ID TSAD1_COMTE Reviewed; 476 AA.
AC P94682;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=4-(hydroxymethyl)benzenesulfonate dehydrogenase TsaD1;
DE EC=1.1.1.257;
DE AltName: Full=Toluenesulfonate aldehyde dehydrogenase TsaD;
GN Name=tsaD1;
OS Comamonas testosteroni (Pseudomonas testosteroni).
OG Plasmid pTSA.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=285;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11, 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=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 [4]
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 [5]
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 [6]
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.5}.
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 Evidence={ECO:0000269|PubMed:8828208};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9006050}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AH010657; AAC44808.1; -; Genomic_DNA.
DR AlphaFoldDB; P94682; -.
DR SMR; P94682; -.
DR KEGG; ag:AAC44808; -.
DR BioCyc; MetaCyc:TSADCOTE-MONOMER; -.
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 CDD; cd07103; ALDH_F5_SSADH_GabD; 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 PANTHER; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43353:SF5; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Direct protein sequencing; NAD; NADP;
KW Oxidoreductase; Plasmid.
FT CHAIN 1..476
FT /note="4-(hydroxymethyl)benzenesulfonate dehydrogenase
FT TsaD1"
FT /id="PRO_0000419117"
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 380
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 476 AA; 51011 MW; 58A7FA86AD2E1349 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
DFVDAFGATQ ALRVGAGMAA ETQMGPVASA RRQAAVQDLI ARSVAAGARP VASAVPEAGY
FVAPTLLADV PLDAPVMSEE PFGPVACAVP FDSLDQAIAQ ANHNPYGLAG YLFTDSAKAI
LAVSERLEVG SLAVNGMGVS VPEAPFGGVK DSGYGSESGT EGMEAFLDTK FMHYVA
//
