NDOC_PSEU8
ID NDOC_PSEU8 Reviewed; 194 AA.
AC P0A113; P23095; Q52125;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Naphthalene 1,2-dioxygenase system, small oxygenase component {ECO:0000250|UniProtKB:P0A112};
DE AltName: Full=ISP NAP {ECO:0000250|UniProtKB:P0A112};
DE AltName: Full=Naphthalene 1,2-dioxygenase ISP beta {ECO:0000303|PubMed:8226631};
DE AltName: Full=Naphthalene 1,2-dioxygenase subunit beta {ECO:0000250|UniProtKB:P0A112};
DE Short=ND subunit beta {ECO:0000250|UniProtKB:P0A112};
DE Short=NDO subunit beta {ECO:0000250|UniProtKB:P0A112};
GN Name=doxD {ECO:0000303|PubMed:8226631};
OS Pseudomonas sp. (strain C18).
OG Plasmid unnamed.
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=69011;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, PATHWAY,
RP AND SUBUNIT.
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 (1.50 ANGSTROMS), AND SUBUNIT.
RX PubMed=16980501; DOI=10.1128/jb.00707-06;
RA Ferraro D.J., Okerlund A.L., Mowers J.C., Ramaswamy S.;
RT "Structural basis for regioselectivity and stereoselectivity of product
RT formation by naphthalene 1,2-dioxygenase.";
RL J. Bacteriol. 188:6986-6994(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS), AND SUBUNIT.
RA Ferraro D.J., Ramaswamy S.;
RT "Naphthalene 1,2-Dioxygenase bound to thioanisole.";
RL Submitted (OCT-2012) to the PDB data bank.
CC -!- FUNCTION: Component of the naphthalene dioxygenase (NDO) multicomponent
CC enzyme system which catalyzes the incorporation of both atoms of
CC molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2-
CC dihydronaphthalene. The beta subunit seems to have a structural role in
CC the holoenzyme. {ECO:0000269|PubMed:8226631}.
CC -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC {ECO:0000305|PubMed:8226631}.
CC -!- SUBUNIT: The naphthalene dioxygenase (NDO) multicomponent enzyme system
CC is composed of an electron transfer component and a dioxygenase
CC component (iron sulfur protein (ISP)). The electron transfer component
CC is composed of a ferredoxin reductase and a ferredoxin (DoxA), and the
CC dioxygenase component is formed of a heterohexamer (trimer of
CC heterodimers) of three large alpha subunits (DoxB) and three small beta
CC subunits (DoxD). {ECO:0000269|PubMed:16980501,
CC ECO:0000305|PubMed:8226631, ECO:0000305|Ref.3}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to degrade
CC naphthalene. {ECO:0000269|PubMed:8226631}.
CC -!- MISCELLANEOUS: Encoded on an unnamed 75 kb plasmid.
CC {ECO:0000305|PubMed:8226631}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC beta subunit family. {ECO:0000305}.
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DR EMBL; M60405; AAA16127.1; -; Genomic_DNA.
DR PIR; S27634; S27634.
DR PDB; 2HMJ; X-ray; 1.50 A; B=1-194.
DR PDB; 2HMK; X-ray; 1.65 A; B=1-194.
DR PDB; 2HML; X-ray; 1.80 A; B=1-194.
DR PDB; 2HMM; X-ray; 1.60 A; B=1-194.
DR PDB; 2HMN; X-ray; 1.70 A; B=1-194.
DR PDB; 2HMO; X-ray; 1.60 A; B=1-194.
DR PDB; 4HJL; X-ray; 1.50 A; B=3-194.
DR PDB; 4HKV; X-ray; 1.65 A; B=1-194.
DR PDB; 4HM0; X-ray; 1.80 A; B=1-194.
DR PDB; 4HM1; X-ray; 1.50 A; B=1-194.
DR PDB; 4HM2; X-ray; 1.60 A; B=1-194.
DR PDB; 4HM3; X-ray; 1.50 A; B=1-194.
DR PDB; 4HM4; X-ray; 1.50 A; B=1-194.
DR PDB; 4HM5; X-ray; 1.50 A; B=1-194.
DR PDB; 4HM6; X-ray; 1.50 A; B=1-194.
DR PDB; 4HM7; X-ray; 1.50 A; B=1-194.
DR PDB; 4HM8; X-ray; 1.30 A; B=1-194.
DR PDBsum; 2HMJ; -.
DR PDBsum; 2HMK; -.
DR PDBsum; 2HML; -.
DR PDBsum; 2HMM; -.
DR PDBsum; 2HMN; -.
DR PDBsum; 2HMO; -.
DR PDBsum; 4HJL; -.
DR PDBsum; 4HKV; -.
DR PDBsum; 4HM0; -.
DR PDBsum; 4HM1; -.
DR PDBsum; 4HM2; -.
DR PDBsum; 4HM3; -.
DR PDBsum; 4HM4; -.
DR PDBsum; 4HM5; -.
DR PDBsum; 4HM6; -.
DR PDBsum; 4HM7; -.
DR PDBsum; 4HM8; -.
DR AlphaFoldDB; P0A113; -.
DR SMR; P0A113; -.
DR UniPathway; UPA00082; -.
DR EvolutionaryTrace; P0A113; -.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR CDD; cd00667; ring_hydroxylating_dioxygenases_beta; 1.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR000391; Rng_hydr_dOase-bsu.
DR Pfam; PF00866; Ring_hydroxyl_B; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase;
KW Oxidoreductase; Plasmid.
FT CHAIN 1..194
FT /note="Naphthalene 1,2-dioxygenase system, small oxygenase
FT component"
FT /id="PRO_0000085073"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:4HM8"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:4HM8"
FT HELIX 28..46
FT /evidence="ECO:0007829|PDB:4HM8"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:4HM8"
FT STRAND 58..69
FT /evidence="ECO:0007829|PDB:4HM8"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:4HM8"
FT HELIX 92..103
FT /evidence="ECO:0007829|PDB:4HM8"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:4HM8"
FT STRAND 115..127
FT /evidence="ECO:0007829|PDB:4HM8"
FT STRAND 134..147
FT /evidence="ECO:0007829|PDB:4HM8"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:4HM8"
FT STRAND 151..165
FT /evidence="ECO:0007829|PDB:4HM8"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:4HM8"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:4HM8"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:4HM8"
SQ SEQUENCE 194 AA; 22935 MW; 168D2E1535E66416 CRC64;
MMINIQEDKL VSAHDAEEIL RFFNCHDSAL QQEATTLLTQ EAHLLDIQAY RAWLEHCVGS
EVQYQVISRE LRAASERRYK LNEAMNVYNE NFQQLKVRVE HQLDPQNWGN SPKLRFTRFI
TNVQAAMDVN DKELLHIRSN VILHRARRGN QVDVFYAARE DKWKRGEGGV RKLVQRFVDY
PERILQTHNL MVFL
