SQUT_SALTY
ID SQUT_SALTY Reviewed; 292 AA.
AC Q9L7R9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 109.
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=STM4022;
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: 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; AF220438; AAF27922.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22861.1; -; Genomic_DNA.
DR RefSeq; NP_462902.1; NC_003197.2.
DR RefSeq; WP_001067421.1; NC_003197.2.
DR PDB; 1TO3; X-ray; 2.70 A; A=2-292.
DR PDB; 7AG7; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-292.
DR PDB; 7NE2; X-ray; 1.50 A; A/B/C/D=1-292.
DR PDBsum; 1TO3; -.
DR PDBsum; 7AG7; -.
DR PDBsum; 7NE2; -.
DR AlphaFoldDB; Q9L7R9; -.
DR SMR; Q9L7R9; -.
DR STRING; 99287.STM4022; -.
DR PaxDb; Q9L7R9; -.
DR PRIDE; Q9L7R9; -.
DR DNASU; 1255548; -.
DR EnsemblBacteria; AAL22861; AAL22861; STM4022.
DR GeneID; 1255548; -.
DR KEGG; stm:STM4022; -.
DR PATRIC; fig|99287.12.peg.4237; -.
DR HOGENOM; CLU_083300_0_0_6; -.
DR OMA; KDITRPS; -.
DR PhylomeDB; Q9L7R9; -.
DR BioCyc; SENT99287:STM4022-MON; -.
DR EvolutionaryTrace; Q9L7R9; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0061595; F:6-deoxy-6-sulfofructose-1-phosphate aldolase activity; IBA:GO_Central.
DR GO; GO:1902777; P:6-sulfoquinovose(1-) catabolic process; IBA:GO_Central.
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_0000203972"
FT CONFLICT 235
FT /note="P -> L (in Ref. 1; AAF27922)"
FT /evidence="ECO:0000305"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:7NE2"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:7NE2"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:7NE2"
FT HELIX 42..56
FT /evidence="ECO:0007829|PDB:7NE2"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:7NE2"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:7NE2"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:7NE2"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:7NE2"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:7NE2"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:7NE2"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:7NE2"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:7NE2"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:7NE2"
FT HELIX 135..150
FT /evidence="ECO:0007829|PDB:7NE2"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:7NE2"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:7NE2"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:7AG7"
FT HELIX 173..184
FT /evidence="ECO:0007829|PDB:7NE2"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:7NE2"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:7NE2"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:7NE2"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:7NE2"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:7NE2"
FT HELIX 234..243
FT /evidence="ECO:0007829|PDB:7NE2"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:7NE2"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:7NE2"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:7NE2"
FT HELIX 265..271
FT /evidence="ECO:0007829|PDB:7NE2"
FT HELIX 273..289
FT /evidence="ECO:0007829|PDB:7NE2"
SQ SEQUENCE 292 AA; 31866 MW; B4BC0AC12D7197E1 CRC64;
MNNYTIKDIT RASGGFAMLA VDQREAMRLM FAAAGAKTPV ADSVLTDFKV NAAKILSPYA
SAVLLDQQFC YRQAVEQNAV AKSCAMIVAA DDFIPGNGIP VDNVVLDKKI NAQAVKRDGA
KALKLLVLWR SDEDAQQRLN MVKEFNELCH SNGLLSIIEP VVRPPRCGDK FDREQAIIDA
AKELGDSGAD LYKVEMPLYG KGARSDLLTA SQRLNGHINM PWVILSSGVD EKLFPRAVRV
AMEAGASGFL AGRAVWSSVI GLPDTELMLR DVSAPKLQRL GEIVDEMMAK RR
