ID ALFC2_PEA Reviewed; 349 AA. AC Q01517; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 2. DT 27-MAR-2024, entry version 106. DE RecName: Full=Fructose-bisphosphate aldolase 2, chloroplastic; DE EC=4.1.2.13; OS Pisum sativum (Garden pea) (Lathyrus oleraceus). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum. OX NCBI_TaxID=3888; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-349, AND PROTEIN SEQUENCE OF 1-32. RC STRAIN=cv. Little Marvel, and cv. Sparkle; TISSUE=Leaf; RX PubMed=1524427; DOI=10.1016/0003-9861(92)90112-a; RA Razdan K., Heinrikson R.L., Zurcher-Neely H., Morris P.W., Anderson L.E.; RT "Chloroplast and cytoplasmic enzymes: isolation and sequencing of cDNAs RT coding for two distinct pea chloroplast aldolases."; RL Arch. Biochem. Biophys. 298:192-197(1992). 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: Plastid, chloroplast. 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; M97477; AAA33643.1; -; Genomic_DNA. DR PIR; S29048; S29048. DR AlphaFoldDB; Q01517; -. DR SMR; Q01517; -. DR SABIO-RK; Q01517; -. DR UniPathway; UPA00109; UER00183. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR CDD; cd00948; FBP_aldolase_I_a; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR029768; Aldolase_I_AS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000741; FBA_I. DR NCBIfam; NF033379; FrucBisAld_I; 1. DR PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1. DR PANTHER; PTHR11627:SF16; FRUCTOSE-BISPHOSPHATE ALDOLASE, CHLOROPLASTIC; 1. DR Pfam; PF00274; Glycolytic; 1. DR SUPFAM; SSF51569; Aldolase; 1. DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1. PE 1: Evidence at protein level; KW Chloroplast; Direct protein sequencing; Glycolysis; Lyase; Plastid; KW Schiff base. FT CHAIN 1..349 FT /note="Fructose-bisphosphate aldolase 2, chloroplastic" FT /id="PRO_0000216926" FT ACT_SITE 177 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 219 FT /note="Schiff-base intermediate with dihydroxyacetone-P" FT /evidence="ECO:0000250" FT BINDING 47 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 137 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 349 FT /note="Necessary for preference for fructose 1,6- FT bisphosphate over fructose 1-phosphate" FT /evidence="ECO:0000250" FT VARIANT 29 FT /note="A -> W (in strain: cv. Little Marvel)" SQ SEQUENCE 349 AA; 37827 MW; E50715D246B5D7D1 CRC64; GSYADELVKT AKTIASPGRG ILAMDESNAT CGKRLDSIGL ENTEANRQAW RTLLVTVPTL GEYISGAILF EETLYQSTVD GRKIVDVLVE QNIIPGIKVD KGLVPLAGSN NESWCQGLDG LASRSAAYYQ QGARFAKWRT VVSIPNGPSA LAVKEAAWGL ARYAAISQDN GLVPIVEPEI LLDGEHGIDR TFEVAQKVWA EVFYYLAENN VQFEGILLKP SMVTPGAESK DKASPTKVAE YTLNLLHRRI PPAVPGIMFL SGGQSEVEAT LNLNAMNKSP NPWHVSFSYA RALQNTALKT WGGLPENVKA AQEALLFRAK SNSLAQLGKY IGDGESEEAK KDCCQGYSY //