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Database: UniProt
Entry: Q1QWN6
LinkDB: Q1QWN6
Original site: Q1QWN6 
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   13-FEB-2019, entry version 91.
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 DSM 3043 / ATCC BAA-138 / NCIMB
OS   13768).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3043 / ATCC BAA-138 / NCIMB 13768;
RX   PubMed=22675587; DOI=10.4056/sigs.2285059;
RA   Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W.,
RA   Detter J.C., Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S.,
RA   Bruce D., Goodwin L., Han C., Tapia R., Saunders E., Schmutz J.,
RA   Brettin T., Larimer F., Land M., Hauser L., Vargas C., Nieto J.J.,
RA   Kyrpides N.C., Ivanova N., Goker M., Klenk H.P., Csonka L.N.,
RA   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=DSM 3043 / ATCC BAA-138 / NCIMB 13768;
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
CC       pathway that only acts on the (S)-enantiomer of 3-sulfolactate.
CC       Together with ComC, provides a racemase system that converts (2S)-
CC       3-sulfolactate to (2R)-3-sulfolactate, which is degraded further
CC       by (2R)-sulfolactate sulfo-lyase. Specific for NAD. Also able to
CC       form sulfolactate from sulfopyruvate.
CC       {ECO:0000269|PubMed:20007648}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-3-sulfolactate + NAD(+) = 3-sulfopyruvate + H(+) +
CC         NADH; Xref=Rhea:RHEA:28194, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57940, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:61289; EC=1.1.1.310;
CC         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}.
DR   EMBL; CP000285; ABE59122.1; -; Genomic_DNA.
DR   RefSeq; WP_011507068.1; NC_007963.1.
DR   ProteinModelPortal; Q1QWN6; -.
DR   SMR; Q1QWN6; -.
DR   STRING; 290398.Csal_1770; -.
DR   PRIDE; Q1QWN6; -.
DR   EnsemblBacteria; ABE59122; ABE59122; Csal_1770.
DR   KEGG; csa:Csal_1770; -.
DR   eggNOG; ENOG4108JQ1; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000136700; -.
DR   KO; K16843; -.
DR   OMA; VCVMNTP; -.
DR   OrthoDB; 1638924at2; -.
DR   BioCyc; CSAL290398:G1GJB-1815-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-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   Complete proteome; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN         1    309       (S)-sulfolactate dehydrogenase.
FT                                /FTId=PRO_0000418761.
FT   NP_BIND     151    152       NAD. {ECO:0000250}.
FT   NP_BIND     231    233       NAD. {ECO:0000250}.
FT   NP_BIND     281    284       NAD. {ECO:0000250}.
FT   ACT_SITE    233    233       {ECO:0000250}.
FT   ACT_SITE    262    262       {ECO:0000250}.
FT   ACT_SITE    281    281       Proton donor. {ECO:0000250}.
FT   BINDING     171    171       NAD. {ECO:0000250}.
FT   BINDING     257    257       NAD. {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
//
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