BNZB_PSEP1
ID BNZB_PSEP1 Reviewed; 187 AA.
AC A5W4F1; P08085; P13451;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Benzene 1,2-dioxygenase subunit beta;
DE EC=1.14.12.3;
DE AltName: Full=Benzene 1,2-dioxygenase P2 subunit;
DE AltName: Full=Toluene 2,3-dioxygenase subunit beta;
DE EC=1.14.12.11;
GN Name=bnzB; Synonyms=todC2; OrderedLocusNames=Pput_2880;
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-12.
RX PubMed=2670929; DOI=10.1016/s0021-9258(18)63793-7;
RA Zylstra G.J., Gibson D.T.;
RT "Toluene degradation by Pseudomonas putida F1. Nucleotide sequence of the
RT todC1C2BADE genes and their expression in Escherichia coli.";
RL J. Biol. Chem. 264:14940-14946(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes both the oxidation of benzene and toluene. The beta
CC subunit may be responsible for the substrate specificity of the enzyme.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzene + H(+) + NADH + O2 = cis-1,2-dihydrobenzene-1,2-diol +
CC NAD(+); Xref=Rhea:RHEA:13813, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16190, ChEBI:CHEBI:16716, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.14.12.3;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + O2 + toluene = (1S,2R)-3-methylcyclohexa-3,5-
CC diene-1,2-diol + NAD(+); Xref=Rhea:RHEA:16737, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:15565, ChEBI:CHEBI:17578,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.12.11;
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- PATHWAY: Aromatic compound metabolism; benzene degradation; catechol
CC 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 two
CC subunits of the hydroxylase component (BnzA and BnzB), a ferredoxin
CC (BnzC) and a ferredoxin reductase (BnzD).
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC beta subunit family. {ECO:0000305}.
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DR EMBL; J04996; AAA26006.1; -; Genomic_DNA.
DR EMBL; CP000712; ABQ79011.1; -; Genomic_DNA.
DR PIR; B29830; B29830.
DR RefSeq; WP_012052600.1; NC_009512.1.
DR PDB; 3EN1; X-ray; 3.20 A; B=1-187.
DR PDB; 3EQQ; X-ray; 3.20 A; B=1-187.
DR PDBsum; 3EN1; -.
DR PDBsum; 3EQQ; -.
DR AlphaFoldDB; A5W4F1; -.
DR SMR; A5W4F1; -.
DR STRING; 351746.Pput_2880; -.
DR EnsemblBacteria; ABQ79011; ABQ79011; Pput_2880.
DR KEGG; ppf:Pput_2880; -.
DR eggNOG; COG5517; Bacteria.
DR HOGENOM; CLU_102527_1_1_6; -.
DR OMA; LQAHQFL; -.
DR OrthoDB; 1736098at2; -.
DR UniPathway; UPA00228; -.
DR UniPathway; UPA00272; UER00391.
DR UniPathway; UPA00273; -.
DR EvolutionaryTrace; A5W4F1; -.
DR GO; GO:0018619; F:benzene 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0018624; F:toluene dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0042184; P:xylene catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00667; ring_hydroxylating_dioxygenases_beta; 1.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR000391; Rng_hydr_dOase-bsu.
DR PANTHER; PTHR41534; PTHR41534; 1.
DR Pfam; PF00866; Ring_hydroxyl_B; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase;
KW Direct protein sequencing; NAD; Oxidoreductase.
FT CHAIN 1..187
FT /note="Benzene 1,2-dioxygenase subunit beta"
FT /id="PRO_0000314466"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 20..38
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 108..120
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 126..139
FT /evidence="ECO:0007829|PDB:3EN1"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 143..157
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 164..174
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:3EN1"
SQ SEQUENCE 187 AA; 22013 MW; 39A5D2BECB6116B5 CRC64;
MIDSANRADV FLRKPAPVAP ELQHEVEQFY YWEAKLLNDR RFEEWFALLA EDIHYFMPIR
TTRIMRDSRL EYSGSREYAH FDDDATMMKG RLRKITSDVS WSENPASRTR HLVSNVMIVG
AEAEGEYEIS SAFIVYRNRL ERQLDIFAGE RRDTLRRNTS EAGFEIVNRT ILIDQSTILA
NNLSFFF
