ALF1_CAEEL
ID ALF1_CAEEL Reviewed; 366 AA.
AC P54216; O45747;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Fructose-bisphosphate aldolase 1;
DE EC=4.1.2.13 {ECO:0000269|PubMed:9056253};
DE AltName: Full=Aldolase CE-1;
DE Short=CE-1 {ECO:0000303|PubMed:9056253};
GN Name=aldo-1; ORFNames=T05D4.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RX PubMed=9056253; DOI=10.1006/abbi.1996.9813;
RA Inoue T., Yatsuki H., Kusakabe T., Joh K., Hori K.;
RT "Caenorhabditis elegans has two isozymic forms, CE-1 and CE-2, of fructose-
RT 1,6-bisphosphate aldolase which are encoded by different genes.";
RL Arch. Biochem. Biophys. 339:226-234(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: May be involved in the metabolism of fructose-bisphosphate
CC (beta-D-fructose 1,6-bisphosphate) and of fructose 1-phosphate.
CC {ECO:0000269|PubMed:9056253}.
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:9056253};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14730;
CC Evidence={ECO:0000269|PubMed:9056253};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16.7 uM for beta-D-fructose 1,6-bisphosphate
CC {ECO:0000269|PubMed:9056253};
CC KM=0.56 mM for fructose 1-phosphate {ECO:0000269|PubMed:9056253};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- INTERACTION:
CC P54216; P54216: aldo-1; NbExp=3; IntAct=EBI-327260, EBI-327260;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DEVELOPMENTAL STAGE: All stages of development.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; D83738; BAA12091.1; -; mRNA.
DR EMBL; Z81115; CAB03291.1; -; Genomic_DNA.
DR PIR; T24514; T24514.
DR RefSeq; NP_741281.1; NM_171235.3.
DR AlphaFoldDB; P54216; -.
DR SMR; P54216; -.
DR BioGRID; 41956; 30.
DR DIP; DIP-25939N; -.
DR IntAct; P54216; 1.
DR STRING; 6239.T05D4.1.1; -.
DR iPTMnet; P54216; -.
DR EPD; P54216; -.
DR PaxDb; P54216; -.
DR PeptideAtlas; P54216; -.
DR EnsemblMetazoa; T05D4.1.1; T05D4.1.1; WBGene00011474.
DR GeneID; 176788; -.
DR KEGG; cel:CELE_T05D4.1; -.
DR UCSC; T05D4.1.1; c. elegans.
DR CTD; 176788; -.
DR WormBase; T05D4.1; CE16341; WBGene00011474; aldo-1.
DR eggNOG; KOG1557; Eukaryota.
DR GeneTree; ENSGT00950000182987; -.
DR HOGENOM; CLU_031243_0_0_1; -.
DR InParanoid; P54216; -.
DR OrthoDB; 799973at2759; -.
DR PhylomeDB; P54216; -.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-70171; Glycolysis.
DR Reactome; R-CEL-70263; Gluconeogenesis.
DR Reactome; R-CEL-70350; Fructose catabolism.
DR UniPathway; UPA00109; UER00183.
DR PRO; PR:P54216; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00011474; Expressed in larva and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:WormBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:WormBase.
DR GO; GO:0000792; C:heterochromatin; ISS:WormBase.
DR GO; GO:0030017; C:sarcomere; HDA:WormBase.
DR GO; GO:0055120; C:striated muscle dense body; HDA:WormBase.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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 Glycolysis; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..366
FT /note="Fructose-bisphosphate aldolase 1"
FT /id="PRO_0000216928"
FT ACT_SITE 189
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 231
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 366
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
FT CONFLICT 172..173
FT /note="GS -> A (in Ref. 2; CAB03291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 366 AA; 39240 MW; 5B9F91D486FFAEB5 CRC64;
MASYSQFLTK AQEDELRSIA NAIVTPGKGI LAADESTGSM DKRLNSIGLE NTEENRRKYR
QLLFTAGADL NKYISGVIMF HETFYQKTDD GKPFTALLQE QGIIPGIKVD KGVVPMAGTI
GEGTTQGLDD LNARCAQYKK DGAQFAKWRC VHKISSTTPS VTALKEIASN LGSRYASICQ
QNGLVPIVEP EILPDGEHCL ARGQKITETV LSYVYHALNE HHVFLEGTLL KPNMVTSGQS
FTGEKPSNAD IGLATVTALQ RGVPSAVPGV VFLSGGQSEE DATLNLNAIN QVSGKKPWAL
TFSYGRALQA SCLAKWAGKD ENIAAAQEVL LHRAQVNSLA SVGKYTGDAS ADAAASQSLF
VANHSY
