SQUU_ECOLI
ID SQUU_ECOLI Reviewed; 298 AA.
AC P0A9V8; P32142; Q2M8H9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=3-sulfolactaldehyde reductase {ECO:0000255|HAMAP-Rule:MF_01913, ECO:0000303|PubMed:24463506};
DE Short=SLA reductase {ECO:0000255|HAMAP-Rule:MF_01913, ECO:0000303|PubMed:24463506};
DE EC=1.1.1.373 {ECO:0000255|HAMAP-Rule:MF_01913, ECO:0000269|PubMed:24463506, ECO:0000269|Ref.6};
DE AltName: Full=4-hydroxybutyrate dehydrogenase {ECO:0000305};
DE EC=1.1.1.61 {ECO:0000269|PubMed:19372223};
DE AltName: Full=Gamma-hydroxybutyrate dehydrogenase {ECO:0000303|PubMed:19372223};
DE Short=GHBDH {ECO:0000303|PubMed:19372223};
DE AltName: Full=Succinic semialdehyde reductase {ECO:0000303|PubMed:19372223};
DE Short=SSA reductase {ECO:0000303|PubMed:19372223};
GN Name=yihU; OrderedLocusNames=b3882, JW3853;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION AS A SUCCINIC SEMIALDEHYDE REDUCTASE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=19372223; DOI=10.1074/jbc.m109.002089;
RA Saito N., Robert M., Kochi H., Matsuo G., Kakazu Y., Soga T., Tomita M.;
RT "Metabolite profiling reveals YihU as a novel hydroxybutyrate dehydrogenase
RT for alternative succinic semialdehyde metabolism in Escherichia coli.";
RL J. Biol. Chem. 284:16442-16451(2009).
RN [5]
RP FUNCTION AS A SULFOLACTALDEHYDE REDUCTASE, CATALYTIC ACTIVITY, INDUCTION,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=K12;
RX PubMed=24463506; DOI=10.1038/nature12947;
RA Denger K., Weiss M., Felux A.K., Schneider A., Mayer C., Spiteller D.,
RA Huhn T., Cook A.M., Schleheck D.;
RT "Sulphoglycolysis in Escherichia coli K-12 closes a gap in the
RT biogeochemical sulphur cycle.";
RL Nature 507:114-117(2014).
RN [6] {ECO:0007744|PDB:6SM7, ECO:0007744|PDB:6SMY, ECO:0007744|PDB:6SMZ}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP NAD AND 2,3-DIHYDROXYPROPANE-1-SULFONATE, FUNCTION, CATALYTIC ACTIVITY,
RP REACTION MECHANISM, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF GLY-122; ARG-123 AND THR-124.
RX DOI=10.1021/acscatal.9b04427;
RA Sharma M., Abayakoon P., Lingford J.P., Epa R., John A., Jin Y.,
RA Goddard-Borger E.D., Davies G.J., Williams S.J.;
RT "Dynamic structural changes accompany the production of
RT dihydroxypropanesulfonate by sulfolactaldehyde reductase.";
RL ACS Catal. 10:2826-2836(2020).
CC -!- FUNCTION: Reduces 3-sulfolactaldehyde (SLA) to 2,3-dihydroxypropane 1-
CC sulfonate (DHPS) (PubMed:24463506, Ref.6). Metabolite profiling studies
CC showed that the enzyme also catalyzes in vitro the NADH-dependent
CC reduction of succinic semialdehyde (SSA) to 4-hydroxybutyrate (GHB),
CC and that it could be involved in the metabolism of SSA, and other
CC potentially toxic intermediates that may accumulate under stress
CC conditions (PubMed:19372223). However, the enzyme exhibits a 42,000-
CC fold greater catalytic efficiency for the reduction of SLA over SSA
CC (Ref.6). Shows no detectable activity on the analogous glycolytic
CC intermediate glyceraldehyde-3-phosphate (Ref.6).
CC {ECO:0000269|PubMed:19372223, ECO:0000269|PubMed:24463506,
CC ECO:0000269|Ref.6}.
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, ECO:0000269|PubMed:24463506, ECO:0000269|Ref.6};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:40513;
CC Evidence={ECO:0000269|PubMed:24463506, ECO:0000269|Ref.6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybutanoate + NAD(+) = H(+) + NADH + succinate
CC semialdehyde; Xref=Rhea:RHEA:23948, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16724, ChEBI:CHEBI:57540, ChEBI:CHEBI:57706,
CC ChEBI:CHEBI:57945; EC=1.1.1.61;
CC Evidence={ECO:0000269|PubMed:19372223};
CC -!- ACTIVITY REGULATION: Inhibited by the NADH analogs tetrahydro-NADH and
CC hexahydro-NADH. {ECO:0000269|Ref.6}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.30 mM for 3-sulfolactaldehyde {ECO:0000269|Ref.6};
CC KM=0.082 mM for NADH {ECO:0000269|Ref.6};
CC KM=4.3 mM for succinic semialdehyde {ECO:0000269|PubMed:19372223};
CC KM=9.0 mM for methylglyoxal {ECO:0000269|PubMed:19372223};
CC KM=102 mM for 4-hydroxybutyrate {ECO:0000269|PubMed:19372223};
CC KM=1.0 mM for 3-hydroxypropane sulfonate
CC {ECO:0000269|PubMed:19372223};
CC Vmax=0.20 umol/min/mg enzyme with succinic semialdehyde as substrate
CC {ECO:0000269|PubMed:19372223};
CC Vmax=0.067 umol/min/mg enzyme with methylglyoxal as substrate
CC {ECO:0000269|PubMed:19372223};
CC Vmax=0.062 umol/min/mg enzyme with 4-hydroxybutyrate as substrate
CC {ECO:0000269|PubMed:19372223};
CC Vmax=9.0 umol/min/mg enzyme with 3-hydroxypropane sulfonate as
CC substrate {ECO:0000269|PubMed:19372223};
CC Note=kcat is 332 sec(-1) with 3-sulfolactaldehyde as substrate. kcat
CC is 548 sec(-1) with NADH as substrate. {ECO:0000269|Ref.6};
CC -!- SUBUNIT: Homotetramer (PubMed:19372223, Ref.6). Dimer of dimers
CC (Ref.6). {ECO:0000269|PubMed:19372223, ECO:0000269|Ref.6}.
CC -!- INDUCTION: Induced during growth with sulfoquinovose.
CC {ECO:0000269|PubMed:24463506}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant displays reduced tolerance to the
CC cytotoxic effects of exogenous addition of succinic semialdehyde.
CC {ECO:0000269|PubMed:19372223}.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. 3-sulfolactaldehyde
CC reductase subfamily. {ECO:0000255|HAMAP-Rule:MF_01913, ECO:0000305}.
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DR EMBL; L19201; AAB03015.1; -; Genomic_DNA.
DR EMBL; U00096; AAD13444.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77427.1; -; Genomic_DNA.
DR PIR; S40826; S40826.
DR RefSeq; NP_418318.1; NC_000913.3.
DR RefSeq; WP_000718893.1; NZ_SSZK01000026.1.
DR PDB; 6SM7; X-ray; 1.88 A; A/B/C/D=1-298.
DR PDB; 6SMY; X-ray; 2.45 A; A/B/C/D=1-298.
DR PDB; 6SMZ; X-ray; 1.75 A; A/B/C/D=1-298.
DR PDBsum; 6SM7; -.
DR PDBsum; 6SMY; -.
DR PDBsum; 6SMZ; -.
DR AlphaFoldDB; P0A9V8; -.
DR SMR; P0A9V8; -.
DR BioGRID; 4260959; 7.
DR DIP; DIP-48142N; -.
DR IntAct; P0A9V8; 7.
DR STRING; 511145.b3882; -.
DR PaxDb; P0A9V8; -.
DR PRIDE; P0A9V8; -.
DR EnsemblBacteria; AAD13444; AAD13444; b3882.
DR EnsemblBacteria; BAE77427; BAE77427; BAE77427.
DR GeneID; 948372; -.
DR KEGG; ecj:JW3853; -.
DR KEGG; eco:b3882; -.
DR PATRIC; fig|1411691.4.peg.2829; -.
DR EchoBASE; EB1793; -.
DR eggNOG; COG2084; Bacteria.
DR HOGENOM; CLU_035117_1_1_6; -.
DR InParanoid; P0A9V8; -.
DR OMA; WSSEVNN; -.
DR PhylomeDB; P0A9V8; -.
DR BioCyc; EcoCyc:EG11847-MON; -.
DR BioCyc; MetaCyc:EG11847-MON; -.
DR BRENDA; 1.1.1.373; 2026.
DR BRENDA; 1.1.1.61; 2026.
DR PRO; PR:P0A9V8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0061596; F:3-sulfolactaldehyde reductase activity; IDA:EcoCyc.
DR GO; GO:0047577; F:4-hydroxybutyrate dehydrogenase activity; IDA:EcoCyc.
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; IEP:EcoCyc.
DR GO; GO:0061720; P:6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde; IDA:EcoCyc.
DR GO; GO:0009407; P:toxin catabolic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..298
FT /note="3-sulfolactaldehyde reductase"
FT /id="PRO_0000173064"
FT ACT_SITE 171
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01913,
FT ECO:0000305|Ref.6"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01913,
FT ECO:0000269|Ref.6, ECO:0000312|PDB:6SMY,
FT ECO:0000312|PDB:6SMZ"
FT BINDING 31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01913,
FT ECO:0000269|Ref.6, ECO:0000312|PDB:6SMY,
FT ECO:0000312|PDB:6SMZ"
FT BINDING 65
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01913,
FT ECO:0000269|Ref.6, ECO:0000312|PDB:6SMY,
FT ECO:0000312|PDB:6SMZ"
FT BINDING 96
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01913,
FT ECO:0000269|Ref.6, ECO:0000312|PDB:6SMY,
FT ECO:0000312|PDB:6SMZ"
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 ECO:0000269|Ref.6, ECO:0000312|PDB:6SMY"
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 ECO:0000269|Ref.6, ECO:0000312|PDB:6SMY"
FT BINDING 240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01913,
FT ECO:0000269|Ref.6, ECO:0000312|PDB:6SMY"
FT MUTAGEN 122
FT /note="G->S: 25-fold decrease in catalytic efficiency with
FT SLA as substrate. 5-fold decrease in catalytic efficiency
FT with NADH as substrate."
FT /evidence="ECO:0000269|Ref.6"
FT MUTAGEN 123
FT /note="R->G: 130-fold decrease in catalytic efficiency with
FT SLA as substrate. 3-fold decrease in catalytic efficiency
FT with NADH as substrate."
FT /evidence="ECO:0000269|Ref.6"
FT MUTAGEN 124
FT /note="T->G: 230-fold decrease in catalytic efficiency with
FT SLA as substrate. 12-fold decrease in catalytic efficiency
FT with NADH as substrate."
FT /evidence="ECO:0000269|Ref.6"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:6SMZ"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:6SMZ"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:6SMZ"
FT HELIX 34..42
FT /evidence="ECO:0007829|PDB:6SMZ"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:6SMZ"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:6SMZ"
FT HELIX 68..76
FT /evidence="ECO:0007829|PDB:6SMZ"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:6SMZ"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:6SMZ"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:6SMZ"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:6SMZ"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:6SMZ"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:6SMZ"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:6SMZ"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:6SMZ"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:6SMZ"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:6SMZ"
FT HELIX 166..194
FT /evidence="ECO:0007829|PDB:6SMZ"
FT HELIX 199..206
FT /evidence="ECO:0007829|PDB:6SMZ"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:6SMZ"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:6SMZ"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:6SMZ"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:6SMZ"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:6SMZ"
FT HELIX 235..251
FT /evidence="ECO:0007829|PDB:6SMZ"
FT HELIX 257..271
FT /evidence="ECO:0007829|PDB:6SMZ"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:6SMZ"
FT HELIX 282..289
FT /evidence="ECO:0007829|PDB:6SMZ"
SQ SEQUENCE 298 AA; 31158 MW; 74FBC8C09FA7881C CRC64;
MAAIAFIGLG QMGSPMASNL LQQGHQLRVF DVNAEAVRHL VDKGATPAAN PAQAAKDAEF
IITMLPNGDL VRNVLFGENG VCEGLSTDAL VIDMSTIHPL QTDKLIADMQ AKGFSMMDVP
VGRTSANAIT GTLLLLAGGT AEQVERATPI LMAMGSELIN AGGPGMGIRV KLINNYMSIA
LNALSAEAAV LCEALNLPFD VAVKVMSGTA AGKGHFTTSW PNKVLSGDLS PAFMIDLAHK
DLGIALDVAN QLHVPMPLGA ASREVYSQAR AAGRGRQDWS AILEQVRVSA GMTAKVKM
