FSA_SALAR
ID FSA_SALAR Reviewed; 220 AA.
AC A9MI17;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=SARI_03548;
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000880; ABX23363.1; -; Genomic_DNA.
DR RefSeq; WP_000424868.1; NC_010067.1.
DR AlphaFoldDB; A9MI17; -.
DR SMR; A9MI17; -.
DR STRING; 41514.SARI_03548; -.
DR EnsemblBacteria; ABX23363; ABX23363; SARI_03548.
DR KEGG; ses:SARI_03548; -.
DR HOGENOM; CLU_079764_2_0_6; -.
DR OMA; QQMLGTP; -.
DR OrthoDB; 784333at2; -.
DR Proteomes; UP000002084; 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; Reference proteome; Schiff base.
FT CHAIN 1..220
FT /note="Fructose-6-phosphate aldolase"
FT /id="PRO_1000081410"
FT ACT_SITE 85
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00496"
SQ SEQUENCE 220 AA; 23559 MW; 22DCD8CD68464167 CRC64;
MELYLDTANV AEVERLARIF PIAGVTTNPS IVAASKESIW DVLPRLQNAI GEEGTLFAQT
MSRDAKGMVE EAKRLNNAIP GIVVKIPVTA EGLAAIKQLK KEGIVTLGTA VYSASQGLLA
ALAGAKYVAP YVNRVDAQGG DGIRMVQELQ TLLERHAPDS MVLAASFKTP RQALDCLLAG
CQAITLPLDV AQQMLNTPAV ESAIEKFEQD WKNAFGNLNL