ISFD_KLEOX
ID ISFD_KLEOX Reviewed; 254 AA.
AC D3U1D9;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Sulfoacetaldehyde reductase;
DE EC=1.1.1.313;
DE AltName: Full=Isethionate formation reductase;
GN Name=isfD;
OS Klebsiella oxytoca.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=571;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=TauN1;
RX PubMed=15883781; DOI=10.1007/s00203-005-0776-7;
RA Styp von Rekowski K., Denger K., Cook A.M.;
RT "Isethionate as a product from taurine during nitrogen-limited growth of
RT Klebsiella oxytoca TauN1.";
RL Arch. Microbiol. 183:325-330(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=TauN1;
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.
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:15883781, ECO:0000269|PubMed:20133363};
CC -!- PATHWAY: Organosulfur degradation.
CC -!- SUBUNIT: Homodimer and heterotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; FJ711704; ACV83928.1; -; Genomic_DNA.
DR EMBL; GQ168677; ADK20104.1; -; Genomic_DNA.
DR RefSeq; WP_049087080.1; NZ_CABGNO010000007.1.
DR PDB; 6IXJ; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-254.
DR PDBsum; 6IXJ; -.
DR AlphaFoldDB; D3U1D9; -.
DR SMR; D3U1D9; -.
DR STRING; 571.MC52_15935; -.
DR PATRIC; fig|571.110.peg.1505; -.
DR eggNOG; COG4221; Bacteria.
DR OrthoDB; 1261526at2; -.
DR BioCyc; MetaCyc:MON-16212; -.
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 3D-structure; Direct protein sequencing; NADP; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15883781"
FT CHAIN 2..254
FT /note="Sulfoacetaldehyde reductase"
FT /id="PRO_0000418489"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 8..32
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:6IXJ"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:6IXJ"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:6IXJ"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:6IXJ"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:6IXJ"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:6IXJ"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:6IXJ"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:6IXJ"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:6IXJ"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:6IXJ"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6IXJ"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:6IXJ"
FT HELIX 114..130
FT /evidence="ECO:0007829|PDB:6IXJ"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:6IXJ"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6IXJ"
FT HELIX 152..171
FT /evidence="ECO:0007829|PDB:6IXJ"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:6IXJ"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:6IXJ"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:6IXJ"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:6IXJ"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:6IXJ"
FT STRAND 232..241
FT /evidence="ECO:0007829|PDB:6IXJ"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6IXJ"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:6IXJ"
SQ SEQUENCE 254 AA; 27296 MW; E30DF1A14A429EA7 CRC64;
MATSKVVFIT GATSGFGEAA AQVFADAGWS LVLSGRRFER LKTLQDKLAS QVPVHIIELD
VRDSDSVAAA VAALPADFAD ITTLINNAGL ALSPQPAQKV DLDDWKTMID TNVTGLVNVT
HALLPTLINH GAGASIINIG SIAGQWPYPG SHVYGASKAF VKQFSYNLRC DLLGTGVRVT
DLAPGIAETE FTLVRTKGDQ AASDNLYRGT TPLSARDIAE QMFYIATLPD HMNINRVEVM
PVRQAWQPFA IDRD
