ALDOA_SALSA
ID ALDOA_SALSA Reviewed; 363 AA.
AC B5DGM7; B5DGM8; B5DGM9; B5RIB3;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Fructose-bisphosphate aldolase A {ECO:0000303|PubMed:23786287};
DE EC=4.1.2.13 {ECO:0000250|UniProtKB:P00883};
DE AltName: Full=Muscle-type aldolase {ECO:0000250|UniProtKB:P00883};
DE AltName: Allergen=Sal s 3.0101 {ECO:0000303|PubMed:23786287};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1] {ECO:0000312|EMBL:ACH70901.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=White muscle {ECO:0000312|EMBL:ACH70901.1};
RX PubMed=19878547; DOI=10.1186/1471-2164-10-502;
RA Andreassen R., Lunner S., Hoyheim B.;
RT "Characterization of full-length sequenced cDNA inserts (FLIcs) from
RT Atlantic salmon (Salmo salar).";
RL BMC Genomics 10:502-502(2009).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-14 AND 323-331, ALLERGEN, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Muscle {ECO:0000269|PubMed:23786287};
RX PubMed=23786287; DOI=10.1111/cea.12117;
RA Kuehn A., Hilger C., Lehners-Weber C., Codreanu-Morel F., Morisset M.,
RA Metz-Favre C., Pauli G., de Blay F., Revets D., Muller C.P., Vogel L.,
RA Vieths S., Hentges F.;
RT "Identification of enolases and aldolases as important fish allergens in
RT cod, salmon and tuna: component resolved diagnosis using parvalbumin and
RT the new allergens.";
RL Clin. Exp. Allergy 43:811-822(2013).
CC -!- FUNCTION: Plays a key role in glycolysis and gluconeogenesis.
CC {ECO:0000250|UniProtKB:P00883}.
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:0000250|UniProtKB:P04075};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14730;
CC Evidence={ECO:0000250|UniProtKB:P04075};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC {ECO:0000250|UniProtKB:P00883}.
CC -!- SUBUNIT: Tetramer. {ECO:0000250|UniProtKB:P00883}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC {ECO:0000269|PubMed:23786287}.
CC -!- MISCELLANEOUS: In vertebrates, three forms of this ubiquitous
CC glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver
CC and aldolase C in brain. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000255}.
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DR EMBL; BT043786; ACH70901.1; -; mRNA.
DR EMBL; BT043787; ACH70902.1; -; mRNA.
DR EMBL; BT043788; ACH70903.1; -; mRNA.
DR EMBL; BT043789; ACH70904.1; -; mRNA.
DR EMBL; BT044037; ACH85353.1; -; mRNA.
DR RefSeq; NP_001133180.1; NM_001139708.1.
DR RefSeq; NP_001133181.1; NM_001139709.1.
DR RefSeq; XP_014014713.1; XM_014159238.1.
DR RefSeq; XP_014014714.1; XM_014159239.1.
DR AlphaFoldDB; B5DGM7; -.
DR SMR; B5DGM7; -.
DR STRING; 8030.ENSSSAP00000045746; -.
DR Allergome; 10151; Sal s 3.
DR Allergome; 10152; Sal s 3.0101.
DR GeneID; 100194623; -.
DR GeneID; 100194624; -.
DR KEGG; sasa:100194623; -.
DR KEGG; sasa:100194624; -.
DR OMA; CLAKYIS; -.
DR OrthoDB; 799973at2759; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000087266; Chromosome ssa19.
DR Bgee; ENSSSAG00000047233; Expressed in muscle tissue and 14 other tissues.
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; -; 1.
DR InterPro; IPR029768; Aldolase_I_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Glycolysis; Lyase; Reference proteome;
KW Schiff base.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:23786287"
FT CHAIN 2..363
FT /note="Fructose-bisphosphate aldolase A"
FT /id="PRO_0000425073"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT ACT_SITE 230
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 304
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT SITE 363
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
SQ SEQUENCE 363 AA; 39556 MW; 97FF0EA19E1D1C72 CRC64;
MPHAFPFLTP DQKKELSDIA LKIVAKGKGI LAADESTGSV AKRFQSINTE NTEENRRLYR
QLLFTADDRA GPCIGGVIFF HETLYQKTDA GKTFPEHVKS RGWVVGIKVD KGVVPLAGTN
GETTTQGLDG LYERCAQYKK DGCDFAKWRC VLKITSTTPS RLAIMENCNV LARYASICQM
HGIVPIVEPE ILPDGDHDLK RTQYVTEKVL AAMYKALSDH HVYLEGTLLK PNMVTAGHSC
SHKYTHQEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SINLNVMNQC PLHRPWALTF
SYGRALQASA LKAWGGKPGN GKAAQEEFIK RALANSLACQ GKYVASGDSA AAGDSLFVAN
HAY
