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Database: UniProt
Entry: A0A2T7PI06_POMCA
LinkDB: A0A2T7PI06_POMCA
Original site: A0A2T7PI06_POMCA 
ID   A0A2T7PI06_POMCA        Unreviewed;       363 AA.
AC   A0A2T7PI06;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068, ECO:0000256|RuleBase:RU003994};
DE            EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068, ECO:0000256|RuleBase:RU003994};
GN   ORFNames=C0Q70_08497 {ECO:0000313|EMBL:PVD33049.1};
OS   Pomacea canaliculata (Golden apple snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX   NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD33049.1, ECO:0000313|Proteomes:UP000245119};
RN   [1] {ECO:0000313|EMBL:PVD33049.1, ECO:0000313|Proteomes:UP000245119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD33049.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PVD33049.1};
RA   Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA   Zhang G., Qian W., Fan W.;
RT   "The genome of golden apple snail Pomacea canaliculata provides insight
RT   into stress tolerance and invasive adaptation.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU003994};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC       {ECO:0000256|ARBA:ARBA00004714, ECO:0000256|RuleBase:RU004257}.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family. {ECO:0000256|ARBA:ARBA00010387, ECO:0000256|RuleBase:RU003994}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PVD33049.1}.
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DR   EMBL; PZQS01000004; PVD33049.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7PI06; -.
DR   STRING; 400727.A0A2T7PI06; -.
DR   EnsemblMetazoa; XM_025234815.1; XP_025090600.1; LOC112561943.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000245119; Miscellaneous, Linkage group lg4.
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:SF80; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR   Pfam; PF00274; Glycolytic; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|RuleBase:RU003994};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003994};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270}.
SQ   SEQUENCE   363 AA;  38872 MW;  96847D7A63E4154E CRC64;
     MPQFAQYLPP EKEEELREIA NAIVAPGKGI LAADESVSTC GKRLQGIGVE NTEENRRAYR
     ELLFTADKTL GDHISGVILF HETLYQKTSD GVPFVQCLKD RGIIPGIKVD KGVVPLAGTF
     NECTTQGLDG LSERCAEYKK AGAHFAKWRC VLKISKNTPS YLAMLENANV LARYASICQQ
     NGIVPIVEPE VLPDGDHDLA ESQAVTEDVL AFVYKALADH HVFLEGTLLK PNMCTPGQSC
     TKKASHEDIA RATVTALARR VPASVAGVTF LSGGQSEEDA TINLNAINQF PGRRPWPLTF
     SYGRALQASV LAAWGGKPQN VSAAQVELLN RSKANGEASM GTYGGGLGGA AGGKSLFVAD
     HAY
//
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