ID Q5QD45_ISOGA Unreviewed; 396 AA.
AC Q5QD45;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068};
DE EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068};
GN Name=fbaC1 {ECO:0000313|EMBL:AAV71137.1};
OS Isochrysis galbana (Marine planktonic alga).
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC Isochrysidaceae; Isochrysis.
OX NCBI_TaxID=37099 {ECO:0000313|EMBL:AAV71137.1};
RN [1] {ECO:0000313|EMBL:AAV71137.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP1323 {ECO:0000313|EMBL:AAV71137.1};
RX PubMed=15470245; DOI=10.1128/EC.3.5.1169-1175.2004;
RA Patron N.J., Rogers M.B., Keeling P.J.;
RT "Gene replacement of fructose-1,6-bisphosphate aldolase supports the
RT hypothesis of a single photosynthetic ancestor of chromalveolates.";
RL Eukaryot. Cell 3:1169-1175(2004).
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; AY699822; AAV71137.1; -; mRNA.
DR AlphaFoldDB; Q5QD45; -.
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 PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 2: Evidence at transcript level;
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..396
FT /note="fructose-bisphosphate aldolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004260980"
SQ SEQUENCE 396 AA; 43099 MW; 3F83B7E198479DDC CRC64;
MLCFQLVVAS AAVVSGLNVG AARSGPITMQ TKTITPMPAT VKPGVVTGQA LWDLLQHAKE
NEYAIPAVNV VSSCSISSCL EAAAKYGGPM IIQFSRGGGQ FIAGKTANND NDAACIAGSV
AGALHVRQVA ELYGVPVILH TDHCQRSWLP WFDGLMEANE KYFAANGEPL FSSHMLDLSE
EPLEENVGTC KEYLERMSKV DLLLEMELGV TGGEEDGVDN SDVDSSRLYT QPEEVWEVYQ
QLSTVPNGRF TVAAAFGNVH GVYAPGNVEL KPEILHNTQK FIAEKLGGGD AKPTLFVFHG
GSGSSREDIR YAIKAGTIKM NIDTDTQWAF WDGIRAYEAK YHDYLQGQIG TPEGELKPNK
KYYDPRMSLR SGEEFMAKRL CEAAEDLNCV NVLSGW
//
