSEEAARG LYTQWVRMMT SPDWAALDAT RPAVSESTHT

« Hide

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 BAA06868.1.
[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 AND IRON-SULFUR (2FE-2S).
[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: ABG99107.1.
D32142 Genomic DNA. Translation: BAA06868.1.

RefSeq

YP_707265.1. NC_008269.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ULI	X-ray	2.20	A/C/E	1-460	[»]
1ULJ	X-ray	2.60	A/C/E	1-460	[»]

ProteinModelPortal

Q53122.

SMR

Q53122. Positions 17-451.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q53122. 1 interaction.

STRING

Q53122.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

4225185.

GenomeReviews

Gene locus RHA1_ro08060 in contig CP000432_GR.

KEGG

rha:RHA1_ro08060.

PATRIC

23213686. VBIRhoJos26306_7407.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG4638.

HOGENOM

HBG705920.

OMA

DMYHAGT.

ProtClustDB

CLSK880425.

Enzyme and pathway databases

BioCyc

RSP101510:RHA1_RO08060-MONOMER.

BRENDA

1.14.12.18. 1423.

Family and domain databases

InterPro

IPR017941. Rieske_2Fe-2S.
IPR015881. Ring-hydroxy_dOase_2Fe2S_BS.
IPR015879. Ring_hydroxy_dOase_asu_C.
IPR001663. Rng_hydr_dOase-A.
[Graphical view]

Gene3D

G3DSA:2.102.10.10. Rieske_reg. 1 hit.

K08689.

Pfam

PF00355. Rieske. 1 hit.
PF00848. Ring_hydroxyl_A. 1 hit.
[Graphical view]

PRINTS

PR00090. RNGDIOXGNASE.

SUPFAM

SSF50022. Rieske_dom. 1 hit.

PROSITE

PS51296. RIESKE. 1 hit.
PS00570. RING_HYDROXYL_ALPHA. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q53122_RHOSR

Accession

Primary (citable) accession number: Q53122

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information