ID H2S1P9_TAKRU Unreviewed; 363 AA.
AC H2S1P9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 62.
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 Name=aldoc {ECO:0000313|Ensembl:ENSTRUP00000006320.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000006320.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000006320.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000006320.3}
RP IDENTIFICATION.
RG Ensembl;
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|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}.
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DR AlphaFoldDB; H2S1P9; -.
DR STRING; 31033.ENSTRUP00000006320; -.
DR Ensembl; ENSTRUT00000006360.3; ENSTRUP00000006320.3; ENSTRUG00000002712.3.
DR eggNOG; KOG1557; Eukaryota.
DR GeneTree; ENSGT00950000182987; -.
DR HOGENOM; CLU_031243_0_0_1; -.
DR InParanoid; H2S1P9; -.
DR OMA; FGSCHAY; -.
DR OrthoDB; 3664741at2759; -.
DR TreeFam; TF314203; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000005226; Chromosome 11.
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:SF3; FRUCTOSE-BISPHOSPHATE ALDOLASE C; 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:UP000005226};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
SQ SEQUENCE 363 AA; 39562 MW; AAFD14699B8B292B CRC64;
MTHQVPTLSE AQKRELHETA LRIVSPGKGI LAADESVGSM GKRLAQVGVE NTEENRRQFR
QILISADDRI NSCLGGVIFF HETLYQYSDN GVSFVKMIRD RDVLVGIKVD KGVVPLAGTA
GETTTQGLDG LSERCAQYKK DGASFAKWRC VLKISDTNPS RLAIMANANV LARYCSICQQ
HGIVPIIEPE VLPDGDHDLK RGQYVTEKVL AAVYKAMSDH HVYLEGTLLK PNMVTAGHSC
SIKYSPEEVA MATVTALRRT VPPAVSGIAF LSGGQSEEEA SIHLNAINNC RLATPWVLTF
SFGRALQASA LRAWRGHKEN EKAAAEQFVE RAEANSLACQ GKYSSGDDCG DVGLHNYGSR
HAY
//
