SQUU_SALTY
ID SQUU_SALTY Reviewed; 298 AA.
AC Q9L7S0;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=3-sulfolactaldehyde reductase {ECO:0000255|HAMAP-Rule:MF_01913};
DE Short=SLA reductase {ECO:0000255|HAMAP-Rule:MF_01913};
DE EC=1.1.1.373 {ECO:0000255|HAMAP-Rule:MF_01913};
GN Name=yihU; OrderedLocusNames=STM4023;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RA Krogan N.J., Zhang R., Neuhard J., Kelln R.A.;
RT "Utilization of dihydroorotate as sole pyrimidine source by Salmonella
RT typhimurium.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Reduces 3-sulfolactaldehyde (SLA) to 2,3-dihydroxypropane 1-
CC sulfonate (DHPS). {ECO:0000255|HAMAP-Rule:MF_01913}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-3-sulfopropanediol + NAD(+) = (2S)-3-sulfolactaldehyde +
CC H(+) + NADH; Xref=Rhea:RHEA:40511, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90109,
CC ChEBI:CHEBI:176527; EC=1.1.1.373; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01913};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:40513;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01913};
CC -!- SIMILARITY: Belongs to the HIBADH-related family. 3-sulfolactaldehyde
CC reductase subfamily. {ECO:0000255|HAMAP-Rule:MF_01913}.
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DR EMBL; AF220438; AAF27921.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22862.1; -; Genomic_DNA.
DR RefSeq; NP_462903.1; NC_003197.2.
DR RefSeq; WP_000268252.1; NC_003197.2.
DR AlphaFoldDB; Q9L7S0; -.
DR SMR; Q9L7S0; -.
DR STRING; 99287.STM4023; -.
DR PaxDb; Q9L7S0; -.
DR EnsemblBacteria; AAL22862; AAL22862; STM4023.
DR GeneID; 1255549; -.
DR KEGG; stm:STM4023; -.
DR PATRIC; fig|99287.12.peg.4238; -.
DR HOGENOM; CLU_035117_1_1_6; -.
DR PhylomeDB; Q9L7S0; -.
DR BioCyc; SENT99287:STM4023-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0061596; F:3-sulfolactaldehyde reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:1902777; P:6-sulfoquinovose(1-) catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.1040.10; -; 1.
DR HAMAP; MF_01913; SLA_reductase; 1.
DR InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR015815; HIBADH-related.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029154; NADP-bd.
DR InterPro; IPR030876; SLA_reductase.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000103; HIBADH; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..298
FT /note="3-sulfolactaldehyde reductase"
FT /id="PRO_0000173065"
FT ACT_SITE 171
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01913"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01913"
FT BINDING 31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01913"
FT BINDING 65
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01913"
FT BINDING 96
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01913"
FT BINDING 123
FT /ligand="2,3-dihydroxypropane-1-sulfonate"
FT /ligand_id="ChEBI:CHEBI:77138"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01913"
FT BINDING 174..178
FT /ligand="2,3-dihydroxypropane-1-sulfonate"
FT /ligand_id="ChEBI:CHEBI:77138"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01913"
FT BINDING 240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01913"
SQ SEQUENCE 298 AA; 31280 MW; 7ED9FA174249240C CRC64;
MAVIAFIGLG QMGSPMASNL LKQGHQLSVF DVNPDAVQRL VDKGAQPASS PAQATIGAEF
VITMLPNGDL VRSVLFGEQG VCETLSREAL VIDMSTIHPL QTDNLIADMQ SKGFSMMDVP
IGRTSDNAIT GTLLLLAGGT AEQVERATPV LMAMGNELVN TGGPGMGIRV KLINNYMSIA
LNALSAEAAV LCEALGLSFD VALKVMSGTA AGKGHFTTTW PNKVMKGDLS PAFMIDLAHK
DLGIALDVAN QLHVPMPLGA ASREVYNLAR AAGRGREDWS AILEQVRISA GLTANVKK
