ID   SQD_PSEPU               Reviewed;         260 AA.
AC   P0DOV5;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2016, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Sulfoquinovose 1-dehydrogenase {ECO:0000305};
DE            Short=SQ dehydrogenase {ECO:0000303|PubMed:26195800};
DE            EC=1.1.1.390 {ECO:0000269|PubMed:26195800};
GN   ORFNames=PpSQ1_00405 {ECO:0000312|EMBL:KHL76346.1};
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 sulfoquinovose to 6-deoxy-6-sulfo-
CC       D-glucono-1,5-lactone, with a strong preference for NAD(+) as the
CC       electron acceptor. Is involved in a degradation pathway of
CC       sulfoquinovose (SQ) that allows P.putida SQ1 to use SQ as the sole
CC       carbon and energy source for growth. {ECO:0000269|PubMed:26195800}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-sulfo-D-quinovose + NAD(+) = 6-deoxy-6-sulfo-D-glucono-1,5-
CC         lactone + H(+) + NADH; Xref=Rhea:RHEA:47896, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:77132,
CC         ChEBI:CHEBI:88091; EC=1.1.1.390;
CC         Evidence={ECO:0000269|PubMed:26195800};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.5 mM for sulfoquinovose with NAD(+) as cosubstrate
CC         {ECO:0000269|PubMed:26195800};
CC         KM=2.4 mM for sulfoquinovose with NADP(+) as cosubstrate
CC         {ECO:0000269|PubMed:26195800};
CC         Vmax=62.8 umol/min/mg enzyme for sulfoquinovose oxidation with NAD(+)
CC         {ECO:0000269|PubMed:26195800};
CC         Vmax=2.7 umol/min/mg enzyme for sulfoquinovose oxidation with NADP(+)
CC         {ECO:0000269|PubMed:26195800};
CC         Note=kcat is 33.8 sec(-1) for sulfoquinovose oxidation with NAD(+).
CC         kcat is 1.4 sec(-1) for sulfoquinovose oxidation with NADP(+).
CC         {ECO:0000269|PubMed:26195800};
CC       pH dependence:
CC         Optimum pH is 8-9. {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 short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; JTCJ01000004; KHL76346.1; -; Genomic_DNA.
DR   RefSeq; WP_039601086.1; NZ_JTCJ01000004.1.
DR   AlphaFoldDB; P0DOV5; -.
DR   SMR; P0DOV5; -.
DR   KEGG; ag:KHL76346; -.
DR   BRENDA; 1.1.1.390; 5092.
DR   GO; GO:0016491; F:oxidoreductase activity; 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   NAD; Oxidoreductase.
FT   CHAIN           1..260
FT                   /note="Sulfoquinovose 1-dehydrogenase"
FT                   /id="PRO_0000438490"
FT   ACT_SITE        160
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
SQ   SEQUENCE   260 AA;  27870 MW;  C42210BE176A8289 CRC64;
     MNRHTDTHYP SLADKVVLIS GGASGIGRAF VEAFVAQGSR VAFLDLDAEA GQGLAHALGA
     NSLFLPCDVR DIERLKACVA EVERTWGAVD VLINNAARDD RHALADVSVE YWDERMQTNL
     RHAFFAAQAV APGMARRGSG AIINMGSISW MRGRPGMVCY TTAKAALNGM TRTLARELGG
     QGIRINSLVP GAIRTERQDA MWAADPAGLE AASQAFIDQQ MLKFRLDASD CARLALFLAS
     DDSRGCTGQN FVVDAGLSIQ