FSA_SALPC
ID FSA_SALPC Reviewed; 220 AA.
AC C0Q463;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Fructose-6-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00496};
DE EC=4.1.2.- {ECO:0000255|HAMAP-Rule:MF_00496};
GN Name=fsa {ECO:0000255|HAMAP-Rule:MF_00496}; OrderedLocusNames=SPC_4219;
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594;
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(2009).
CC -!- FUNCTION: Catalyzes the reversible formation of fructose 6-phosphate
CC from dihydroxyacetone and D-glyceraldehyde 3-phosphate via an
CC aldolization reaction. {ECO:0000255|HAMAP-Rule:MF_00496}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 6-phosphate = D-glyceraldehyde 3-phosphate +
CC dihydroxyacetone; Xref=Rhea:RHEA:28002, ChEBI:CHEBI:16016,
CC ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00496};
CC -!- SUBUNIT: Homodecamer. {ECO:0000255|HAMAP-Rule:MF_00496}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00496}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 3A subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00496}.
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; CP000857; ACN48282.1; -; Genomic_DNA.
DR RefSeq; WP_000424866.1; NC_012125.1.
DR AlphaFoldDB; C0Q463; -.
DR SMR; C0Q463; -.
DR EnsemblBacteria; ACN48282; ACN48282; SPC_4219.
DR KEGG; sei:SPC_4219; -.
DR HOGENOM; CLU_079764_2_0_6; -.
DR OMA; QQMLGTP; -.
DR Proteomes; UP000001599; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097023; F:fructose 6-phosphate aldolase activity; IEA:RHEA.
DR GO; GO:0006000; P:fructose metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00956; Transaldolase_FSA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00496; F6P_aldolase; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR023001; F6P_aldolase.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR004731; Transaldolase_3B/F6P_aldolase.
DR InterPro; IPR018225; Transaldolase_AS.
DR InterPro; IPR033919; TSA/FSA_arc/bac.
DR PANTHER; PTHR10683; PTHR10683; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR TIGRFAMs; TIGR00875; fsa_talC_mipB; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Lyase; Schiff base.
FT CHAIN 1..220
FT /note="Fructose-6-phosphate aldolase"
FT /id="PRO_1000198461"
FT ACT_SITE 85
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00496"
SQ SEQUENCE 220 AA; 23525 MW; 333921DD60B3A167 CRC64;
MELYLDTANV AEVERLARIF PIAGVTTNPS IVAASKESIW DVLPRLQNAI GEEGTLFAQT
MSRDAKGMVE EAKRLNNAIP GIVVKIPVTA EGLAAIKLLK KEGIVTLGTA VYSASQGLLA
ALAGAKYVAP YVNRVDAQGG DGIRMVQELQ TLLEHHAPDS MVLAASFKTP RQALDCLLAG
CQAITLPLDV AQQMLNTPAV ESAIEKFEQD WKNAFGNLNL