SQUT_ECOLI
ID SQUT_ECOLI Reviewed; 292 AA.
AC P32141; Q2M8H8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 138.
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=b3881, JW3852;
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, CATALYTIC ACTIVITY, INDUCTION, DISRUPTION PHENOTYPE, AND
RP 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).
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, ECO:0000269|PubMed:24463506}.
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 ECO:0000269|PubMed:24463506};
CC -!- INDUCTION: Induced during growth with sulfoquinovose.
CC {ECO:0000269|PubMed:24463506}.
CC -!- DISRUPTION PHENOTYPE: Mutant fails to grow on sulfoquinovose as a sole
CC carbon source. {ECO:0000269|PubMed:24463506}.
CC -!- SIMILARITY: Belongs to the aldolase LacD family. {ECO:0000255|HAMAP-
CC Rule:MF_01912}.
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; L19201; AAB03014.1; -; Genomic_DNA.
DR EMBL; U00096; AAD13443.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77428.1; -; Genomic_DNA.
DR PIR; S40825; S40825.
DR RefSeq; NP_418317.1; NC_000913.3.
DR RefSeq; WP_001046453.1; NZ_STEB01000017.1.
DR PDB; 7AG1; X-ray; 2.00 A; X/Z=1-292.
DR PDBsum; 7AG1; -.
DR AlphaFoldDB; P32141; -.
DR SMR; P32141; -.
DR BioGRID; 4262639; 8.
DR IntAct; P32141; 5.
DR STRING; 511145.b3881; -.
DR jPOST; P32141; -.
DR PaxDb; P32141; -.
DR PRIDE; P32141; -.
DR EnsemblBacteria; AAD13443; AAD13443; b3881.
DR EnsemblBacteria; BAE77428; BAE77428; BAE77428.
DR GeneID; 66672213; -.
DR GeneID; 948373; -.
DR KEGG; ecj:JW3852; -.
DR KEGG; eco:b3881; -.
DR PATRIC; fig|1411691.4.peg.2830; -.
DR EchoBASE; EB1792; -.
DR eggNOG; COG3684; Bacteria.
DR HOGENOM; CLU_083300_0_0_6; -.
DR InParanoid; P32141; -.
DR OMA; KDITRPS; -.
DR PhylomeDB; P32141; -.
DR BioCyc; EcoCyc:EG11846-MON; -.
DR BioCyc; MetaCyc:EG11846-MON; -.
DR PRO; PR:P32141; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0061595; F:6-deoxy-6-sulfofructose-1-phosphate aldolase activity; IDA:EcoCyc.
DR GO; GO:1902777; P:6-sulfoquinovose(1-) catabolic process; IMP:EcoCyc.
DR GO; GO:0061720; P:6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Lyase; Reference proteome.
FT CHAIN 1..292
FT /note="Sulfofructosephosphate aldolase"
FT /id="PRO_0000203969"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:7AG1"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:7AG1"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:7AG1"
FT HELIX 42..56
FT /evidence="ECO:0007829|PDB:7AG1"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:7AG1"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:7AG1"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:7AG1"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:7AG1"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:7AG1"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:7AG1"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:7AG1"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:7AG1"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:7AG1"
FT HELIX 135..151
FT /evidence="ECO:0007829|PDB:7AG1"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:7AG1"
FT HELIX 173..184
FT /evidence="ECO:0007829|PDB:7AG1"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:7AG1"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:7AG1"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:7AG1"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:7AG1"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:7AG1"
FT HELIX 234..243
FT /evidence="ECO:0007829|PDB:7AG1"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:7AG1"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:7AG1"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:7AG1"
FT HELIX 265..271
FT /evidence="ECO:0007829|PDB:7AG1"
FT HELIX 273..292
FT /evidence="ECO:0007829|PDB:7AG1"
SQ SEQUENCE 292 AA; 31983 MW; 4A54012E39FF447F CRC64;
MNKYTINDIT RASGGFAMLA VDQREAMRMM FAAAGAPAPV ADSVLTDFKV NAAKALSPYA
SAILVDQQFC YRQVVEQNAI AKSCAMIVAA DEFIPGNGIP VDSVVIDRKI NPLQIKQDGG
KALKLLVLWR SDEDAQQRLD MVKEFNELCH SHGLVSIIEP VVRPPRRGDK FDREQAIIDA
AKELGDSGAD LYKVEMPLYG KGPQQELLCA SQRLNDHINM PWVILSSGVD EKLFPRAVRV
AMTAGASGFL AGRAVWASVV GLPDNELMLR DVCAPKLQQL GDIVDEMMAK RR
