NAGAA_RALSP
ID NAGAA_RALSP Reviewed; 328 AA.
AC O52378;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Naphthalene 1,2-dioxygenase/salicylate 5-hydroxylase systems, ferredoxin--NAD(P)(+), reductase component {ECO:0000303|PubMed:11872705};
DE Short=NDO/S5H systems, ferredoxin--NAD(P)(+), reductase component {ECO:0000303|PubMed:11872705};
DE EC=1.18.1.7 {ECO:0000269|PubMed:11872705};
DE AltName: Full=Ferredoxin reductase NagAa {ECO:0000303|PubMed:9573207};
DE AltName: Full=Ferredoxin--NAD(P)(+) reductase (naphthalene dioxygenase/salicylate 5-hydroxylase ferredoxin-specific) {ECO:0000303|PubMed:9573207};
GN Name=nagAa {ECO:0000303|PubMed:9573207};
OS Ralstonia sp.
OG Plasmid pWWU2 {ECO:0000312|EMBL:AAD12606.1}.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=54061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND SUBUNIT.
RC STRAIN=U2 {ECO:0000312|EMBL:AAD12606.1};
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, SUBSTRATE SPECIFICITY, PATHWAY, AND SUBUNIT.
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 two multicomponent enzyme systems which are
CC involved in the catabolism of naphthalene (PubMed:9573207,
CC PubMed:11872705). Plays a role as an electron transfer component for
CC both salicylate 5-hydroxylase (S5H) and naphthalene 1,2-dioxygenase
CC (NDO) systems, by transferring electrons from NAD(P)H to the oxygenase
CC component via the ferredoxin NagAb (PubMed:9573207, PubMed:11872705).
CC The electron transport chain from the two systems can use both NADH and
CC NADPH as electron donors at approximately similar rates
CC (PubMed:11872705). {ECO:0000269|PubMed:11872705,
CC ECO:0000269|PubMed:9573207}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16521, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.18.1.7;
CC Evidence={ECO:0000269|PubMed:11872705};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:20125, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.18.1.7;
CC Evidence={ECO:0000269|PubMed:11872705};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:Q52126,
CC ECO:0000255|PROSITE-ProRule:PRU00465};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|PROSITE-ProRule:PRU00465};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q52126};
CC -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC {ECO:0000269|PubMed:11872705, ECO:0000269|PubMed:9573207}.
CC -!- SUBUNIT: Ferredoxin reductase NagAa belongs to both the salicylate 5-
CC hydroxylase (S5H) and the naphthalene 1,2-dioxygenase (NDO)
CC multicomponent enzyme systems. The NDO multicomponent enzyme system is
CC composed of an electron transfer component and a dioxygenase component
CC (iron sulfur protein (ISP)). The electron transfer component is
CC 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). The S5H multicomponent enzyme
CC system is composed of an electron transfer component and a
CC monooxygenase component. The electron transfer component is comprised
CC of a ferredoxin reductase (NagAa) and a ferredoxin (NagAb), and the
CC monooxygenase component is formed by a large subunit (NagG) and a small
CC subunit (NagH). {ECO:0000269|PubMed:11872705,
CC ECO:0000269|PubMed:9573207}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin reductase family. {ECO:0000305}.
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DR EMBL; AF036940; AAD12606.1; -; Genomic_DNA.
DR AlphaFoldDB; O52378; -.
DR SMR; O52378; -.
DR KEGG; ag:AAD12606; -.
DR BRENDA; 1.18.1.7; 5275.
DR UniPathway; UPA00082; -.
DR GO; GO:1902494; C:catalytic complex; IDA:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:RHEA.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022900; P:electron transport chain; IDA:UniProtKB.
DR GO; GO:1901170; P:naphthalene catabolic process; IDA:UniProtKB.
DR GO; GO:0046244; P:salicylic acid catabolic process; IDA:UniProtKB.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; FAD; Flavoprotein; Iron;
KW Iron-sulfur; Metal-binding; NAD; NADP; Oxidoreductase; Plasmid.
FT CHAIN 1..328
FT /note="Naphthalene 1,2-dioxygenase/salicylate 5-hydroxylase
FT systems, ferredoxin--NAD(P)(+), reductase component"
FT /id="PRO_0000421806"
FT DOMAIN 1..89
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 96..193
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 35
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 40
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 43
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 73
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 328 AA; 35085 MW; 36B948E841C2983C CRC64;
MELVVEPLNL HLNAETGSTL LDVLRSNEVP ISYSCMSGRC GTCRCRVIAG HLRDNGPETG
RPQAGKGTYV LACQAVLTED CTIEIPESDE IVVHPARIVK GTVTAIDEAT HDIRRLRIKL
AKPLEFSPGQ YATVQFTPEC VRPYSMAGLP SDAEMEFQIR AVPGGHVSNY VFNELSVGAS
VRISGPLGTA YLRRTHTGPM LCVGGGTGLA PVLSIVRGAL ESGMSNPIHL YFGVRSEQDI
YDEERLHALA ARFPNLKVNV VVATGPAGPG RRSGLVTDLI GRDLPNLAGW RAYLCGAPAM
VEALNLLVAR LGIVPGHIHA DAFYPSGV
