ID A0A2Y9J6M8_ENHLU Unreviewed; 364 AA.
AC A0A2Y9J6M8;
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=LOC111145727 {ECO:0000313|RefSeq:XP_022356592.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022356592.1};
RN [1] {ECO:0000313|RefSeq:XP_022356592.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022356592.1};
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_022356592.1; XM_022500884.1.
DR AlphaFoldDB; A0A2Y9J6M8; -.
DR STRING; 391180.A0A2Y9J6M8; -.
DR KEGG; elk:111145727; -.
DR OrthoDB; 3664741at2759; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000248482; 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:UP000248482};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
SQ SEQUENCE 364 AA; 39648 MW; 80003840CB74E176 CRC64;
MAYRFPALTS EQKKELSEIA QRIVAHGKGI LAADESVGTM GNRLQRIKVE NTEENRRQFR
EILFTVDTSI NQSIGGVILF HETLYQKDSQ GKLFRNILKE KGIVVGIKLD QGGAPLAGTN
KETTIQGLDG LSERCAQYKR DGADFGKWRA VLRIDNQCPS SLAIQENANA LARYASICQQ
NGLVPIVEPE VIPDGDHDLE HCQYVTEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHAC
TKKYTPEQVA MATVTALHRT VPAAVPGICF LSGGMSEEDA TLNLNAINLC PLPKPWKLSF
SYGRALQASA LAAWGGKAAN KKATQEAFMK RAVANCQAAQ GQYVHTGSSG TTSTQSLFTA
CYTY
//
