ID A0A368G9E6_ANCCA Unreviewed; 351 AA.
AC A0A368G9E6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=ANCCAN_13018 {ECO:0000313|EMBL:RCN41011.1};
OS Ancylostoma caninum (Dog hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN41011.1, ECO:0000313|Proteomes:UP000252519};
RN [1] {ECO:0000313|EMBL:RCN41011.1, ECO:0000313|Proteomes:UP000252519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Baltimore {ECO:0000313|EMBL:RCN41011.1,
RC ECO:0000313|Proteomes:UP000252519};
RA Mitreva M.;
RT "Draft genome of the hookworm Ancylostoma caninum.";
RL Submitted (OCT-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RCN41011.1}.
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DR EMBL; JOJR01000253; RCN41011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368G9E6; -.
DR STRING; 29170.A0A368G9E6; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000252519; 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; 3.
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:SF80; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR Pfam; PF00274; Glycolytic; 2.
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:UP000252519};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
SQ SEQUENCE 351 AA; 38295 MW; 5B4FFB7518B07323 CRC64;
MASYSQYLTK EKEDELRGIA NAIVSAGKGI LAADESTGSM EKRLKSIGLE NTEENRRKYR
QLLFTGNPDL GKHISGVIMF HETFYQKADD GSRFVDVLKK QGIIPGIKVD KGVVPMAGTV
GEATTQGLDD LNQRCAQYKK ASISFVLKIP GKGTKELHAN LLGNRDSDGA QFAKWRCVHK
ISVTTPSHTA LVEIAQVLAR YASICQQNGL VPIVEPEILP DGEHDIDRCQ KITETVLSYC
YRALNDHHVF LEGTLLKPNM VTAGQSFKGK KPSPDEVQGK KPWVLTFSYG RALQASCLAK
WSGKDENVKA AQAVLLKRAQ ANSLASVGKY TGDPNADAAA SKSLFVANHA Y
//