ID   SUYA_CHRSD              Reviewed;          94 AA.
AC   Q1QWP1;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=(2R)-sulfolactate sulfo-lyase subunit alpha;
DE            EC=4.4.1.24 {ECO:0000269|PubMed:20007648};
DE   AltName: Full=Sulfolactate sulfo-lyase A;
GN   Name=suyA; OrderedLocusNames=Csal_1765;
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 SUBUNIT.
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: Together with SuyB, desulfonates sulfolactate to pyruvate and
CC       sulfite. {ECO:0000269|PubMed:20007648}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-sulfolactate = H(+) + pyruvate + sulfite;
CC         Xref=Rhea:RHEA:21428, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17359, ChEBI:CHEBI:58738; EC=4.4.1.24;
CC         Evidence={ECO:0000269|PubMed:20007648};
CC   -!- SUBUNIT: (2R)-sulfolactate sulfo-lyase is composed of a SuyA and a SuyB
CC       subunit. {ECO:0000305|PubMed:20007648}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; CP000285; ABE59117.1; -; Genomic_DNA.
DR   RefSeq; WP_011507063.1; NC_007963.1.
DR   AlphaFoldDB; Q1QWP1; -.
DR   SMR; Q1QWP1; -.
DR   STRING; 290398.Csal_1765; -.
DR   EnsemblBacteria; ABE59117; ABE59117; Csal_1765.
DR   KEGG; csa:Csal_1765; -.
DR   eggNOG; COG2721; Bacteria.
DR   HOGENOM; CLU_084161_2_0_6; -.
DR   OMA; NCKTKRW; -.
DR   OrthoDB; 1994547at2; -.
DR   BioCyc; MetaCyc:MON-15869; -.
DR   Proteomes; UP000000239; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0034010; F:sulfolactate sulfo-lyase activity; IEA:UniProtKB-EC.
DR   CDD; cd11613; SAF_AH_GD; 1.
DR   InterPro; IPR013974; SAF.
DR   InterPro; IPR044144; UxaA/GarD_SAF.
DR   Pfam; PF08666; SAF; 1.
DR   SMART; SM00858; SAF; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Lyase; Reference proteome.
FT   CHAIN           1..94
FT                   /note="(2R)-sulfolactate sulfo-lyase subunit alpha"
FT                   /id="PRO_0000418741"
FT   DOMAIN          16..90
FT                   /note="AFP-like"
SQ   SEQUENCE   94 AA;  10548 MW;  C44078207E145C5B CRC64;
     MSIDFVVHDA DDAVGVVVVE GVEAGQMLTG WVMDQDRTLQ FEVKDAIPIG HKLAIRDLAE
     DETVIKYSVD IGRVVQSIRQ GEHVHVHNVK TKRW