NAHC_PSEU8
ID NAHC_PSEU8 Reviewed; 302 AA.
AC P0A108; Q57145;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 52.
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=doxG;
OS Pseudomonas sp. (strain C18).
OG Plasmid unnamed.
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=69011;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C18; PLASMID=unnamed;
RX PubMed=8226631; DOI=10.1128/jb.175.21.6890-6901.1993;
RA Denome S.A., Stanley D.C., Olson E.S., Young K.D.;
RT "Metabolism of dibenzothiophene and naphthalene in Pseudomonas strains:
RT complete DNA sequence of an upper naphthalene catabolic pathway.";
RL J. Bacteriol. 175:6890-6901(1993).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1-302 IN COMPLEX WITH SUBSTRATE
RP ANALOGS AND IRON ION, AND COFACTOR.
RA Neau D.B., Kelker M.S., Maaroufi H., Colbert C.L., Eltis L.D., Bolin J.T.;
RT "Structural explanation for success and failure in the enzymatic ring-
RT cleavage of 3,4 dihydroxybiphenyl and related PCB metabolites.";
RL Submitted (MAR-2007) to the PDB data bank.
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:0000269|Ref.2};
CC -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC -!- MISCELLANEOUS: Encoded on an unnamed 75 kb plasmid.
CC {ECO:0000305|PubMed:8226631}.
CC -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; M60405; AAA16130.1; -; Genomic_DNA.
DR PDB; 2EHZ; X-ray; 1.35 A; A=1-302.
DR PDB; 2EI0; X-ray; 1.60 A; A=1-302.
DR PDB; 2EI1; X-ray; 1.52 A; A=1-302.
DR PDB; 2EI2; X-ray; 1.69 A; A=1-302.
DR PDB; 2EI3; X-ray; 1.90 A; A=1-302.
DR PDBsum; 2EHZ; -.
DR PDBsum; 2EI0; -.
DR PDBsum; 2EI1; -.
DR PDBsum; 2EI2; -.
DR PDBsum; 2EI3; -.
DR AlphaFoldDB; P0A108; -.
DR SMR; P0A108; -.
DR DrugBank; DB07610; 1,2-Dihydroxynaphthalene.
DR DrugBank; DB07478; 3,4-Biphenyldiol.
DR DrugBank; DB02923; Biphenyl-2,3-Diol.
DR UniPathway; UPA00082; -.
DR EvolutionaryTrace; P0A108; -.
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 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase; Iron;
KW Metal-binding; Oxidoreductase; Plasmid; Repeat.
FT CHAIN 1..302
FT /note="1,2-dihydroxynaphthalene dioxygenase"
FT /id="PRO_0000085023"
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 BINDING 152
FT /ligand="substrate"
FT BINDING 199..200
FT /ligand="substrate"
FT BINDING 215
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 215
FT /ligand="substrate"
FT BINDING 256
FT /ligand="substrate"
FT BINDING 266
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:2EHZ"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:2EHZ"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:2EHZ"
FT STRAND 41..52
FT /evidence="ECO:0007829|PDB:2EHZ"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:2EHZ"
FT STRAND 63..74
FT /evidence="ECO:0007829|PDB:2EHZ"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:2EHZ"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:2EHZ"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:2EHZ"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:2EHZ"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:2EHZ"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:2EHZ"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:2EHZ"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:2EHZ"
FT STRAND 187..199
FT /evidence="ECO:0007829|PDB:2EHZ"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:2EHZ"
FT STRAND 210..222
FT /evidence="ECO:0007829|PDB:2EHZ"
FT HELIX 223..235
FT /evidence="ECO:0007829|PDB:2EHZ"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:2EHZ"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:2EHZ"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:2EHZ"
FT STRAND 262..269
FT /evidence="ECO:0007829|PDB:2EHZ"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:2EHZ"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:2EHZ"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:2EHZ"
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
