ID Q84X64_PHATR Unreviewed; 439 AA.
AC Q84X64;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068};
DE EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068};
GN Name=FbaC2 {ECO:0000313|EMBL:AAO43262.1};
OS Phaeodactylum tricornutum (Diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC Phaeodactylum.
OX NCBI_TaxID=2850 {ECO:0000313|EMBL:AAO43262.1};
RN [1] {ECO:0000313|EMBL:AAO43262.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16273368; DOI=10.1007/s00294-005-0033-2;
RA Kroth P.G., Schroers Y., Kilian O.;
RT "The peculiar distribution of class I and class II aldolases in diatoms and
RT in red algae.";
RL Curr. Genet. 48:389-400(2005).
CC -!- FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone
CC phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate
CC (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and
CC the reverse reaction in glycolysis. {ECO:0000256|ARBA:ARBA00002181}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC Evidence={ECO:0000256|ARBA:ARBA00000441};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC {ECO:0000256|ARBA:ARBA00004714}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000256|ARBA:ARBA00005812}.
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DR EMBL; AY212505; AAO43262.1; -; Genomic_DNA.
DR AlphaFoldDB; Q84X64; -.
DR HOGENOM; CLU_036923_0_0_1; -.
DR UniPathway; UPA00109; UER00183.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00946; FBP_aldolase_IIA; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR006411; Fruct_bisP_bact.
DR NCBIfam; TIGR00167; cbbA; 1.
DR NCBIfam; TIGR01520; FruBisAldo_II_A; 1.
DR PANTHER; PTHR30559:SF0; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR30559; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 2; 1.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..439
FT /note="fructose-bisphosphate aldolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004300003"
SQ SEQUENCE 439 AA; 47935 MW; 38BA33EF2AB0BAF8 CRC64;
MKMAVVAFFV IAQCGAFAPA HYSRTVTSST LLGAKEKGGT SKELDLPCAD ECAISKYPNL
PESIHPGVLS GQAQMDLLNH AKEHGYAIPA VNCVSNSGIN ACLEAARKND APIIIQFSSG
GSQFYGGKGL DNSNYRAAIA GAVSGAFHVR TMAEQYGVPV ILHTDHCAKK LLPWIDGLLS
ASERYYEQHG EPLFSSHMID LSEEPIEENI EICKEYLTRM DKIGILLEME LGITGGEEDG
VDNSDRPIED LYSKPEEIYQ VYEELMKISD KFTVAAAFGN VHGVYSPGNV KLEPKILSRA
QDYISEKLGD KAPADKKPVA FVFHGGSGSD VADIQEAIGY GVIKMNIDTD TQWSYWEGIK
NFETKYHDYL QTQIGNPDGP DKPNKKYYDP RESMRAAEVN TVARLGKSYA DLKCQNILGL
GEVEPADNVL GPRRGGLPV
//
