ID   CBAB_COMTE              Reviewed;         315 AA.
AC   Q44257; O08106;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=3-chlorobenzoate-3,4-dioxygenase reductase subunit;
DE            EC=1.14.-.-;
GN   Name=cbaB;
OS   Comamonas testosteroni (Pseudomonas testosteroni).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BR60 / Isolate Bloody Run creek; TRANSPOSON=Tn5271;
RX   PubMed=7704279; DOI=10.1099/13500872-141-2-485;
RA   Nakatsu C.H., Straus N.A., Wyndham R.C.;
RT   "The nucleotide sequence of the Tn5271 3-chlorobenzoate 3,4-dioxygenase
RT   genes (cbaAB) unites the class IA oxygenases in a single lineage.";
RL   Microbiology 141:485-495(1995).
RN   [2]
RP   SEQUENCE REVISION.
RA   Wyndham R.C.;
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC   -!- SUBUNIT: This dioxygenase system consists of two proteins: phthalate
CC       oxygenase and phthalate oxygenase reductase.
CC   -!- SIMILARITY: Belongs to the PDR/VanB family. {ECO:0000305}.
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DR   EMBL; U18133; AAC45717.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q44257; -.
DR   SMR; Q44257; -.
DR   PRIDE; Q44257; -.
DR   BioCyc; MetaCyc:MON-14757; -.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
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; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR000951; Ph_dOase_redase.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   PRINTS; PR00409; PHDIOXRDTASE.
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   3: Inferred from homology;
KW   2Fe-2S; Aromatic hydrocarbons catabolism; Electron transport; Flavoprotein;
KW   FMN; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Transport.
FT   CHAIN           1..315
FT                   /note="3-chlorobenzoate-3,4-dioxygenase reductase subunit"
FT                   /id="PRO_0000189395"
FT   DOMAIN          7..109
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   DOMAIN          228..315
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         1..103
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         264
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         269
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         272
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         302
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ   SEQUENCE   315 AA;  34669 MW;  B88E16DA94A8E7A3 CRC64;
     MVAIDQHDTY SVRVISRSHL SKDIVQVELE ESSQRPLPDY EPGSHVDIYV QDDLVRQYSL
     VKASDAQASY QIAFKVKRDQ GSATELMCEL LRVGATTRIS APRNAFALDP QARETVLICG
     GIGITPMVHM AMTLVKAKRP WSMHIASRDG DELDLLGPLG SCSEISRYIS SQGDRLPIRD
     LAERAPANAH LYFCGPEGML QEFLAATQHR DPATVHYEQF QAAPSTGNEF TVNLARSGAQ
     YVVREGETIL DVLRNAGHHV TSSCRQGICG MCETTLISGV PDHRDRLLTD SEKASGRTML
     ICCSRALSPE LTLDL