ID E1JDG4_ECOLX Unreviewed; 220 AA.
AC E1JDG4;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Fructose-6-phosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00496};
DE EC=4.1.2.- {ECO:0000256|HAMAP-Rule:MF_00496};
GN Name=fsa {ECO:0000256|HAMAP-Rule:MF_00496,
GN ECO:0000313|EMBL:EFK66102.1};
GN ORFNames=HMPREF9347_05014 {ECO:0000313|EMBL:EFK66102.1};
OS Escherichia coli MS 124-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=679205 {ECO:0000313|EMBL:EFK66102.1, ECO:0000313|Proteomes:UP000003390};
RN [1] {ECO:0000313|EMBL:EFK66102.1, ECO:0000313|Proteomes:UP000003390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 124-1 {ECO:0000313|EMBL:EFK66102.1,
RC ECO:0000313|Proteomes:UP000003390};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (JUL-2010) 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:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00001649, ECO:0000256|HAMAP-
CC Rule:MF_00496};
CC -!- SUBUNIT: Homodecamer. {ECO:0000256|HAMAP-Rule:MF_00496}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00496}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 3A subfamily.
CC {ECO:0000256|ARBA:ARBA00005763, ECO:0000256|HAMAP-Rule:MF_00496}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFK66102.1}.
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DR EMBL; ADWT01000068; EFK66102.1; -; Genomic_DNA.
DR RefSeq; WP_000424845.1; NZ_ADWT01000068.1.
DR AlphaFoldDB; E1JDG4; -.
DR GeneID; 75203223; -.
DR Proteomes; UP000003390; Unassembled WGS sequence.
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; Aldolase class I; 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 NCBIfam; TIGR00875; fsa_talC_mipB; 1.
DR PANTHER; PTHR10683:SF40; FRUCTOSE-6-PHOSPHATE ALDOLASE 1-RELATED; 1.
DR PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00496};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00496};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00496};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_00496}.
FT ACT_SITE 85
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00496"
SQ SEQUENCE 220 AA; 23543 MW; 83062E3D4347B20B CRC64;
MELYLDTANV AEVERLARIF PIAGVTTNPS IIAASKESIW EVLPRLQKAI GDEGILFAQT
MSRDAQGMVE EAKRLRDAIP GIVVKIPVTS EGLAAIKMLK KEGITTLGTA VYSAAQGLLA
ALAGAKYVAP YVNRVDAQGG DGIRTVQELQ ALLEMHAPES MVLAASFKTP RQALDCLLAG
CESITLPLDV AQQMLNTPAV ESAIEKFEHD WNAAFGTTHL
//