ID   NDOA_PSEU8              Reviewed;         104 AA.
AC   P0A186; O07829; P23082; Q52123;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Naphthalene 1,2-dioxygenase system, ferredoxin component {ECO:0000303|PubMed:8226631};
GN   Name=doxA {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, PATHWAY, 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).
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. Functions as an intermediate electron transfer
CC       protein via a specific interaction with iron sulfur protein components
CC       (ISP) (DoxB and DoxD). {ECO:0000305|PubMed:8226631}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000250|UniProtKB:P0A185,
CC         ECO:0000255|PROSITE-ProRule:PRU00628};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.
CC       {ECO:0000250|UniProtKB:P0A185, ECO:0000255|PROSITE-ProRule:PRU00628};
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:0000305|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       ferredoxin component family. {ECO:0000305}.
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DR   EMBL; M60405; AAA16124.1; -; Genomic_DNA.
DR   PIR; S27631; S27631.
DR   AlphaFoldDB; P0A186; -.
DR   SMR; P0A186; -.
DR   UniPathway; UPA00082; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; ISS:UniProtKB.
DR   Gene3D; 2.102.10.10; -; 1.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   Pfam; PF00355; Rieske; 1.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; Aromatic hydrocarbons catabolism; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Plasmid; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P0A185"
FT   CHAIN           2..104
FT                   /note="Naphthalene 1,2-dioxygenase system, ferredoxin
FT                   component"
FT                   /id="PRO_0000201694"
FT   DOMAIN          6..101
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         45
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P0A185,
FT                   ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         47
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P0A185,
FT                   ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         64
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P0A185,
FT                   ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         67
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P0A185,
FT                   ECO:0000255|PROSITE-ProRule:PRU00628"
SQ   SEQUENCE   104 AA;  11446 MW;  475625DCC3EDCD41 CRC64;
     MTVKWIEAVA LSDILEGDVL GVTVEGKELA LYEVEGEIYA TDNLCTHGSA RMSDGYLEGR
     EIECPLHQGR FDVCTGKALC APVTQNIKTY PVKIENLRVM IDLS