CBDC_BURCE
ID CBDC_BURCE Reviewed; 339 AA.
AC Q51603; O08068;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=2-halobenzoate 1,2-dioxygenase electron transfer component;
DE Includes:
DE RecName: Full=Ferredoxin;
DE Includes:
DE RecName: Full=Ferredoxin--NAD(+) reductase;
DE EC=1.18.1.3;
GN Name=cbdC;
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 1-19, 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: Electron transfer component of 2-halobenzoate 1,2-dioxygenase
CC system.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
CC -!- PATHWAY: Xenobiotic degradation; benzoate degradation via CoA ligation.
CC -!- SUBUNIT: Monomer. It is part of 2-halobenzoate dioxygenase two
CC component enzyme system. The other component is a dioxygenase component
CC consisting of 3 large (CbdA) subunits and 3 small (CbdB) subunits.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin reductase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X79076; CAA55683.1; -; Genomic_DNA.
DR AlphaFoldDB; Q51603; -.
DR SMR; Q51603; -.
DR KEGG; ag:CAA55683; -.
DR BioCyc; MetaCyc:MON-14765; -.
DR UniPathway; UPA00233; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010128; P:benzoate catabolic process via CoA ligation; IEA:UniProtKB-UniPathway.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Direct protein sequencing; FAD;
KW Flavoprotein; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase;
KW Plasmid.
FT CHAIN 1..339
FT /note="2-halobenzoate 1,2-dioxygenase electron transfer
FT component"
FT /id="PRO_0000167656"
FT DOMAIN 3..96
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 103..203
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 98..336
FT /note="Ferredoxin-reductase"
FT BINDING 40
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 45
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 80
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 339 AA; 37265 MW; 075DFCC7A9F9AE63 CRC64;
MLHSIALRFE DDVTYFITSS EHETVADAAY QHGIRIPLDC RNGVCGTCKG FCEHGEYDGG
DYIEDALSAD EAREGFVLPC QMQARTDCVV RILASSSACQ VKKSTMTGQM TEIDRGSSST
LQFTLAIDPS SKVDFLPGQY AQLRIPGTTE SRAYSYSSMP GSSHVTFLVR DVPNGKMSGY
LRNQATITET FTFDGPYGAF YLREPVRPIL MLAGGTGLAP FLSMLQYMAG LQRNDLPSVR
LVYGVNRDDD LVGLDKLDEL ATQLSGFSYI TTVVDKDSAQ LRRGYVTQQI TNDDMNGGDV
DIYVCGPPPM VEAVRSWLAA EKLNPVNFYF EKFAPTVGN
