ID   TECA4_CUPXP             Reviewed;         410 AA.
AC   O24679;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Chlorobenzene dioxygenase, ferredoxin reductase component {ECO:0000305};
DE            EC=1.18.1.3 {ECO:0000250|UniProtKB:Q0S032};
GN   Name=tecA4 {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   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2
CC         oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16521, Rhea:RHEA-
CC         COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.18.1.3;
CC         Evidence={ECO:0000250|UniProtKB:Q0S032};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:O85675};
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 reductase family. {ECO:0000305}.
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DR   EMBL; U78099; AAC46393.1; -; Genomic_DNA.
DR   SMR; O24679; -.
DR   BioCyc; MetaCyc:MON-14393; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR028202; Reductase_C.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF14759; Reductase_C; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
DR   SUPFAM; SSF55424; SSF55424; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; FAD; Flavoprotein; NAD; Oxidoreductase.
FT   CHAIN           1..410
FT                   /note="Chlorobenzene dioxygenase, ferredoxin reductase
FT                   component"
FT                   /id="PRO_0000453518"
FT   BINDING         4..35
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         145..173
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   410 AA;  42962 MW;  C54CD810E03D536C CRC64;
     MATHVAIIGN GVAGFTTAQA LRAEGFEGRI SLIGNEPHLP YDRPSLSKAV LGGSLEHPPV
     LAEADWYGEA RIDMLSGRSV TNLNVDARTI SLDDGSTFAA DAIVIATGSR ARTLALPGSQ
     LTGVVTLRTN DDVRPLCRGW TPATRLVIAG GGLIGCEVAT TARKLGLAVT ILESADELLV
     RVLGRRIGAW LRGLLTELGV RVELGTGVAG FSGDDRLEEV LASDGRRFAA DNALVCIGAE
     PEDQLARQAG LSCDRGVIVD DHGATHAEGV FAVGDAASWP LRDGGRRSLE TYMNAQRQAA
     AVAAAILGKH GSAPQVPVSW TEIAGHRMQM AGDIEGPGEF VLRGTLGDGA ALLFRLRDGR
     IQAVVAVDAP RDFAMAARLV EARAAIEPAR LADFSNSMRD LVRAQQGDSA