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Database: UniProt
Entry: A0A384AGF6_BALAS
LinkDB: A0A384AGF6_BALAS
Original site: A0A384AGF6_BALAS 
ID   A0A384AGF6_BALAS        Unreviewed;       364 AA.
AC   A0A384AGF6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|RuleBase:RU003994};
DE            EC=4.1.2.13 {ECO:0000256|RuleBase:RU003994};
GN   Name=ALDOA {ECO:0000313|RefSeq:XP_007186435.1,
GN   ECO:0000313|RefSeq:XP_007186436.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007186436.1};
RN   [1] {ECO:0000313|RefSeq:XP_007186435.1, ECO:0000313|RefSeq:XP_007186436.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007186435.1,
RC   ECO:0000313|RefSeq:XP_007186436.1};
RG   RefSeq;
RL   Submitted (JAN-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|ARBA:ARBA00036745};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14730;
CC         Evidence={ECO:0000256|ARBA:ARBA00036745};
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   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band
CC       {ECO:0000256|ARBA:ARBA00004355}. Cytoplasm, myofibril, sarcomere, M
CC       line {ECO:0000256|ARBA:ARBA00037833}.
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   RefSeq; XP_007186435.1; XM_007186373.2.
DR   RefSeq; XP_007186436.1; XM_007186374.1.
DR   AlphaFoldDB; A0A384AGF6; -.
DR   STRING; 310752.A0A384AGF6; -.
DR   GeneID; 103005198; -.
DR   KEGG; bacu:103005198; -.
DR   CTD; 226; -.
DR   InParanoid; A0A384AGF6; -.
DR   OrthoDB; 3664741at2759; -.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000261681; Unplaced.
DR   GO; GO:0031674; C:I band; IEA:UniProtKB-SubCell.
DR   GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
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:SF1; FRUCTOSE-BISPHOSPHATE ALDOLASE A; 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:UP000261681};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270}.
SQ   SEQUENCE   364 AA;  39386 MW;  5DC7BF4960924E34 CRC64;
     MPHQHPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR
     QLLLTADDRV NPCIGGVILF HETLYQKTDD GRPFPQVIKA KGGVVGIKVD KGVVPLAGTN
     GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS ALAIMENANV LARYASICQQ
     NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSAH HVYLEGTLLK PNMVTPGHAC
     THKYSHEEIA MATVTALRRT VPPAVPGITF LSGGQSEEEA SINLSAINKC HLLKPWALTF
     SYGRALQASA LKAWGGKKEN LKAAQEEYIK RALANSLACQ GKYTPSGKAG AAASESLFIS
     NHAY
//
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