ALDOA_RABIT
ID ALDOA_RABIT Reviewed; 364 AA.
AC P00883; Q28671;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Fructose-bisphosphate aldolase A;
DE EC=4.1.2.13 {ECO:0000269|PubMed:20129922};
DE AltName: Full=Muscle-type aldolase;
GN Name=ALDOA;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6546378; DOI=10.1016/s0021-9258(17)43576-9;
RA Tolan D.R., Amsden A.B., Putney S.D., Urdea M.S., Penhoet E.E.;
RT "The complete nucleotide sequence for rabbit muscle aldolase A messenger
RT RNA.";
RL J. Biol. Chem. 259:1127-1131(1984).
RN [2]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-364.
RC TISSUE=Muscle;
RX PubMed=4417717;
RA Sajgo M., Hajos G.;
RT "The amino acid sequence of rabbit muscle aldolase.";
RL Acta Biochim. Biophys. Acad. Sci. Hung. 9:239-241(1974).
RN [3]
RP PROTEIN SEQUENCE OF 2-364.
RC TISSUE=Muscle;
RX PubMed=4812352; DOI=10.1126/science.183.4130.1204;
RA Lai C.-Y., Nakai N., Chang D.;
RT "Amino acid sequence of rabbit muscle aldolase and the structure of the
RT active center.";
RL Science 183:1204-1206(1974).
RN [4]
RP PROTEIN SEQUENCE OF 2-165.
RX PubMed=1122141; DOI=10.1016/0003-9861(75)90397-5;
RA Nakai N., Chang D., Lai C.-Y.;
RT "Studies on the structure of rabbit muscle aldolase. Ordering of the
RT tryptic peptides; sequence of 164 amino acid residues in the NH2-terminal
RT BrCN peptide.";
RL Arch. Biochem. Biophys. 166:347-357(1975).
RN [5]
RP PROTEIN SEQUENCE OF 174-201, AND SEQUENCE REVISION.
RX PubMed=534504; DOI=10.1042/bj1830429;
RA Benfield P.A., Forcina B.G., Gibbons I., Perham R.N.;
RT "Extended amino acid sequences around the active-site lysine residue of
RT class-I fructose 1,6-bisphosphate aldolases from rabbit muscle, sturgeon
RT muscle, trout muscle and ox liver.";
RL Biochem. J. 183:429-444(1979).
RN [6]
RP PROTEIN SEQUENCE OF 252-364, AND SEQUENCE REVISION.
RX PubMed=1122142; DOI=10.1016/0003-9861(75)90398-7;
RA Lai C.-Y.;
RT "Studies on the structure of rabbit muscle aldolase. Determination of the
RT primary structure of the COOH-terminal BrCN peptide; the complete sequence
RT of the subunit polypeptide chain.";
RL Arch. Biochem. Biophys. 166:358-368(1975).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 38-56 AND 350-364.
RX PubMed=6687628; DOI=10.1038/302718a0;
RA Putney S.D., Herlihy W.C., Schimmel P.R.;
RT "A new troponin T and cDNA clones for 13 different muscle proteins, found
RT by shotgun sequencing.";
RL Nature 302:718-721(1983).
RN [8]
RP ACTIVE SITE, AND DEAMIDATION AT ASN-361.
RX PubMed=4857186; DOI=10.1016/s0006-291x(74)80360-8;
RA Hartman F.C., Welch M.H.;
RT "Identification of the histidyl residue of rabbit muscle aldolase alkylated
RT by N-bromoacetylethanolamine phosphate.";
RL Biochem. Biophys. Res. Commun. 57:85-92(1974).
RN [9]
RP ACTIVE SITE.
RX PubMed=5453; DOI=10.1016/s0021-9258(17)33499-3;
RA Hartman F.C., Brown J.P.;
RT "Affinity labeling of a previously undetected essential lysyl residue in
RT class I fructose bisphosphate aldolase.";
RL J. Biol. Chem. 251:3057-3062(1976).
RN [10]
RP SUBSTRATE-BINDING SITE.
RX PubMed=499203; DOI=10.1111/j.1432-1033.1979.tb13258.x;
RA Patthy L., Varadi A., Thesz J., Kovacs K.;
RT "Identification of the C-1-phosphate-binding arginine residue of rabbit-
RT muscle aldolase. Isolation of 1,2-cyclohexanedione-labeled peptide by
RT chemisorption chromatography.";
RL Eur. J. Biochem. 99:309-313(1979).
RN [11]
RP INTERACTION WITH FBP2, AND SUBCELLULAR LOCATION.
RX PubMed=15757649; DOI=10.1016/j.febslet.2005.01.071;
RA Mamczur P., Rakus D., Gizak A., Dus D., Dzugaj A.;
RT "The effect of calcium ions on subcellular localization of aldolase-FBPase
RT complex in skeletal muscle.";
RL FEBS Lett. 579:1607-1612(2005).
RN [12]
RP INTERACTION WITH FBP2.
RX PubMed=18214967; DOI=10.1002/prot.21909;
RA Gizak A., Maciaszczyk E., Dzugaj A., Eschrich K., Rakus D.;
RT "Evolutionary conserved N-terminal region of human muscle fructose 1,6-
RT bisphosphatase regulates its activity and the interaction with aldolase.";
RL Proteins 72:209-216(2008).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=8989320; DOI=10.1038/nsb0197-36;
RA Blom N., Sygusch J.;
RT "Product binding and role of the C-terminal region in class I D-fructose
RT 1,6-bisphosphate aldolase.";
RL Nat. Struct. Biol. 4:36-39(1997).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-345 IN COMPLEX WITH SUBSTRATE,
RP SUBUNIT, AND MUTAGENESIS OF GLU-35; ARG-43; LYS-147 AND ARG-304.
RX PubMed=10504235; DOI=10.1021/bi9828371;
RA Choi K.H., Mazurkie A.S., Morris A.J., Utheza D., Tolan D.R., Allen K.N.;
RT "Structure of a fructose-1,6-bis(phosphate) aldolase liganded to its
RT natural substrate in a cleavage-defective mutant at 2.3 A.";
RL Biochemistry 38:12655-12664(1999).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS), AND MUTAGENESIS OF GLU-188; GLU-190
RP AND LYS-230.
RX PubMed=11779856; DOI=10.1074/jbc.m107600200;
RA Maurady A., Zdanov A., de Moissac D., Beaudry D., Sygusch J.;
RT "A conserved glutamate residue exhibits multifunctional catalytic roles in
RT D-fructose-1,6-bisphosphate aldolases.";
RL J. Biol. Chem. 277:9474-9483(2002).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH WAS, AND FUNCTION.
RX PubMed=17329259; DOI=10.1074/jbc.m611505200;
RA St-Jean M., Izard T., Sygusch J.;
RT "A hydrophobic pocket in the active site of glycolytic aldolase mediates
RT interactions with Wiskott-Aldrich syndrome protein.";
RL J. Biol. Chem. 282:14309-14315(2007).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 5-344 OF MUTANT VAL-129, AND
RP SUBUNIT.
RX PubMed=18453690; DOI=10.1107/s0907444908004976;
RA Sherawat M., Tolan D.R., Allen K.N.;
RT "Structure of a rabbit muscle fructose-1,6-bisphosphate aldolase A dimer
RT variant.";
RL Acta Crystallogr. D 64:543-550(2008).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SNX9, INTERACTION
RP WITH SNX9, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=20129922; DOI=10.1074/jbc.m109.092049;
RA Rangarajan E.S., Park H., Fortin E., Sygusch J., Izard T.;
RT "Mechanism of aldolase control of sorting nexin 9 function in
RT endocytosis.";
RL J. Biol. Chem. 285:11983-11990(2010).
CC -!- FUNCTION: Plays a key role in glycolysis and gluconeogenesis. In
CC addition, may also function as scaffolding protein.
CC {ECO:0000269|PubMed:17329259}.
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:0000269|PubMed:20129922};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14730;
CC Evidence={ECO:0000305|PubMed:20129922};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SUBUNIT: Homotetramer. Interacts with SNX9 and WAS. Interacts with
CC FBP2; the interaction blocks FBP2 inhibition by physiological
CC concentrations of AMP and reduces inhibition by Ca(2+).
CC {ECO:0000269|PubMed:10504235, ECO:0000269|PubMed:15757649,
CC ECO:0000269|PubMed:17329259, ECO:0000269|PubMed:18214967,
CC ECO:0000269|PubMed:18453690, ECO:0000269|PubMed:20129922}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band
CC {ECO:0000269|PubMed:15757649}. Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000269|PubMed:15757649}. Note=In skeletal muscle, accumulates
CC around the M line and within the I band, colocalizing with FBP2 on both
CC sides of the Z line in the absence of Ca(2+).
CC -!- PTM: Asn-361 in form alpha is deaminated to Asp in form beta.
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.
CC -!- MISCELLANEOUS: Alkylation of Arg-43 inactivates the enzyme.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/ALD/";
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DR EMBL; K02300; AAA31156.1; -; mRNA.
DR EMBL; V00876; CAA24245.1; -; mRNA.
DR EMBL; V00877; CAA24246.1; -; mRNA.
DR PIR; A92444; ADRBA.
DR RefSeq; NP_001075707.1; NM_001082238.1.
DR RefSeq; XP_008256151.1; XM_008257929.2.
DR RefSeq; XP_008256152.1; XM_008257930.2.
DR RefSeq; XP_017197924.1; XM_017342435.1.
DR PDB; 1ADO; X-ray; 1.90 A; A/B/C/D=2-364.
DR PDB; 1EWD; X-ray; 2.46 A; A/B/C/D=2-364.
DR PDB; 1EWE; X-ray; 2.60 A; A/B/C/D=2-364.
DR PDB; 1EX5; X-ray; 2.20 A; A/B/C/D=2-364.
DR PDB; 1J4E; X-ray; 2.65 A; A/B/C/D=2-364.
DR PDB; 1ZAH; X-ray; 1.80 A; A/B/C/D=2-364.
DR PDB; 1ZAI; X-ray; 1.76 A; A/B/C/D=2-364.
DR PDB; 1ZAJ; X-ray; 1.89 A; A/B/C/D=2-364.
DR PDB; 1ZAL; X-ray; 1.89 A; A/B/C/D=2-364.
DR PDB; 2OT0; X-ray; 2.05 A; A/B/C/D=2-364.
DR PDB; 2OT1; X-ray; 2.05 A; A/B/C/D=2-364.
DR PDB; 2QUT; X-ray; 1.88 A; A/B/C/D=2-364.
DR PDB; 2QUU; X-ray; 1.98 A; A/B/C/D=2-364.
DR PDB; 2QUV; X-ray; 2.22 A; A/B/C/D=2-364.
DR PDB; 3B8D; X-ray; 2.00 A; A/B/C/D=2-364.
DR PDB; 3BV4; X-ray; 1.70 A; A=5-344.
DR PDB; 3DFN; X-ray; 1.86 A; A/B/C/D=2-364.
DR PDB; 3DFO; X-ray; 1.94 A; A/B/C/D=2-364.
DR PDB; 3DFP; X-ray; 2.05 A; A/B/C/D=2-364.
DR PDB; 3DFQ; X-ray; 1.82 A; A/B/C/D=2-364.
DR PDB; 3DFS; X-ray; 2.03 A; A/B/C/D=2-364.
DR PDB; 3DFT; X-ray; 1.94 A; A/B/C/D=2-364.
DR PDB; 3LGE; X-ray; 2.20 A; A/B/C/D=2-364.
DR PDB; 3TU9; X-ray; 2.09 A; A/B/C/D=2-364.
DR PDB; 5F4X; X-ray; 1.84 A; A/B/C/D=2-364.
DR PDB; 5TLE; X-ray; 1.58 A; A/B/C/D=2-364.
DR PDB; 5TLH; X-ray; 2.20 A; A/B/C/D=2-364.
DR PDB; 5TLW; X-ray; 2.29 A; A/B/C/D=2-364.
DR PDB; 5TLZ; X-ray; 1.97 A; A/B/C/D=2-364.
DR PDB; 5VY5; EM; 2.60 A; A/B/C/D=2-364.
DR PDB; 6ALD; X-ray; 2.30 A; A/B/C/D=2-364.
DR PDB; 6MWQ; EM; 3.00 A; A/B/C/D=12-348.
DR PDB; 6V20; EM; 2.13 A; A/B/C/D=3-345.
DR PDB; 7K9L; EM; 4.90 A; A/B/C/D=2-364.
DR PDB; 7K9X; EM; 3.80 A; A/B/C/D=2-364.
DR PDB; 7KA2; EM; 3.60 A; A/B/C/D=2-364.
DR PDB; 7KA3; EM; 3.30 A; A/B/C/D=2-364.
DR PDB; 7KA4; EM; 2.80 A; A/B/C/D=2-364.
DR PDB; 7VDC; EM; 3.28 A; A/B/C/D=1-364.
DR PDBsum; 1ADO; -.
DR PDBsum; 1EWD; -.
DR PDBsum; 1EWE; -.
DR PDBsum; 1EX5; -.
DR PDBsum; 1J4E; -.
DR PDBsum; 1ZAH; -.
DR PDBsum; 1ZAI; -.
DR PDBsum; 1ZAJ; -.
DR PDBsum; 1ZAL; -.
DR PDBsum; 2OT0; -.
DR PDBsum; 2OT1; -.
DR PDBsum; 2QUT; -.
DR PDBsum; 2QUU; -.
DR PDBsum; 2QUV; -.
DR PDBsum; 3B8D; -.
DR PDBsum; 3BV4; -.
DR PDBsum; 3DFN; -.
DR PDBsum; 3DFO; -.
DR PDBsum; 3DFP; -.
DR PDBsum; 3DFQ; -.
DR PDBsum; 3DFS; -.
DR PDBsum; 3DFT; -.
DR PDBsum; 3LGE; -.
DR PDBsum; 3TU9; -.
DR PDBsum; 5F4X; -.
DR PDBsum; 5TLE; -.
DR PDBsum; 5TLH; -.
DR PDBsum; 5TLW; -.
DR PDBsum; 5TLZ; -.
DR PDBsum; 5VY5; -.
DR PDBsum; 6ALD; -.
DR PDBsum; 6MWQ; -.
DR PDBsum; 6V20; -.
DR PDBsum; 7K9L; -.
DR PDBsum; 7K9X; -.
DR PDBsum; 7KA2; -.
DR PDBsum; 7KA3; -.
DR PDBsum; 7KA4; -.
DR PDBsum; 7VDC; -.
DR AlphaFoldDB; P00883; -.
DR PCDDB; P00883; -.
DR SASBDB; P00883; -.
DR SMR; P00883; -.
DR BioGRID; 1172078; 2.
DR IntAct; P00883; 1.
DR MINT; P00883; -.
DR STRING; 9986.ENSOCUP00000008499; -.
DR BindingDB; P00883; -.
DR ChEMBL; CHEMBL4695; -.
DR MoonProt; P00883; -.
DR iPTMnet; P00883; -.
DR MetOSite; P00883; -.
DR PRIDE; P00883; -.
DR Ensembl; ENSOCUT00000009869; ENSOCUP00000008499; ENSOCUG00000006329.
DR GeneID; 100009055; -.
DR KEGG; ocu:100009055; -.
DR CTD; 226; -.
DR eggNOG; KOG1557; Eukaryota.
DR GeneTree; ENSGT00950000182987; -.
DR HOGENOM; CLU_031243_1_0_1; -.
DR InParanoid; P00883; -.
DR OMA; DYREMLF; -.
DR OrthoDB; 799973at2759; -.
DR BRENDA; 4.1.2.13; 1749.
DR SABIO-RK; P00883; -.
DR UniPathway; UPA00109; UER00183.
DR EvolutionaryTrace; P00883; -.
DR PRO; PR:P00883; -.
DR Proteomes; UP000001811; Chromosome 6.
DR Bgee; ENSOCUG00000006329; Expressed in skeletal muscle tissue and 18 other tissues.
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; IDA:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; IDA:UniProtKB.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IMP:CAFA.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:CAFA.
DR GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
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 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Glycolysis; Hydroxylation; Isopeptide bond; Lyase; Phosphoprotein;
KW Reference proteome; Schiff base; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1122141,
FT ECO:0000269|PubMed:4812352"
FT CHAIN 2..364
FT /note="Fructose-bisphosphate aldolase A"
FT /id="PRO_0000216938"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:11779856"
FT ACT_SITE 230
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000269|PubMed:11779856"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10504235,
FT ECO:0007744|PDB:6ALD"
FT BINDING 272..274
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10504235,
FT ECO:0007744|PDB:6ALD"
FT BINDING 304
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10504235,
FT ECO:0007744|PDB:6ALD"
FT SITE 73
FT /note="Essential for substrate cleavage"
FT SITE 108
FT /note="Essential for substrate cleavage"
FT SITE 147
FT /note="Alkylation inactivates the enzyme"
FT SITE 362
FT /note="Alkylation inactivates the enzyme; essential for the
FT subsequent hydrolysis of the dihydroxyacetone Schiff base"
FT SITE 364
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MOD_RES 42
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MOD_RES 99
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MOD_RES 111
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09972"
FT MOD_RES 111
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05065"
FT MOD_RES 147
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MOD_RES 312
FT /note="N6-malonyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 330
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MOD_RES 361
FT /note="Deamidated asparagine; in form beta"
FT /evidence="ECO:0000269|PubMed:4857186"
FT CROSSLNK 42
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT CROSSLNK 42
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MUTAGEN 35
FT /note="E->A: Reduces activity 14-fold."
FT /evidence="ECO:0000269|PubMed:10504235"
FT MUTAGEN 43
FT /note="R->A: Reduces activity 14-fold."
FT /evidence="ECO:0000269|PubMed:10504235"
FT MUTAGEN 129
FT /note="D->V: Alters protein-protein interactions, leading
FT to a dimeric protein."
FT MUTAGEN 147
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10504235"
FT MUTAGEN 188
FT /note="E->A: Reduces activity over 100-fold."
FT /evidence="ECO:0000269|PubMed:11779856"
FT MUTAGEN 188
FT /note="E->Q: Reduces activity over 1000-fold."
FT /evidence="ECO:0000269|PubMed:11779856"
FT MUTAGEN 190
FT /note="E->Q: Reduces activity 20-fold."
FT /evidence="ECO:0000269|PubMed:11779856"
FT MUTAGEN 230
FT /note="K->M: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11779856"
FT MUTAGEN 304
FT /note="R->A: Reduces activity 400-fold."
FT /evidence="ECO:0000269|PubMed:10504235"
FT CONFLICT 35
FT /note="E -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 274..276
FT /note="GQS -> SQE (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="S -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 294..296
FT /note="KPW -> WPK (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="S -> R (in Ref. 7; CAA24246)"
FT /evidence="ECO:0000305"
FT HELIX 10..23
FT /evidence="ECO:0007829|PDB:5TLE"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:5TLE"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:5TLE"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:5TLE"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:5TLE"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:5TLE"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:5TLE"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:5TLE"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:5TLE"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:1EWE"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:5TLE"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:5TLE"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:5TLE"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:5TLE"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:5TLE"
FT HELIX 131..140
FT /evidence="ECO:0007829|PDB:5TLE"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:5TLE"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:5TLE"
FT HELIX 161..180
FT /evidence="ECO:0007829|PDB:5TLE"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:5TLE"
FT HELIX 199..219
FT /evidence="ECO:0007829|PDB:5TLE"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:5TLE"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:5TLE"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:5TLE"
FT HELIX 277..289
FT /evidence="ECO:0007829|PDB:5TLE"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:2QUV"
FT STRAND 296..303
FT /evidence="ECO:0007829|PDB:5TLE"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:5TLE"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:5TLE"
FT HELIX 321..338
FT /evidence="ECO:0007829|PDB:5TLE"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:5TLE"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:1ZAI"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:3DFQ"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:1ADO"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:5TLE"
SQ SEQUENCE 364 AA; 39343 MW; E61BCBC60F668324 CRC64;
MPHSHPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR
QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN
GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS ALAIMENANV LARYASICQQ
NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC
TQKYSHEEIA MATVTALRRT VPPAVTGVTF LSGGQSEEEA SINLNAINKC PLLKPWALTF
SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG AAASESLFIS
NHAY
