SLAD_PSEPU
ID SLAD_PSEPU Reviewed; 486 AA.
AC P0DOV9;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=3-sulfolactaldehyde dehydrogenase {ECO:0000303|PubMed:26195800};
DE Short=SLA dehydrogenase {ECO:0000303|PubMed:26195800};
DE EC=1.2.1.97 {ECO:0000269|PubMed:26195800};
GN ORFNames=PpSQ1_00395 {ECO:0000312|EMBL:KHL76344.1};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SQ1;
RX PubMed=27408681; DOI=10.1186/s40793-015-0033-x;
RA Felux A.K., Franchini P., Schleheck D.;
RT "Permanent draft genome sequence of sulfoquinovose-degrading Pseudomonas
RT putida strain SQ1.";
RL Stand. Genomic Sci. 10:42-42(2015).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC STRAIN=SQ1;
RX PubMed=26195800; DOI=10.1073/pnas.1507049112;
RA Felux A.K., Spiteller D., Klebensberger J., Schleheck D.;
RT "Entner-Doudoroff pathway for sulfoquinovose degradation in Pseudomonas
RT putida SQ1.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E4298-E4305(2015).
CC -!- FUNCTION: Catalyzes the oxidation of (2S)-3-sulfolactaldehyde to (2S)-
CC 3-sulfolactate, using both NAD(+) and NADP(+) as electron acceptors. Is
CC involved in a degradation pathway of sulfoquinovose (SQ) that allows
CC P.putida SQ1 to use SQ as the sole carbon and energy source for growth.
CC {ECO:0000269|PubMed:26195800}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-3-sulfolactaldehyde + H2O + NADP(+) = (2S)-3-sulfolactate
CC + 2 H(+) + NADPH; Xref=Rhea:RHEA:47928, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:61289, ChEBI:CHEBI:90109; EC=1.2.1.97;
CC Evidence={ECO:0000269|PubMed:26195800};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-3-sulfolactaldehyde + H2O + NAD(+) = (2S)-3-sulfolactate
CC + 2 H(+) + NADH; Xref=Rhea:RHEA:47932, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:61289, ChEBI:CHEBI:90109; EC=1.2.1.97;
CC Evidence={ECO:0000269|PubMed:26195800};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mM for 4-oxobutanoate with NAD(+) as cosubstrate
CC {ECO:0000269|PubMed:26195800};
CC KM=0.14 mM for 4-oxobutanoate with NADP(+) as cosubstrate
CC {ECO:0000269|PubMed:26195800};
CC Vmax=12.6 umol/min/mg enzyme for 4-oxobutanoate oxidation with NAD(+)
CC {ECO:0000269|PubMed:26195800};
CC Vmax=12.2 umol/min/mg enzyme for 4-oxobutanoate oxidation with
CC NADP(+) {ECO:0000269|PubMed:26195800};
CC Note=kcat is 11.8 sec(-1) for 4-oxobutanoate oxidation with NAD(+).
CC kcat is 11.4 sec(-1) for 4-oxobutanoate oxidation with NADP(+).
CC {ECO:0000269|PubMed:26195800};
CC -!- INDUCTION: Is highly up-regulated during growth on sulfoquinovose,
CC compared to growth on glucose or succinate (at protein level).
CC {ECO:0000269|PubMed:26195800}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; JTCJ01000004; KHL76344.1; -; Genomic_DNA.
DR RefSeq; WP_039601084.1; NZ_JTCJ01000004.1.
DR AlphaFoldDB; P0DOV9; -.
DR SMR; P0DOV9; -.
DR GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IEA:InterPro.
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; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR010102; Succ_semiAld_DH.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01780; SSADH; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW NAD; NADP; Oxidoreductase.
FT CHAIN 1..486
FT /note="3-sulfolactaldehyde dehydrogenase"
FT /id="PRO_0000438494"
FT ACT_SITE 256
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT ACT_SITE 290
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 157..158
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 181..184
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 234..235
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 257
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 387
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P25526"
SQ SEQUENCE 486 AA; 52149 MW; BD0D663F48A255FC CRC64;
MLELKDPSLL KQQAFIDGLW VSADSGETFA VTNPATGDEL ARIPQMGAAE AERAVLAAHR
AFKPWKRKTA KERAELLQRW YALMLENQED LARLLTAEQG KPLAEAHGEL GNGMSFVQWF
AEEAKRVYGD TIPQPSADKR LIVTKEPIGV TAAITPWNFP HAMITRKVAP ALAAGCSMVL
RPASQTPLSA LALVALAERA GIPAGVFSVV TGSATQIGSV LTGHPLVRKF SFTGSTPVGK
LLIGQCAETV KKVSMELGGN APFIVFDDAD LDLAVEGAML SKFRNAGQTC VCANRIYVQD
GIYERFAEKL AAAASGLRLG NGVEAGVTQG PMIDENAVRK VEEHISDALE KGARLIAGGQ
RHALGGSFFE PTVLTEVTAQ MKVAHEETFG PLAPLFRFSS EDEVVELANA TEFGLASYFY
SRDIGRVLRV SEDLEYGMVG VNTAAIANEM APFGGVKQSG LGREGSRYGI EDYLEIKYVC
LGGVDR
