F16P1_PIG
ID F16P1_PIG Reviewed; 338 AA.
AC P00636;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Fructose-1,6-bisphosphatase 1;
DE Short=FBPase 1;
DE EC=3.1.3.11 {ECO:0000269|PubMed:15767255, ECO:0000305|PubMed:1313579};
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase 1;
DE AltName: Full=Liver FBPase;
GN Name=FBP1; Synonyms=FBP;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RC TISSUE=Kidney;
RX PubMed=1313579; DOI=10.1073/pnas.89.7.3080;
RA Williams M.K., Kantrowitz E.R.;
RT "Isolation and sequence analysis of the cDNA for pig kidney fructose 1,6-
RT bisphosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3080-3082(1992).
RN [2]
RP PROTEIN SEQUENCE OF 2-336, ACETYLATION AT THR-2, AND PHOSPHORYLATION AT
RP SER-208.
RC TISSUE=Kidney cortex;
RX PubMed=6296821; DOI=10.1073/pnas.79.23.7161;
RA Marcus F., Edelstein I., Reardon I., Heinrikson R.L.;
RT "Complete amino acid sequence of pig kidney fructose-1,6-bisphosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:7161-7165(1982).
RN [3]
RP PROTEIN SEQUENCE OF 2-24 AND 44-61, AND ACETYLATION AT THR-2.
RC TISSUE=Kidney;
RX PubMed=6291465; DOI=10.1016/0003-9861(82)90547-1;
RA McGregor J.S., Hannappel E., Xu G.-J., Pontremoli S., Horecker B.L.;
RT "Conservation of primary structure at the proteinase-sensitive site of
RT fructose 1,6-bisphosphatases.";
RL Arch. Biochem. Biophys. 217:652-664(1982).
RN [4]
RP SUBSTRATE-BINDING SITE, LIGANDS, AND REVIEW.
RX PubMed=6277165; DOI=10.1002/9780470122983.ch2;
RA Benkovic S.J., Demaine M.M.;
RT "Mechanism of action of fructose 1,6-bisphosphatase.";
RL Adv. Enzymol. Relat. Areas Mol. Biol. 53:45-82(1982).
RN [5] {ECO:0007744|PDB:2FBP, ECO:0007744|PDB:3FBP}
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH
RP FRUCTOSE-2,6-BISPHOSPHATE, AND SEQUENCE REVISION.
RX PubMed=2157849; DOI=10.1016/0022-2836(90)90329-k;
RA Ke H.M., Thorpe C.M., Seaton B.A., Lipscomb W.N., Marcus F.;
RT "Structure refinement of fructose-1,6-bisphosphatase and its fructose 2,6-
RT bisphosphate complex at 2.8-A resolution.";
RL J. Mol. Biol. 212:513-539(1990).
RN [6] {ECO:0007744|PDB:1FBP}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-6-PHOSPHATE;
RP AMP AND MAGNESIUM, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=2164670; DOI=10.1073/pnas.87.14.5243;
RA Ke H.M., Zhang Y.P., Lipscomb W.N.;
RT "Crystal structure of fructose-1,6-bisphosphatase complexed with fructose
RT 6-phosphate, AMP, and magnesium.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5243-5247(1990).
RN [7] {ECO:0007744|PDB:5FBP}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-6-PHOSPHATE.
RX PubMed=1849642; DOI=10.1073/pnas.88.8.2989;
RA Ke H.M., Zhang Y.P., Liang J.-Y., Lipscomb W.N.;
RT "Crystal structure of the neutral form of fructose-1,6-bisphosphatase
RT complexed with the product fructose 6-phosphate at 2.1-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:2989-2993(1991).
RN [8] {ECO:0007744|PDB:1FPB}
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH
RP FRUCTOSE-2,6-BISPHOSPHATE.
RX PubMed=1312721; DOI=10.1073/pnas.89.6.2404;
RA Liang J.-Y., Huang S., Zhang Y.P., Ke H.M., Lipscomb W.N.;
RT "Crystal structure of the neutral form of fructose 1,6-bisphosphatase
RT complexed with regulatory inhibitor fructose 2,6-bisphosphate at 2.6-A
RT resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2404-2408(1992).
RN [9] {ECO:0007744|PDB:1CNQ}
RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) IN COMPLEX WITH ZINC IONS, COFACTOR,
RP AND ACTIVITY REGULATION.
RX PubMed=9708979; DOI=10.1021/bi981112u;
RA Choe J.-Y., Poland B.W., Fromm H.J., Honzatko R.B.;
RT "Role of a dynamic loop in cation activation and allosteric regulation of
RT recombinant porcine fructose-1,6-bisphosphatase.";
RL Biochemistry 37:11441-11450(1998).
RN [10] {ECO:0007744|PDB:1EYI, ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK}
RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) IN COMPLEXES WITH
RP FRUCTOSE-6-PHOSPHATE; PHOSPHATE; AMP; MAGNESIUM AND ZINC IONS, SUBUNIT, AND
RP ACTIVITY REGULATION.
RX PubMed=10913263; DOI=10.1021/bi000574g;
RA Choe J.-Y., Fromm H.J., Honzatko R.B.;
RT "Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis
RT and allosteric inhibition revealed in product complexes.";
RL Biochemistry 39:8565-8574(2000).
RN [11] {ECO:0007744|PDB:1NUW, ECO:0007744|PDB:1NUX, ECO:0007744|PDB:1NUY}
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM IONS;
RP FRUCTOSE-6-PHOSPHATE AND PHOSPHATE, COFACTOR, AND ENZYME MECHANISM.
RX PubMed=12595528; DOI=10.1074/jbc.m212395200;
RA Choe J.-Y., Iancu C.V., Fromm H.J., Honzatko R.B.;
RT "Metaphosphate in the active site of fructose-1,6-bisphosphatase.";
RL J. Biol. Chem. 278:16015-16020(2003).
RN [12] {ECO:0007744|PDB:1Q9D}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH THE SYNTHETIC
RP INHIBITOR OC252; FRUCTOSE-6-PHOSPHATE; PHOSPHATE AND DIVALENT METAL
RP CATIONS, COFACTOR, SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=14530289; DOI=10.1074/jbc.m308396200;
RA Choe J.-Y., Nelson S.W., Arienti K.L., Axe F.U., Collins T.L., Jones T.K.,
RA Kimmich R.D.A., Newman M.J., Norvell K., Ripka W.C., Romano S.J.,
RA Short K.M., Slee D.H., Fromm H.J., Honzatko R.B.;
RT "Inhibition of fructose-1,6-bisphosphatase by a new class of allosteric
RT effectors.";
RL J. Biol. Chem. 278:51176-51183(2003).
RN [13] {ECO:0007744|PDB:1YXI, ECO:0007744|PDB:1YYZ, ECO:0007744|PDB:1YZ0}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT LEU-55 IN COMPLEXES WITH
RP AMP; FRUCTORSE-6-PHOSPHAT; PHOSPHATE AND MAGNESIUM IONS, SUBUNIT, COFACTOR,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=15767255; DOI=10.1074/jbc.m501011200;
RA Iancu C.V., Mukund S., Fromm H.J., Honzatko R.B.;
RT "R-state AMP complex reveals initial steps of the quaternary transition of
RT fructose-1,6-bisphosphatase.";
RL J. Biol. Chem. 280:19737-19745(2005).
RN [14] {ECO:0007744|PDB:2QVU, ECO:0007744|PDB:2QVV}
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM IONS AND
RP FRUCTOSE-2,6-DIPHOSPHATE, SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=17933867; DOI=10.1074/jbc.m707302200;
RA Hines J.K., Chen X., Nix J.C., Fromm H.J., Honzatko R.B.;
RT "Structures of mammalian and bacterial fructose-1,6-bisphosphatase reveal
RT the basis for synergism in AMP/fructose 2,6-bisphosphate inhibition.";
RL J. Biol. Chem. 282:36121-36131(2007).
CC -!- FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to
CC fructose 6-phosphate in the presence of divalent cations, acting as a
CC rate-limiting enzyme in gluconeogenesis. Plays a role in regulating
CC glucose sensing and insulin secretion of pancreatic beta-cells. Appears
CC to modulate glycerol gluconeogenesis in liver. Important regulator of
CC appetite and adiposity; increased expression of the protein in liver
CC after nutrient excess increases circulating satiety hormones and
CC reduces appetite-stimulating neuropeptides and thus seems to provide a
CC feedback mechanism to limit weight gain.
CC {ECO:0000250|UniProtKB:P09467}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
CC Evidence={ECO:0000269|PubMed:15767255, ECO:0000305|PubMed:1313579};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12595528, ECO:0000269|PubMed:14530289,
CC ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:9708979};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000269|PubMed:12595528,
CC ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255,
CC ECO:0000269|PubMed:9708979};
CC -!- ACTIVITY REGULATION: Subject to complex allosteric regulation. The
CC enzyme can assume an active R-state, or an inactive T-state.
CC Intermediate conformations may exist. AMP acts as allosteric inhibitor.
CC AMP binding affects the turnover of bound substrate and not the
CC affinity for substrate. Fructose 2,6-bisphosphate acts as competitive
CC inhibitor. Fructose 2,6-bisphosphate and AMP have synergistic effects.
CC {ECO:0000269|PubMed:10913263, ECO:0000269|PubMed:14530289,
CC ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:17933867,
CC ECO:0000269|PubMed:2164670, ECO:0000269|PubMed:9708979}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 uM for fructose-1,6-diphosphate {ECO:0000269|PubMed:15767255};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10913263,
CC ECO:0000269|PubMed:1312721, ECO:0000269|PubMed:14530289,
CC ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:17933867,
CC ECO:0000269|PubMed:1849642, ECO:0000269|PubMed:2157849,
CC ECO:0000269|PubMed:2164670, ECO:0000269|PubMed:9708979}.
CC -!- MISCELLANEOUS: The molecule has a highly reactive cysteine residue
CC (Cys-117 or Cys-129), which tends to form mixed disulfides (e.g. with
CC homocystine) but is not essential for enzyme activity.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}.
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DR EMBL; M86347; AAA31035.1; -; mRNA.
DR PIR; S37696; PAPGF.
DR RefSeq; NP_999144.1; NM_213979.1.
DR PDB; 1CNQ; X-ray; 2.27 A; A=2-338.
DR PDB; 1EYI; X-ray; 2.32 A; A=2-338.
DR PDB; 1EYJ; X-ray; 2.28 A; A/B=2-338.
DR PDB; 1EYK; X-ray; 2.23 A; A/B=2-338.
DR PDB; 1FBC; X-ray; 2.60 A; A/B=2-336.
DR PDB; 1FBD; X-ray; 2.90 A; A/B=2-336.
DR PDB; 1FBE; X-ray; 3.00 A; A/B=2-336.
DR PDB; 1FBF; X-ray; 2.70 A; A/B=2-336.
DR PDB; 1FBG; X-ray; 3.00 A; A/B=2-336.
DR PDB; 1FBH; X-ray; 2.50 A; A/B=2-336.
DR PDB; 1FBP; X-ray; 2.50 A; A/B=2-336.
DR PDB; 1FJ6; X-ray; 2.50 A; A=2-338.
DR PDB; 1FJ9; X-ray; 2.50 A; A/B=2-338.
DR PDB; 1FPB; X-ray; 2.60 A; A/B=2-336.
DR PDB; 1FPD; X-ray; 2.10 A; A/B=2-336.
DR PDB; 1FPE; X-ray; 2.20 A; A/B=2-336.
DR PDB; 1FPF; X-ray; 2.10 A; A/B=2-336.
DR PDB; 1FPG; X-ray; 2.30 A; A/B=2-336.
DR PDB; 1FPI; X-ray; 2.30 A; A/B=2-336.
DR PDB; 1FPJ; X-ray; 2.20 A; A/B=2-336.
DR PDB; 1FPK; X-ray; 3.00 A; A/B=2-336.
DR PDB; 1FPL; X-ray; 2.30 A; A/B=2-336.
DR PDB; 1FRP; X-ray; 2.00 A; A/B=2-336.
DR PDB; 1FSA; X-ray; 2.30 A; A/B=2-338.
DR PDB; 1KZ8; X-ray; 2.00 A; A/F=2-338.
DR PDB; 1LEV; X-ray; 2.15 A; A/F=2-338.
DR PDB; 1NUW; X-ray; 1.30 A; A=2-338.
DR PDB; 1NUX; X-ray; 1.60 A; A=2-338.
DR PDB; 1NUY; X-ray; 1.30 A; A=2-338.
DR PDB; 1NUZ; X-ray; 1.90 A; A=2-338.
DR PDB; 1NV0; X-ray; 1.80 A; A=2-338.
DR PDB; 1NV1; X-ray; 1.90 A; A=2-338.
DR PDB; 1NV2; X-ray; 2.10 A; A=2-338.
DR PDB; 1NV3; X-ray; 2.00 A; A=2-338.
DR PDB; 1NV4; X-ray; 1.90 A; A=2-338.
DR PDB; 1NV5; X-ray; 1.90 A; A=2-338.
DR PDB; 1NV6; X-ray; 2.15 A; A=2-338.
DR PDB; 1NV7; X-ray; 2.15 A; A/B=2-338.
DR PDB; 1Q9D; X-ray; 2.35 A; A/B=2-338.
DR PDB; 1RDX; X-ray; 2.75 A; A/B=2-338.
DR PDB; 1RDY; X-ray; 2.20 A; A/B=2-338.
DR PDB; 1RDZ; X-ray; 2.05 A; A/B=2-338.
DR PDB; 1YXI; X-ray; 2.00 A; A=2-338.
DR PDB; 1YYZ; X-ray; 1.85 A; A=2-338.
DR PDB; 1YZ0; X-ray; 2.07 A; A/B=2-338.
DR PDB; 2F3B; X-ray; 1.80 A; A=1-338.
DR PDB; 2F3D; X-ray; 1.83 A; A=1-338.
DR PDB; 2FBP; X-ray; 2.80 A; A/B=2-336.
DR PDB; 2QVU; X-ray; 1.50 A; A/B=2-338.
DR PDB; 2QVV; X-ray; 2.03 A; A/B=2-338.
DR PDB; 3FBP; X-ray; 2.80 A; A/B=2-336.
DR PDB; 4FBP; X-ray; 2.50 A; A/B/C/D=2-336.
DR PDB; 4GBV; X-ray; 2.90 A; A=2-336.
DR PDB; 4GBW; X-ray; 2.00 A; A=2-336.
DR PDB; 4GWS; X-ray; 2.75 A; A/B=2-338.
DR PDB; 4GWU; X-ray; 3.00 A; A=2-338.
DR PDB; 4GWW; X-ray; 3.20 A; A=2-338.
DR PDB; 4GWX; X-ray; 2.35 A; A=2-338.
DR PDB; 4GWY; X-ray; 3.00 A; A=2-338.
DR PDB; 4GWZ; X-ray; 2.60 A; A/B=2-338.
DR PDB; 4GX3; X-ray; 2.25 A; A/B=2-338.
DR PDB; 4GX4; X-ray; 2.50 A; A/B=2-338.
DR PDB; 4GX6; X-ray; 2.50 A; A/B=2-338.
DR PDB; 4H45; X-ray; 3.10 A; A=2-338.
DR PDB; 4H46; X-ray; 2.50 A; A=2-338.
DR PDB; 4KXP; X-ray; 2.70 A; A/B=1-338.
DR PDB; 5FBP; X-ray; 2.10 A; A/B=2-336.
DR PDBsum; 1CNQ; -.
DR PDBsum; 1EYI; -.
DR PDBsum; 1EYJ; -.
DR PDBsum; 1EYK; -.
DR PDBsum; 1FBC; -.
DR PDBsum; 1FBD; -.
DR PDBsum; 1FBE; -.
DR PDBsum; 1FBF; -.
DR PDBsum; 1FBG; -.
DR PDBsum; 1FBH; -.
DR PDBsum; 1FBP; -.
DR PDBsum; 1FJ6; -.
DR PDBsum; 1FJ9; -.
DR PDBsum; 1FPB; -.
DR PDBsum; 1FPD; -.
DR PDBsum; 1FPE; -.
DR PDBsum; 1FPF; -.
DR PDBsum; 1FPG; -.
DR PDBsum; 1FPI; -.
DR PDBsum; 1FPJ; -.
DR PDBsum; 1FPK; -.
DR PDBsum; 1FPL; -.
DR PDBsum; 1FRP; -.
DR PDBsum; 1FSA; -.
DR PDBsum; 1KZ8; -.
DR PDBsum; 1LEV; -.
DR PDBsum; 1NUW; -.
DR PDBsum; 1NUX; -.
DR PDBsum; 1NUY; -.
DR PDBsum; 1NUZ; -.
DR PDBsum; 1NV0; -.
DR PDBsum; 1NV1; -.
DR PDBsum; 1NV2; -.
DR PDBsum; 1NV3; -.
DR PDBsum; 1NV4; -.
DR PDBsum; 1NV5; -.
DR PDBsum; 1NV6; -.
DR PDBsum; 1NV7; -.
DR PDBsum; 1Q9D; -.
DR PDBsum; 1RDX; -.
DR PDBsum; 1RDY; -.
DR PDBsum; 1RDZ; -.
DR PDBsum; 1YXI; -.
DR PDBsum; 1YYZ; -.
DR PDBsum; 1YZ0; -.
DR PDBsum; 2F3B; -.
DR PDBsum; 2F3D; -.
DR PDBsum; 2FBP; -.
DR PDBsum; 2QVU; -.
DR PDBsum; 2QVV; -.
DR PDBsum; 3FBP; -.
DR PDBsum; 4FBP; -.
DR PDBsum; 4GBV; -.
DR PDBsum; 4GBW; -.
DR PDBsum; 4GWS; -.
DR PDBsum; 4GWU; -.
DR PDBsum; 4GWW; -.
DR PDBsum; 4GWX; -.
DR PDBsum; 4GWY; -.
DR PDBsum; 4GWZ; -.
DR PDBsum; 4GX3; -.
DR PDBsum; 4GX4; -.
DR PDBsum; 4GX6; -.
DR PDBsum; 4H45; -.
DR PDBsum; 4H46; -.
DR PDBsum; 4KXP; -.
DR PDBsum; 5FBP; -.
DR AlphaFoldDB; P00636; -.
DR SMR; P00636; -.
DR STRING; 9823.ENSSSCP00000011671; -.
DR BindingDB; P00636; -.
DR ChEMBL; CHEMBL2263; -.
DR DrugCentral; P00636; -.
DR iPTMnet; P00636; -.
DR PaxDb; P00636; -.
DR PeptideAtlas; P00636; -.
DR PRIDE; P00636; -.
DR Ensembl; ENSSSCT00000065852; ENSSSCP00000049752; ENSSSCG00000031174.
DR Ensembl; ENSSSCT00005040060; ENSSSCP00005024518; ENSSSCG00005024872.
DR Ensembl; ENSSSCT00015088932; ENSSSCP00015036278; ENSSSCG00015066376.
DR Ensembl; ENSSSCT00015089465; ENSSSCP00015036500; ENSSSCG00015066376.
DR Ensembl; ENSSSCT00025019008; ENSSSCP00025007679; ENSSSCG00025014230.
DR Ensembl; ENSSSCT00030006729; ENSSSCP00030002968; ENSSSCG00030004973.
DR Ensembl; ENSSSCT00035035384; ENSSSCP00035014027; ENSSSCG00035026802.
DR Ensembl; ENSSSCT00050015866; ENSSSCP00050006487; ENSSSCG00050011780.
DR Ensembl; ENSSSCT00055027666; ENSSSCP00055022027; ENSSSCG00055014004.
DR Ensembl; ENSSSCT00070042384; ENSSSCP00070035635; ENSSSCG00070021304.
DR GeneID; 397038; -.
DR KEGG; ssc:397038; -.
DR CTD; 2203; -.
DR VGNC; VGNC:96297; FBP1.
DR eggNOG; KOG1458; Eukaryota.
DR GeneTree; ENSGT00390000015513; -.
DR InParanoid; P00636; -.
DR OMA; NSRFWEP; -.
DR OrthoDB; 1381522at2759; -.
DR BRENDA; 3.1.3.11; 6170.
DR SABIO-RK; P00636; -.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; P00636; -.
DR PRO; PR:P00636; -.
DR Proteomes; UP000008227; Chromosome 10.
DR Proteomes; UP000314985; Chromosome 10.
DR Bgee; ENSSSCG00000031174; Expressed in kidney and 44 other tissues.
DR ExpressionAtlas; P00636; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0016208; F:AMP binding; ISS:UniProtKB.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0048029; F:monosaccharide binding; ISS:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0071286; P:cellular response to magnesium ion; ISS:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0006000; P:fructose metabolic process; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0045820; P:negative regulation of glycolytic process; ISS:UniProtKB.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006111; P:regulation of gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0005986; P:sucrose biosynthetic process; IBA:GO_Central.
DR CDD; cd00354; FBPase; 1.
DR HAMAP; MF_01855; FBPase_class1; 1.
DR InterPro; IPR044015; FBPase_C_dom.
DR InterPro; IPR000146; FBPase_class-1.
DR InterPro; IPR033391; FBPase_N.
DR InterPro; IPR028343; FBPtase.
DR InterPro; IPR020548; Fructose_bisphosphatase_AS.
DR PANTHER; PTHR11556; PTHR11556; 1.
DR Pfam; PF00316; FBPase; 1.
DR Pfam; PF18913; FBPase_C; 1.
DR PIRSF; PIRSF500210; FBPtase; 1.
DR PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR PRINTS; PR00115; F16BPHPHTASE.
DR PROSITE; PS00124; FBPASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Allosteric enzyme; Carbohydrate metabolism;
KW Direct protein sequencing; Gluconeogenesis; Hydrolase; Magnesium;
KW Metal-binding; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6291465,
FT ECO:0000269|PubMed:6296821"
FT CHAIN 2..338
FT /note="Fructose-1,6-bisphosphatase 1"
FT /id="PRO_0000200500"
FT BINDING 18..22
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:10913263,
FT ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:2164670,
FT ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK,
FT ECO:0007744|PDB:1FBP, ECO:0007744|PDB:1FJ9,
FT ECO:0007744|PDB:1FPD, ECO:0007744|PDB:1FPE,
FT ECO:0007744|PDB:1FPF, ECO:0007744|PDB:1FPG,
FT ECO:0007744|PDB:1FPI, ECO:0007744|PDB:1FPJ,
FT ECO:0007744|PDB:1FPL, ECO:0007744|PDB:1FRP,
FT ECO:0007744|PDB:1FSA, ECO:0007744|PDB:1KZ8,
FT ECO:0007744|PDB:1NV7, ECO:0007744|PDB:1RDY,
FT ECO:0007744|PDB:1RDZ, ECO:0007744|PDB:1YYZ,
FT ECO:0007744|PDB:1YZ0, ECO:0007744|PDB:2F3D,
FT ECO:0007744|PDB:4FBP, ECO:0007744|PDB:4GBV,
FT ECO:0007744|PDB:4GBW, ECO:0007744|PDB:4GWS,
FT ECO:0007744|PDB:4GWY, ECO:0007744|PDB:4GWZ,
FT ECO:0007744|PDB:4GX4, ECO:0007744|PDB:4GX6,
FT ECO:0007744|PDB:4H46, ECO:0007744|PDB:4KXP"
FT BINDING 28..32
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:10913263,
FT ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:2164670,
FT ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK,
FT ECO:0007744|PDB:1FBP, ECO:0007744|PDB:1FJ9,
FT ECO:0007744|PDB:1FPD, ECO:0007744|PDB:1FPE,
FT ECO:0007744|PDB:1FPF, ECO:0007744|PDB:1FPG,
FT ECO:0007744|PDB:1FPI, ECO:0007744|PDB:1FPJ,
FT ECO:0007744|PDB:1FPL, ECO:0007744|PDB:1FRP,
FT ECO:0007744|PDB:1FSA, ECO:0007744|PDB:1KZ8,
FT ECO:0007744|PDB:1NV7, ECO:0007744|PDB:1RDY,
FT ECO:0007744|PDB:1RDZ, ECO:0007744|PDB:1YYZ,
FT ECO:0007744|PDB:1YZ0, ECO:0007744|PDB:2F3D,
FT ECO:0007744|PDB:4FBP, ECO:0007744|PDB:4GBV,
FT ECO:0007744|PDB:4GBW, ECO:0007744|PDB:4GWS,
FT ECO:0007744|PDB:4GWY, ECO:0007744|PDB:4GWZ,
FT ECO:0007744|PDB:4GX4, ECO:0007744|PDB:4GX6,
FT ECO:0007744|PDB:4H46, ECO:0007744|PDB:4KXP"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:2164670"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:2164670"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:2164670"
FT BINDING 113..114
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:10913263,
FT ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:2164670,
FT ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK,
FT ECO:0007744|PDB:1FBP, ECO:0007744|PDB:1FJ9,
FT ECO:0007744|PDB:1FPD, ECO:0007744|PDB:1FPE,
FT ECO:0007744|PDB:1FPF, ECO:0007744|PDB:1FPG,
FT ECO:0007744|PDB:1FPI, ECO:0007744|PDB:1FPJ,
FT ECO:0007744|PDB:1FPL, ECO:0007744|PDB:1FRP,
FT ECO:0007744|PDB:1FSA, ECO:0007744|PDB:1KZ8,
FT ECO:0007744|PDB:1NV7, ECO:0007744|PDB:1RDY,
FT ECO:0007744|PDB:1RDZ, ECO:0007744|PDB:1YYZ,
FT ECO:0007744|PDB:1YZ0, ECO:0007744|PDB:2F3D,
FT ECO:0007744|PDB:4FBP, ECO:0007744|PDB:4GBV,
FT ECO:0007744|PDB:4GBW, ECO:0007744|PDB:4GWS,
FT ECO:0007744|PDB:4GWY, ECO:0007744|PDB:4GWZ,
FT ECO:0007744|PDB:4GX4, ECO:0007744|PDB:4GX6,
FT ECO:0007744|PDB:4H46, ECO:0007744|PDB:4KXP"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:2164670"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:2164670"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:2164670"
FT BINDING 122..125
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10913263,
FT ECO:0000269|PubMed:12595528, ECO:0000269|PubMed:1312721,
FT ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255,
FT ECO:0000269|PubMed:17933867, ECO:0000269|PubMed:1849642,
FT ECO:0000269|PubMed:2157849, ECO:0000269|PubMed:2164670,
FT ECO:0007744|PDB:1EYI, ECO:0007744|PDB:1EYJ,
FT ECO:0007744|PDB:1EYK, ECO:0007744|PDB:1FBC,
FT ECO:0007744|PDB:1FBD, ECO:0007744|PDB:1FBE,
FT ECO:0007744|PDB:1FBH, ECO:0007744|PDB:1FPB,
FT ECO:0007744|PDB:1FPD, ECO:0007744|PDB:1FPE,
FT ECO:0007744|PDB:1FPF, ECO:0007744|PDB:1FPG,
FT ECO:0007744|PDB:1FPI, ECO:0007744|PDB:1FPJ,
FT ECO:0007744|PDB:1FPL, ECO:0007744|PDB:1FRP,
FT ECO:0007744|PDB:1NUW, ECO:0007744|PDB:1NUX,
FT ECO:0007744|PDB:1NUY, ECO:0007744|PDB:1NUZ,
FT ECO:0007744|PDB:1NV0, ECO:0007744|PDB:1NV1,
FT ECO:0007744|PDB:1RDX, ECO:0007744|PDB:2QVU,
FT ECO:0007744|PDB:2QVV, ECO:0007744|PDB:4GWU,
FT ECO:0007744|PDB:5FBP"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:2164670"
FT BINDING 141
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:2164670"
FT BINDING 213..216
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10913263,
FT ECO:0000269|PubMed:12595528, ECO:0000269|PubMed:1312721,
FT ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255,
FT ECO:0000269|PubMed:17933867, ECO:0000269|PubMed:1849642,
FT ECO:0000269|PubMed:2157849, ECO:0000269|PubMed:2164670,
FT ECO:0007744|PDB:1CNQ, ECO:0007744|PDB:1EYI,
FT ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK,
FT ECO:0007744|PDB:1FBP, ECO:0007744|PDB:1FJ6,
FT ECO:0007744|PDB:1FJ9, ECO:0007744|PDB:1FRP,
FT ECO:0007744|PDB:1FSA, ECO:0007744|PDB:1KZ8,
FT ECO:0007744|PDB:1LEV, ECO:0007744|PDB:1NUW,
FT ECO:0007744|PDB:1NUX, ECO:0007744|PDB:1NUY,
FT ECO:0007744|PDB:1NUZ, ECO:0007744|PDB:1NV0,
FT ECO:0007744|PDB:1NV1, ECO:0007744|PDB:1NV2,
FT ECO:0007744|PDB:1NV3, ECO:0007744|PDB:1NV4,
FT ECO:0007744|PDB:1NV5, ECO:0007744|PDB:1NV6,
FT ECO:0007744|PDB:1NV7, ECO:0007744|PDB:1Q9D,
FT ECO:0007744|PDB:1RDY, ECO:0007744|PDB:1RDZ,
FT ECO:0007744|PDB:1YXI, ECO:0007744|PDB:1YYZ,
FT ECO:0007744|PDB:1YZ0, ECO:0007744|PDB:2F3B,
FT ECO:0007744|PDB:2F3D, ECO:0007744|PDB:2QVU,
FT ECO:0007744|PDB:2QVV, ECO:0007744|PDB:3FBP,
FT ECO:0007744|PDB:4GBV, ECO:0007744|PDB:4GBW,
FT ECO:0007744|PDB:4GWS, ECO:0007744|PDB:4GWU,
FT ECO:0007744|PDB:4GWW, ECO:0007744|PDB:4GWX,
FT ECO:0007744|PDB:4GWY, ECO:0007744|PDB:4GWZ,
FT ECO:0007744|PDB:4GX3, ECO:0007744|PDB:4GX4,
FT ECO:0007744|PDB:4GX6, ECO:0007744|PDB:4H45,
FT ECO:0007744|PDB:4H46, ECO:0007744|PDB:4KXP,
FT ECO:0007744|PDB:5FBP"
FT BINDING 244..249
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10913263,
FT ECO:0000269|PubMed:12595528, ECO:0000269|PubMed:1312721,
FT ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255,
FT ECO:0000269|PubMed:17933867, ECO:0000269|PubMed:1849642,
FT ECO:0000269|PubMed:2157849, ECO:0000269|PubMed:2164670,
FT ECO:0007744|PDB:1CNQ, ECO:0007744|PDB:1EYI,
FT ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK,
FT ECO:0007744|PDB:1FBP, ECO:0007744|PDB:1FJ6,
FT ECO:0007744|PDB:1FJ9, ECO:0007744|PDB:1FSA,
FT ECO:0007744|PDB:1KZ8, ECO:0007744|PDB:1LEV,
FT ECO:0007744|PDB:1NUW, ECO:0007744|PDB:1NUX,
FT ECO:0007744|PDB:1NUY, ECO:0007744|PDB:1NUZ,
FT ECO:0007744|PDB:1NV0, ECO:0007744|PDB:1NV1,
FT ECO:0007744|PDB:1NV2, ECO:0007744|PDB:1NV3,
FT ECO:0007744|PDB:1NV4, ECO:0007744|PDB:1NV5,
FT ECO:0007744|PDB:1NV6, ECO:0007744|PDB:1NV7,
FT ECO:0007744|PDB:1Q9D, ECO:0007744|PDB:1RDY,
FT ECO:0007744|PDB:1RDZ, ECO:0007744|PDB:1YXI,
FT ECO:0007744|PDB:1YYZ, ECO:0007744|PDB:1YZ0,
FT ECO:0007744|PDB:2F3B, ECO:0007744|PDB:2F3D,
FT ECO:0007744|PDB:4GBV, ECO:0007744|PDB:4GBW,
FT ECO:0007744|PDB:4GWS, ECO:0007744|PDB:4GWW,
FT ECO:0007744|PDB:4GWX, ECO:0007744|PDB:4GWY,
FT ECO:0007744|PDB:4GWZ, ECO:0007744|PDB:4GX3,
FT ECO:0007744|PDB:4GX4, ECO:0007744|PDB:4GX6,
FT ECO:0007744|PDB:4H45, ECO:0007744|PDB:4H46,
FT ECO:0007744|PDB:4KXP, ECO:0007744|PDB:5FBP"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10913263,
FT ECO:0000269|PubMed:12595528, ECO:0000269|PubMed:1312721,
FT ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255,
FT ECO:0000269|PubMed:17933867, ECO:0000269|PubMed:1849642,
FT ECO:0000269|PubMed:2157849, ECO:0000269|PubMed:2164670,
FT ECO:0007744|PDB:1CNQ, ECO:0007744|PDB:1EYI,
FT ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK,
FT ECO:0007744|PDB:1FJ6, ECO:0007744|PDB:1FJ9,
FT ECO:0007744|PDB:1FPB, ECO:0007744|PDB:1FRP,
FT ECO:0007744|PDB:1FSA, ECO:0007744|PDB:1KZ8,
FT ECO:0007744|PDB:1LEV, ECO:0007744|PDB:1NUW,
FT ECO:0007744|PDB:1NUX, ECO:0007744|PDB:1NUY,
FT ECO:0007744|PDB:1NUZ, ECO:0007744|PDB:1NV0,
FT ECO:0007744|PDB:1NV1, ECO:0007744|PDB:1NV2,
FT ECO:0007744|PDB:1NV3, ECO:0007744|PDB:1NV4,
FT ECO:0007744|PDB:1NV5, ECO:0007744|PDB:1NV6,
FT ECO:0007744|PDB:1NV7, ECO:0007744|PDB:1Q9D,
FT ECO:0007744|PDB:1RDY, ECO:0007744|PDB:1RDZ,
FT ECO:0007744|PDB:1YXI, ECO:0007744|PDB:1YYZ,
FT ECO:0007744|PDB:1YZ0, ECO:0007744|PDB:2F3B,
FT ECO:0007744|PDB:2F3D, ECO:0007744|PDB:2QVU,
FT ECO:0007744|PDB:2QVV, ECO:0007744|PDB:4GBV,
FT ECO:0007744|PDB:4GBW, ECO:0007744|PDB:4GWS,
FT ECO:0007744|PDB:4GWU, ECO:0007744|PDB:4GWW,
FT ECO:0007744|PDB:4GWX, ECO:0007744|PDB:4GWY,
FT ECO:0007744|PDB:4GWZ, ECO:0007744|PDB:4GX3,
FT ECO:0007744|PDB:4GX4, ECO:0007744|PDB:4GX6,
FT ECO:0007744|PDB:4H45, ECO:0007744|PDB:4H46,
FT ECO:0007744|PDB:4KXP, ECO:0007744|PDB:5FBP"
FT BINDING 275..277
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10913263,
FT ECO:0000269|PubMed:12595528, ECO:0000269|PubMed:1312721,
FT ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255,
FT ECO:0000269|PubMed:17933867, ECO:0000269|PubMed:1849642,
FT ECO:0000269|PubMed:2157849, ECO:0000269|PubMed:2164670,
FT ECO:0007744|PDB:1CNQ, ECO:0007744|PDB:1EYI,
FT ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK,
FT ECO:0007744|PDB:1FBP, ECO:0007744|PDB:1FJ6,
FT ECO:0007744|PDB:1FJ9, ECO:0007744|PDB:1FSA,
FT ECO:0007744|PDB:1KZ8, ECO:0007744|PDB:1LEV,
FT ECO:0007744|PDB:1NUW, ECO:0007744|PDB:1NUX,
FT ECO:0007744|PDB:1NUY, ECO:0007744|PDB:1NUZ,
FT ECO:0007744|PDB:1NV0, ECO:0007744|PDB:1NV1,
FT ECO:0007744|PDB:1NV2, ECO:0007744|PDB:1NV3,
FT ECO:0007744|PDB:1NV4, ECO:0007744|PDB:1NV5,
FT ECO:0007744|PDB:1NV7, ECO:0007744|PDB:1Q9D,
FT ECO:0007744|PDB:1RDY, ECO:0007744|PDB:1RDZ,
FT ECO:0007744|PDB:1YXI, ECO:0007744|PDB:1YYZ,
FT ECO:0007744|PDB:1YZ0, ECO:0007744|PDB:2F3B,
FT ECO:0007744|PDB:2F3D, ECO:0007744|PDB:4GBW,
FT ECO:0007744|PDB:4GWS, ECO:0007744|PDB:4GWW,
FT ECO:0007744|PDB:4GWX, ECO:0007744|PDB:4GWZ,
FT ECO:0007744|PDB:4GX3, ECO:0007744|PDB:4GX4,
FT ECO:0007744|PDB:4GX6, ECO:0007744|PDB:4H45,
FT ECO:0007744|PDB:4H46, ECO:0007744|PDB:4KXP,
FT ECO:0007744|PDB:5FBP"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:2164670"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|PubMed:6291465,
FT ECO:0000269|PubMed:6296821"
FT MOD_RES 151
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXD6"
FT MOD_RES 208
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:6296821"
FT MOD_RES 216
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXD6"
FT MOD_RES 245
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXD6"
FT MOD_RES 265
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09467"
FT MUTAGEN 55
FT /note="A->L: Destabilizes the inactive T-state and promotes
FT transition to the R-state."
FT CONFLICT 2
FT /note="T -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 4
FT /note="Q -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="S -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="G -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:1NUW"
FT HELIX 30..50
FT /evidence="ECO:0007829|PDB:1NUW"
FT TURN 51..56
FT /evidence="ECO:0007829|PDB:1NUW"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:1NUW"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1NV1"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1NUW"
FT HELIX 73..88
FT /evidence="ECO:0007829|PDB:1NUW"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:1NUW"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1FSA"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1NUW"
FT STRAND 111..122
FT /evidence="ECO:0007829|PDB:1NUW"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1NUW"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:1NUW"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:1NUW"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2QVU"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3FBP"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:1NUW"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1NUW"
FT STRAND 161..178
FT /evidence="ECO:0007829|PDB:1NUW"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:1NUW"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:1NUW"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:1NUW"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:1NUW"
FT HELIX 214..219
FT /evidence="ECO:0007829|PDB:1NUW"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:1NUW"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1LEV"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:1FBC"
FT HELIX 249..259
FT /evidence="ECO:0007829|PDB:1NUW"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:1NUW"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:1FPD"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:1FBP"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:1NUW"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:1NUW"
FT HELIX 282..291
FT /evidence="ECO:0007829|PDB:1NUW"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:1NUW"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:1NUW"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:1NUW"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:1FBP"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:1NUW"
FT HELIX 322..334
FT /evidence="ECO:0007829|PDB:1NUW"
SQ 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
