[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 17483 / DSM 6506 / JCM 6159 / Stanier 109; Hamann C.; "Naphthalene dioxygenase genes from Pseudomonas fluorescens."; Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.

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.
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: 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 large alpha subunit (ndoB) and a small beta subunit (ndoC).
SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family.
SIMILARITY: Contains 1 Rieske domain.

Copyright

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Cross-references

Sequence databases

EMBL

AF004283; AAB61370.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P23094; 1O7N. [HSSP ENTRY / PDB]

SMR

O07824; 1-447.

ModBase

O07824.

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.

Gene3D

G3DSA:2.102.10.10; Rieske_reg; 1.

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

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; Plasmid.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 449`	`449`	`Naphthalene 1,2-dioxygenase subunit alpha.`	`PRO_0000085055`
`DOMAIN`	`39 137`	`99`	`Rieske.`
`METAL`	`81 81`		`Iron-sulfur (2Fe-2S) (By similarity).`
`METAL`	`83 83`		`Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity).`
`METAL`	`101 101`		`Iron-sulfur (2Fe-2S) (By similarity).`
`METAL`	`104 104`		`Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity).`
`METAL`	`208 208`		`Iron (By similarity).`
`METAL`	`213 213`		`Iron (By similarity).`
`METAL`	`362 362`		`Iron (By similarity).`

Sequence information

Length: 449 AA [This is the length of the unprocessed precursor]

Molecular weight: 49514 Da [This is the MW of the unprocessed precursor]

CRC64: 186A7924AD437A1C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNYKNKILVS ESGLTQKHLI HGDEELFQHE LRTIXARNWL FLTHDSLIPS PGDYVTAKMG 

        70         80         90        100        110        120 
IDEVIVSRQS DGSIRAFLNV CRHRGKTLVN AEAGNAKGFV CSYHGWGFGS NGELQSVPFE 

       130        140        150        160        170        180 
KELYGESLNK KCLGLKEVAR VESFHGFIYG CFDQEAPSLM DYLGDAAWYL EPIFKHSGGL 

       190        200        210        220        230        240 
ELVGPPGKVV IKANWKAPAE NFVGDAYHVG WTHASSLRTG ESIFSSLAGN AVLPPEGAGL 

       250        260        270        280        290        300 
QMTSKYGSGM GVLWDGYSGV HSADLVPELM AFGGAKQERL NKEIGDVPAR IYRSHLNCTV 

       310        320        330        340        350        360 
FPNNSVLTCS GVFKVWNPID ANTTEVWTYA IVEKDMPEDL KRRLADAVQR TFGPAGFWES 

       370        380        390        400        410        420 
DDNDNMETAS QNGKKYQSRD SDLISNLGFG KDVYGDAVYP GVVGKSAIGE TSYRGFYRAY 

       430        440 
QAHVSSSNWA EFEDASSTWH TELTKTTDR

O07824 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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