ID   NDOA_PSEFL              Reviewed;          87 AA.
AC   O07823;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Naphthalene 1,2-dioxygenase system, ferredoxin component {ECO:0000250|UniProtKB:P0A185};
DE   Flags: Fragment;
GN   Name=ndoA {ECO:0000250|UniProtKB:P0A185}; Synonyms=ndoC1;
OS   Pseudomonas fluorescens.
OG   Plasmid.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 17483 / DSM 6506 / JCM 6159 / NCIMB 10529 / Stanier 109;
RA   Hamann C.;
RT   "Naphthalene dioxygenase genes from Pseudomonas fluorescens.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
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) (NdoB and NdoC). {ECO:0000250|UniProtKB:P0A185}.
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:0000250|UniProtKB:P0A185}.
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 (NdoR) and a ferredoxin (NdoA),
CC       and the dioxygenase component is formed of a heterohexamer (trimer of
CC       heterodimers) of three large alpha subunits (NdoB) and three small beta
CC       subunits (NdoC). {ECO:0000250|UniProtKB:P0A185}.
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       ferredoxin component family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF004283; AAB61369.1; -; Genomic_DNA.
DR   AlphaFoldDB; O07823; -.
DR   SMR; O07823; -.
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   3: Inferred from homology;
KW   2Fe-2S; Aromatic hydrocarbons catabolism; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Plasmid; Transport.
FT   CHAIN           <1..87
FT                   /note="Naphthalene 1,2-dioxygenase system, ferredoxin
FT                   component"
FT                   /id="PRO_0000201692"
FT   DOMAIN          <1..84
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         28
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         30
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         50
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P0A185,
FT                   ECO:0000255|PROSITE-ProRule:PRU00628"
FT   NON_TER         1
SQ   SEQUENCE   87 AA;  9563 MW;  A7E38926584624E5 CRC64;
     DVLGVTVEGK DLALYEVEGE IYATDDLCTH GAARMSDGYL EGREIECPLH QGRFDVCTGR
     ALCAPVTENI KTYAVKIENL RVMIDLS