TSAM1_COMTE
ID TSAM1_COMTE Reviewed; 347 AA.
AC P94679;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Toluene-4-sulfonate monooxygenase system iron-sulfur subunit TsaM1;
DE EC=1.14.14.-;
DE AltName: Full=TS methylmonooxygenase system, oxygenase M;
DE AltName: Full=Toluenesulfonate methyl-monooxygenase oxygenase component TsaM1;
GN Name=tsaM1; Synonyms=tsaM;
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 PROTEIN SEQUENCE OF 1-24 AND
RP 136-162.
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 PROTEIN SEQUENCE OF 1-17, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, AND SUBUNIT.
RX PubMed=2050632; DOI=10.1128/jb.173.12.3741-3748.1991;
RA Locher H.H., Leisinger T., Cook A.M.;
RT "4-Toluene sulfonate methyl-monooxygenase from Comamonas testosteroni T-2:
RT purification and some properties of the oxygenase component.";
RL J. Bacteriol. 173:3741-3748(1991).
RN [5]
RP PROTEIN SEQUENCE OF 1-11, 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: 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. Can use toluene-4-sulfonate, p-toluate, m-toluate and 4-
CC ethylbenzoate as substrates, but not p-xylene, toluene and p-cresol.
CC Catalyzes also the demethylation of 4-methoxybenzoate to 4-
CC hydroxybenzoate. {ECO:0000269|PubMed:2050632, ECO:0000269|Ref.5}.
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; Evidence={ECO:0000269|PubMed:2050632};
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. {ECO:0000269|PubMed:2050632}.
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DR EMBL; AF311437; AAC44804.1; -; Genomic_DNA.
DR AlphaFoldDB; P94679; -.
DR SMR; P94679; -.
DR KEGG; ag:AAC44804; -.
DR BioCyc; MetaCyc:TSAMCOTE-MON; -.
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 1: Evidence at protein level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Direct protein sequencing; FAD;
KW Flavoprotein; Iron; Iron-sulfur; Metal-binding; Monooxygenase;
KW Oxidoreductase; Plasmid.
FT CHAIN 1..347
FT /note="Toluene-4-sulfonate monooxygenase system iron-sulfur
FT subunit TsaM1"
FT /id="PRO_0000419119"
FT DOMAIN 7..109
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 50
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 67
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 70
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT CONFLICT 4..6
FT /note="RNC -> INN (in Ref. 4; AA sequence and 5; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="W -> A (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 39557 MW; 09594DE7F5DD222F CRC64;
MFIRNCWYVA AWDTEIPAEG LFHRTLLNEP VLLYRDTQGR VVALENRCCH RSAPLHIGRQ
EGDCVRCLYH GLKFNPSGAC VEIPGQEQIP PKTCIKSYPV VERNRLVWIW MGDPARANPD
DIVDYFWHDS PEWRMKPGYI HYQANYKLIV DNLLDFTHLA WVHPTTLGTD SAASLKPVIE
RDTTGTGKLT ITRWYLNDDM SNLHKGVAKF EGKADRWQIY QWSPPALLRM DTGSAPTGTG
APEGRRVPEA VQFRHTSIQT PETETTSHYW FCQARNFDLD DEALTEKIYQ GVVVAFEEDR
TMIEAHEKIL SQVPDRPMVP IAADAGLNQG RWLLDRLLKA ENGGTAP
