NDOB_PSEFL
ID NDOB_PSEFL Reviewed; 449 AA.
AC O07824;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Naphthalene 1,2-dioxygenase system, large oxygenase component {ECO:0000250|UniProtKB:P0A110};
DE EC=1.14.12.12 {ECO:0000250|UniProtKB:P0A110};
DE AltName: Full=ISP NAP {ECO:0000250|UniProtKB:P0A110};
DE AltName: Full=Naphthalene 1,2-dioxygenase ISP alpha {ECO:0000250|UniProtKB:P0A110};
DE AltName: Full=Naphthalene 1,2-dioxygenase subunit alpha {ECO:0000250|UniProtKB:P0A110};
DE Short=ND subunit alpha {ECO:0000250|UniProtKB:P0A110};
DE Short=NDO subunit alpha {ECO:0000250|UniProtKB:P0A110};
GN Name=ndoB {ECO:0000250|UniProtKB:P0A110}; Synonyms=ndoC2;
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. The alpha subunit has a catalytic role in the
CC holoenzyme. {ECO:0000250|UniProtKB:P0A110}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + naphthalene + O2 = (1R,2S)-1,2-
CC dihydronaphthalene-1,2-diol + NAD(+); Xref=Rhea:RHEA:19173,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16482,
CC ChEBI:CHEBI:44343, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.14.12.12; Evidence={ECO:0000250|UniProtKB:P0A110};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:P0A110,
CC ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P0A110, ECO:0000255|PROSITE-ProRule:PRU00628};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P0A110};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:P0A110};
CC -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC {ECO:0000250|UniProtKB:P0A110}.
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:P0A110}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000305}.
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DR EMBL; AF004283; AAB61370.1; -; Genomic_DNA.
DR UniPathway; UPA00082; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0018625; F:naphthalene 1,2-dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08881; RHO_alpha_C_NDO-like; 1.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR043266; RHO_NdoB-like_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756; PTHR43756; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase; Plasmid.
FT CHAIN 1..449
FT /note="Naphthalene 1,2-dioxygenase system, large oxygenase
FT component"
FT /id="PRO_0000085055"
FT DOMAIN 39..137
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 81
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 83
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 101
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 104
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 208
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
FT BINDING 362
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
SQ SEQUENCE 449 AA; 49514 MW; 186A7924AD437A1C CRC64;
MNYKNKILVS ESGLTQKHLI HGDEELFQHE LRTIXARNWL FLTHDSLIPS PGDYVTAKMG
IDEVIVSRQS DGSIRAFLNV CRHRGKTLVN AEAGNAKGFV CSYHGWGFGS NGELQSVPFE
KELYGESLNK KCLGLKEVAR VESFHGFIYG CFDQEAPSLM DYLGDAAWYL EPIFKHSGGL
ELVGPPGKVV IKANWKAPAE NFVGDAYHVG WTHASSLRTG ESIFSSLAGN AVLPPEGAGL
QMTSKYGSGM GVLWDGYSGV HSADLVPELM AFGGAKQERL NKEIGDVPAR IYRSHLNCTV
FPNNSVLTCS GVFKVWNPID ANTTEVWTYA IVEKDMPEDL KRRLADAVQR TFGPAGFWES
DDNDNMETAS QNGKKYQSRD SDLISNLGFG KDVYGDAVYP GVVGKSAIGE TSYRGFYRAY
QAHVSSSNWA EFEDASSTWH TELTKTTDR
