ID   NDOC_RALSP              Reviewed;         194 AA.
AC   O52383;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Naphthalene 1,2-dioxygenase system, small oxygenase component {ECO:0000303|PubMed:11872705};
DE   AltName: Full=ISP NAP {ECO:0000250|UniProtKB:P0A112};
DE   AltName: Full=Naphthalene 1,2-dioxygenase ISP beta {ECO:0000250|UniProtKB:P0A112};
DE   AltName: Full=Naphthalene 1,2-dioxygenase subunit beta {ECO:0000303|PubMed:11872705};
DE            Short=ND subunit beta {ECO:0000250|UniProtKB:P0A112};
DE            Short=NDO subunit betaa {ECO:0000303|PubMed:11872705};
GN   Name=nagAd {ECO:0000303|PubMed:9573207};
OS   Ralstonia sp.
OG   Plasmid pWWU2 {ECO:0000312|EMBL:AAD12611.1}.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=54061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC   STRAIN=U2;
RX   PubMed=9573207; DOI=10.1128/jb.180.9.2522-2530.1998;
RA   Fuenmayor S.L., Wild M., Boyes A.L., Williams P.A.;
RT   "A gene cluster encoding steps in conversion of naphthalene to gentisate in
RT   Pseudomonas sp. strain U2.";
RL   J. Bacteriol. 180:2522-2530(1998).
RN   [2]
RP   FUNCTION, PATHWAY, SUBUNIT, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=U2;
RX   PubMed=11872705; DOI=10.1128/jb.184.6.1547-1555.2002;
RA   Zhou N.Y., Al-Dulayymi J., Baird M.S., Williams P.A.;
RT   "Salicylate 5-hydroxylase from Ralstonia sp. strain U2: a monooxygenase
RT   with close relationships to and shared electron transport proteins with
RT   naphthalene dioxygenase.";
RL   J. Bacteriol. 184:1547-1555(2002).
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 (PubMed:9573207, PubMed:11872705). Also able to use
CC       styrene as substrate (PubMed:11872705). The beta subunit seems to have
CC       a structural role in the holoenzyme. {ECO:0000269|PubMed:11872705,
CC       ECO:0000269|PubMed:9573207}.
CC   -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC       {ECO:0000305|PubMed:11872705}.
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 (NagAa) and a ferredoxin (NagAb),
CC       and the dioxygenase component is formed by a large alpha subunit
CC       (NagAc) and a small beta subunit (NagAd). {ECO:0000269|PubMed:11872705,
CC       ECO:0000269|PubMed:9573207}.
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       beta subunit family. {ECO:0000305}.
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DR   EMBL; AF036940; AAD12611.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52383; -.
DR   SMR; O52383; -.
DR   UniPathway; UPA00082; -.
DR   GO; GO:1902494; C:catalytic complex; IDA:UniProtKB.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:1901170; P:naphthalene catabolic process; IGI:UniProtKB.
DR   CDD; cd00667; ring_hydroxylating_dioxygenases_beta; 1.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR000391; Rng_hydr_dOase-bsu.
DR   PANTHER; PTHR41534; PTHR41534; 1.
DR   Pfam; PF00866; Ring_hydroxyl_B; 1.
DR   SUPFAM; SSF54427; SSF54427; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Oxidoreductase; Plasmid.
FT   CHAIN           1..194
FT                   /note="Naphthalene 1,2-dioxygenase system, small oxygenase
FT                   component"
FT                   /id="PRO_0000421812"
SQ   SEQUENCE   194 AA;  23014 MW;  FF8715F9D20D5FBC CRC64;
     MMINTQEDKL VSAHDAEEFH RFFVGHDSDL QQEVTTLLTR EAHLLDIQAY NAWLEHCVAP
     EIKYQVISRE FRSTSERRYQ LNDAVNIYNE NYQHLKVRVE HQMDPQNWAN SPKIRFTRFV
     TNVTAAKDKI VPDLLHVRSN LILHRARRGN QVDVFYATRE DKWKRIEGGG IQLVERLVDY
     PERILQTHNL MTFL