ID A0A0N4TKF1_BRUPA Unreviewed; 382 AA.
AC A0A0N4TKF1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=BPAG_LOCUS8773 {ECO:0000313|EMBL:VDN89959.1};
OS Brugia pahangi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0000881101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BPAG_0000881101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN89959.1, ECO:0000313|Proteomes:UP000278627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-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}.
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DR EMBL; UZAD01013140; VDN89959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4TKF1; -.
DR STRING; 6280.A0A0N4TKF1; -.
DR WBParaSite; BPAG_0000881101-mRNA-1; BPAG_0000881101-mRNA-1; BPAG_0000881101.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000038020; Unplaced.
DR Proteomes; UP000278627; Unassembled WGS sequence.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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:SF9; FRUCTOSE-BISPHOSPHATE ALDOLASE 2; 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:UP000278627};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
SQ SEQUENCE 382 AA; 42540 MW; 3D54F177E569C810 CRC64;
MPLNIYRILV DGALVITISI LLTYHRNISD KSVLEEKEAV VVVATLNRNQ KDELHTIARK
LVESGKGILA ADESIDTIGK RFAMIGMENN VRNRKNYRYM LFTTPNISQY ISGIILHEET
FSQRDDAGKP FVDIVKEAGI LPGIKLDKGL EPFDGGLEYI TRGLDDLKER AEYFKKGGCQ
FAKWRCVYKI SDVTPSRKVL KENAKILAQY AVLSQQAGLV PIIEPEVLSD GAHDLEKAEN
VTEQVLAEVY KSLHDHGVYL EGTLLKPNMV IPGSKFTGKV GHDRIAKETF RALTRTVPAA
VPGIVFLSGG QLEKDATRNL NEINKIAINK PWKLSFSYGR ALQTSALKEL TISGSKEAQT
TFRHRAKLNA LAVEGNYIDD LE
//
