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NDOR_PSEPU
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   03-AUG-2022, entry version 134.
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; Proteobacteria; 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:MON-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:0008937; F:ferredoxin-NAD(P) reductase 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:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
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; 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
 
 
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