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Fructose-1,6-bisphosphatase 1 (FBPase 1) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 1) (Liver FBPase)

 F16P1_PIG               Reviewed;         338 AA.
P00636;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
28-FEB-2018, entry version 156.
RecName: Full=Fructose-1,6-bisphosphatase 1;
Short=FBPase 1;
EC=3.1.3.11;
AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase 1;
AltName: Full=Liver FBPase;
Name=FBP1; Synonyms=FBP;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=1313579; DOI=10.1073/pnas.89.7.3080;
Williams M.K., Kantrowitz E.R.;
"Isolation and sequence analysis of the cDNA for pig kidney fructose
1,6-bisphosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 89:3080-3082(1992).
[2]
PROTEIN SEQUENCE OF 2-336, ACETYLATION AT THR-2, AND PHOSPHORYLATION
AT SER-208.
TISSUE=Kidney cortex;
PubMed=6296821; DOI=10.1073/pnas.79.23.7161;
Marcus F., Edelstein I., Reardon I., Heinrikson R.L.;
"Complete amino acid sequence of pig kidney fructose-1,6-
bisphosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 79:7161-7165(1982).
[3]
PROTEIN SEQUENCE OF 2-24 AND 44-61, AND ACETYLATION AT THR-2.
TISSUE=Kidney;
PubMed=6291465; DOI=10.1016/0003-9861(82)90547-1;
McGregor J.S., Hannappel E., Xu G.-J., Pontremoli S., Horecker B.L.;
"Conservation of primary structure at the proteinase-sensitive site of
fructose 1,6-bisphosphatases.";
Arch. Biochem. Biophys. 217:652-664(1982).
[4]
SUBSTRATE-BINDING SITE, LIGANDS, AND REVIEW.
PubMed=6277165;
Benkovic S.J., Demaine M.M.;
"Mechanism of action of fructose 1,6-bisphosphatase.";
Adv. Enzymol. Relat. Areas Mol. Biol. 53:45-82(1982).
[5]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH
FRUCTOSE-2,6-BISPHOSPHATE, AND SEQUENCE REVISION.
PubMed=2157849; DOI=10.1016/0022-2836(90)90329-K;
Ke H.M., Thorpe C.M., Seaton B.A., Lipscomb W.N., Marcus F.;
"Structure refinement of fructose-1,6-bisphosphatase and its fructose
2,6-bisphosphate complex at 2.8-A resolution.";
J. Mol. Biol. 212:513-539(1990).
[6]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH
FRUCTOSE-6-PHOSPHATE; AMP AND MAGNESIUM, ENZYME REGULATION, AND
SUBUNIT.
PubMed=2164670; DOI=10.1073/pnas.87.14.5243;
Ke H.M., Zhang Y.P., Lipscomb W.N.;
"Crystal structure of fructose-1,6-bisphosphatase complexed with
fructose 6-phosphate, AMP, and magnesium.";
Proc. Natl. Acad. Sci. U.S.A. 87:5243-5247(1990).
[7]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH
FRUCTOSE-6-PHOSPHATE.
PubMed=1849642; DOI=10.1073/pnas.88.8.2989;
Ke H.M., Zhang Y.P., Liang J.-Y., Lipscomb W.N.;
"Crystal structure of the neutral form of fructose-1,6-bisphosphatase
complexed with the product fructose 6-phosphate at 2.1-A resolution.";
Proc. Natl. Acad. Sci. U.S.A. 88:2989-2993(1991).
[8]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH
FRUCTOSE-2,6-BISPHOSPHATE.
PubMed=1312721; DOI=10.1073/pnas.89.6.2404;
Liang J.-Y., Huang S., Zhang Y.P., Ke H.M., Lipscomb W.N.;
"Crystal structure of the neutral form of fructose 1,6-bisphosphatase
complexed with regulatory inhibitor fructose 2,6-bisphosphate at 2.6-A
resolution.";
Proc. Natl. Acad. Sci. U.S.A. 89:2404-2408(1992).
[9]
X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) IN COMPLEX WITH ZINC IONS,
COFACTOR, AND ENZYME REGULATION.
PubMed=9708979; DOI=10.1021/bi981112u;
Choe J.-Y., Poland B.W., Fromm H.J., Honzatko R.B.;
"Role of a dynamic loop in cation activation and allosteric regulation
of recombinant porcine fructose-1,6-bisphosphatase.";
Biochemistry 37:11441-11450(1998).
[10]
X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) IN COMPLEXES WITH
FRUCTOSE-6-PHOSPHATE; PHOSPHATE; AMP; MAGNESIUM AND ZINC IONS,
SUBUNIT, AND ENZYME REGULATION.
PubMed=10913263; DOI=10.1021/bi000574g;
Choe J.-Y., Fromm H.J., Honzatko R.B.;
"Crystal structures of fructose 1,6-bisphosphatase: mechanism of
catalysis and allosteric inhibition revealed in product complexes.";
Biochemistry 39:8565-8574(2000).
[11]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM
IONS; FRUCTOSE-6-PHOSPHATE AND PHOSPHATE, COFACTOR, AND ENZYME
MECHANISM.
PubMed=12595528; DOI=10.1074/jbc.M212395200;
Choe J.-Y., Iancu C.V., Fromm H.J., Honzatko R.B.;
"Metaphosphate in the active site of fructose-1,6-bisphosphatase.";
J. Biol. Chem. 278:16015-16020(2003).
[12]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH THE SYNTHETIC
INHIBITOR OC252; FRUCTOSE-6-PHOSPHATE; PHOSPHATE AND DIVALENT METAL
CATIONS, COFACTOR, SUBUNIT, AND ENZYME REGULATION.
PubMed=14530289; DOI=10.1074/jbc.M308396200;
Choe J.-Y., Nelson S.W., Arienti K.L., Axe F.U., Collins T.L.,
Jones T.K., Kimmich R.D.A., Newman M.J., Norvell K., Ripka W.C.,
Romano S.J., Short K.M., Slee D.H., Fromm H.J., Honzatko R.B.;
"Inhibition of fructose-1,6-bisphosphatase by a new class of
allosteric effectors.";
J. Biol. Chem. 278:51176-51183(2003).
[13]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT LEU-55 IN COMPLEXES
WITH AMP; FRUCTORSE-6-PHOSPHAT; PHOSPHATE AND MAGNESIUM IONS, SUBUNIT,
COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
PubMed=15767255; DOI=10.1074/jbc.M501011200;
Iancu C.V., Mukund S., Fromm H.J., Honzatko R.B.;
"R-state AMP complex reveals initial steps of the quaternary
transition of fructose-1,6-bisphosphatase.";
J. Biol. Chem. 280:19737-19745(2005).
[14]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM IONS
AND FRUCTOSE-2,6-DIPHOSPHATE, SUBUNIT, AND ENZYME REGULATION.
PubMed=17933867; DOI=10.1074/jbc.M707302200;
Hines J.K., Chen X., Nix J.C., Fromm H.J., Honzatko R.B.;
"Structures of mammalian and bacterial fructose-1,6-bisphosphatase
reveal the basis for synergism in AMP/fructose 2,6-bisphosphate
inhibition.";
J. Biol. Chem. 282:36121-36131(2007).
-!- FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to
fructose 6-phosphate in the presence of divalent cations, acting
as a rate-limiting enzyme in gluconeogenesis. Plays a role in
regulating glucose sensing and insulin secretion of pancreatic
beta-cells. Appears to modulate glycerol gluconeogenesis in liver.
Important regulator of appetite and adiposity; increased
expression of the protein in liver after nutrient excess increases
circulating satiety hormones and reduces appetite-stimulating
neuropeptides and thus seems to provide a feedback mechanism to
limit weight gain (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D-
fructose 6-phosphate + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:12595528,
ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255,
ECO:0000269|PubMed:9708979};
Note=Binds 3 Mg(2+) ions per subunit.
{ECO:0000269|PubMed:12595528, ECO:0000269|PubMed:14530289,
ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:9708979};
-!- ENZYME REGULATION: Subject to complex allosteric regulation. The
enzyme can assume an active R-state, or an inactive T-state.
Intermediate conformations may exist. AMP acts as allosteric
inhibitor. AMP binding affects the turnover of bound substrate and
not the affinity for substrate. Fructose 2,6-bisphosphate acts as
competitive inhibitor. Fructose 2,6-bisphosphate and AMP have
synergistic effects. {ECO:0000269|PubMed:10913263,
ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255,
ECO:0000269|PubMed:17933867, ECO:0000269|PubMed:2164670,
ECO:0000269|PubMed:9708979}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.2 uM for fructose-1,6-diphosphate
{ECO:0000269|PubMed:15767255};
-!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10913263,
ECO:0000269|PubMed:1312721, ECO:0000269|PubMed:14530289,
ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:17933867,
ECO:0000269|PubMed:1849642, ECO:0000269|PubMed:2157849,
ECO:0000269|PubMed:2164670, ECO:0000269|PubMed:9708979}.
-!- MISCELLANEOUS: The molecule has a highly reactive cysteine residue
(Cys-117 or Cys-129), which tends to form mixed disulfides (e.g.
with homocystine) but is not essential for enzyme activity.
-!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}.
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EMBL; M86347; AAA31035.1; -; mRNA.
PIR; S37696; PAPGF.
RefSeq; NP_999144.1; NM_213979.1.
UniGene; Ssc.5127; -.
PDB; 1CNQ; X-ray; 2.27 A; A=2-338.
PDB; 1EYI; X-ray; 2.32 A; A=2-338.
PDB; 1EYJ; X-ray; 2.28 A; A/B=2-338.
PDB; 1EYK; X-ray; 2.23 A; A/B=2-338.
PDB; 1FBC; X-ray; 2.60 A; A/B=2-336.
PDB; 1FBD; X-ray; 2.90 A; A/B=2-336.
PDB; 1FBE; X-ray; 3.00 A; A/B=2-336.
PDB; 1FBF; X-ray; 2.70 A; A/B=2-336.
PDB; 1FBG; X-ray; 3.00 A; A/B=2-336.
PDB; 1FBH; X-ray; 2.50 A; A/B=2-336.
PDB; 1FBP; X-ray; 2.50 A; A/B=2-336.
PDB; 1FJ6; X-ray; 2.50 A; A=2-338.
PDB; 1FJ9; X-ray; 2.50 A; A/B=2-338.
PDB; 1FPB; X-ray; 2.60 A; A/B=2-336.
PDB; 1FPD; X-ray; 2.10 A; A/B=2-336.
PDB; 1FPE; X-ray; 2.20 A; A/B=2-336.
PDB; 1FPF; X-ray; 2.10 A; A/B=2-336.
PDB; 1FPG; X-ray; 2.30 A; A/B=2-336.
PDB; 1FPI; X-ray; 2.30 A; A/B=2-336.
PDB; 1FPJ; X-ray; 2.20 A; A/B=2-336.
PDB; 1FPK; X-ray; 3.00 A; A/B=2-336.
PDB; 1FPL; X-ray; 2.30 A; A/B=2-336.
PDB; 1FRP; X-ray; 2.00 A; A/B=2-336.
PDB; 1FSA; X-ray; 2.30 A; A/B=2-338.
PDB; 1KZ8; X-ray; 2.00 A; A/F=2-338.
PDB; 1LEV; X-ray; 2.15 A; A/F=2-338.
PDB; 1NUW; X-ray; 1.30 A; A=2-338.
PDB; 1NUX; X-ray; 1.60 A; A=2-338.
PDB; 1NUY; X-ray; 1.30 A; A=2-338.
PDB; 1NUZ; X-ray; 1.90 A; A=2-338.
PDB; 1NV0; X-ray; 1.80 A; A=2-338.
PDB; 1NV1; X-ray; 1.90 A; A=2-338.
PDB; 1NV2; X-ray; 2.10 A; A=2-338.
PDB; 1NV3; X-ray; 2.00 A; A=2-338.
PDB; 1NV4; X-ray; 1.90 A; A=2-338.
PDB; 1NV5; X-ray; 1.90 A; A=2-338.
PDB; 1NV6; X-ray; 2.15 A; A=2-338.
PDB; 1NV7; X-ray; 2.15 A; A/B=2-338.
PDB; 1Q9D; X-ray; 2.35 A; A/B=2-338.
PDB; 1RDX; X-ray; 2.75 A; A/B=2-338.
PDB; 1RDY; X-ray; 2.20 A; A/B=2-338.
PDB; 1RDZ; X-ray; 2.05 A; A/B=2-338.
PDB; 1YXI; X-ray; 2.00 A; A=2-338.
PDB; 1YYZ; X-ray; 1.85 A; A=2-338.
PDB; 1YZ0; X-ray; 2.07 A; A/B=2-338.
PDB; 2F3B; X-ray; 1.80 A; A=1-338.
PDB; 2F3D; X-ray; 1.83 A; A=1-338.
PDB; 2FBP; X-ray; 2.80 A; A/B=2-336.
PDB; 2QVU; X-ray; 1.50 A; A/B=2-338.
PDB; 2QVV; X-ray; 2.03 A; A/B=2-338.
PDB; 3FBP; X-ray; 2.80 A; A/B=2-336.
PDB; 4FBP; X-ray; 2.50 A; A/B/C/D=2-336.
PDB; 4GBV; X-ray; 2.90 A; A=2-336.
PDB; 4GBW; X-ray; 2.00 A; A=2-336.
PDB; 4GWS; X-ray; 2.75 A; A/B=2-338.
PDB; 4GWU; X-ray; 3.00 A; A=2-338.
PDB; 4GWW; X-ray; 3.20 A; A=2-338.
PDB; 4GWX; X-ray; 2.35 A; A=2-338.
PDB; 4GWY; X-ray; 3.00 A; A=2-338.
PDB; 4GWZ; X-ray; 2.60 A; A/B=2-338.
PDB; 4GX3; X-ray; 2.25 A; A/B=2-338.
PDB; 4GX4; X-ray; 2.50 A; A/B=2-338.
PDB; 4GX6; X-ray; 2.50 A; A/B=2-338.
PDB; 4H45; X-ray; 3.10 A; A=2-338.
PDB; 4H46; X-ray; 2.50 A; A=2-338.
PDB; 4KXP; X-ray; 2.70 A; A/B=1-338.
PDB; 5FBP; X-ray; 2.10 A; A/B=2-336.
PDBsum; 1CNQ; -.
PDBsum; 1EYI; -.
PDBsum; 1EYJ; -.
PDBsum; 1EYK; -.
PDBsum; 1FBC; -.
PDBsum; 1FBD; -.
PDBsum; 1FBE; -.
PDBsum; 1FBF; -.
PDBsum; 1FBG; -.
PDBsum; 1FBH; -.
PDBsum; 1FBP; -.
PDBsum; 1FJ6; -.
PDBsum; 1FJ9; -.
PDBsum; 1FPB; -.
PDBsum; 1FPD; -.
PDBsum; 1FPE; -.
PDBsum; 1FPF; -.
PDBsum; 1FPG; -.
PDBsum; 1FPI; -.
PDBsum; 1FPJ; -.
PDBsum; 1FPK; -.
PDBsum; 1FPL; -.
PDBsum; 1FRP; -.
PDBsum; 1FSA; -.
PDBsum; 1KZ8; -.
PDBsum; 1LEV; -.
PDBsum; 1NUW; -.
PDBsum; 1NUX; -.
PDBsum; 1NUY; -.
PDBsum; 1NUZ; -.
PDBsum; 1NV0; -.
PDBsum; 1NV1; -.
PDBsum; 1NV2; -.
PDBsum; 1NV3; -.
PDBsum; 1NV4; -.
PDBsum; 1NV5; -.
PDBsum; 1NV6; -.
PDBsum; 1NV7; -.
PDBsum; 1Q9D; -.
PDBsum; 1RDX; -.
PDBsum; 1RDY; -.
PDBsum; 1RDZ; -.
PDBsum; 1YXI; -.
PDBsum; 1YYZ; -.
PDBsum; 1YZ0; -.
PDBsum; 2F3B; -.
PDBsum; 2F3D; -.
PDBsum; 2FBP; -.
PDBsum; 2QVU; -.
PDBsum; 2QVV; -.
PDBsum; 3FBP; -.
PDBsum; 4FBP; -.
PDBsum; 4GBV; -.
PDBsum; 4GBW; -.
PDBsum; 4GWS; -.
PDBsum; 4GWU; -.
PDBsum; 4GWW; -.
PDBsum; 4GWX; -.
PDBsum; 4GWY; -.
PDBsum; 4GWZ; -.
PDBsum; 4GX3; -.
PDBsum; 4GX4; -.
PDBsum; 4GX6; -.
PDBsum; 4H45; -.
PDBsum; 4H46; -.
PDBsum; 4KXP; -.
PDBsum; 5FBP; -.
ProteinModelPortal; P00636; -.
SMR; P00636; -.
STRING; 9823.ENSSSCP00000011671; -.
BindingDB; P00636; -.
ChEMBL; CHEMBL2263; -.
iPTMnet; P00636; -.
PaxDb; P00636; -.
PeptideAtlas; P00636; -.
PRIDE; P00636; -.
Ensembl; ENSSSCT00000065852; ENSSSCP00000049752; ENSSSCG00000031174.
GeneID; 397038; -.
KEGG; ssc:397038; -.
CTD; 2203; -.
eggNOG; KOG1458; Eukaryota.
eggNOG; COG0158; LUCA.
GeneTree; ENSGT00390000015513; -.
HOGENOM; HOG000191265; -.
HOVERGEN; HBG005627; -.
InParanoid; P00636; -.
KO; K03841; -.
BRENDA; 3.1.3.11; 6170.
Reactome; R-SSC-70263; Gluconeogenesis.
SABIO-RK; P00636; -.
UniPathway; UPA00138; -.
EvolutionaryTrace; P00636; -.
PRO; PR:P00636; -.
Proteomes; UP000008227; Chromosome 10.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0016208; F:AMP binding; ISS:UniProtKB.
GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
GO; GO:0048029; F:monosaccharide binding; ISS:UniProtKB.
GO; GO:0001191; F:transcriptional repressor activity, RNA polymerase II transcription factor binding; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; ISS:UniProtKB.
GO; GO:0071286; P:cellular response to magnesium ion; ISS:UniProtKB.
GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
GO; GO:0006002; P:fructose 6-phosphate metabolic process; ISS:UniProtKB.
GO; GO:0006000; P:fructose metabolic process; IBA:GO_Central.
GO; GO:0006094; P:gluconeogenesis; ISS:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0045820; P:negative regulation of glycolytic process; ISS:UniProtKB.
GO; GO:0046580; P:negative regulation of Ras protein signal transduction; ISS:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
GO; GO:0006111; P:regulation of gluconeogenesis; ISS:UniProtKB.
GO; GO:0005986; P:sucrose biosynthetic process; IBA:GO_Central.
CDD; cd00354; FBPase; 1.
HAMAP; MF_01855; FBPase_class1; 1.
InterPro; IPR000146; FBPase_class-1.
InterPro; IPR033391; FBPase_N.
InterPro; IPR028343; FBPtase.
InterPro; IPR020548; Fructose_bisphosphatase_AS.
PANTHER; PTHR11556; PTHR11556; 1.
Pfam; PF00316; FBPase; 1.
PIRSF; PIRSF500210; FBPtase; 1.
PIRSF; PIRSF000904; FBPtase_SBPase; 1.
PRINTS; PR00115; F16BPHPHTASE.
PROSITE; PS00124; FBPASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Allosteric enzyme; Carbohydrate metabolism;
Complete proteome; Direct protein sequencing; Gluconeogenesis;
Hydrolase; Magnesium; Metal-binding; Phosphoprotein;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:6291465,
ECO:0000269|PubMed:6296821}.
CHAIN 2 338 Fructose-1,6-bisphosphatase 1.
/FTId=PRO_0000200500.
NP_BIND 18 22 AMP. {ECO:0000269|PubMed:2164670}.
NP_BIND 28 32 AMP. {ECO:0000269|PubMed:2164670}.
NP_BIND 113 114 AMP. {ECO:0000269|PubMed:2164670}.
REGION 122 125 Substrate binding.
REGION 213 216 Substrate binding.
REGION 244 249 Substrate binding.
REGION 275 277 Substrate binding.
METAL 69 69 Magnesium 1.
{ECO:0000269|PubMed:2164670}.
METAL 98 98 Magnesium 1.
{ECO:0000269|PubMed:2164670}.
METAL 98 98 Magnesium 2.
{ECO:0000269|PubMed:2164670}.
METAL 119 119 Magnesium 2.
{ECO:0000269|PubMed:2164670}.
METAL 119 119 Magnesium 3.
{ECO:0000269|PubMed:2164670}.
METAL 121 121 Magnesium 2; via carbonyl oxygen.
{ECO:0000269|PubMed:2164670}.
METAL 122 122 Magnesium 3.
{ECO:0000269|PubMed:2164670}.
METAL 281 281 Magnesium 3.
{ECO:0000269|PubMed:2164670}.
BINDING 141 141 AMP. {ECO:0000269|PubMed:2164670}.
BINDING 265 265 Substrate.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000269|PubMed:6291465,
ECO:0000269|PubMed:6296821}.
MOD_RES 151 151 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9QXD6}.
MOD_RES 208 208 Phosphoserine; by PKA.
{ECO:0000269|PubMed:6296821}.
MOD_RES 216 216 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9QXD6}.
MOD_RES 245 245 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9QXD6}.
MOD_RES 265 265 Phosphotyrosine.
{ECO:0000250|UniProtKB:P09467}.
MUTAGEN 55 55 A->L: Destabilizes the inactive T-state
and promotes transition to the R-state.
CONFLICT 2 2 T -> A (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 4 4 Q -> E (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 21 21 E -> Q (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 97 97 S -> T (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 157 157 G -> E (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 200 200 D -> N (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 229 229 Q -> E (in Ref. 2; AA sequence).
{ECO:0000305}.
HELIX 14 24 {ECO:0000244|PDB:1NUW}.
HELIX 30 50 {ECO:0000244|PDB:1NUW}.
TURN 51 56 {ECO:0000244|PDB:1NUW}.
STRAND 59 64 {ECO:0000244|PDB:1NUW}.
STRAND 66 68 {ECO:0000244|PDB:1NV1}.
STRAND 70 72 {ECO:0000244|PDB:1NUW}.
HELIX 73 88 {ECO:0000244|PDB:1NUW}.
STRAND 92 97 {ECO:0000244|PDB:1NUW}.
STRAND 101 105 {ECO:0000244|PDB:1FSA}.
HELIX 108 110 {ECO:0000244|PDB:1NUW}.
STRAND 111 122 {ECO:0000244|PDB:1NUW}.
HELIX 124 126 {ECO:0000244|PDB:1NUW}.
TURN 127 130 {ECO:0000244|PDB:1NUW}.
STRAND 133 141 {ECO:0000244|PDB:1NUW}.
STRAND 144 146 {ECO:0000244|PDB:2QVU}.
STRAND 147 149 {ECO:0000244|PDB:3FBP}.
HELIX 150 153 {ECO:0000244|PDB:1NUW}.
HELIX 157 159 {ECO:0000244|PDB:1NUW}.
STRAND 161 178 {ECO:0000244|PDB:1NUW}.
STRAND 181 188 {ECO:0000244|PDB:1NUW}.
TURN 189 192 {ECO:0000244|PDB:1NUW}.
STRAND 193 198 {ECO:0000244|PDB:1NUW}.
STRAND 208 211 {ECO:0000244|PDB:1NUW}.
HELIX 214 219 {ECO:0000244|PDB:1NUW}.
HELIX 222 232 {ECO:0000244|PDB:1NUW}.
STRAND 235 237 {ECO:0000244|PDB:1LEV}.
STRAND 242 245 {ECO:0000244|PDB:1FBC}.
HELIX 249 259 {ECO:0000244|PDB:1NUW}.
STRAND 262 265 {ECO:0000244|PDB:1NUW}.
STRAND 268 270 {ECO:0000244|PDB:1FPD}.
TURN 271 273 {ECO:0000244|PDB:1FBP}.
STRAND 275 277 {ECO:0000244|PDB:1NUW}.
TURN 278 281 {ECO:0000244|PDB:1NUW}.
HELIX 282 291 {ECO:0000244|PDB:1NUW}.
STRAND 295 297 {ECO:0000244|PDB:1NUW}.
STRAND 299 302 {ECO:0000244|PDB:1NUW}.
HELIX 303 305 {ECO:0000244|PDB:1NUW}.
STRAND 309 312 {ECO:0000244|PDB:1FBP}.
STRAND 317 320 {ECO:0000244|PDB:1NUW}.
HELIX 322 334 {ECO:0000244|PDB:1NUW}.
SEQUENCE 338 AA; 36779 MW; 610BF8D3C6D320F6 CRC64;
MTDQAAFDTN IVTLTRFVME EGRKARGTGE MTQLLNSLCT AVKAISTAVR KAGIAHLYGI
AGSTNVTGDQ VKKLDVLSND LVINVLKSSF ATCVLVSEED KNAIIVEPEK RGKYVVCFDP
LDGSSNIDCL VSIGTIFGIY RKNSTDEPSE KDALQPGRNL VAAGYALYGS ATMLVLAMVN
GVNCFMLDPA IGEFILVDRD VKIKKKGSIY SINEGYAKEF DPAITEYIQR KKFPPDNSAP
YGARYVGSMV ADVHRTLVYG GIFMYPANKK SPKGKLRLLY ECNPMAYVME KAGGLATTGK
EAVLDIVPTD IHQRAPIILG SPEDVTELLE IYQKHAAK


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