ID   TSAD2_COMTE             Reviewed;         477 AA.
AC   Q9AHG1;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Putative 4-(hydroxymethyl)benzenesulfonate dehydrogenase TsaD2;
DE            EC=1.1.1.257;
DE   AltName: Full=Toluenesulfonate aldehyde dehydrogenase TsaD;
GN   Name=tsaD2;
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=13680097; DOI=10.1007/s00203-003-0594-8;
RA   Tralau T., Cook A.M., Ruff J.;
RT   "An additional regulator, TsaQ, is involved with TsaR in regulation of
RT   transport during the degradation of p-toluenesulfonate in Comamonas
RT   testosteroni T-2.";
RL   Arch. Microbiol. 180:319-326(2003).
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).
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}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-(hydroxymethyl)benzenesulfonate + NAD(+) = 4-
CC         formylbenzenesulfonate + H(+) + NADH; Xref=Rhea:RHEA:24412,
CC         ChEBI:CHEBI:11944, ChEBI:CHEBI:11987, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.257;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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; AAK37995.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AHG1; -.
DR   SMR; Q9AHG1; -.
DR   GO; GO:0018462; F:4-(hydroxymethyl)benzenesulfonate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   5: Uncertain;
KW   Aromatic hydrocarbons catabolism; NAD; Oxidoreductase; Plasmid.
FT   CHAIN           1..477
FT                   /note="Putative 4-(hydroxymethyl)benzenesulfonate
FT                   dehydrogenase TsaD2"
FT                   /id="PRO_0000419118"
FT   ACT_SITE        252
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        286
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         154..155
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         178..181
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         230..231
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         381
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   477 AA;  51082 MW;  0BF5679664D90173 CRC64;
     MSTVLYRCPE LLIGGEWRPG RHEQRLVVRN PATGEPLDEL RLASADDLQL ALQTTQQAFE
     HWRQVPAHER CARLERGVAR LRENTERIAH LLTLEQGKTL AEARMECAMA ADLIKWYAEE
     ARRVYGRVIP ARLPNSRMEV FKFPVGPVAA FSPWNFPLVL SARKLGGAIA AGCSIVLKAA
     EETPASVAAM VDCLNQELPP GVVQLLYGVP AEVSQALIAS PVVRKVTFTG SVPVGRHLAE
     LSARHLKRIT LELGGHAPVI VCGDADIART VNLMVQHKFR NAGQACLAPT RFFVDRRIYG
     DFVDAFGAAT QALRVGAGMA AETQMGPVAS ARRQAAVQDL IARSVAAGAR PVASAVPEAG
     YFVAPTLLAD VPLDAPVMSE EPFGPVACAV PFDSLDQAIA QANHNPYGLA GYLFTDSAKA
     ILAVSERLEV GSLAVNGMGV SVPEAPFGGV KDSGYGSESG TEGMEAFLDT KFMHYVA