ID NDOR_PSEPU Reviewed; 328 AA.
AC Q52126; O33460; Q52122;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 08-NOV-2023, entry version 139.
DE RecName: Full=Naphthalene 1,2-dioxygenase system ferredoxin--NAD(P)(+), reductase component {ECO:0000303|PubMed:2294092};
DE EC=1.18.1.7 {ECO:0000269|PubMed:2294092, ECO:0000269|PubMed:7037744};
DE AltName: Full=Ferredoxin--NAD(P)(+) reductase (naphthalene dioxygenase ferredoxin-specific) {ECO:0000303|PubMed:2294092};
GN Name=ndoR; Synonyms=nahA1, nahAA {ECO:0000303|PubMed:8486285};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OG Plasmid pDTG1, Plasmid NAH7, and Plasmid NPL1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=9816-4, and
RC ATCC 17485 / DSM 50208 / JCM 6158 / NCIMB 12092 / Stanier 111 / Biotype A;
RC PLASMID=NAH7, and pDTG1;
RX PubMed=8486285; DOI=10.1016/0378-1119(93)90613-8;
RA Simon M.J., Osslund T.D., Saunders R., Ensley B.D., Suggs S.,
RA Harcourt A.A., Suen W.-C., Cruden D.L., Gibson D.T., Zylstra G.J.;
RT "Sequences of genes encoding naphthalene dioxygenase in Pseudomonas putida
RT strains G7 and NCIB 9816-4.";
RL Gene 127:31-37(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BS202; PLASMID=NPL1;
RX PubMed=8787402; DOI=10.1128/aem.62.6.2053-2058.1996;
RA Pellizari V.H., Bezborodnikov S.G., Quensen J.F. III, Tiedje J.M.;
RT "Evaluation of strains isolated by growth on naphthalene and biphenyl for
RT hybridization of genes to dioxygenase probes and polychlorinated biphenyl-
RT degrading ability.";
RL Appl. Environ. Microbiol. 62:2053-2058(1996).
RN [3]
RP PROTEIN SEQUENCE OF 1-25, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, SUBUNIT, AND SUBSTRATE SPECIFICITY.
RC STRAIN=DSM 8368 / NCIMB 9816 / PG;
RX PubMed=2294092; DOI=10.1128/jb.172.1.457-464.1990;
RA Haigler B.E., Gibson D.T.;
RT "Purification and properties of NADH-ferredoxin NAP reductase, a component
RT of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816.";
RL J. Bacteriol. 172:457-464(1990).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBSTRATE SPECIFICITY.
RC STRAIN=DSM 8368 / NCIMB 9816 / PG;
RX PubMed=7037744; DOI=10.1128/jb.149.3.948-954.1982;
RA Ensley B.D., Gibson D.T., Laborde A.L.;
RT "Oxidation of naphthalene by a multicomponent enzyme system from
RT Pseudomonas sp. strain NCIB 9816.";
RL J. Bacteriol. 149:948-954(1982).
RN [5]
RP FUNCTION, SUBSTRATE SPECIFICITY, AND PATHWAY.
RC STRAIN=NCIMB 9816-4;
RX PubMed=10692370; DOI=10.1128/jb.182.6.1641-1649.2000;
RA Parales R.E., Lee K., Resnick S.M., Jiang H., Lessner D.J., Gibson D.T.;
RT "Substrate specificity of naphthalene dioxygenase: effect of specific amino
RT acids at the active site of the enzyme.";
RL J. Bacteriol. 182:1641-1649(2000).
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:2294092, PubMed:7037744, PubMed:10692370).
CC Ferredoxin reductase catalyzes the transfer of electrons from NADH to
CC ferredoxin (NdoA) (PubMed:2294092). NADPH is also effective but yields
CC only 39% of the activity obtained with NADH (PubMed:2294092,
CC PubMed:7037744). Also able to catalyze the cis-dihydroxylation of
CC biphenyl and phenanthrene (PubMed:10692370).
CC {ECO:0000269|PubMed:10692370, ECO:0000269|PubMed:2294092,
CC ECO:0000269|PubMed:7037744}.
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; Evidence={ECO:0000269|PubMed:2294092,
CC ECO:0000269|PubMed:7037744};
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; Evidence={ECO:0000269|PubMed:2294092,
CC ECO:0000269|PubMed:7037744};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:2294092, ECO:0000305|PubMed:7037744};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:2294092};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:2294092, ECO:0000269|PubMed:7037744};
CC Note=Binds 1 mole of FAD per mole of enzyme. Also able to use FMN, but
CC the activity is less than that obtained with FAD.
CC {ECO:0000269|PubMed:2294092, ECO:0000269|PubMed:7037744};
CC -!- ACTIVITY REGULATION: Strongly inhibited by p-chloromercuribenzoate.
CC Also inhibited by N-ethylmaleimide and o-phenanthroline.
CC {ECO:0000269|PubMed:2294092}.
CC -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC {ECO:0000305|PubMed:10692370}.
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:0000305|PubMed:2294092}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin reductase component family. {ECO:0000305}.
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DR EMBL; AF491307; AAA25904.1; -; Genomic_DNA.
DR EMBL; M83949; AAA25900.1; -; Genomic_DNA.
DR EMBL; AF010471; AAB62705.1; -; Genomic_DNA.
DR PIR; JN0640; JN0640.
DR PIR; JN0642; JN0642.
DR RefSeq; NP_863070.1; NC_004999.1.
DR RefSeq; WP_011117469.1; NC_004999.1.
DR RefSeq; YP_534820.1; NC_007926.1.
DR AlphaFoldDB; Q52126; -.
DR SMR; Q52126; -.
DR KEGG; ag:AAA25904; -.
DR BioCyc; MetaCyc:MONOMER-12800; -.
DR BRENDA; 1.18.1.7; 5092.
DR UniPathway; UPA00082; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IDA:UniProtKB.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06187; O2ase_reductase_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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 PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF5; PROTEIN RFBI; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 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; Direct protein sequencing; FAD;
KW Flavoprotein; Iron; Iron-sulfur; Metal-binding; NAD; NADP; Oxidoreductase;
KW Plasmid.
FT CHAIN 1..328
FT /note="Naphthalene 1,2-dioxygenase system ferredoxin--
FT NAD(P)(+), reductase component"
FT /id="PRO_0000167657"
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"
FT VARIANT 8
FT /note="N -> K (in strain: BS202)"
FT VARIANT 11
FT /note="I -> L (in strain: G7)"
FT VARIANT 13
FT /note="P -> S (in strain: G7)"
FT VARIANT 16
FT /note="A -> P (in strain: G7)"
FT VARIANT 36
FT /note="L -> M (in strain: G7)"
FT VARIANT 48
FT /note="I -> T (in strain: G7)"
FT VARIANT 58..59
FT /note="EN -> GS (in strain: G7)"
FT VARIANT 61..62
FT /note="QS -> LP (in strain: G7)"
FT VARIANT 65
FT /note="T -> V (in strain: G7)"
FT VARIANT 67..68
FT /note="KQ -> EH (in strain: G7)"
FT VARIANT 79
FT /note="G -> H (in strain: G7)"
FT VARIANT 85
FT /note="V -> I (in strain: G7)"
FT VARIANT 88
FT /note="A -> T (in strain: G7)"
FT VARIANT 121
FT /note="S -> A (in strain: G7)"
FT VARIANT 195
FT /note="K -> N (in strain: G7)"
FT VARIANT 222
FT /note="S -> L (in strain: G7)"
FT VARIANT 264
FT /note="T -> M (in strain: G7)"
FT VARIANT 270
FT /note="G -> S (in strain: G7)"
FT VARIANT 276
FT /note="I -> V (in strain: G7)"
FT VARIANT 285
FT /note="L -> I (in strain: G7)"
SQ SEQUENCE 328 AA; 35501 MW; 4E6237C85CCDF685 CRC64;
MELLIQPNNR IIPFSAGANL LEVLRENGVA ISYSCLSGRC GTCRCRVIDG SVIDSGAENG
QSNLTDKQYV LACQSVLTGN CAIEVPEADE IVTHPARIIK GTVVAVESPT HDIRRLRVRL
SKPFEFSPGQ YATLQFSPEH ARPYSMAGLP DDQEMEFHIR KVPGGRVTEY VFEHVREGTS
IKLSGPLGTA YLRQKHTGPM LCVGGGTGLA PVLSIVRGAL KSGMTNPILL YFGVRSQQDL
YDAERLHKLA ADHPQLTVHT VIATGPINEG QRAGLITDVI EKDILSLAGW RAYLCGAPAM
VEALCTVTKH LGISPEHIYA DAFYPGGI
//
