ID   TSAB2_COMTE             Reviewed;         317 AA.
AC   Q9AHG2;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Putative toluene-4-sulfonate monooxygenase system reductase subunit TsaB2;
DE            EC=1.5.1.-;
DE   AltName: Full=Toluenesulfonate methyl-monooxygenase reductase component TsaB2;
GN   Name=tsaB2;
OS   Comamonas testosteroni (Pseudomonas testosteroni).
OG   Plasmid pTSA.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND LACK OF EXPRESSION.
RC   STRAIN=DSM 6577 / T-2;
RX   PubMed=11282598; DOI=10.1128/aem.67.4.1508-1516.2001;
RA   Tralau T., Cook A.M., Ruff J.;
RT   "Map of the IncP1beta plasmid pTSA encoding the widespread genes (tsa) for
RT   p-toluenesulfonate degradation in Comamonas testosteroni T-2.";
RL   Appl. Environ. Microbiol. 67:1508-1516(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 6577 / T-2;
RX   PubMed=15176949; DOI=10.1042/bj20040652;
RA   Mampel J., Maier E., Tralau T., Ruff J., Benz R., Cook A.M.;
RT   "A novel outer-membrane anion channel (porin) as part of a putatively two-
RT   component transport system for 4-toluenesulphonate in Comamonas
RT   testosteroni T-2.";
RL   Biochem. J. 383:91-99(2004).
CC   -!- FUNCTION: Involved in the toluene-4-sulfonate degradation pathway.
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Monomer. Part of the p-toluenesulfonate methyl-monooxygenase
CC       complex TsaBM, comprising the reductase TsaB and the oxygenase TsaM.
CC   -!- CAUTION: Could be the product of a pseudogene. Probably not expressed,
CC       due to the absence of promoter-like sequences upstream of the operon
CC       tsaMBCD2 (PubMed:11282598). {ECO:0000305|PubMed:11282598}.
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DR   EMBL; AF311437; AAK37997.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AHG2; -.
DR   SMR; Q9AHG2; -.
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:0004497; F:monooxygenase 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; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR000951; Ph_dOase_redase.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 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   5: Uncertain;
KW   2Fe-2S; Aromatic hydrocarbons catabolism; Electron transport; Flavoprotein;
KW   FMN; Iron; Iron-sulfur; Metal-binding; Monooxygenase; NAD; Oxidoreductase;
KW   Plasmid; Transport.
FT   CHAIN           1..317
FT                   /note="Putative toluene-4-sulfonate monooxygenase system
FT                   reductase subunit TsaB2"
FT                   /id="PRO_0000419122"
FT   DOMAIN          4..106
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   DOMAIN          232..317
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         110..220
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         271
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         274
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ   SEQUENCE   317 AA;  34215 MW;  55ECF057AD09F460 CRC64;
     MSADVPVTVA AVRAVARDVL ALELRHANGQ PLPGASAGAH IDLALPNGLV RQYSLVNATG
     QATMDCYQVA VGWDANSRGG SVWIHEKLKV GQALRVSAPR NLFEMAPEHR RVLLLAGGIG
     VTPIYAMAQA CAQQGVDVEL WASARSAPRL AYLEELKALL GQRLHLHADD EQGGPMNLTE
     RLATQRWDAV YACGPAPMLD ALTAATAHWA PGSVRMERFK GAEQPASERQ PFELVLQRAG
     LSTTVDAHES VLDAMERVGV DFPWSCREGI CGTCEAPVLE GEVQHLDYVL SPEERAEQRR
     MMVCVSRCGG GRLVLDI