ID F4V022_ECOLX Unreviewed; 244 AA.
AC F4V022;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
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 ORFNames=ECNG_03510 {ECO:0000313|EMBL:EGI41888.1};
OS Escherichia coli TA280.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=656444 {ECO:0000313|EMBL:EGI41888.1, ECO:0000313|Proteomes:UP000004877};
RN [1] {ECO:0000313|EMBL:EGI41888.1, ECO:0000313|Proteomes:UP000004877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TA280 {ECO:0000313|EMBL:EGI41888.1,
RC ECO:0000313|Proteomes:UP000004877};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Escherichia coli TA280.";
RL Submitted (JAN-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}.
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DR EMBL; GL884339; EGI41888.1; -; Genomic_DNA.
DR AlphaFoldDB; F4V022; -.
DR HOGENOM; CLU_079764_2_0_6; -.
DR Proteomes; UP000004877; 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 109
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00496"
SQ SEQUENCE 244 AA; 26110 MW; CFCAA88F02DDD4C3 CRC64;
MRQLFREFSR DSLHSDKKYI LRMVMELYLD TSDVVAVKAL SRIFPLAGVT TNPSIIAAGK
KPLEVVLPEL HEAMGGQGRL FAQVMATTAE GMVNDARKLR SIIADIVVKV PVTAEGLAAI
KMLKAEGIPT LGTAVYGAAQ GLLSALAGAE YVAPYVNRID AQGGCGIQTV TDLHQLLKMH
APQAKVLAAS FKTPRQALDC LLAGCESITL PLDVAQQMIS YPAVDAAVAK FEQDWQGAFG
RTSI
//
