ID   ISFD2_CHRSD             Reviewed;         252 AA.
AC   Q1QU27;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Sulfoacetaldehyde reductase 2;
DE            EC=1.1.1.313;
DE   AltName: Full=Isethionate formation reductase 2;
GN   Name=isfD2; OrderedLocusNames=Csal_2684;
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, AND 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. Constitutively
CC       expressed enzyme that only mediates a small part of the activity
CC       observed in taurine-grown cells. {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   -!- PATHWAY: Organosulfur degradation.
CC   -!- SUBUNIT: Homodimer and heterotetramer. {ECO:0000269|PubMed:20133363}.
CC   -!- INDUCTION: Constitutively expressed. {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; ABE60031.1; -; Genomic_DNA.
DR   RefSeq; WP_011507977.1; NC_007963.1.
DR   AlphaFoldDB; Q1QU27; -.
DR   SMR; Q1QU27; -.
DR   STRING; 290398.Csal_2684; -.
DR   PRIDE; Q1QU27; -.
DR   EnsemblBacteria; ABE60031; ABE60031; Csal_2684.
DR   KEGG; csa:Csal_2684; -.
DR   eggNOG; COG4221; Bacteria.
DR   HOGENOM; CLU_010194_2_10_6; -.
DR   OMA; VMMMPED; -.
DR   OrthoDB; 1261526at2; -.
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..252
FT                   /note="Sulfoacetaldehyde reductase 2"
FT                   /id="PRO_0000418491"
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   252 AA;  27318 MW;  8CA5248DE5D94BCC CRC64;
     MSDIVLITGA TSGFGRAAAR RFADAGWSLI LTGRREERLT ELAEELSQRV RVHTAVLDVR
     DEKAVQSVID ELPEAFRRVK TLVNNAGLAL APQPAQDVDL ADWHTMIDTN IKGLVNVTHA
     VLPTLIETGA GASIVNLGSV AGQWPYPGSH VYGASKAFVQ QFTYNLRCDL QGTGVRVTDV
     APGMAETEFT LVRTGGDQAA SDALYRDTTP LQAEDVAELI FYTATLPAHV NVNRLEVMPT
     RQAWSAFAVD RD