ID   SQUT_ECO57              Reviewed;         292 AA.
AC   Q8X8D5;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Sulfofructosephosphate aldolase {ECO:0000255|HAMAP-Rule:MF_01912};
DE            Short=SFP aldolase {ECO:0000255|HAMAP-Rule:MF_01912};
DE            EC=4.1.2.57 {ECO:0000255|HAMAP-Rule:MF_01912};
GN   Name=yihT; OrderedLocusNames=Z5418, ECs4804;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Cleaves 6-deoxy-6-sulfo-D-fructose 1-phosphate (SFP) to form
CC       dihydroxyacetone phosphate (DHAP) and 3-sulfolactaldehyde (SLA).
CC       {ECO:0000255|HAMAP-Rule:MF_01912}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-deoxy-6-sulfo-D-fructose 1-phosphate = (2S)-3-
CC         sulfolactaldehyde + dihydroxyacetone phosphate; Xref=Rhea:RHEA:40515,
CC         ChEBI:CHEBI:57642, ChEBI:CHEBI:77134, ChEBI:CHEBI:90109; EC=4.1.2.57;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01912};
CC   -!- SIMILARITY: Belongs to the aldolase LacD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01912}.
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DR   EMBL; AE005174; AAG59071.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB38227.1; -; Genomic_DNA.
DR   PIR; C86076; C86076.
DR   PIR; D91229; D91229.
DR   RefSeq; NP_312831.1; NC_002695.1.
DR   RefSeq; WP_001046461.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8X8D5; -.
DR   SMR; Q8X8D5; -.
DR   STRING; 155864.EDL933_5201; -.
DR   EnsemblBacteria; AAG59071; AAG59071; Z5418.
DR   EnsemblBacteria; BAB38227; BAB38227; ECs_4804.
DR   GeneID; 915094; -.
DR   KEGG; ece:Z5418; -.
DR   KEGG; ecs:ECs_4804; -.
DR   PATRIC; fig|386585.9.peg.5019; -.
DR   eggNOG; COG3684; Bacteria.
DR   HOGENOM; CLU_083300_0_0_6; -.
DR   OMA; KDITRPS; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0061595; F:6-deoxy-6-sulfofructose-1-phosphate aldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1902777; P:6-sulfoquinovose(1-) catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01912; SFP_aldolase; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR017291; SFP_aldolase_YihT.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF037840; Aldolase_YihT; 1.
DR   SMART; SM01133; DeoC; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome.
FT   CHAIN           1..292
FT                   /note="Sulfofructosephosphate aldolase"
FT                   /id="PRO_0000203970"
SQ   SEQUENCE   292 AA;  31997 MW;  A1E10133934C48C4 CRC64;
     MNKYTINDIT RASGGFAMLA VDQREAMRMM FAAAGAPAPV ADSVLTDFKV NAAKTLSPYA
     SAILVDQQFC YRQVVEQNAI AKSCAMIVAA DEFIPGNGIP VDSVVIDRKI NPLQIKQDGG
     KALKLLVLWR SDEDAQQRLD MVKEFNELCH SHGLVSIIEP VVRPPRRGDK FDREQAIIDA
     AKELGDSGAD LYKVEMPLYG KGPQQELLSA SQRLNDHINM PWVILSSGVD EKLFPRAVRV
     AMTAGASGFL AGRAVWASVV GLPDNELMLR DVCAPKLQQL GDIVDEMMAK RR