ID A0A3B3Q4V6_9TELE Unreviewed; 364 AA.
AC A0A3B3Q4V6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|RuleBase:RU003994};
DE EC=4.1.2.13 {ECO:0000256|RuleBase:RU003994};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000001642.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000001642.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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|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 -!- 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 AlphaFoldDB; A0A3B3Q4V6; -.
DR STRING; 1676925.ENSPKIP00000001642; -.
DR Ensembl; ENSPKIT00000025568.1; ENSPKIP00000001642.1; ENSPKIG00000019855.1.
DR GeneTree; ENSGT00950000182987; -.
DR OrthoDB; 3664741at2759; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0034451; C:centriolar satellite; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 Schiff base {ECO:0000256|ARBA:ARBA00023270}.
SQ SEQUENCE 364 AA; 39526 MW; 3A8198D8AEABB07D CRC64;
MTHQYPSLSP EQKKELSTIA QRIVAPGKGI LAADESVGTM GKRLQKINVE NNEENRRFFR
DLLFSVDSSI ANSIGGVIFF HETLYQKSDK GVLFPKLIKE KGIVVGIKVD KGTAGLNGTD
GETTTQGLDG LAERCAQYKK DGCDFAKWRC VLKISDGCPS ALAIAENANV LARYASICQQ
NGLVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTAGHSC
PKKFSPEEVA MATVSALRRT VPASVPGICF LSGGQSEEEA SLNLNAINQT PLHRPWKLTF
SYGRALQASA LSAWKGKQEN KQAAQNAFCT RAKINGLASR GEYKPAGEAN QAATQSLFTA
SYVY
//
