NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BE-81;
PubMed=3667527 [NCBI, ExPASy, EBI, Israel, Japan]
Irie S., Doi S., Yorifuji T., Takagi M., Yano K.;
"Nucleotide sequencing and characterization of the genes encoding benzene oxidation enzymes of Pseudomonas putida.";
J. Bacteriol. 169:5174-5179(1987).

Comments

FUNCTION: Catalyzes both the oxidation of benzene and toluene.
CATALYTIC ACTIVITY: Benzene + NADH + O₂ = cis-cyclohexa-3,5-diene-1,2-diol + NAD⁺.
CATALYTIC ACTIVITY: Toluene + NADH + O₂ = (1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD⁺.
COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity).
COFACTOR: Binds 1 iron ion per subunit (By similarity).
PATHWAY: Aromatic compound metabolism; benzene degradation; catechol from benzene: step 1/2 .
PATHWAY: Xenobiotic degradation; toluene degradation .
PATHWAY: Xenobiotic degradation; xylene degradation .
SUBUNIT: This dioxygenase system consists of four proteins: the two subunits of the hydroxylase component (bnzA and bnzB), a ferredoxin (bnzC) and a ferredoxin reductase (bnzD).
SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family.
SIMILARITY: Contains 1 Rieske domain.
SEQUENCE CAUTION:
- Sequence=AAA25735.1; Type=Frameshift; Positions=330, 339, 360, 362, 368, 393;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M17904; AAA25735.1; ALT_FRAME; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A29830; A29830.

3D structure databases

HSSP

P23094; 1O7N. [HSSP ENTRY / PDB]

ModBase

P0C618.

Ontologies

GO:0051537;	Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0018619;	Molecular function: benzene 1,2-dioxygenase activity (inferred from electronic annotation from EC).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0016702;	Molecular function: oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen (inferred from electronic annotation from UniProtKB-KW).
GO:0018624;	Molecular function: toluene dioxygenase activity (inferred from electronic annotation from EC).
GO:0019439;	Biological process: aromatic compound catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR005806; Rieske_reg.
IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
IPR015879; Ring_hydroxy_dOase_asu_C.
IPR001663; Rng_hydr_dOase-A.
Graphical view of domain structure.

PANTHER

PTHR21266:SF2; Rng_hydr_dOase-A; 1.

Pfam

PF00355; Rieske; 1.
PF00848; Ring_hydroxyl_A; 1.
Pfam graphical view of domain structure.

PRINTS

PR00090; RNGDIOXGNASE.

PROSITE

PS51296; RIESKE; 1.
PS00570; RING_HYDROXYL_ALPHA; 1.
PROSITE graphical view of domain structure (profiles).

Other

ProtoNet

P0C618.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

2Fe-2S; Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 450`	`450`	`Benzene 1,2-dioxygenase subunit alpha.`	`PRO_0000085045`
`DOMAIN`	`54 163`	`110`	`Rieske.`
`METAL`	`96 96`		`Iron-sulfur (2Fe-2S) (By similarity).`
`METAL`	`98 98`		`Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity).`
`METAL`	`116 116`		`Iron-sulfur (2Fe-2S) (By similarity).`
`METAL`	`119 119`		`Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity).`
`METAL`	`222 222`		`Iron (By similarity).`
`METAL`	`228 228`		`Iron (By similarity).`

Sequence information

Length: 450 AA [This is the length of the unprocessed precursor]

Molecular weight: 50944 Da [This is the MW of the unprocessed precursor]

CRC64: 038C80F197F3485D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNQTDTSPIR LRRSWNTSEI EALFDEHAGR IDPRIYTDED LYQLELERVF ARSWLLLGHE 

        70         80         90        100        110        120 
TQIRKPGDYI TTYMGEDPVV VVRQKDASIA VFLNQCRHRG MRICRADAGN AKAFTCSYHG 

       130        140        150        160        170        180 
WAYDTAGNLV NVPYEAESFA CLNKKEWSPL KARVETYKGL IFANWDENAV DLDTYLGEAK 

       190        200        210        220        230        240 
FYMDHMLDRT EAGTEAIPGV QKWVIPCNWK FAAEQFCSDM YHAGTTSHLS GILAGLPEDL 

       250        260        270        280        290        300 
EMADLAPPTV GKQYRASWGG HGSGFYVGDP NLMLAIMGPK VTSYWTEGPA SEKAAERLGS 

       310        320        330        340        350        360 
VERGSKLMVE HMTVFPTCSF LPGINTVRTW HPRGPNEVEV WAFTVVDADA PDDIKEEFRR 

       370        380        390        400        410        420 
QTLRTFSAGG VFEQDDGENW VEIQHILRGH KARSRPFNAE MSMDQTVDND PVYPGRISNN 

       430        440        450 
VYSEEAARGL YAHWLRMMTS PDWDALKATR

P0C618 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools