ALF_DROME
ID ALF_DROME Reviewed; 361 AA.
AC P07764; A4V3F9; A5XCY2; P29841; Q24236; Q24237; Q7KRY9; Q8IMS1; Q8MQQ4;
AC Q9VBG2; Q9VBG3;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Fructose-bisphosphate aldolase;
DE EC=4.1.2.13;
GN Name=Ald1 {ECO:0000312|FlyBase:FBgn0000064};
GN ORFNames=CG6058 {ECO:0000312|FlyBase:FBgn0000064};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS ALPHA;
RP BETA AND GAMMA), AND TISSUE SPECIFICITY.
RC STRAIN=Oregon-R;
RX PubMed=1339430; DOI=10.1093/oxfordjournals.jbchem.a123958;
RA Kai T., Sugimoto Y., Kusakabe T., Zhang R., Koga K., Hori K.;
RT "Gene structure and multiple mRNA species of Drosophila melanogaster
RT aldolase generating three isozymes with different enzymatic properties.";
RL J. Biochem. 112:677-688(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
RP ALPHA; BETA AND GAMMA).
RC STRAIN=Oregon-R;
RX PubMed=1740444; DOI=10.1016/s0021-9258(19)50619-6;
RA Shaw-Lee R., Lissemore J.L., Sullivan D.T., Tolan D.R.;
RT "Alternative splicing of fructose 1,6-bisphosphate aldolase transcripts in
RT Drosophila melanogaster predicts three isozymes.";
RL J. Biol. Chem. 267:3959-3967(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS BETA
RP AND GAMMA).
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=1732743; DOI=10.1128/mcb.12.2.773-783.1992;
RA Kim J., Yim J.J., Wang S., Dorsett D.;
RT "Alternate use of divergent forms of an ancient exon in the fructose-1,6-
RT bisphosphate aldolase gene of Drosophila melanogaster.";
RL Mol. Cell. Biol. 12:773-783(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), AND PROTEIN SEQUENCE OF 354-361
RP (ISOFORM ALPHA).
RC STRAIN=Oregon-R;
RX PubMed=7487099; DOI=10.1006/abbi.1995.9953;
RA Sugimoto Y., Kusakabe T., Kai T., Okamura T., Koga K., Hori K.;
RT "Analysis of the in vitro translation product of a novel-type Drosophila
RT melanogaster aldolase mRNA in which two carboxyl-terminal exons remain
RT unspliced.";
RL Arch. Biochem. Biophys. 323:361-366(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DPF3, DPF4, HFL12, HFL13, HFL15, HFL16, HFL8, SC12, SC19, VT1, VT39,
RC and VT41;
RX PubMed=17379620; DOI=10.1093/molbev/msm057;
RA Flowers J., Sezgin E., Kumagai S., Duvernell D., Matzkin L., Schmidt P.,
RA Eanes W.;
RT "Adaptive evolution of metabolic pathways in Drosophila.";
RL Mol. Biol. Evol. 24:1347-1354(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [7]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS BETA AND GAMMA).
RC STRAIN=Berkeley; TISSUE=Embryo, Larva, and Pupae;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [9]
RP PROTEIN SEQUENCE OF 2-361 (ISOFORM GAMMA), AND ACETYLATION AT THR-2.
RX PubMed=3918528; DOI=10.1016/0006-291x(85)90591-1;
RA Malek A.A., Suter F.X., Frank G., Brenner-Holzach O.;
RT "Amino acid sequence of an invertebrate FBP aldolase (from Drosophila
RT melanogaster).";
RL Biochem. Biophys. Res. Commun. 126:199-205(1985).
RN [10]
RP PROTEIN SEQUENCE OF 2-361 (ISOFORM GAMMA).
RX PubMed=3140728; DOI=10.1016/0003-9861(88)90232-9;
RA Malek A.A., Hy M., Honegger A., Rose K., Brenner-Holzach O.;
RT "Fructose-1,6-bisphosphate aldolase from Drosophila melanogaster: primary
RT structure analysis, secondary structure prediction, and comparison with
RT vertebrate aldolases.";
RL Arch. Biochem. Biophys. 266:10-31(1988).
RN [11]
RP PRELIMINARY PROTEIN SEQUENCE OF 170-272.
RX PubMed=6805442; DOI=10.1016/0003-9861(82)90011-x;
RA Brenner-Holzach O., Zumsteg C.;
RT "Fructose 1,6-bisphosphate aldolase of Drosophila melanogaster: comparative
RT sequence analyses around the substrate-binding lysyl residue.";
RL Arch. Biochem. Biophys. 214:89-101(1982).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8537310; DOI=10.1093/oxfordjournals.jbchem.a124876;
RA Zhang R., Kai T., Sugimoto Y., Kusakabe T., Takasaki Y., Koga K., Hori K.;
RT "Drosophila melanogaster aldolase: characterization of the isozymes alpha,
RT beta, and gamma generated from a single gene.";
RL J. Biochem. 118:183-188(1995).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND ACETYLATION AT THR-2.
RX PubMed=1959612; DOI=10.1016/0014-5793(91)80875-4;
RA Hester G., Brenner-Holzach O., Rossi F.A., Struck-Donatz M.,
RA Winterhalter K.H., Smit J.D.G., Piontek K.;
RT "The crystal structure of fructose-1,6-bisphosphate aldolase from
RT Drosophila melanogaster at 2.5-A resolution.";
RL FEBS Lett. 292:237-242(1991).
CC -!- FUNCTION: May take part in developmental stage-specific or tissue
CC -specific sugar-phosphate metabolisms. Protein acts on two substrates
CC fructose 1,6-bisphosphate and fructose 1-phosphate (like other class I
CC aldolases). {ECO:0000269|PubMed:8537310}.
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:0000269|PubMed:8537310};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.2-7.8 for isozyme alpha, and 7.2-7.5 for isozymes
CC beta and gamma. {ECO:0000269|PubMed:8537310};
CC Temperature dependence:
CC Thermostability of the isozymes, calculated as the temperature
CC causing half maximal stability, is 42-43 degrees Celsius for isozymes
CC alpha and beta and 45 degrees Celsius for isozyme gamma.
CC {ECO:0000269|PubMed:8537310};
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:8537310}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Two additional mRNAs also exist (Alpha-beta and Beta-gamma).
CC The translation product of Alpha-beta mRNA is isoform Alpha.;
CC Name=Gamma; Synonyms=4C, B, C, D;
CC IsoId=P07764-1; Sequence=Displayed;
CC Name=Alpha; Synonyms=4A, E;
CC IsoId=P07764-2; Sequence=VSP_000223;
CC Name=Beta; Synonyms=4B, H;
CC IsoId=P07764-3; Sequence=VSP_000221;
CC -!- TISSUE SPECIFICITY: Isozyme gamma is mainly expressed in the heads and
CC partly in the thoraxes of adult flies. Isozyme alpha is expressed in
CC all adult tissues. Isozyme beta is mainly expressed in adult abdominal
CC regions and is also expressed in lesser amounts in other parts of the
CC body and in earlier developmental stages. Isozyme alpha-beta shows
CC strong expression in the abdomens of adults. Isozyme beta-gamma is
CC expressed in adult heads. {ECO:0000269|PubMed:1339430,
CC ECO:0000269|PubMed:8537310}.
CC -!- DEVELOPMENTAL STAGE: Isozyme gamma is first detected during late
CC embryogenesis, is present through larval stages, declines in abundance
CC during pupal stages and is maximum at eclosion. Isozyme beta is
CC abundant during the earliest stages of embryogenesis, declines in
CC amount and increases prior to hatching. Isozyme alpha is found only
CC during the adult stage. Expression correlates to dietary behavior: high
CC dietary activity in the larvae and adults causes active glycolysis and
CC high expression levels. Isozyme alpha-beta is detected in the pupae and
CC adults and isozyme beta-gamma in the adult.
CC {ECO:0000269|PubMed:8537310}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM75045.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=ABH06768.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABH06769.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABH06770.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABH06771.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABH06772.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABH06773.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABH06774.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABH06775.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABH06776.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABH06777.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABH06778.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABH06779.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA42666.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D10446; BAA01236.1; -; Genomic_DNA.
DR EMBL; D10446; BAA01237.1; -; Genomic_DNA.
DR EMBL; D10446; BAA01238.1; -; Genomic_DNA.
DR EMBL; M98351; AAA99426.1; -; Genomic_DNA.
DR EMBL; M98351; AAA99427.1; -; Genomic_DNA.
DR EMBL; M98351; AAA99428.1; -; Genomic_DNA.
DR EMBL; X60064; CAA42666.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X60064; CAA42667.1; -; Genomic_DNA.
DR EMBL; X60064; CAA42668.1; -; Genomic_DNA.
DR EMBL; D10762; BAA01592.1; -; mRNA.
DR EMBL; DQ864133; ABH06768.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DQ864134; ABH06769.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DQ864135; ABH06770.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DQ864136; ABH06771.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DQ864137; ABH06772.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DQ864138; ABH06773.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DQ864139; ABH06774.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DQ864140; ABH06775.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DQ864141; ABH06776.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DQ864142; ABH06777.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DQ864143; ABH06778.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DQ864144; ABH06779.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014297; AAF56579.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14381.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14382.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14384.1; -; Genomic_DNA.
DR EMBL; AE014297; AAS65220.1; -; Genomic_DNA.
DR EMBL; AY058667; AAL13896.1; -; mRNA.
DR EMBL; AY128452; AAM75045.1; ALT_FRAME; mRNA.
DR PIR; A42027; ADFFR.
DR PIR; A42263; A42263.
DR PIR; B42027; ADFF.
DR PIR; B42263; B42263.
DR PIR; C42263; C42263.
DR PIR; JX0233; JX0233.
DR PIR; S68360; S68360.
DR RefSeq; NP_001262985.1; NM_001276056.1. [P07764-3]
DR RefSeq; NP_001287541.1; NM_001300612.1. [P07764-1]
DR RefSeq; NP_524515.2; NM_079791.5. [P07764-2]
DR RefSeq; NP_733140.2; NM_170261.3. [P07764-3]
DR RefSeq; NP_733141.1; NM_170262.2. [P07764-1]
DR RefSeq; NP_733142.1; NM_170263.4. [P07764-1]
DR RefSeq; NP_733143.1; NM_170264.3. [P07764-1]
DR RefSeq; NP_733144.3; NM_170265.4. [P07764-1]
DR RefSeq; NP_733145.3; NM_170266.4. [P07764-2]
DR RefSeq; NP_996300.1; NM_206577.3. [P07764-3]
DR PDB; 1FBA; X-ray; 1.90 A; A/B/C/D=2-361.
DR PDBsum; 1FBA; -.
DR AlphaFoldDB; P07764; -.
DR SMR; P07764; -.
DR BioGRID; 68080; 94.
DR IntAct; P07764; 67.
DR STRING; 7227.FBpp0302781; -.
DR iPTMnet; P07764; -.
DR PaxDb; P07764; -.
DR PRIDE; P07764; -.
DR DNASU; 43183; -.
DR EnsemblMetazoa; FBtr0084994; FBpp0084367; FBgn0000064. [P07764-1]
DR EnsemblMetazoa; FBtr0084995; FBpp0084368; FBgn0000064. [P07764-1]
DR EnsemblMetazoa; FBtr0084999; FBpp0084372; FBgn0000064. [P07764-1]
DR EnsemblMetazoa; FBtr0085000; FBpp0084373; FBgn0000064. [P07764-2]
DR EnsemblMetazoa; FBtr0085001; FBpp0089214; FBgn0000064. [P07764-3]
DR EnsemblMetazoa; FBtr0114544; FBpp0113036; FBgn0000064. [P07764-2]
DR EnsemblMetazoa; FBtr0306657; FBpp0297612; FBgn0000064. [P07764-3]
DR EnsemblMetazoa; FBtr0310660; FBpp0302780; FBgn0000064. [P07764-1]
DR EnsemblMetazoa; FBtr0310661; FBpp0302781; FBgn0000064. [P07764-3]
DR EnsemblMetazoa; FBtr0339614; FBpp0308680; FBgn0000064. [P07764-1]
DR GeneID; 43183; -.
DR KEGG; dme:Dmel_CG6058; -.
DR CTD; 43183; -.
DR FlyBase; FBgn0000064; Ald1.
DR VEuPathDB; VectorBase:FBgn0000064; -.
DR eggNOG; KOG1557; Eukaryota.
DR GeneTree; ENSGT00950000182987; -.
DR HOGENOM; CLU_031243_0_0_1; -.
DR InParanoid; P07764; -.
DR OMA; DYREMLF; -.
DR PhylomeDB; P07764; -.
DR Reactome; R-DME-114608; Platelet degranulation.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-70171; Glycolysis.
DR Reactome; R-DME-70263; Gluconeogenesis.
DR Reactome; R-DME-70350; Fructose catabolism.
DR SABIO-RK; P07764; -.
DR SignaLink; P07764; -.
DR UniPathway; UPA00109; UER00183.
DR BioGRID-ORCS; 43183; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Ald; fly.
DR EvolutionaryTrace; P07764; -.
DR GenomeRNAi; 43183; -.
DR PRO; PR:P07764; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0000064; Expressed in second segment of antenna (Drosophila) and 25 other tissues.
DR ExpressionAtlas; P07764; baseline and differential.
DR Genevisible; P07764; DM.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0031430; C:M band; IDA:FlyBase.
DR GO; GO:0030018; C:Z disc; IDA:FlyBase.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:FlyBase.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; IMP:FlyBase.
DR GO; GO:0006096; P:glycolytic process; IDA:FlyBase.
DR GO; GO:0007498; P:mesoderm development; NAS:FlyBase.
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; Acetylation; Alternative splicing; Direct protein sequencing;
KW Glycolysis; Lyase; Reference proteome; Schiff base.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1959612,
FT ECO:0000269|PubMed:3918528"
FT CHAIN 2..361
FT /note="Fructose-bisphosphate aldolase"
FT /id="PRO_0000216927"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 230
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT BINDING 56
FT /ligand="substrate"
FT BINDING 147
FT /ligand="substrate"
FT SITE 361
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|PubMed:1959612,
FT ECO:0000269|PubMed:3918528"
FT VAR_SEQ 335..361
FT /note="GDAAQGKYVAGSAGAGSGSLFVANHAY -> SQACQGIYVPGSIPSFAGNAN
FT LFVAQHKY (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_000221"
FT VAR_SEQ 336..361
FT /note="DAAQGKYVAGSAGAGSGSLFVANHAY -> EAACGNYTAGSVKGFAGKDTLH
FT VDDHRY (in isoform Alpha)"
FT /evidence="ECO:0000303|PubMed:7487099"
FT /id="VSP_000223"
FT CONFLICT 40
FT /note="M -> H (in Ref. 1; BAA01236/BAA01237/BAA01238 and 4;
FT BAA01592)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="K -> E (in Ref. 3; CAA42666/CAA42667)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="Q -> E (in Ref. 1; BAA01236/BAA01237/BAA01238 and 4;
FT BAA01592)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="R -> G (in Ref. 3; CAA42666/CAA42667)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="A -> T (in Ref. 3; CAA42666/CAA42667)"
FT /evidence="ECO:0000305"
FT HELIX 10..23
FT /evidence="ECO:0007829|PDB:1FBA"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1FBA"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:1FBA"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:1FBA"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:1FBA"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1FBA"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1FBA"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:1FBA"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:1FBA"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1FBA"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1FBA"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1FBA"
FT HELIX 131..140
FT /evidence="ECO:0007829|PDB:1FBA"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:1FBA"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1FBA"
FT HELIX 161..180
FT /evidence="ECO:0007829|PDB:1FBA"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:1FBA"
FT HELIX 199..219
FT /evidence="ECO:0007829|PDB:1FBA"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:1FBA"
FT HELIX 245..259
FT /evidence="ECO:0007829|PDB:1FBA"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:1FBA"
FT HELIX 276..286
FT /evidence="ECO:0007829|PDB:1FBA"
FT STRAND 295..302
FT /evidence="ECO:0007829|PDB:1FBA"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:1FBA"
FT HELIX 307..313
FT /evidence="ECO:0007829|PDB:1FBA"
FT HELIX 320..337
FT /evidence="ECO:0007829|PDB:1FBA"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:1FBA"
FT TURN 344..347
FT /evidence="ECO:0007829|PDB:1FBA"
SQ SEQUENCE 361 AA; 39047 MW; D8DA46E273668CE9 CRC64;
MTTYFNYPSK ELQDELREIA QKIVAPGKGI LAADESGPTM GKRLQDIGVE NTEDNRRAYR
QLLFSTDPKL AENISGVILF HETLYQKADD GTPFAEILKK KGIILGIKVD KGVVPLFGSE
DEVTTQGLDD LAARCAQYKK DGCDFAKWRC VLKIGKNTPS YQSILENANV LARYASICQS
QRIVPIVEPE VLPDGDHDLD RAQKVTETVL AAVYKALSDH HVYLEGTLLK PNMVTAGQSA
KKNTPEEIAL ATVQALRRTV PAAVTGVTFL SGGQSEEEAT VNLSAINNVP LIRPWALTFS
YGRALQASVL RAWAGKKENI AAGQNELLKR AKANGDAAQG KYVAGSAGAG SGSLFVANHA
Y
