ID   ISFD_CHRSD              Reviewed;         253 AA.
AC   Q1R183;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Sulfoacetaldehyde reductase;
DE            EC=1.1.1.313;
DE   AltName: Full=Isethionate formation reductase;
GN   Name=isfD; OrderedLocusNames=Csal_0161;
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, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   INDUCTION.
RC   STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX   PubMed=20133363; DOI=10.1099/mic.0.036699-0;
RA   Krejcik Z., Hollemeyer K., Smits T.H., Cook A.M.;
RT   "Isethionate formation from taurine in Chromohalobacter salexigens:
RT   purification of sulfoacetaldehyde reductase.";
RL   Microbiology 156:1547-1555(2010).
CC   -!- FUNCTION: Catalyzes the formation of isethionate from 2-
CC       sulfoacetaldehyde in the deaminative pathway of taurine. The enzyme is
CC       specific for NADPH; NADH is not a substrate. Responsible for most of
CC       the activity observed in taurine-grown cells.
CC       {ECO:0000269|PubMed:20133363}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hydroxyethane-1-sulfonate + NADP(+) = H(+) + NADPH +
CC         sulfoacetaldehyde; Xref=Rhea:RHEA:29591, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58246, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:61904; EC=1.1.1.313;
CC         Evidence={ECO:0000269|PubMed:20133363};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.13 mM for 2-sulfoacetaldehyde {ECO:0000269|PubMed:20133363};
CC         KM=0.061 mM for NADPH {ECO:0000269|PubMed:20133363};
CC       pH dependence:
CC         Optimum pH is 6.5-9.5. {ECO:0000269|PubMed:20133363};
CC   -!- PATHWAY: Organosulfur degradation.
CC   -!- SUBUNIT: Homodimer and heterotetramer. {ECO:0000269|PubMed:20133363}.
CC   -!- INDUCTION: By taurine. {ECO:0000269|PubMed:20133363}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; CP000285; ABE57525.1; -; Genomic_DNA.
DR   RefSeq; WP_011505471.1; NC_007963.1.
DR   AlphaFoldDB; Q1R183; -.
DR   SMR; Q1R183; -.
DR   STRING; 290398.Csal_0161; -.
DR   EnsemblBacteria; ABE57525; ABE57525; Csal_0161.
DR   KEGG; csa:Csal_0161; -.
DR   eggNOG; COG4221; Bacteria.
DR   HOGENOM; CLU_010194_2_10_6; -.
DR   OMA; ERKFDGH; -.
DR   OrthoDB; 1261526at2; -.
DR   BioCyc; MetaCyc:MON-16213; -.
DR   Proteomes; UP000000239; Chromosome.
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   Pfam; PF00106; adh_short; 1.
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   NADP; Oxidoreductase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..253
FT                   /note="Sulfoacetaldehyde reductase"
FT                   /id="PRO_0000418490"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         6..30
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   253 AA;  27183 MW;  F6414DE437BA55D0 CRC64;
     MTDCVFITGA TSGFGRAAAH RFAAAGWSLV LTGRRLERLE ALKEELQGRV PVHIIALDVR
     DSDVVDAAVA ALPEGFTRVR TLLNNAGLAL APQSAQHTDR SDWHTMIDTN VTGLVNVTHA
     LLPTLIDVGE GATIVNVGSI AGQWPYPGSH VYGASKAFVK QFSYNLRCDL LGTGVRVTDL
     APGIAETEFT LVRTGGDQAA SDALYRGTTA LTAEDIAEQM FYIATLPPHV NFNRLEVMPT
     RQAWSAFAID YDA