ALF2_CAEEL
ID ALF2_CAEEL Reviewed; 366 AA.
AC P46563;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Fructose-bisphosphate aldolase 2;
DE EC=4.1.2.13;
DE AltName: Full=Aldolase CE-2;
DE Short=CE2;
GN Name=aldo-2; ORFNames=F01F1.12;
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 -!- 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: Restricted to the embryo and early larval stages.
CC -!- SIMILARITY: Belongs to the class I 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; D83739; BAA12092.1; -; mRNA.
DR EMBL; FO080705; CCD65997.1; -; Genomic_DNA.
DR PIR; T15951; T15951.
DR RefSeq; NP_001021240.1; NM_001026069.5.
DR AlphaFoldDB; P46563; -.
DR SMR; P46563; -.
DR BioGRID; 41049; 41.
DR DIP; DIP-24398N; -.
DR IntAct; P46563; 4.
DR STRING; 6239.F01F1.12a.1; -.
DR iPTMnet; P46563; -.
DR EPD; P46563; -.
DR PaxDb; P46563; -.
DR PeptideAtlas; P46563; -.
DR PRIDE; P46563; -.
DR EnsemblMetazoa; F01F1.12.1; F01F1.12.1; WBGene00017166.
DR EnsemblMetazoa; F01F1.12.2; F01F1.12.2; WBGene00017166.
DR GeneID; 175827; -.
DR KEGG; cel:CELE_F01F1.12; -.
DR UCSC; F01F1.12a; c. elegans.
DR CTD; 175827; -.
DR WormBase; F01F1.12; CE01225; WBGene00017166; aldo-2.
DR eggNOG; KOG1557; Eukaryota.
DR GeneTree; ENSGT00950000182987; -.
DR HOGENOM; CLU_031243_0_0_1; -.
DR InParanoid; P46563; -.
DR OMA; THQDIAM; -.
DR OrthoDB; 799973at2759; -.
DR PhylomeDB; P46563; -.
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 SignaLink; P46563; -.
DR UniPathway; UPA00109; UER00183.
DR PRO; PR:P46563; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00017166; Expressed in embryo and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:WormBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000792; C:heterochromatin; ISS:WormBase.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; ISS:WormBase.
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 2: Evidence at transcript level;
KW Glycolysis; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..366
FT /note="Fructose-bisphosphate aldolase 2"
FT /id="PRO_0000216929"
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 233
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 150
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"
SQ SEQUENCE 366 AA; 38846 MW; D6BD9D1469E69834 CRC64;
MATVGGAFKD SLTQAQKDEL HQIALKIVQD GKGILAADES TGTIGKRLDA INLENNETNR
QKYRQLLFTT PNLNQHISGV ILYEETFHQS TDKGEKFTDL LIKQGIVPGI KLDLGVVPLA
GTIGEGTTQG LDKLAERAAA FKKGGCGFAK WRCVLNIGTH TPSHLGMLEN ANVLARYASI
CQANGLVPIV EPEVLCDGEH DLARAQKVTE QVLAFVYKAL ADHHVYLEGT LLKPNMVTPG
QSSASKASHE AIGLATVTAL RRGVPAAVPG ITFLSGGQSE LDATANLNAI NSVQLGKPWK
LTFSYGRALQ ASVLKAWGGK DENIAAAQKT LLHRSKANGD ASLGKYAGED AAGAAAESLF
VAKHSY
