CBDA_BURCE
ID CBDA_BURCE Reviewed; 465 AA.
AC Q51601;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=2-halobenzoate 1,2-dioxygenase large subunit;
DE EC=1.14.12.13;
DE AltName: Full=2-chlorobenzoate 1,2-dioxygenase;
GN Name=cbdA;
OS Burkholderia cepacia (Pseudomonas cepacia).
OG Plasmid pBAH1.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2CBS;
RX PubMed=7530709; DOI=10.1128/jb.177.3.667-675.1995;
RA Haak B., Fetzner S., Lingens F.;
RT "Cloning, nucleotide sequence, and expression of the plasmid-encoded genes
RT for the two-component 2-halobenzoate 1,2-dioxygenase from Pseudomonas
RT cepacia 2CBS.";
RL J. Bacteriol. 177:667-675(1995).
RN [2]
RP PROTEIN SEQUENCE OF 2-21, AND CHARACTERIZATION.
RC STRAIN=2CBS;
RX PubMed=1370284; DOI=10.1128/jb.174.1.279-290.1992;
RA Fetzner S., Mueller R., Lingens F.;
RT "Purification and some properties of 2-halobenzoate 1,2-dioxygenase, a two-
RT component enzyme system from Pseudomonas cepacia 2CBS.";
RL J. Bacteriol. 174:279-290(1992).
CC -!- FUNCTION: Component of 2-halobenzoate dioxygenase multicomponent enzyme
CC system which catalyzes the incorporation of both atoms of molecular
CC oxygen into 2-halobenzoate to form catechol.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-halobenzoate + H(+) + NADH + O2 = a halide anion +
CC catechol + CO2 + NAD(+); Xref=Rhea:RHEA:53736, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16042, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:18135, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:70856; EC=1.14.12.13;
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(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Xenobiotic degradation; benzoate degradation via CoA ligation.
CC -!- SUBUNIT: Heterohexamer of 3 large (CbdA) subunits and 3 small (CbdB)
CC subunits. The heterohexamer is part of 2-halobenzoate dioxygenase two
CC component enzyme system. The other component is a NADH:acceptor
CC reductase (CdbC).
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000305}.
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DR EMBL; X79076; CAA55681.1; -; Genomic_DNA.
DR AlphaFoldDB; Q51601; -.
DR SMR; Q51601; -.
DR PRIDE; Q51601; -.
DR KEGG; ag:CAA55681; -.
DR BioCyc; MetaCyc:MON-14763; -.
DR UniPathway; UPA00233; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018626; F:2-chlorobenzoate 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0010128; P:benzoate catabolic process via CoA ligation; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.102.10.10; -; 1.
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;
KW Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; NAD;
KW Oxidoreductase; Plasmid.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1370284"
FT CHAIN 2..465
FT /note="2-halobenzoate 1,2-dioxygenase large subunit"
FT /id="PRO_0000085051"
FT DOMAIN 56..154
FT /note="Rieske"
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 100
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 118
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 121
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 227
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 465 AA; 52478 MW; 08747DF6FB8D30DC CRC64;
MSTPLIAGTG PSAVRQLISN AVQNDPVSGN FRCRRDIFTD AALFDYEMKY IFEQNWVFLA
HESQVANPDD YLVSNIGRQP VIITRNKAGD VSAVINACSH RGAELCRRKQ GNRSTFTCQF
HGWTFSNTGK LLKVKDGQDD NYPEGFNVDG SHDLTRIPSF ANYRGFLFGS MNPDACPIEE
HLGGSKAILD QVIDQTPGEL EVLRGSSSYI YDGNWKLQIE NGADGYHVGS VHWNYVATIG
RRDRTSDTIR TVDVTTWSKK NIGGTYTFEH GHMLLWTRLP NPEVRPVFAR REELKARVGE
EVADAIVNQT RNLCIYPNLY VMDQISTQIR VVRPISVDKT EVTIYCFAPR DESEEVRNAR
IRQYEDFFNV SGMGTPDDLE EFRACQSGYR GSAREWNDLS RGAPHWISGP DDNARRLGLA
PLMSGARMED EGLFVQQHTY WAETMLRGIE AEPKVFNVQP VEVAQ
