ID   TSAC_COMTE              Reviewed;         252 AA.
AC   P94681;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=4-formylbenzenesulfonate dehydrogenase TsaC1/TsaC2;
DE            EC=1.2.1.62;
DE   AltName: Full=Toluenesulfonate zinc-independent alcohol dehydrogenase TsaC;
GN   Name=tsaC1; Synonyms=tsaC;
GN   and
GN   Name=tsaC2;
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 1-10, AND SUBUNIT.
RC   STRAIN=DSM 6577 / T-2; PLASMID=pTSA;
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; PLASMID=pTSA;
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; PLASMID=pTSA;
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).
RN   [5]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=8828208; DOI=10.1099/00221287-142-9-2419;
RA   Junker F., Saller E., Schlaefli Oppenberg H.R., Kroneck P.M., Leisinger T.,
RA   Cook A.M.;
RT   "Degradative pathways for p-toluenecarboxylate and p-toluenesulfonate and
RT   their multicomponent oxygenases in Comamonas testosteroni strains PSB-4 and
RT   T-2.";
RL   Microbiology 142:2419-2427(1996).
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. {ECO:0000269|PubMed:8828208, ECO:0000269|Ref.4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-formylbenzenesulfonate + H2O + NAD(+) = 4-sulfobenzoate + 2
CC         H(+) + NADH; Xref=Rhea:RHEA:18833, ChEBI:CHEBI:11987,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:20476,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.62;
CC         Evidence={ECO:0000269|PubMed:8828208};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9006050}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
CC   -!- CAUTION: TsaC2 is probably the product of a pseudogene and is not
CC       expressed, due to the absence of promoter-like sequences upstream of
CC       the operon tsaMBCD2. {ECO:0000305|PubMed:11282598}.
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DR   EMBL; AF311437; AAC44807.1; -; Genomic_DNA.
DR   EMBL; AF311437; AAK37998.1; -; Genomic_DNA.
DR   AlphaFoldDB; P94681; -.
DR   SMR; P94681; -.
DR   KEGG; ag:AAC44807; -.
DR   BioCyc; MetaCyc:TSACCOTE-MON; -.
DR   GO; GO:0018482; F:4-formylbenzenesulfonate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Direct protein sequencing; NAD;
KW   Oxidoreductase; Plasmid.
FT   CHAIN           1..252
FT                   /note="4-formylbenzenesulfonate dehydrogenase TsaC1/TsaC2"
FT                   /id="PRO_0000419116"
FT   ACT_SITE        155
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         9..36
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   252 AA;  26438 MW;  763A74DDABD2755C CRC64;
     MNLNKQVAIV TGGASGFGAA IARRLSQAGA AVLVADLNAE GAQRMATELN AAGGRALGMA
     CDVSKEADYR AVVDAAIAQL GGLHIVVNNA GTTHRNKPAL AVTEDEFDRV YRVNLKSVYW
     SAQCALPHFA QQGHGVMVNV ASTTGVRPGP GLTWYSGSKA AMINLTKGLA LEFARSGVRI
     NAVNPMIGET PMMADFMGME DTPANRERFL SRIPLGRFTR PDDVASAVAF LASDDASFLT
     GVCLDVDGGR NI