TSAB1_COMTE
ID TSAB1_COMTE Reviewed; 317 AA.
AC P94680;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Toluene-4-sulfonate monooxygenase system reductase subunit TsaB1;
DE EC=1.5.1.-;
DE AltName: Full=TS methylmonooxygenase system, reductase B;
DE AltName: Full=Toluenesulfonate methyl-monooxygenase reductase component TsaB1;
GN Name=tsaB1; Synonyms=tsaB;
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], PROTEIN SEQUENCE OF 3-30, AND SUBUNIT.
RC STRAIN=DSM 6577 / T-2;
RX PubMed=9006050; DOI=10.1128/jb.179.3.919-927.1997;
RA Junker F., Kiewitz R., Cook A.M.;
RT "Characterization of the p-toluenesulfonate operon tsaMBCD and tsaR in
RT Comamonas testosteroni T-2.";
RL J. Bacteriol. 179:919-927(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [3]
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).
RN [4]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX DOI=10.1099/00221287-137-9-2201;
RA Locher H.H., Malli C., Hooper S.W., Vorherr T., Leisinger T., Cook A.M.;
RT "Degradation of p-toluic acid (p-toluenecarboxylic acid) and p-
RT toluenesulphonic acid via oxygenation of the methyl sidechain is initiated
RT by the same set of enzymes in Comamonas testosteroni T-2.";
RL J. Gen. Microbiol. 137:2201-2208(1991).
CC -!- FUNCTION: Iron-sulfur flavoprotein carrying electrons from NADH to the
CC oxygenase TsaM. Involved in the toluene-4-sulfonate degradation
CC pathway. {ECO:0000269|Ref.4}.
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 {ECO:0000269|PubMed:9006050}.
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DR EMBL; AF311437; AAC44805.1; -; Genomic_DNA.
DR AlphaFoldDB; P94680; -.
DR SMR; P94680; -.
DR KEGG; ag:AAC44805; -.
DR BioCyc; MetaCyc:MON-5161; -.
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 1: Evidence at protein level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW Electron transport; Flavoprotein; FMN; Iron; Iron-sulfur; Metal-binding;
KW Monooxygenase; NAD; Oxidoreductase; Plasmid; Transport.
FT CHAIN 1..317
FT /note="Toluene-4-sulfonate monooxygenase system reductase
FT subunit TsaB1"
FT /id="PRO_0000419121"
FT DOMAIN 2..108
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT DOMAIN 230..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"
FT BINDING 304
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 317 AA; 34186 MW; EB21C7CE82CF965E CRC64;
MSADVPVTVA AVRAVARDVL ALELRHANGQ PLPGASAGAH IDLALPNGLV RQYSLVNATG
QATMDCYQVA VGWDANSRGG SVWIHEKLKV GQALRVTHRA TCSEMAPEHR RVLLLAGGIG
VTPIYAMAQA CAQQGVDVEL WASARSAPRL AYLEELKALL GQRLHLHADD EQGGPMNLTE
RLATQRWDAV YACGPAPMLD ALTAATAHWA PGSVRMERFK GAEQPASERQ PFELVLQRAG
LSTTVDAHES VLDAMERVGV DFPWSCREGI CGTCEAPVLE GEVQHLDYVL SPEERAEQRR
MMVCVSRCGG GRLVLDI
