TECA1_CUPXP
ID TECA1_CUPXP Reviewed; 449 AA.
AC O24676;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Chlorobenzene dioxygenase subunit alpha {ECO:0000305};
DE EC=1.14.12.26 {ECO:0000269|PubMed:11526005, ECO:0000269|PubMed:9249026};
GN Name=tecA1 {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 alpha subunit is
CC responsible for substrate specificity (PubMed:9791099).
CC {ECO:0000269|PubMed:11526005, ECO:0000269|PubMed:9249026,
CC 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 -!- 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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:Q53122};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250|UniProtKB:Q53122};
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 alpha subunit family. {ECO:0000305}.
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DR EMBL; U78099; AAC46390.1; -; Genomic_DNA.
DR SMR; O24676; -.
DR BioCyc; MetaCyc:MON-14390; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08881; RHO_alpha_C_NDO-like; 1.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR043266; RHO_NdoB-like_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756; PTHR43756; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase.
FT CHAIN 1..449
FT /note="Chlorobenzene dioxygenase subunit alpha"
FT /id="PRO_0000453515"
FT DOMAIN 54..163
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 96
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 98
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 116
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 119
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 222
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q53122"
FT BINDING 228
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q53122"
FT BINDING 376
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q53122"
SQ SEQUENCE 449 AA; 50541 MW; EB873EB2B005D575 CRC64;
MNHTDTSPIK LRKNWNAREM QALFDERAGR TDPRIYTDED LYQIELERVF GRSWLLLGHE
TQIKKPGDYT TNYMGEDPVL VVRQKDGSIA VFLNQCRHRG MRICRSDAGN AKAFTCSYHG
WAYDTAGNLV NVPFEAESFP CLDKKEWSPL KARVATYKGL IFANWDHDAP DLDTYLGEAK
FYMDHMLDRT EAGTEAIPGV QKWVIPCNWK LAAEQFCWDA YHAATTAHLS GILAGLPDGV
ELADLAPPTV GKQYRAPWGG HGSGFFIGEP DLLLAIMGPK ITSYWTEGPA SEKAAQRLGS
VERGSKLTVE HMTVFPTCSF LLGANTVRTW HPRGPNEVEV WAFTVVDADA PDDIKEEFRR
QTVRTFSAGG VFEQDDGENW VEIQHVLRGH KARSRPFNAE MSMGQTIDDD PVYPGRISNV
YSDEAARGFY AQWLRMMTSS DWAALNATR
