ALF_ENCCU
ID ALF_ENCCU Reviewed; 338 AA.
AC Q8SSM8;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Fructose-bisphosphate aldolase;
DE EC=4.1.2.13;
GN OrderedLocusNames=ECU01_0240;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11157783; DOI=10.1101/gr.164301;
RA Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M.,
RA Weissenbach J., Saurin W., Vivares C.P.;
RT "Sequence and analysis of chromosome I of the amitochondriate intracellular
RT parasite Encephalitozoon cuniculi (Microspora).";
RL Genome Res. 11:198-207(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16691553; DOI=10.1002/pmic.200500796;
RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT (microsporidia): a reference map for proteins expressed in late sporogonial
RT stages.";
RL Proteomics 6:3625-3635(2006).
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 -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC {ECO:0000269|PubMed:16691553}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; AL391737; CAD24894.1; -; Genomic_DNA.
DR RefSeq; XP_965859.1; XM_960766.1.
DR PDB; 3MBD; X-ray; 2.00 A; A=1-338.
DR PDB; 3MBF; X-ray; 2.37 A; A=1-338.
DR PDB; 3QRH; X-ray; 2.00 A; A=1-338.
DR PDBsum; 3MBD; -.
DR PDBsum; 3MBF; -.
DR PDBsum; 3QRH; -.
DR AlphaFoldDB; Q8SSM8; -.
DR SMR; Q8SSM8; -.
DR STRING; 284813.Q8SSM8; -.
DR GeneID; 860198; -.
DR KEGG; ecu:ECU01_0240; -.
DR VEuPathDB; MicrosporidiaDB:ECU01_0240; -.
DR HOGENOM; CLU_031243_0_0_1; -.
DR InParanoid; Q8SSM8; -.
DR OMA; DYREMLF; -.
DR OrthoDB; 799973at2759; -.
DR BRENDA; 4.1.2.13; 7412.
DR UniPathway; UPA00109; UER00183.
DR EvolutionaryTrace; Q8SSM8; -.
DR Proteomes; UP000000819; Chromosome I.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycolysis; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..338
FT /note="Fructose-bisphosphate aldolase"
FT /id="PRO_0000381751"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 221
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:3MBD"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3MBD"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:3MBD"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:3MBD"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:3MBD"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3MBD"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:3MBD"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:3MBD"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:3MBD"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:3MBD"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:3MBD"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:3MBD"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:3MBD"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3MBD"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:3MBD"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:3MBD"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:3MBD"
FT HELIX 152..171
FT /evidence="ECO:0007829|PDB:3MBD"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:3MBD"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:3MBD"
FT HELIX 190..210
FT /evidence="ECO:0007829|PDB:3MBD"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3MBD"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:3MBD"
FT HELIX 237..251
FT /evidence="ECO:0007829|PDB:3MBD"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:3MBD"
FT HELIX 268..280
FT /evidence="ECO:0007829|PDB:3MBD"
FT STRAND 286..294
FT /evidence="ECO:0007829|PDB:3MBD"
FT HELIX 295..305
FT /evidence="ECO:0007829|PDB:3MBD"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:3MBD"
FT HELIX 312..330
FT /evidence="ECO:0007829|PDB:3MBD"
SQ SEQUENCE 338 AA; 37917 MW; 2158A1DAE05A7AF9 CRC64;
MMDCDHLLRL GMTAKKILEN GKGILAADET PKTLGRRFEK LGITNTEENR RKFREILFST
KGIERYIGGV ILNQETFEQT SGSGVPLTEL LKKKGIEIGI KLDKGLIDYK EKEKISVGLE
DLDLRCKSSA FKDATFAKWR SLFYFYDGIP SEDCINENCS ILAKYAIICQ KNGLVPIVEP
EVFLEGDYSM KRSYEVTRQI LSTLMKYLNY ELVYIPGVLI KASYVTSGQL SNEKYTPKKV
ATFTLRALLS TIPCGIPGIV FLSGGHGSED AIGFLNAINM ERGCRTWSLS FSFARALTDG
VLETWRGDDS NIEEAQKILL ETSFKACRGA EGKLWDQE
