ID   TSAM2_COMTE             Reviewed;         346 AA.
AC   Q9AHG3;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Putative toluene-4-sulfonate monooxygenase system iron-sulfur subunit TsaM2;
DE            EC=1.14.14.-;
DE   AltName: Full=Toluenesulfonate methyl-monooxygenase oxygenase component TsaM2;
GN   Name=tsaM2;
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).
RN   [3]
RP   FUNCTION.
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: Involved in the toluene-4-sulfonate degradation pathway. Does
CC       not discriminate between the sulfonate and the carboxyl substituents
CC       and can also be involved in the p-toluenecarboxylate degradation
CC       pathway (By similarity). {ECO:0000250, ECO:0000269|Ref.3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADH + O2 + toluene-4-sulfonate = 4-
CC         (hydroxymethyl)benzenesulfonate + H2O + NAD(+); Xref=Rhea:RHEA:51024,
CC         ChEBI:CHEBI:11944, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:27023, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945;
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.;
CC   -!- SUBUNIT: Homotetramer. Part of the p-toluenesulfonate methyl-
CC       monooxygenase complex TsaBM, comprising the reductase TsaB and the
CC       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; AAK37996.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AHG3; -.
DR   SMR; Q9AHG3; -.
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:0018652; F:toluene-sulfonate methyl-monooxygenase activity; IEA:RHEA.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.102.10.10; -; 1.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR044043; VanA_C_cat.
DR   Pfam; PF00355; Rieske; 1.
DR   Pfam; PF19112; VanA_C; 1.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   5: Uncertain;
KW   2Fe-2S; Aromatic hydrocarbons catabolism; FAD; Flavoprotein; Iron;
KW   Iron-sulfur; Metal-binding; Monooxygenase; Oxidoreductase; Plasmid.
FT   CHAIN           1..346
FT                   /note="Putative toluene-4-sulfonate monooxygenase system
FT                   iron-sulfur subunit TsaM2"
FT                   /id="PRO_0000419120"
FT   DOMAIN          7..108
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         47
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         49
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         66
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
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"
SQ   SEQUENCE   346 AA;  38884 MW;  0222DA7E58859CB9 CRC64;
     MLVKNTWYVA GMATDCSRKP LARTFLNEKV VLFRTHDGHA VALEDRCCHR LAPLSLGDVE
     DAGIRCRYHG MVFNASGACV EIPGQEQIPP GMCVRRFPLV ERHGLLWIWM GDPARANPDD
     IVDELWNGAP EWRTDSGYIH YQANYQLIVD NLLDFTHLAW VHPTTLGTDS AASLKPVIER
     DTTGTGKLTI TRWYLNDDMS NLHKGVAKFE GKADRWQIYQ WSPPALLRMD TGSAPTGTGA
     PEGRRVPEAV QFRHTSIQTP ETETTSHYWF CQARNFDLDD EALTEKIYQG VVVAFEEDRT
     MIEAQQKILS QVPDRPMVPI AADAGLNQGR WLLDRLLKAE NGGTAP