SQUU_SHIFL
ID SQUU_SHIFL Reviewed; 298 AA.
AC P0A9V9; P32142;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=SF3954, S3792;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005674; AAN45389.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18811.1; -; Genomic_DNA.
DR RefSeq; NP_709682.1; NC_004337.2.
DR RefSeq; WP_000718893.1; NZ_WPGW01000092.1.
DR AlphaFoldDB; P0A9V9; -.
DR SMR; P0A9V9; -.
DR STRING; 198214.SF3954; -.
DR EnsemblBacteria; AAN45389; AAN45389; SF3954.
DR EnsemblBacteria; AAP18811; AAP18811; S3792.
DR GeneID; 1027487; -.
DR KEGG; sfl:SF3954; -.
DR KEGG; sfx:S3792; -.
DR PATRIC; fig|198214.7.peg.4659; -.
DR HOGENOM; CLU_035117_1_1_6; -.
DR OMA; WSSEVNN; -.
DR OrthoDB; 1194694at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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: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_0000173066"
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; 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
