ID A0A2K5E190_AOTNA Unreviewed; 364 AA.
AC A0A2K5E190;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|RuleBase:RU003994};
DE EC=4.1.2.13 {ECO:0000256|RuleBase:RU003994};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000026938.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000026938.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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_012319976.1; XM_012464553.1.
DR RefSeq; XP_012319977.1; XM_012464554.1.
DR RefSeq; XP_012319978.1; XM_012464555.1.
DR Ensembl; ENSANAT00000044900.1; ENSANAP00000026937.1; ENSANAG00000031251.1.
DR Ensembl; ENSANAT00000044901.1; ENSANAP00000026938.1; ENSANAG00000031251.1.
DR GeneID; 105725495; -.
DR CTD; 226; -.
DR GeneTree; ENSGT00950000182987; -.
DR OMA; WRAVITI; -.
DR OrthoDB; 3664741at2759; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000233020; 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:UP000233020};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
SQ SEQUENCE 364 AA; 39459 MW; EAFADEB0BD047A2E CRC64;
MPYQYPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR
QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN
GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS ALAIMENANV LARYASICQQ
NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC
TQKFSHEEIA MATVTALRRT VPPAVPGITF LSGGQSEEEA SINLNAINKC PLLKPWALTF
SYGRALQASA LKAWGGKKEN KKAAQEEYIK RALANSLACQ GKYTPSGQAG AAASESLFIS
NHAY
//
