ALF_TRYBB
ID ALF_TRYBB Reviewed; 372 AA.
AC P07752;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Fructose-bisphosphate aldolase, glycosomal;
DE EC=4.1.2.13;
GN Name=ALD;
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2998772; DOI=10.1002/j.1460-2075.1985.tb04035.x;
RA Clayton C.E.;
RT "Structure and regulated expression of genes encoding fructose biphosphate
RT aldolase in Trypanosoma brucei.";
RL EMBO J. 4:2997-3003(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=427;
RX PubMed=2349093; DOI=10.1093/nar/18.10.2967;
RA Vijayasarathy S., Ernest I., Itzhaki J., Sherman D., Mowatt M.R.,
RA Michels P.A.M., Clayton C.E.;
RT "The genes encoding fructose bisphosphate aldolase in Trypanosoma brucei
RT are interspersed with unrelated genes.";
RL Nucleic Acids Res. 18:2967-2975(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3386689; DOI=10.1016/0166-6851(88)90121-1;
RA Marchand M., Poliszczak A., Gibson W.C., Wierenga R.K., Opperdoes F.R.,
RA Michels P.A.M.;
RT "Characterization of the genes for fructose-bisphosphate aldolase in
RT Trypanosoma brucei.";
RL Mol. Biochem. Parasitol. 29:65-76(1988).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 12-371.
RX PubMed=10891264; DOI=10.1006/jmbi.2000.3910;
RA Chudzik D.M., Michels P.A.M., de Walque S., Hol W.G.J.;
RT "Structures of type 2 peroxisomal targeting signals in two trypanosomatid
RT aldolases.";
RL J. Mol. Biol. 300:697-707(2000).
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 -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SUBCELLULAR LOCATION: Glycosome.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; X03061; CAA26867.1; -; mRNA.
DR EMBL; X52586; CAA36819.1; -; Genomic_DNA.
DR EMBL; M19994; AAA30153.1; -; Genomic_DNA.
DR PIR; A24678; ADUT.
DR PIR; A54500; A54500.
DR PDB; 1F2J; X-ray; 1.90 A; A=2-371.
DR PDBsum; 1F2J; -.
DR AlphaFoldDB; P07752; -.
DR SMR; P07752; -.
DR ELM; P07752; -.
DR BindingDB; P07752; -.
DR ChEMBL; CHEMBL4916; -.
DR SABIO-RK; P07752; -.
DR UniPathway; UPA00109; UER00183.
DR EvolutionaryTrace; P07752; -.
DR GO; GO:0020015; C:glycosome; IDA:GeneDB.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:GeneDB.
DR GO; GO:0006096; P:glycolytic process; IDA:GeneDB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR029768; Aldolase_I_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycolysis; Glycosome; Lyase; Peroxisome; Schiff base.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..372
FT /note="Fructose-bisphosphate aldolase, glycosomal"
FT /id="PRO_0000216935"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 240
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT BINDING 66
FT /ligand="substrate"
FT BINDING 157
FT /ligand="substrate"
FT SITE 372
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
FT CONFLICT 254..255
FT /note="GH -> AT (in Ref. 3; AAA30153)"
FT /evidence="ECO:0000305"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:1F2J"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1F2J"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:1F2J"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:1F2J"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:1F2J"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:1F2J"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:1F2J"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1F2J"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:1F2J"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:1F2J"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1F2J"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:1F2J"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:1F2J"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1F2J"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:1F2J"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1F2J"
FT HELIX 141..150
FT /evidence="ECO:0007829|PDB:1F2J"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:1F2J"
FT HELIX 171..190
FT /evidence="ECO:0007829|PDB:1F2J"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:1F2J"
FT HELIX 209..230
FT /evidence="ECO:0007829|PDB:1F2J"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:1F2J"
FT HELIX 256..270
FT /evidence="ECO:0007829|PDB:1F2J"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:1F2J"
FT HELIX 287..297
FT /evidence="ECO:0007829|PDB:1F2J"
FT STRAND 306..313
FT /evidence="ECO:0007829|PDB:1F2J"
FT HELIX 314..324
FT /evidence="ECO:0007829|PDB:1F2J"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:1F2J"
FT HELIX 331..349
FT /evidence="ECO:0007829|PDB:1F2J"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:1F2J"
SQ SEQUENCE 372 AA; 41178 MW; 30F1F26F0D54211D CRC64;
MSKRVEVLLT QLPAYNRLKT PYEAELIETA KKMTAPGKGL LAADESTGSC SKRFAGIGLS
NTAEHRRQYR ALMLECEGFE QYISGVILHD ETVYQKAKTG ETFPQYLRRR GVVPGIKTDC
GLEPLVEGAK GEQMTAGLDG YIKRAKKYYA MGCRFCKWRN VYKIQNGTVS EAVVRFNAET
LARYAILSQL CGLVPIVEPE VMIDGTHDIE TCQRVSQHVW SEVVSALHRH GVVWEGCLLK
PNMVVPGAES GLKGHAEQVA EYTVKTLARV IPPALPGVTF LSGGLSEVMA SEYLNAMNNC
PLPRPWKLTF SYARALQSSA IKRWGGKESG VEAGRRAFMH RAKMNSLAQL GKYNRADDDK
DSQSLYVAGN TY
