NDOB_PSEAI
ID NDOB_PSEAI Reviewed; 449 AA.
AC Q51494;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=pahA3;
OS Pseudomonas aeruginosa.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PaK1;
RA Takizawa N., Iida T., Yamauchi K., Satoh S., Wang Y., Fukuda M.,
RA Kiyohara H.;
RT "The molecular analysis of an NAH7-type gene cluster, pah, located on the
RT chromosome of Pseudomonas aeruginosa PaK1.";
RL Submitted (APR-1996) 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; D84146; BAA12240.1; -; Genomic_DNA.
DR AlphaFoldDB; Q51494; -.
DR SMR; Q51494; -.
DR PRIDE; Q51494; -.
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.
FT CHAIN 1..449
FT /note="Naphthalene 1,2-dioxygenase system, large oxygenase
FT component"
FT /id="PRO_0000085052"
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; 49716 MW; 35A189136722A21C CRC64;
MNYKNKNLVS ESGLTQKHLI HGDEELFQRE LETIFARNWL FLTHDSLIPS PGDYVTAKMG
VDEVIVSRQN DGSIRAFLNV CRHRGKTLVH AEAGNAKGFV CSYHGWGFGA NGELQSVPFE
KELYGEALDK KCMGLKEVAR VESFHGFIYG CFDEEAPSLK DYMGDAGWYL EPMFKHSGGL
ELIGPPGKVI IKANWKAPAE NFTGDAYHVG WTHASSLRSG QSVFSSLAGN AALPPEGAGL
QMTSKYGSGM GVLWDGYSGV HSADLVPELM AFGGAKQERL NKEIGEVRAR IYRSHLNCTV
FPNNSFLTCS GVFKVWHPID ANTTEVWTYA MVEKDMPEDL KRRLVDAVQR TFGPAGFWES
DDNDNMETVS QNAKKYQSRD GDLVSNLGFG GDVYGDEVYP GIVGKSAIGE TSYRGFYRAY
GAHISSSSWA EFEDVSKNWH TELAKTTDR
