ALF_THECA
ID ALF_THECA Reviewed; 305 AA.
AC Q703I2; P83739;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Fructose-bisphosphate aldolase;
DE Short=FBP aldolase;
DE Short=FBPA;
DE EC=4.1.2.13;
DE AltName: Full=Fructose-1,6-bisphosphate aldolase;
GN Name=fba {ECO:0000312|EMBL:CAF32659.1};
OS Thermus caldophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=272;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, AND X-RAY CRYSTALLOGRAPHY (2.2
RP ANGSTROMS).
RX PubMed=14561141; DOI=10.2174/0929866033478735;
RA Lee J.H., Im Y.J., Rho S.-H., Park S.H., Kim M.-K., Cho S.J., Kim T.-Y.,
RA Oh J.H., Shin H.-J., Lee D.-S., Eom S.H.;
RT "Crystallization and preliminary X-ray analysis of class II fructose-1,6-
RT bisphosphate aldolase from Thermus caldophilus.";
RL Protein Pept. Lett. 10:511-515(2003).
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:0000250}.
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:0000305};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC provides a structural contribution. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:14561141}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ621816; CAF32659.1; -; Genomic_DNA.
DR EMBL; AY526903; AAS19362.1; -; Genomic_DNA.
DR PDB; 2FJK; X-ray; 2.20 A; A/B/C/D=1-305.
DR PDBsum; 2FJK; -.
DR AlphaFoldDB; Q703I2; -.
DR SMR; Q703I2; -.
DR PRIDE; Q703I2; -.
DR BRENDA; 4.1.2.13; 6330.
DR UniPathway; UPA00109; UER00183.
DR EvolutionaryTrace; Q703I2; -.
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:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00947; TBP_aldolase_IIB; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR011289; Fruc_bis_ald_class-2.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR TIGRFAMs; TIGR00167; cbbA; 1.
DR TIGRFAMs; TIGR01859; fruc_bis_ald; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycolysis; Lyase; Metal-binding; Zinc.
FT CHAIN 1..305
FT /note="Fructose-bisphosphate aldolase"
FT /id="PRO_0000178752"
FT ACT_SITE 80
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 209..211
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 251..254
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT HELIX 6..14
FT /evidence="ECO:0007829|PDB:2FJK"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:2FJK"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:2FJK"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:2FJK"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:2FJK"
FT HELIX 50..68
FT /evidence="ECO:0007829|PDB:2FJK"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:2FJK"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:2FJK"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:2FJK"
FT HELIX 108..124
FT /evidence="ECO:0007829|PDB:2FJK"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:2FJK"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:2FJK"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:2FJK"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:2FJK"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:2FJK"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:2FJK"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:2FJK"
FT HELIX 215..223
FT /evidence="ECO:0007829|PDB:2FJK"
FT HELIX 236..244
FT /evidence="ECO:0007829|PDB:2FJK"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:2FJK"
FT HELIX 254..270
FT /evidence="ECO:0007829|PDB:2FJK"
FT HELIX 277..299
FT /evidence="ECO:0007829|PDB:2FJK"
SQ SEQUENCE 305 AA; 32987 MW; 9FE260186F29B98A CRC64;
MLVTGLEILR KARAEGYGVG AFNTNNMEFT QAILEAAEEM KSPVILALSE GAMKYGGRAL
TRMVVALAQE ARVPVAVHLD HGSSYESVLK ALREGFTSVM IDKSHEDFET NVRETKRVVE
AAHAVGVTVE AELGRLAGIE EHVAVDEKDA LLTNPEEARI FMERTGADYL AVAIGTSHGA
YKGKGRPFID HPRLARIAKL VPAPLVLHGA SAVPQELVER FRAAGGEIGE ASGIHPEDIK
KAISLGIAKI NTDTDLRLAF TALVRETLGK NPKEFDPRKY LGPAREAVKE VVKSRMELFG
SVGRA
