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P0A111 (NDOB_PSEU8) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Naphthalene 1,2-dioxygenase subunit alpha
EC=1.14.12.12
Alternative name(s):
Naphthalene 1,2-dioxygenase ISP alpha
Gene names
Name:doxB
Encoded onPlasmid
OrganismPseudomonas sp. (strain C18)
Taxonomic identifier69011 [NCBI]
Taxonomic lineageBacteria › Proteobacteria

Protein attributes

Sequence length449 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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 By similarity.

Binds 1 iron ion By similarity.

Pathway

Aromatic compound metabolism; naphthalene degradation.

Subunit structure

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 and ferredoxin (doxA), and ISP is composed of a large alpha subunit (doxB) and a small beta subunit (doxD) Probable.

Sequence similarities

Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family.

Contains 1 Rieske domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 449449Naphthalene 1,2-dioxygenase subunit alpha
PRO_0000085054

Regions

Domain39 – 13799Rieske

Sites

Metal binding811Iron-sulfur (2Fe-2S) By similarity
Metal binding831Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
Metal binding1011Iron-sulfur (2Fe-2S) By similarity
Metal binding1041Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
Metal binding2081Iron By similarity
Metal binding2131Iron By similarity
Metal binding3621Iron By similarity

Secondary structure

1 ................................................................................................ 449
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A111 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 1FD2F42296B4F7A8

FASTA44949,608
        10         20         30         40         50         60 
MNYNNKILVS ESGLSQKHLI HGDEELFQHE LKTIFARNWL FLTHDSLIPA PGDYVTAKMG 

        70         80         90        100        110        120 
IDEVIVSRQN DGSIRAFLNV CRHRGKTLVS VEAGNAKGFV CSYHGWGFGS NGELQSVPFE 

       130        140        150        160        170        180 
KDLYGESLNK KCLGLKEVAR VESFHGFIYG CFDQEAPPLM DYLGDAAWYL EPMFKHSGGL 

       190        200        210        220        230        240 
ELVGPPGKVV IKANWKAPAE NFVGDAYHVG WTHASSLRSG ESIFSSLAGN AALPPEGAGL 

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

       310        320        330        340        350        360 
FPNNSMLTCS GVFKVWNPID ANTTEVWTYA IVEKDMPEDL KRRLADSVQR TFGPAGFWES 

       370        380        390        400        410        420 
DDNDNMETAS QNGKKYQSRD SDLLSNLGFG EDVYGDAVYP GVVGKSAIGE TSYRGFYRAY 

       430        440 
QAHVSSSNWA EFEHASSTWH TELTKTTDR

« Hide

References

[1]"Metabolism of dibenzothiophene and naphthalene in Pseudomonas strains: complete DNA sequence of an upper naphthalene catabolic pathway."
Denome S.A., Stanley D.C., Olson E.S., Young K.D.
J. Bacteriol. 175:6890-6901(1993) [PubMed: 8226631] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M60405 Genomic DNA. Translation: AAA16125.1.
PIRS27632.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HMJX-ray1.50A1-449[»]
2HMKX-ray1.65A1-449[»]
2HMLX-ray1.80A1-449[»]
2HMMX-ray1.60A1-449[»]
2HMNX-ray1.70A1-449[»]
2HMOX-ray1.60A1-449[»]
ProteinModelPortalP0A111.
SMRP0A111. Positions 1-447.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR017941. Rieske_2Fe-2S.
IPR015881. Ring-hydroxy_dOase_2Fe2S_BS.
IPR015879. Ring_hydroxy_dOase_asu_C.
IPR001663. Rng_hydr_dOase-A.
[Graphical view]
Gene3DG3DSA:2.102.10.10. Rieske_reg. 1 hit.
PfamPF00355. Rieske. 1 hit.
PF00848. Ring_hydroxyl_A. 1 hit.
[Graphical view]
PRINTSPR00090. RNGDIOXGNASE.
SUPFAMSSF50022. Rieske_dom. 1 hit.
PROSITEPS51296. RIESKE. 1 hit.
PS00570. RING_HYDROXYL_ALPHA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNDOB_PSEU8
AccessionPrimary (citable) accession number: P0A111
Secondary accession number(s): O07830 expand/collapse secondary AC list , O33461, P23094, Q52124
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: June 28, 2011
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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