Reviewed, UniProtKB/Swiss-Prot Q51495 (NDOC_PSEAE)

Names and origin

Protein names

Recommended name:
    Naphthalene 1,2-dioxygenase subunit beta
    EC=1.14.12.12
Alternative name(s):
    Naphthalene 1,2-dioxygenase ISP beta

Gene names

Name:	ndoC
Synonyms:	pahA4

Organism

Pseudomonas aeruginosa

Taxonomic identifier

287 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	193 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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. 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. Binds 1 iron ion Probable.
Pathway	Aromatic compound metabolism; naphtalene 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 (ndoR) and ferredoxin (ndoA), and ISP is composed of a large alpha subunit (ndoB) and a small beta subunit (ndoC).
Sequence similarities	Belongs to the bacterial ring-hydroxylating dioxygenase beta subunit family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	NAD
Molecular function	Dioxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	naphthalene 1,2-dioxygenase activity Inferred from electronic annotation. Source: EC oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 193	193	Naphthalene 1,2-dioxygenase subunit beta		PRO_0000085074

Sequences

	Sequence		Length	Mass (Da)
	Q51495-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 3341AEF611A4478F	FASTA	193	23,001
	10 20 30 40 50 60 MMINIQEDKL VSAHDAEEFL RFFNSGDEAL QQEATTLLTR EAHLLDIQAY RAWLEHCVDS 70 80 90 100 110 120 EVKYQIISRE LRSASERRYQ LNETMNIFNE NYEQLEVRVA HQLDPQNWGN SPKVRFTRFI 130 140 150 160 170 180 TNIQAAMDEN EDLLHIRSNL IVHRARRGNQ VDVFYATRED KWKRGEDGAR KLVQRLIDYP 190 ERTFQTHNVM IFM

References

[1]

"The molecular analysis of an NAH7-type gene cluster, pah, located on the chromosome of Pseudomonas aeruginosa PaK1." Takizawa N., Iida T., Yamauchi K., Satoh S., Wang Y., Fukuda M., Kiyohara H. Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: PaK1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D84146 Genomic DNA. Translation: BAA12241.1.
3D structure databases
HSSP	HSSP built from PDB template 1O7G based on UniProtKB P23095.
SMR	Q51495. Positions 2-193.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.14.12.12. 354.
Family and domain databases
InterPro	IPR000391. Rng_hydr_dOase-bsu. [Graphical view]
Pfam	PF00866. Ring_hydroxyl_B. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NDOC_PSEAE

Accession

Primary (citable) accession number: Q51495

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	March 3, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)