ID W8V2C4_KLEPN Unreviewed; 220 AA.
AC W8V2C4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=KPNJ2_05309 {ECO:0000313|EMBL:AHM82073.1};
OS Klebsiella pneumoniae 30684/NJST258_2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1420013 {ECO:0000313|EMBL:AHM82073.1, ECO:0000313|Proteomes:UP000019586};
RN [1] {ECO:0000313|EMBL:AHM82073.1, ECO:0000313|Proteomes:UP000019586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30684/NJST258_2 {ECO:0000313|EMBL:AHM82073.1};
RX PubMed=24639510; DOI=10.1073/pnas.1321364111;
RA Deleo F.R., Chen L., Porcella S.F., Martens C.A., Kobayashi S.D.,
RA Porter A.R., Chavda K.D., Jacobs M.R., Mathema B., Olsen R.J., Bonomo R.A.,
RA Musser J.M., Kreiswirth B.N.;
RT "Molecular dissection of the evolution of carbapenem-resistant multilocus
RT sequence type 258 Klebsiella pneumoniae.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:4988-4993(2014).
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; CP006918; AHM82073.1; -; Genomic_DNA.
DR RefSeq; WP_002882982.1; NZ_CP006918.1.
DR AlphaFoldDB; W8V2C4; -.
DR KEGG; kps:KPNJ2_05309; -.
DR PATRIC; fig|1420013.3.peg.4973; -.
DR HOGENOM; CLU_079764_2_0_6; -.
DR Proteomes; UP000019586; 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; 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; 23339 MW; F1D88754A04E5C49 CRC64;
MELYLDTANV AEVERLARIY PLAGVTTNPS IIAAGKVPVW DVLPRLQKAV GPKGTLFAQT
MSRDAQGMVE EAKRLSNSVP GIVVKIPVTA EGLAAIKLLK KEGIPTLGTA VYSASQGLLA
ALAGAKYVAP YVNRVDAQGG DGIRMVQELQ SLLEMHAPES KVLAASFKTP RQALDCLLAG
CEAITLPLDV AQQMLGTPAV ESAIEKFEQD WNNAFGTLNL
//
