NDOA_PSEPU
ID NDOA_PSEPU Reviewed; 104 AA.
AC P0A185; O07829; P23082; Q52123;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Naphthalene 1,2-dioxygenase system, ferredoxin component {ECO:0000303|PubMed:2294093};
GN Name=ndoA {ECO:0000303|PubMed:3243438};
GN Synonyms=nahAB {ECO:0000303|PubMed:8486285}, ndoC1;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OG Plasmid pDTG1, and Plasmid NAH7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 8368 / NCIMB 9816 / PG;
RX PubMed=3243438; DOI=10.1016/0378-1119(88)90500-8;
RA Kurkela S., Lehvaeslaiho H., Palva E.T., Teeri T.H.;
RT "Cloning, nucleotide sequence and characterization of genes encoding
RT naphthalene dioxygenase of Pseudomonas putida strain NCIB9816.";
RL Gene 73:355-362(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-9.
RC STRAIN=ATCC 17485 / DSM 50208 / JCM 6158 / NCIMB 12092 / Stanier 111 /
RC Biotype A, and NCIMB 9816-4; 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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 17484 / DSM 50222 / NCIMB 10535 / Stanier 110 / Biotype B;
RA Hamann C.;
RT "Naphthalene dioxygenase genes from Pseudomonas putida.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=DSM 8368 / NCIMB 9816 / PG;
RX PubMed=6874638; DOI=10.1128/jb.155.2.505-511.1983;
RA Ensley B.D., Gibson D.T.;
RT "Naphthalene dioxygenase: purification and properties of a terminal
RT oxygenase component.";
RL J. Bacteriol. 155:505-511(1983).
RN [5]
RP FUNCTION, COFACTOR, AND SUBUNIT.
RX PubMed=2294093; DOI=10.1128/jb.172.1.465-468.1990;
RA Haigler B.E., Gibson D.T.;
RT "Purification and properties of ferredoxin NAP, a component of naphthalene
RT dioxygenase from Pseudomonas sp. strain NCIB 9816.";
RL J. Bacteriol. 172:465-468(1990).
RN [6]
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).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-104 IN COMPLEX WITH [2FE-2S]
RP CLUSTER, AND COFACTOR.
RX PubMed=18719951; DOI=10.1007/s00775-008-0413-4;
RA Brown E.N., Friemann R., Karlsson A., Parales J.V., Couture M.M.,
RA Eltis L.D., Ramaswamy S.;
RT "Determining Rieske cluster reduction potentials.";
RL J. Biol. Inorg. Chem. 13:1301-1313(2008).
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:6874638, PubMed:2294093, PubMed:10692370).
CC Functions as an intermediate electron transfer protein via a specific
CC interaction with iron sulfur protein components (ISP) (NdoB and NdoC)
CC (PubMed:2294093). Also able to catalyze the cis-dihydroxylation of
CC biphenyl and phenanthrene (PubMed:10692370).
CC {ECO:0000269|PubMed:10692370, ECO:0000269|PubMed:2294093,
CC ECO:0000269|PubMed:6874638}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:18719951, ECO:0000269|PubMed:2294093};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:2294093};
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:2294093,
CC ECO:0000305|PubMed:6874638}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin component family. {ECO:0000305}.
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DR EMBL; M23914; AAB47590.1; -; Genomic_DNA.
DR EMBL; AF491307; AAA25905.1; -; Genomic_DNA.
DR EMBL; M83949; AAA25901.1; -; Genomic_DNA.
DR EMBL; AF004284; AAB61372.1; -; Genomic_DNA.
DR PIR; JN0641; JN0641.
DR PIR; JN0643; JN0643.
DR RefSeq; NP_863071.1; NC_004999.1.
DR RefSeq; WP_011117470.1; NC_004999.1.
DR RefSeq; YP_534821.1; NC_007926.1.
DR PDB; 2QPZ; X-ray; 1.85 A; A=2-104.
DR PDBsum; 2QPZ; -.
DR AlphaFoldDB; P0A185; -.
DR SMR; P0A185; -.
DR KEGG; ag:AAA25905; -.
DR BioCyc; MetaCyc:MON-12801; -.
DR UniPathway; UPA00082; -.
DR EvolutionaryTrace; P0A185; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IDA:UniProtKB.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Aromatic hydrocarbons catabolism;
KW Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Plasmid; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8486285"
FT CHAIN 2..104
FT /note="Naphthalene 1,2-dioxygenase system, ferredoxin
FT component"
FT /id="PRO_0000201693"
FT DOMAIN 6..101
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 45
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:18719951,
FT ECO:0007744|PDB:2QPZ"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:18719951,
FT ECO:0007744|PDB:2QPZ"
FT BINDING 64
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:18719951,
FT ECO:0007744|PDB:2QPZ"
FT BINDING 67
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:18719951,
FT ECO:0007744|PDB:2QPZ"
FT VARIANT 3
FT /note="V -> E (in strain: G7)"
FT VARIANT 15
FT /note="L -> P (in strain: G7)"
FT VARIANT 49
FT /note="S -> A (in strain: G7)"
FT VARIANT 77
FT /note="K -> R (in strain: G7)"
FT VARIANT 85
FT /note="Q -> E (in strain: G7)"
FT VARIANT 91
FT /note="P -> A (in strain: G7)"
FT VARIANT 104
FT /note="S -> GEF (in strain: G7)"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:2QPZ"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:2QPZ"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:2QPZ"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:2QPZ"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:2QPZ"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:2QPZ"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2QPZ"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2QPZ"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:2QPZ"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2QPZ"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:2QPZ"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2QPZ"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:2QPZ"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:2QPZ"
SQ SEQUENCE 104 AA; 11446 MW; 475625DCC3EDCD41 CRC64;
MTVKWIEAVA LSDILEGDVL GVTVEGKELA LYEVEGEIYA TDNLCTHGSA RMSDGYLEGR
EIECPLHQGR FDVCTGKALC APVTQNIKTY PVKIENLRVM IDLS
