NDOB_RALSP
ID NDOB_RALSP Reviewed; 447 AA.
AC O52382;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Naphthalene 1,2-dioxygenase system, large oxygenase component {ECO:0000303|PubMed:11872705};
DE EC=1.14.12.12 {ECO:0000269|PubMed:11872705};
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:0000303|PubMed:11872705};
DE Short=ND subunit alpha {ECO:0000250|UniProtKB:P0A110};
DE Short=NDO subunit alpha {ECO:0000303|PubMed:11872705};
GN Name=nagAc {ECO:0000303|PubMed:9573207};
OS Ralstonia sp.
OG Plasmid pWWU2 {ECO:0000312|EMBL:AAD12610.1}.
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, CATALYTIC ACTIVITY, 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). The alpha subunit
CC has a catalytic role in the holoenzyme. Also able to use styrene as
CC substrate (PubMed:11872705). {ECO:0000269|PubMed:11872705,
CC ECO:0000269|PubMed:9573207}.
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:0000269|PubMed:11872705};
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: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 alpha subunit family. {ECO:0000305}.
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DR EMBL; AF036940; AAD12610.1; -; Genomic_DNA.
DR AlphaFoldDB; O52382; -.
DR SMR; O52382; -.
DR UniPathway; UPA00082; -.
DR GO; GO:1902494; C:catalytic complex; IDA:UniProtKB.
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; IEA:UniProtKB-EC.
DR GO; GO:1901170; P:naphthalene catabolic process; IGI:UniProtKB.
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 1: Evidence at protein level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase; Plasmid.
FT CHAIN 1..447
FT /note="Naphthalene 1,2-dioxygenase system, large oxygenase
FT component"
FT /id="PRO_0000421811"
FT DOMAIN 37..135
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 79
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 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 99
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 102
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 206
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
FT BINDING 211
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
FT BINDING 360
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
SQ SEQUENCE 447 AA; 49571 MW; 4553AAF4B4410ED0 CRC64;
MIYENLVSEA GLTQKHLIHG DKELFQHELK TIFARNWLFL THDSLIPSPG DYVTAKMGVD
EVIVSRQNDG SVRAFLNVCR HRGKTLVHAE AGNAKGFVCS YHGWGFGSNG ELQSVPFEKE
LYGDTIKKKC LGLKEVPRIE SFHGFIYGCF DAEAPTLVDY LGDAAWYLEP IFKHSGGLEL
VGPPGKVVIK ANWKAPAENF VGDAYHVGWT HASSLRSGQS IFTPLAGNAM LPPEGAGLQM
TSKYGSGMGV LWDGYSGVHS ADLVPEMMAF GGAKQEKLAK EIGDVRARIY RSHLNCTVFP
NNSILTCSGV FKVWNPIDEN TTEVWTYAIV EKDMPEDLKR RLADAVQRTF GPAGFWESDD
NDNMETESQN AKKYQSSNSD LIANLGFGKD VYGDECYPGV VAKSAIGETS YRGFYRAYQA
HISSSNWAEF ENTSRNWHTE LTKTTDR
