ID   NAHC1_PSEPU             Reviewed;         302 AA.
AC   P11861;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 93.
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 NAH7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 17485 / DSM 50208 / JCM 6158 / NCIMB 12092 / Stanier 111 /
RC   Biotype A;
RX   PubMed=2670937; DOI=10.1016/s0021-9258(19)84830-5;
RA   Harayama S., Rekik M.;
RT   "Bacterial aromatic ring-cleavage enzymes are classified into two different
RT   gene families.";
RL   J. Biol. Chem. 264:15328-15333(1989).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP   SPECIFICITY, COFACTOR, AND ACTIVITY REGULATION.
RC   STRAIN=DSM 8368 / NCIMB 9816 / PG;
RX   PubMed=7204331; DOI=10.1128/jb.143.2.668-673.1980;
RA   Patel T.R., Barnsley E.A.;
RT   "Naphthalene metabolism by pseudomonads: purification and properties of
RT   1,2-dihydroxynaphthalene oxygenase.";
RL   J. Bacteriol. 143:668-673(1980).
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. Can also cleave 3-methylcatechol and
CC       4-methylcatechol. {ECO:0000269|PubMed:7204331}.
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         Evidence={ECO:0000269|PubMed:7204331};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:7204331};
CC   -!- ACTIVITY REGULATION: Inhibited by bathophenanthroline sulfonate, o-
CC       phenanthroline, 8-hydroxyquinoline, 2,2'-dipyridyl and p-
CC       chlormercuribenzoate. Also inhibited by Hg(2+), Cu(2+), Co(2+) and
CC       Fe(3+) ions. {ECO:0000269|PubMed:7204331}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.15 mM for 3-methylcatechol (at pH 5.5)
CC         {ECO:0000269|PubMed:7204331};
CC         KM=0.28 mM for 1,2-DHN (at pH 5.5) {ECO:0000269|PubMed:7204331};
CC       pH dependence:
CC         Optimum pH is 6.5. {ECO:0000269|PubMed:7204331};
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; J04994; AAA91577.1; -; Genomic_DNA.
DR   PIR; A34343; A34343.
DR   RefSeq; WP_011475381.1; NC_007926.1.
DR   RefSeq; YP_534826.1; NC_007926.1.
DR   AlphaFoldDB; P11861; -.
DR   SMR; P11861; -.
DR   KEGG; ag:AAA91577; -.
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; IDA:UniProtKB.
DR   GO; GO:1901170; P:naphthalene catabolic process; IDA: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   1: Evidence at protein level;
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_0000085021"
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;  33883 MW;  D05D7457842AC40D CRC64;
     MSKQAAVIEL GYMGISVKDP DAWKSFAMNM LGLQVLDEGE KDRFYLRMDY WHHRIVVHHS
     AEDDLEYLGW RVAGKPEFEA LGQKLIDAGY KIRVCDKVEA QERMVLGLMK TEDPGGNPTE
     IFWGPRIDMS NPFHPGRPLH GKFVTGDQGL GHCIVRQTDV AAAHKFYSLL GFRGDVEYRI
     PLPNGMTAEL SFMHCNARDH SIAFGAMPAA KRLNHLMLEY THMEDLGYTH QQFVKNEIDI
     ALQLGIHAND KALTFYGATP SGWLIEPGWR GATAIDEAEY YVGDIFGHGV EAPGYGLDVK
     LS