ID   SLCC_CHRSD              Reviewed;         309 AA.
AC   Q1QWN6;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=(S)-sulfolactate dehydrogenase;
DE            EC=1.1.1.310;
DE   AltName: Full=(2S)-3-sulfolactate dehydrogenase;
DE   AltName: Full=(S)-sulfolactate oxidoreductase;
GN   Name=slcC; OrderedLocusNames=Csal_1770;
OS   Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS   NCIMB 13768 / 1H11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX   PubMed=22675587; DOI=10.4056/sigs.2285059;
RA   Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA   Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA   Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA   Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA   Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT   "Complete genome sequence of the halophilic and highly halotolerant
RT   Chromohalobacter salexigens type strain (1H11(T)).";
RL   Stand. Genomic Sci. 5:379-388(2011).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX   PubMed=20007648; DOI=10.1099/mic.0.034736-0;
RA   Denger K., Cook A.M.;
RT   "Racemase activity effected by two dehydrogenases in sulfolactate
RT   degradation by Chromohalobacter salexigens: purification of (S)-
RT   sulfolactate dehydrogenase.";
RL   Microbiology 156:967-974(2010).
CC   -!- FUNCTION: Dehydrogenase of the (R,S)-sulfolactate degradation pathway
CC       that only acts on the (S)-enantiomer of 3-sulfolactate. Together with
CC       ComC, provides a racemase system that converts (2S)-3-sulfolactate to
CC       (2R)-3-sulfolactate, which is degraded further by (2R)-sulfolactate
CC       sulfo-lyase. Specific for NAD. Also able to form sulfolactate from
CC       sulfopyruvate. {ECO:0000269|PubMed:20007648}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-3-sulfolactate + NAD(+) = 3-sulfopyruvate + H(+) + NADH;
CC         Xref=Rhea:RHEA:28194, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57940, ChEBI:CHEBI:57945, ChEBI:CHEBI:61289;
CC         EC=1.1.1.310; Evidence={ECO:0000269|PubMed:20007648};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2 mM for NAD {ECO:0000269|PubMed:20007648};
CC         KM=7 mM for (2S)-3-sulfolactate {ECO:0000269|PubMed:20007648};
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; CP000285; ABE59122.1; -; Genomic_DNA.
DR   RefSeq; WP_011507068.1; NC_007963.1.
DR   AlphaFoldDB; Q1QWN6; -.
DR   SMR; Q1QWN6; -.
DR   STRING; 290398.Csal_1770; -.
DR   EnsemblBacteria; ABE59122; ABE59122; Csal_1770.
DR   KEGG; csa:Csal_1770; -.
DR   eggNOG; COG0111; Bacteria.
DR   HOGENOM; CLU_019796_1_3_6; -.
DR   OMA; EQALFMM; -.
DR   OrthoDB; 1638924at2; -.
DR   BioCyc; MetaCyc:MON-15867; -.
DR   Proteomes; UP000000239; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0102155; F:S-sulfolactate dehydrogenase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..309
FT                   /note="(S)-sulfolactate dehydrogenase"
FT                   /id="PRO_0000418761"
FT   ACT_SITE        233
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        262
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        281
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         151..152
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         231..233
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         281..284
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   309 AA;  33135 MW;  4B2AC12D988EC3E1 CRC64;
     MSDVLISEFM DEAAVADLER DCSVTFDATL VDDRARLLSS GAGVRALIVR NRTRVDRELL
     ARFPDLRAVG RLGVGLDNID VDACRESDIA VLPATGGNTV SVAEYVLTGI FMLRRGAYLS
     TPRVLAGEWP RQALMGHETQ GATLGLVGFG GIARDLARRA QCLGMQVMAH DPFVPADDAA
     WQTVERAERL ATLLEKADAV SLHVPLSEGT RHLIDGEALA TMKPGSLLIN TARGGIVDER
     ALAASLRDRH LGGAMLDVFE EEPLTADSVL SGVEGLIATP HIAGVTHESN ERISWITVDN
     VRRALGVRA