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-MAR-2009, entry version 28.
DE   RecName: Full=Naphthalene 1,2-dioxygenase subunit beta;
DE            EC=1.14.12.12;
DE   AltName: Full=Naphthalene 1,2-dioxygenase ISP beta;
GN   Name=doxD;
OS   Pseudomonas sp. (strain C18).
OG   Plasmid.
OC   Bacteria; Proteobacteria.
OX   NCBI_TaxID=69011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=94042852; PubMed=8226631;
RA   Denome S.A., Stanley D.C., Olson E.S., Young K.D.;
RT   "Metabolism of dibenzothiophene and naphthalene in Pseudomonas
RT   strains: complete DNA sequence of an upper naphthalene catabolic
RT   pathway.";
RL   J. Bacteriol. 175:6890-6901(1993).
CC   -!- FUNCTION: Component of the naphthalene dioxygenase (NDO)
CC       multicomponent enzyme system which catalyzes the incorporation of
CC       both atoms of molecular oxygen into naphthalene to form cis-
CC       naphthalene dihydrodiol. The beta subunit may be responsible for
CC       the substrate specificity of the enzyme.
CC   -!- CATALYTIC ACTIVITY: Naphthalene + NADH + O(2) = (1R,2S)-1,2-
CC       dihydronaphthalene-1,2-diol + NAD(+).
CC   -!- COFACTOR: Binds 1 2Fe-2S cluster (By similarity).
CC   -!- COFACTOR: Binds 1 iron ion (By similarity).
CC   -!- PATHWAY: Aromatic compound metabolism; naphtalene degradation.
CC   -!- SUBUNIT: Naphthalene dioxygenase (NDO) multicomponent enzyme
CC       system is composed of an electron transfer component and an iron
CC       sulfur protein (ISP). The electron transfer component is composed
CC       of ferredoxin reductase and ferredoxin (doxA), and ISP is composed
CC       of a large alpha subunit (doxB) and a small beta subunit (doxD)
CC       (Probable).
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating
CC       dioxygenase beta subunit family.
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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   PDBsum; 2HMJ; -.
DR   PDBsum; 2HMK; -.
DR   PDBsum; 2HML; -.
DR   PDBsum; 2HMM; -.
DR   PDBsum; 2HMN; -.
DR   PDBsum; 2HMO; -.
DR   GO; GO:0018625; F:naphthalene 1,2-dioxygenase activity; IEA:EC.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000391; Rng_hydr_dOase-bsu.
DR   Pfam; PF00866; Ring_hydroxyl_B; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase; NAD;
KW   Oxidoreductase; Plasmid.
FT   CHAIN         1    194       Naphthalene 1,2-dioxygenase subunit beta.
FT                                /FTId=PRO_0000085073.
FT   TURN          5      7
FT   HELIX        13     24
FT   HELIX        28     46
FT   HELIX        50     57
FT   STRAND       58     69
FT   STRAND       84     90
FT   HELIX        92    103
FT   HELIX       108    110
FT   STRAND      115    127
FT   STRAND      134    147
FT   TURN        148    150
FT   STRAND      151    165
FT   HELIX       167    169
FT   STRAND      171    179
FT   STRAND      183    185
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
//