ID A0A0N4YEY5_NIPBR Unreviewed; 314 AA.
AC A0A0N4YEY5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=NBR_LOCUS15290 {ECO:0000313|EMBL:VDL78884.1};
OS Nippostrongylus brasiliensis (Rat hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Heligmosomidae; Nippostrongylus.
OX NCBI_TaxID=27835 {ECO:0000313|Proteomes:UP000038043, ECO:0000313|WBParaSite:NBR_0001528901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:NBR_0001528901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL78884.1, ECO:0000313|Proteomes:UP000271162}
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; UYSL01021672; VDL78884.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4YEY5; -.
DR STRING; 27835.A0A0N4YEY5; -.
DR WBParaSite; NBR_0001528901-mRNA-1; NBR_0001528901-mRNA-1; NBR_0001528901.
DR OMA; NKPWKLS; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000038043; Unplaced.
DR Proteomes; UP000271162; 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; 2.
DR InterPro; IPR029768; Aldolase_I_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
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:UP000271162};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..314
FT /note="Fructose-bisphosphate aldolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033232152"
SQ SEQUENCE 314 AA; 33660 MW; 46CB70B5D7C534D8 CRC64;
MIGSLWWVSA SLLLRSISGE GPPIDTCPSA GSRSSSVTHT MAEVGGSYKD SLTQEQKDDL
RAIAEKIVAD GKGILAADES TGTIGKRLSA ISLENNEDNR RKYRQLLFTT PNIGQHISGV
ILYEETFNQS TDSGEKFVDV LIKQGIVPGI KLDLGVTEQV LAYVYKALAD HHVYLEGTLL
KPNMVTPGQD CPTKATHEEI GLATVTALRR GVPAAVPGIT FLSGGQSELD ATANLHAINT
VKLLKPWKLT FSYGRALQAS VLKAWQGKDE NIEAAQKVLL HRAQANGMAS LGKYEGEDAA
GAAAESLFIA KHSY
//
