ID A0A2Y9QKQ7_DELLE Unreviewed; 364 AA.
AC A0A2Y9QKQ7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|RuleBase:RU003994};
DE EC=4.1.2.13 {ECO:0000256|RuleBase:RU003994};
GN Name=ALDOB {ECO:0000313|RefSeq:XP_022455953.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022455953.1};
RN [1] {ECO:0000313|RefSeq:XP_022455953.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022455953.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00036662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14730;
CC Evidence={ECO:0000256|ARBA:ARBA00036662};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14731;
CC Evidence={ECO:0000256|ARBA:ARBA00036662};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1-phosphate = D-glyceraldehyde +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:30851, ChEBI:CHEBI:17378,
CC ChEBI:CHEBI:57642, ChEBI:CHEBI:138881;
CC Evidence={ECO:0000256|ARBA:ARBA00036152};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30852;
CC Evidence={ECO:0000256|ARBA:ARBA00036152};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30853;
CC Evidence={ECO:0000256|ARBA:ARBA00036152};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
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 -!- PATHWAY: Carbohydrate metabolism; fructose metabolism.
CC {ECO:0000256|ARBA:ARBA00037915}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriolar satellite
CC {ECO:0000256|ARBA:ARBA00004607}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000256|ARBA:ARBA00010387, ECO:0000256|RuleBase:RU003994}.
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DR RefSeq; XP_022455953.1; XM_022600245.1.
DR AlphaFoldDB; A0A2Y9QKQ7; -.
DR STRING; 9749.A0A2Y9QKQ7; -.
DR KEGG; dle:111188054; -.
DR InParanoid; A0A2Y9QKQ7; -.
DR OrthoDB; 3664741at2759; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0034451; C:centriolar satellite; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0061609; F:fructose-1-phosphate aldolase activity; IEA:RHEA.
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:SF2; FRUCTOSE-BISPHOSPHATE ALDOLASE B; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Glycolysis {ECO:0000256|RuleBase:RU003994};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003994};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
SQ SEQUENCE 364 AA; 39425 MW; 11B33EF968CD244A CRC64;
MACQFPALTS EQKKELSEIA QCIVAGGKGI LAADESVGTM GSRLQRIKVE NTEENRRQFR
EILFTVDDSI SQSIGGVILF HETLYQKDSQ GRLFRDILKE KGIVVGIKLD QGGAPLAGTN
KETTIQGLDG LSERCAQYKK DGANFGKWRA VLKIDNQCPS HLAIQENANT LARYASICQQ
NGLVPIVEPE VLADGDHDME HCQYVTEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHAS
TKKYTPEQVA MATVTALYRT VPAAVPGICF LSGGMSEEDA TLNLNAINLC PLPKPWKLSF
SYGRALQASA LAAWSGKAAN KKATQEAFMK RALANCQAAK GQYVHTGSSG AASTQSLFTA
CYTY
//
