UniProt functional annotation for P0A110

UniProt code: P0A110.

Organism: Pseudomonas putida (Arthrobacter siderocapsulatus).
Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.
 
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-(1R,2S)-dihydroxy-1,2- dihydronaphthalene. The alpha subunit has a catalytic role in the holoenzyme. Also able to catalyze the cis-dihydroxylation of biphenyl and phenanthrene (PubMed:10692370). {ECO:0000269|PubMed:10692370, ECO:0000269|PubMed:6874638}.
 
Catalytic activity: Reaction=H(+) + NADH + naphthalene + O2 = (1R,2S)-1,2- dihydronaphthalene-1,2-diol + NAD(+); Xref=Rhea:RHEA:19173, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16482, ChEBI:CHEBI:44343, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.12.12; Evidence={ECO:0000269|PubMed:10692370, ECO:0000269|PubMed:6874638};
Cofactor: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; Evidence={ECO:0000269|PubMed:10669618, ECO:0000269|PubMed:12586937, ECO:0000269|PubMed:15942729, ECO:0000269|PubMed:6874638, ECO:0000269|PubMed:9634695}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:10669618, ECO:0000269|PubMed:12586937, ECO:0000269|PubMed:15942729, ECO:0000269|PubMed:6874638, ECO:0000269|PubMed:9634695};
Cofactor: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:10669618, ECO:0000269|PubMed:12586937, ECO:0000269|PubMed:15942729, ECO:0000269|PubMed:9634695}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:10669618, ECO:0000269|PubMed:12586937, ECO:0000269|PubMed:15942729, ECO:0000269|PubMed:9634695};
Pathway: Aromatic compound metabolism; naphthalene degradation. {ECO:0000305|PubMed:10692370}.
Subunit: The naphthalene dioxygenase (NDO) multicomponent enzyme system is composed of an electron transfer component and a dioxygenase component (iron sulfur protein (ISP)). The electron transfer component is composed of a ferredoxin reductase (NdoR) and a ferredoxin (NdoA), and the dioxygenase component is formed of a heterohexamer (trimer of heterodimers) of three large alpha subunits (NdoB) and three small beta subunits (NdoC). {ECO:0000269|PubMed:12586937, ECO:0000269|PubMed:15942729, ECO:0000269|PubMed:9634695, ECO:0000305|PubMed:6874638}.
Similarity: Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.