ID   TECA2_CUPXP             Reviewed;         187 AA.
AC   O24677;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Chlorobenzene dioxygenase subunit beta {ECO:0000305};
DE            EC=1.14.12.26 {ECO:0000269|PubMed:11526005, ECO:0000269|PubMed:9249026};
GN   Name=tecA2 {ECO:0000303|PubMed:9249026};
OS   Cupriavidus sp. (strain PS12).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus; unclassified Cupriavidus.
OX   NCBI_TaxID=393999;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   SUBUNIT.
RC   STRAIN=PS12;
RX   PubMed=9249026; DOI=10.1111/j.1432-1033.1997.00190.x;
RA   Beil S., Happe B., Timmis K.N., Pieper D.H.;
RT   "Genetic and biochemical characterization of the broad spectrum
RT   chlorobenzene dioxygenase from Burkholderia sp. strain PS12--dechlorination
RT   of 1,2,4,5-tetrachlorobenzene.";
RL   Eur. J. Biochem. 247:190-199(1997).
RN   [2]
RP   FUNCTION.
RC   STRAIN=PS12;
RX   PubMed=9791099; DOI=10.1128/jb.180.21.5520-5528.1998;
RA   Beil S., Mason J.R., Timmis K.N., Pieper D.H.;
RT   "Identification of chlorobenzene dioxygenase sequence elements involved in
RT   dechlorination of 1,2,4,5-tetrachlorobenzene.";
RL   J. Bacteriol. 180:5520-5528(1998).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=PS12;
RX   PubMed=11526005; DOI=10.1128/aem.67.9.4057-4063.2001;
RA   Pollmann K., Beil S., Pieper D.H.;
RT   "Transformation of chlorinated benzenes and toluenes by Ralstonia sp.
RT   strain PS12 tecA (tetrachlorobenzene dioxygenase) and tecB (chlorobenzene
RT   dihydrodiol dehydrogenase) gene products.";
RL   Appl. Environ. Microbiol. 67:4057-4063(2001).
CC   -!- FUNCTION: Part of the oxygenase component of the chlorobenzene
CC       dioxygenase system that catalyzes the dihydroxylation of a range of
CC       aromatic compounds, including chlorinated benzenes and toluenes, and
CC       dinuclear aromatics such as biphenyl and dibenzo-p-dioxin
CC       (PubMed:9249026, PubMed:9791099, PubMed:11526005). The beta subunit is
CC       not directly involved in the control of substrate specificity
CC       (PubMed:9791099). {ECO:0000269|PubMed:11526005,
CC       ECO:0000269|PubMed:9249026, ECO:0000269|PubMed:9791099}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chlorobenzene + H(+) + NADH + O2 = (1R,2R)-3-chlorocyclohexa-
CC         3,5-diene-1,2-diol + NAD(+); Xref=Rhea:RHEA:57512, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:19981, ChEBI:CHEBI:28097,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.12.26;
CC         Evidence={ECO:0000269|PubMed:11526005, ECO:0000269|PubMed:9249026};
CC   -!- PATHWAY: Aromatic compound metabolism. {ECO:0000305}.
CC   -!- SUBUNIT: This dioxygenase system consists of four proteins: the two
CC       subunits of the oxygenase component (TecA1 and TecA2), a ferredoxin
CC       (TecA3) and a ferredoxin reductase (TecA4).
CC       {ECO:0000305|PubMed:9249026}.
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       beta subunit family. {ECO:0000305}.
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DR   EMBL; U78099; AAC46391.1; -; Genomic_DNA.
DR   SMR; O24677; -.
DR   BioCyc; MetaCyc:MON-14391; -.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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   Aromatic hydrocarbons catabolism; Dioxygenase; NAD; Oxidoreductase.
FT   CHAIN           1..187
FT                   /note="Chlorobenzene dioxygenase subunit beta"
FT                   /id="PRO_0000453516"
SQ   SEQUENCE   187 AA;  21893 MW;  DEFB28BCD3D64679 CRC64;
     MLDSVKRADV FLRKPAPVAP ELQHEIEQFY YWEAKLLNDR RFEEWFALLA ADIHYFMPIR
     TTRIMRDARL EYSGTGEHAH FDDDAAMMKG RLRKVTSDVG WSENPASRTR HLVSNVMIAD
     GPVEGEYEIS SAFIVYRNRL ERQLDIFAGE RRDTLRRNKT ETGFEIVNRT ILIDQSTILA
     NNLSFFF