ID   TECA3_CUPXP             Reviewed;         107 AA.
AC   O24678;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Chlorobenzene dioxygenase, ferredoxin component {ECO:0000305};
GN   Name=tecA3 {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, AND 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=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 chlorobenzene dioxygenase system that catalyzes
CC       the dihydroxylation of a range of aromatic compounds, including
CC       chlorinated benzenes and toluenes, and dinuclear aromatics such as
CC       biphenyl and dibenzo-p-dioxin. {ECO:0000269|PubMed:11526005,
CC       ECO:0000269|PubMed:9249026}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00628};
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       ferredoxin component family. {ECO:0000305}.
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DR   EMBL; U78099; AAC46392.1; -; Genomic_DNA.
DR   SMR; O24678; -.
DR   BioCyc; MetaCyc:MON-14392; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.102.10.10; -; 1.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   Pfam; PF00355; Rieske; 1.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; Aromatic hydrocarbons catabolism; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Transport.
FT   CHAIN           1..107
FT                   /note="Chlorobenzene dioxygenase, ferredoxin component"
FT                   /id="PRO_0000453517"
FT   DOMAIN          4..99
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         43
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         45
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         62
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         65
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ   SEQUENCE   107 AA;  11679 MW;  1EFA5F2FF866AAF1 CRC64;
     MAWTYIMRQS DLPPGEMQRH EGGPEPVMVC NVDGEFFAVQ DTCTHGNWAL SDGYLDGGVV
     ECTLHFGKFC VRTGKVKALP ACKPIKVFPI KVEGGDVHVD LDAGEVK