[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=NCIMB 9816; DOI=10.1016/0378-1119(88)90500-8; PubMed=3243438 [NCBI, ExPASy, EBI, Israel, Japan] Kurkela S., Lehvaeslaiho H., Palva E.T., Teeri T.H.; "Cloning, nucleotide sequence and characterization of genes encoding naphthalene dioxygenase of Pseudomonas putida strain NCIB9816."; Gene 73:355-362(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PLASMID=pDTG1; STRAIN=NCIMB 9816-4; DOI=10.1016/S0378-1119(96)00462-3; PubMed=8973308 [NCBI, ExPASy, EBI, Israel, Japan] Parales J.V., Kumar A., Parales R.E., Gibson D.T.; "Cloning and sequencing of the genes encoding 2-nitrotoluene dioxygenase from Pseudomonas sp. JS42."; Gene 181:57-61(1996).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PLASMID=NAH7; STRAIN=ATCC 17485 / DSM 50208 / Stanier 111 / JCM 6158 / Biotype A; DOI=10.1016/0378-1119(93)90613-8; PubMed=8486285 [NCBI, ExPASy, EBI, Israel, Japan] Simon M.J., Osslund T.D., Saunders R., Ensley B.D., Suggs S., Harcourt A.A., Suen W.-C., Cruden D.L., Gibson D.T., Zylstra G.J.; "Sequences of genes encoding naphthalene dioxygenase in Pseudomonas putida strains G7 and NCIB 9816-4."; Gene 127:31-37(1993).
[4]	X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS). STRAIN=NCIMB 9816-4; DOI=10.1016/S0969-2126(98)00059-8; PubMed=9634695 [NCBI, ExPASy, EBI, Israel, Japan] Kauppi B., Lee K., Carredano E., Parales R.E., Gibson D.T., Eklund H., Ramaswamy S.; "Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1,2-dioxygenase."; Structure 6:571-586(1998).

Comments

FUNCTION: Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-naphthalene dihydrodiol. The beta subunit may be responsible for the substrate specificity of the enzyme.
CATALYTIC ACTIVITY: Naphthalene + NADH + O₂ = (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD⁺.
COFACTOR: Binds 1 2Fe-2S cluster (Probable).
COFACTOR: Binds 1 iron ion (Probable).
PATHWAY: Aromatic compound metabolism; naphtalene degradation .
SUBUNIT: The naphthalene dioxygenase (NDO) multicomponent enzyme system is composed of an electron transfer component and an iron sulfur protein (ISP). The electron transfer component is composed of ferredoxin reductase (ndoR) and ferredoxin (ndoA), and ISP is composed of a hexamer of three large alpha subunits (ndoB) and three small beta subunits (ndoC).
INTERACTION:
P0A110:ndoB; NbExp=2; IntAct=EBI-1029028, EBI-1029015;
SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase beta subunit family.

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

M23914; AAB47592.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U49496; AAA92142.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M83949; AAA25903.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JN0645; JN0645.
JS0072; JS0072.

RefSeq

NP_863073.1; -.

3D structure databases

PDB

1EG9; X-ray; 1.60 A; B=1-194.	[ExPASy / RCSB / EBI]
1NDO; X-ray; 2.25 A; B/D/F=1-194.	[ExPASy / RCSB / EBI]
1O7G; X-ray; 1.70 A; B=1-194.	[ExPASy / RCSB / EBI]
1O7H; X-ray; 2.20 A; B=1-194.	[ExPASy / RCSB / EBI]
1O7M; X-ray; 1.75 A; B=1-194.	[ExPASy / RCSB / EBI]
1O7N; X-ray; 1.40 A; B=1-194.	[ExPASy / RCSB / EBI]
1O7P; X-ray; 1.95 A; B=1-194.	[ExPASy / RCSB / EBI]
1O7W; X-ray; 1.90 A; B=1-194.	[ExPASy / RCSB / EBI]
1UUV; X-ray; 1.65 A; B=1-194.	[ExPASy / RCSB / EBI]
1UUW; X-ray; 2.30 A; B=1-194.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1EG9; -.
1NDO; -.
1O7G; -.
1O7H; -.
1O7M; -.
1O7N; -.
1O7P; -.
1O7W; -.
1UUV; -.
1UUW; -.

ModBase

P0A112.

Protein-protein interaction databases

IntAct

P0A112; -.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-12803; -.

Ontologies

GO:0018625;	Molecular function: naphthalene 1,2-dioxygenase activity (inferred from electronic annotation from EC).
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:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
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 UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000391; Rng_hydr_dOase-B.
Graphical view of domain structure.

Pfam

PF00866; Ring_hydroxyl_B; 1.
Pfam graphical view of domain structure.

ProtoNet

P0A112.

Genome annotation databases

GeneID

1343188; -.

Other

UniRef

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

Keywords

3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase; NAD; Oxidoreductase; Plasmid.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 194`	`194`	`Naphthalene 1,2-dioxygenase subunit beta.`	`PRO_0000085072`
`VARIANT`	`17 17`	`1`	`E -> Q (in strain: G7).`
`VARIANT`	`19 19`	`1`	`I -> F (in strain: G7).`
`VARIANT`	`28 28`	`1`	`S -> A (in strain: G7).`
`VARIANT`	`39 40`	`2`	`TQ -> NR (in strain: G7).`
`VARIANT`	`99 99`	`1`	`V -> I (in strain: G7).`
`VARIANT`	`109 109`	`1`	`G -> S (in strain: G7).`
`VARIANT`	`127 127`	`1`	`M -> R (in strain: G7).`
`VARIANT`	`130 130`	`1`	`N -> D (in strain: G7).`
`VARIANT`	`132 132`	`1`	`K -> E (in strain: G7).`
`TURN`	`5 7`	`3`
`HELIX`	`13 23`	`11`
`HELIX`	`28 46`	`19`
`HELIX`	`50 57`	`8`
`STRAND`	`58 69`	`12`
`STRAND`	`84 90`	`7`
`HELIX`	`92 103`	`12`
`HELIX`	`108 110`	`3`
`STRAND`	`115 127`	`13`
`STRAND`	`134 147`	`14`
`TURN`	`148 150`	`3`
`STRAND`	`151 167`	`17`
`STRAND`	`170 179`	`10`
`STRAND`	`183 185`	`3`

Sequence information

Length: 194 AA [This is the length of the unprocessed precursor]

Molecular weight: 22935 Da [This is the MW of the unprocessed precursor]

CRC64: 168D2E1535E66416 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MMINIQEDKL VSAHDAEEIL RFFNCHDSAL QQEATTLLTQ EAHLLDIQAY RAWLEHCVGS 

        70         80         90        100        110        120 
EVQYQVISRE LRAASERRYK LNEAMNVYNE NFQQLKVRVE HQLDPQNWGN SPKLRFTRFI 

       130        140        150        160        170        180 
TNVQAAMDVN DKELLHIRSN VILHRARRGN QVDVFYAARE DKWKRGEGGV RKLVQRFVDY 

       190 
PERILQTHNL MVFL

P0A112 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