CBAA_COMTE
ID CBAA_COMTE Reviewed; 432 AA.
AC Q44256; O08105;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=3-chlorobenzoate-3,4-dioxygenase oxygenase subunit;
DE EC=1.14.-.-;
GN Name=cbaA;
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).
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000305};
CC Note=Binds 1 Fe cation. {ECO:0000305};
CC -!- SUBUNIT: This dioxygenase system consists of two proteins: an oxygenase
CC and an oxygenase reductase.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000305}.
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DR EMBL; U18133; AAC45716.1; -; Genomic_DNA.
DR AlphaFoldDB; Q44256; -.
DR SMR; Q44256; -.
DR BioCyc; MetaCyc:MON-14756; -.
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 Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR045623; LigXa_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR Pfam; PF19301; LigXa_C; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase.
FT CHAIN 1..432
FT /note="3-chlorobenzoate-3,4-dioxygenase oxygenase subunit"
FT /id="PRO_0000085050"
FT DOMAIN 27..133
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 69
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 71
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 88
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 91
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 180
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 432 AA; 48927 MW; 216CF50FE14EBEE2 CRC64;
MALTKDNEDL VRVGRGTPMG GLMREYWIPA LKSTELEAGG SPVRLLLLGE KLVAFREPSG
AVGVMDSRCP HRGVSLFMGR VEEGGLRCVY HGWKFSAEGK CVDMPSVRPE DEFKNSVRVA
RYPVKEMAGV VWVYMGTRKV LPELPRLEVL NLPENEVDVI CLQRKSNWLQ NLEGEIDTSH
FNFLHVGGLH ADEVPDDHPL KYTAQVAPQY LVKETALGTC YAAQVPAEED HTYTRFAHFL
FPFWALIPQA DIAQNILARA WVPMDDEHTM MFFFRWTGSK AKRLDTPLKS GSPMPGVTLT
DMKYKENTTD WYGRWQPLGD ESNDWLIDRD LQKVGRVFSG IYGIHAQDQA MTDSMGPIID
HGLEQLAPTD LMIVRTRRRI LKALRAHEAN GTLPPGVDEA DQYFTPRSGY YLTPKSVDWE
TAYEQRIEGL VR