ID   BNZA_PSEPU              Reviewed;         450 AA.
AC   P0C618; P08084; P13450;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   16-JUN-2009, entry version 10.
DE   RecName: Full=Benzene 1,2-dioxygenase subunit alpha;
DE            EC=1.14.12.3;
DE   AltName: Full=Benzene 1,2-dioxygenase P1 subunit;
DE   AltName: Full=Toluene 2,3-dioxygenase subunit alpha;
DE            EC=1.14.12.11;
GN   Name=bnzA; Synonyms=todC1;
OS   Pseudomonas putida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BE-81;
RX   MEDLINE=88032840; PubMed=3667527;
RA   Irie S., Doi S., Yorifuji T., Takagi M., Yano K.;
RT   "Nucleotide sequencing and characterization of the genes encoding
RT   benzene oxidation enzymes of Pseudomonas putida.";
RL   J. Bacteriol. 169:5174-5179(1987).
CC   -!- FUNCTION: Catalyzes both the oxidation of benzene and toluene.
CC   -!- CATALYTIC ACTIVITY: Benzene + NADH + O(2) = cis-cyclohexa-3,5-
CC       diene-1,2-diol + NAD(+).
CC   -!- CATALYTIC ACTIVITY: Toluene + NADH + O(2) = (1S,2R)-3-
CC       methylcyclohexa-3,5-diene-1,2-diol + NAD(+).
CC   -!- COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC   -!- PATHWAY: Aromatic compound metabolism; benzene degradation;
CC       catechol from benzene: step 1/2.
CC   -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC   -!- PATHWAY: Xenobiotic degradation; xylene degradation.
CC   -!- SUBUNIT: This dioxygenase system consists of four proteins: the
CC       two subunits of the hydroxylase component (bnzA and bnzB), a
CC       ferredoxin (bnzC) and a ferredoxin reductase (bnzD).
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating
CC       dioxygenase alpha subunit family.
CC   -!- SIMILARITY: Contains 1 Rieske domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA25735.1; Type=Frameshift; Positions=330, 339, 360, 362, 368, 393;
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DR   EMBL; M17904; AAA25735.1; ALT_FRAME; Genomic_DNA.
DR   PIR; A29830; A29830.
DR   HSSP; P23094; 1O7N.
DR   BRENDA; 1.14.12.11; 403.
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:0018624; F:toluene dioxygenase activity; IEA:EC.
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   3: Inferred from homology;
KW   2Fe-2S; Aromatic hydrocarbons catabolism; Dioxygenase; Iron;
KW   Iron-sulfur; Metal-binding; NAD; Oxidoreductase.
FT   CHAIN         1    450       Benzene 1,2-dioxygenase subunit alpha.
FT                                /FTId=PRO_0000085045.
FT   DOMAIN       54    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;  50944 MW;  038C80F197F3485D CRC64;
     MNQTDTSPIR LRRSWNTSEI EALFDEHAGR IDPRIYTDED LYQLELERVF ARSWLLLGHE
     TQIRKPGDYI TTYMGEDPVV VVRQKDASIA VFLNQCRHRG MRICRADAGN AKAFTCSYHG
     WAYDTAGNLV NVPYEAESFA CLNKKEWSPL KARVETYKGL IFANWDENAV DLDTYLGEAK
     FYMDHMLDRT EAGTEAIPGV QKWVIPCNWK FAAEQFCSDM YHAGTTSHLS GILAGLPEDL
     EMADLAPPTV GKQYRASWGG HGSGFYVGDP NLMLAIMGPK VTSYWTEGPA SEKAAERLGS
     VERGSKLMVE HMTVFPTCSF LPGINTVRTW HPRGPNEVEV WAFTVVDADA PDDIKEEFRR
     QTLRTFSAGG VFEQDDGENW VEIQHILRGH KARSRPFNAE MSMDQTVDND PVYPGRISNN
     VYSEEAARGL YAHWLRMMTS PDWDALKATR
//