ID BEDC1_PSEPU Reviewed; 450 AA. AC Q07944; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-JUN-2009, entry version 56. DE RecName: Full=Benzene 1,2-dioxygenase subunit alpha; DE EC=1.14.12.3; GN Name=bedC1; OS Pseudomonas putida. OG Plasmid pHMT112. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-15. RC STRAIN=ML2; RX MEDLINE=93345820; PubMed=8344526; DOI=10.1016/0378-1119(93)90343-2; RA Tan H.-M., Tang H.-Y., Joannou C., Abdel-Wahab N.H., Mason J.R.; RT "The Pseudomonas putida ML2 plasmid-encoded genes for benzene RT dioxygenase are unusual in codon usage and low in G+C content."; RL Gene 130:33-39(1993). CC -!- CATALYTIC ACTIVITY: Benzene + NADH + O(2) = cis-cyclohexa-3,5- CC diene-1,2-diol + NAD(+). CC -!- COFACTOR: Binds 1 2Fe-2S cluster (Probable). CC -!- COFACTOR: Binds 1 iron ion (Probable). CC -!- PATHWAY: Aromatic compound metabolism; benzene degradation; CC catechol from benzene: step 1/2. CC -!- SUBUNIT: This dioxygenase system consists of four proteins: the CC two subunits of the hydroxylase component (bedC1 and bedC2), a CC ferredoxin (bedB) and a ferredoxin reductase (bedA). 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; AF148496; AAA17758.1; -; Genomic_DNA. DR PIR; JN0812; JN0812. DR HSSP; P23094; 1O7N. DR SMR; Q07944; 15-450. DR BioCyc; MetaCyc:MON-12880; -. DR BRENDA; 1.14.12.3; 403. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0018619; F:benzene 1,2-dioxygenase activity; IEA:EC. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. 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 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 1: Evidence at protein level; KW 2Fe-2S; Aromatic hydrocarbons catabolism; Dioxygenase; KW Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; NAD; KW Oxidoreductase; Plasmid. FT CHAIN 1 450 Benzene 1,2-dioxygenase subunit alpha. FT /FTId=PRO_0000085044. FT DOMAIN 56 163 Rieske. FT METAL 96 96 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 98 98 Iron-sulfur (2Fe-2S); via pros nitrogen FT (By similarity). FT METAL 116 116 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 119 119 Iron-sulfur (2Fe-2S); via pros nitrogen FT (By similarity). FT METAL 222 222 Iron (By similarity). FT METAL 228 228 Iron (By similarity). SQ SEQUENCE 450 AA; 51109 MW; 1ECD5EA6C4CF72C8 CRC64; MNQTETTPIR VRKNWKTSEI ETLFDEQAGR IDPRIYTDED LYQLELERVF ARSWLLLGHE THIRKPGDYF TTYMGEDPVV VVRQKDASIA VFLNQCRHRG MRICRSDAGN AKAFTCSYHG WAYDTAGNLI NVPYEAESFA CLDKKEWSPL KARVETYKGL IFANWDENAI DLDTYLGEAK FYMDHMLDRT EAGTEVIPGI QKWVIPCNWK FAAEQFCSDM YHAGTTAHLS GIIAGLPEDL ELADLAPPKF GKQYRASWGG HGSGFYIGDP NMMLAMMGPK VTSYLTEGPA AEKAAERLGS IERGTKIMLE HMTVFPTCSF LPGVNTIRTW HPRGPNEVEV WAFTVVDADA PDDIKEEFRR QTLRTFSAGG VFEQDDGENW VEIQHILRGH KARSRPFNAE MSMGQTVDND PIYPGRISNN VYSEEAARGL YAHWLKMMTS PDWEALKATR //