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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//