ID NDOB_PSEFL Reviewed; 449 AA. AC O07824; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 16-JUN-2009, entry version 55. DE RecName: Full=Naphthalene 1,2-dioxygenase subunit alpha; DE EC=1.14.12.12; DE AltName: Full=Naphthalene 1,2-dioxygenase ISP alpha; GN Name=ndoB; Synonyms=ndoC2; OS Pseudomonas fluorescens. OG Plasmid. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=294; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 17483 / DSM 6506 / JCM 6159 / Stanier 109; RA Hamann C.; RT "Naphthalene dioxygenase genes from Pseudomonas fluorescens."; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the naphthalene dioxygenase (NDO) CC multicomponent enzyme system which catalyzes the incorporation of CC both atoms of molecular oxygen into naphthalene to form cis- CC naphthalene dihydrodiol. CC -!- CATALYTIC ACTIVITY: Naphthalene + NADH + O(2) = (1R,2S)-1,2- CC dihydronaphthalene-1,2-diol + NAD(+). CC -!- COFACTOR: Binds 1 2Fe-2S cluster (Probable). CC -!- COFACTOR: Binds 1 iron ion (Probable). CC -!- PATHWAY: Aromatic compound metabolism; naphtalene degradation. CC -!- SUBUNIT: Naphthalene dioxygenase (NDO) multicomponent enzyme CC system is composed of an electron transfer component and an iron CC sulfur protein (ISP). The electron transfer component is composed CC of ferredoxin reductase (ndoR) and ferredoxin (ndoA), and ISP is CC composed of a large alpha subunit (ndoB) and a small beta subunit CC (ndoC). CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating CC dioxygenase alpha subunit family. CC -!- SIMILARITY: Contains 1 Rieske domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF004283; AAB61370.1; -; Genomic_DNA. DR HSSP; P23094; 1O7N. DR SMR; O07824; 1-447. DR BRENDA; 1.14.12.12; 329. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0018625; F:naphthalene 1,2-dioxygenase activity; IEA:EC. DR GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW. DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR017941; Rieske_2Fe-2S. DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS. DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C. DR InterPro; IPR001663; Rng_hydr_dOase-A. DR Gene3D; G3DSA:2.102.10.10; Rieske_reg; 1. DR PANTHER; PTHR21266:SF2; Rng_hydr_dOase-A; 1. DR Pfam; PF00355; Rieske; 1. DR Pfam; PF00848; Ring_hydroxyl_A; 1. DR PRINTS; PR00090; RNGDIOXGNASE. DR PROSITE; PS51296; RIESKE; 1. DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1. PE 3: Inferred from homology; KW 2Fe-2S; Aromatic hydrocarbons catabolism; Dioxygenase; Iron; KW Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Plasmid. FT CHAIN 1 449 Naphthalene 1,2-dioxygenase subunit FT alpha. FT /FTId=PRO_0000085055. FT DOMAIN 39 137 Rieske. FT METAL 81 81 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 83 83 Iron-sulfur (2Fe-2S); via pros nitrogen FT (By similarity). FT METAL 101 101 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 104 104 Iron-sulfur (2Fe-2S); via pros nitrogen FT (By similarity). FT METAL 208 208 Iron (By similarity). FT METAL 213 213 Iron (By similarity). FT METAL 362 362 Iron (By similarity). SQ SEQUENCE 449 AA; 49514 MW; 186A7924AD437A1C CRC64; MNYKNKILVS ESGLTQKHLI HGDEELFQHE LRTIXARNWL FLTHDSLIPS PGDYVTAKMG IDEVIVSRQS DGSIRAFLNV CRHRGKTLVN AEAGNAKGFV CSYHGWGFGS NGELQSVPFE KELYGESLNK KCLGLKEVAR VESFHGFIYG CFDQEAPSLM DYLGDAAWYL EPIFKHSGGL ELVGPPGKVV IKANWKAPAE NFVGDAYHVG WTHASSLRTG ESIFSSLAGN AVLPPEGAGL QMTSKYGSGM GVLWDGYSGV HSADLVPELM AFGGAKQERL NKEIGDVPAR IYRSHLNCTV FPNNSVLTCS GVFKVWNPID ANTTEVWTYA IVEKDMPEDL KRRLADAVQR TFGPAGFWES DDNDNMETAS QNGKKYQSRD SDLISNLGFG KDVYGDAVYP GVVGKSAIGE TSYRGFYRAY QAHVSSSNWA EFEDASSTWH TELTKTTDR //