ID   NAHC2_PSEPU             Reviewed;         302 AA.
AC   P0A109; Q57145;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=1,2-dihydroxynaphthalene dioxygenase;
DE            Short=1,2-DHN dioxygenase;
DE            Short=DHNDO;
DE            EC=1.13.11.56;
DE   AltName: Full=1,2-dihydroxynaphthalene oxygenase;
GN   Name=nahC;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OG   Plasmid NPL1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BS202;
RA   Bezborodnikov S.G., Boronin A.M., Tiedje J.M.;
RT   "Nucleotide sequences of genes encoding an upper pathway of naphthalene
RT   metabolism of NPL1 plasmid from Pseudomonas putida strain BS202.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the naphthalene catabolic pathway. Catalyzes the
CC       meta-cleavage of 1,2-dihydroxynaphthalene (1,2-DHN) to yield 2-
CC       hydroxychromene-2-carboxylic acid (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=naphthalene-1,2-diol + O2 = 2-hydroxychromene-2-carboxylate +
CC         H(+); Xref=Rhea:RHEA:27310, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17435, ChEBI:CHEBI:59350; EC=1.13.11.56;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC   -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC   -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; AF010471; AAB62711.1; -; Genomic_DNA.
DR   RefSeq; NP_863076.1; NC_004999.1.
DR   RefSeq; WP_011117404.1; NC_004999.1.
DR   AlphaFoldDB; P0A109; -.
DR   SMR; P0A109; -.
DR   UniPathway; UPA00082; -.
DR   GO; GO:0018554; F:1,2-dihydroxynaphthalene dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; ISS:UniProtKB.
DR   GO; GO:1901170; P:naphthalene catabolic process; ISS:UniProtKB.
DR   Gene3D; 3.10.180.10; -; 2.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR   InterPro; IPR037523; VOC.
DR   InterPro; IPR000486; Xdiol_ring_cleave_dOase_1/2.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   SUPFAM; SSF54593; SSF54593; 1.
DR   PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1.
DR   PROSITE; PS51819; VOC; 2.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Metal-binding;
KW   Oxidoreductase; Plasmid; Repeat.
FT   CHAIN           1..302
FT                   /note="1,2-dihydroxynaphthalene dioxygenase"
FT                   /id="PRO_0000085022"
FT   DOMAIN          9..124
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          149..270
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         152
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         199..200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   302 AA;  33942 MW;  C2A3DAECFB6FB833 CRC64;
     MSKQAAVIEL GYMGISVKDP DAWKSFATDM LGLQVLDEGE KDRFYLRMDY WHHRIVVHHN
     GQDDLEYLGW RVAGKPEFEA LGQKLIDAGY KIRICDKVEA QERMVLGLMK TEDPGGNPTE
     IFWGPRIDMS NPFHPGRPLH GKFVTGDQGL GHCIVRQTDV AEAHKFYSLL GFRGDVEYRI
     PLPNGMTAEL SFMHCNARDH SIAFGAMPAA KRLNHLMLEY THMEDLGYTH QQFVKNEIDI
     ALQLGIHAND KALTFYGATP SGWLIEPGWR GATAIDEAEY YVGDIFGHGV EATGYGLDVK
     LS