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 02-SEP-2026, entry version 190. 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 an allosteric CC inhibitor. AMP binding affects the turnover of bound substrate and not CC the affinity for substrate. Fructose 2,6-bisphosphate acts as a CC competitive inhibitor. Fructose 2,6-bisphosphate and AMP have CC synergistic effects. {ECO:0000269|PubMed:10913263, CC ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255, CC ECO:0000269|PubMed:17933867, ECO:0000269|PubMed:2164670, CC 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}. 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 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 AlphaFoldDB; P00636; -. DR MDRepo; P00636; -. DR SMR; P00636; -. DR FunCoup; P00636; 731. DR STRING; 9823.ENSSSCP00000049752; -. DR BindingDB; P00636; -. DR ChEMBL; CHEMBL2263; -. DR DrugCentral; P00636; -. DR iPTMnet; P00636; -. DR PaxDb; 9823-ENSSSCP00000049752; -. DR PeptideAtlas; P00636; -. DR Ensembl; ENSSSCT00000065852.3; ENSSSCP00000049752.1; ENSSSCG00000031174.3. DR Ensembl; ENSSSCT00005040060.1; ENSSSCP00005024518.1; ENSSSCG00005024872.1. DR Ensembl; ENSSSCT00015088932.1; ENSSSCP00015036278.1; ENSSSCG00015066376.1. DR Ensembl; ENSSSCT00015089465.1; ENSSSCP00015036500.1; ENSSSCG00015066376.1. DR Ensembl; ENSSSCT00025019008.1; ENSSSCP00025007679.1; ENSSSCG00025014230.1. DR Ensembl; ENSSSCT00030006729.1; ENSSSCP00030002968.1; ENSSSCG00030004973.1. DR Ensembl; ENSSSCT00035035384.1; ENSSSCP00035014027.1; ENSSSCG00035026802.1. DR Ensembl; ENSSSCT00050015866.1; ENSSSCP00050006487.1; ENSSSCG00050011780.1. DR Ensembl; ENSSSCT00055027666.1; ENSSSCP00055022027.1; ENSSSCG00055014004.1. DR Ensembl; ENSSSCT00070042384.1; ENSSSCP00070035635.1; ENSSSCG00070021304.1. DR Ensembl; ENSSSCT00085001969; ENSSSCP00085001490; ENSSSCG00085001316. 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; YIPENCP; -. DR OrthoDB; 10256725at2759; -. DR BRENDA; 3.1.3.11; 6170. DR Reactome; R-SSC-70263; Gluconeogenesis. DR SABIO-RK; P00636; -. DR UniPathway; UPA00138; -. DR EvolutionaryTrace; P00636; -. DR PRO; PR:P00636; -. DR Proteomes; UP000008227; Chromosome 10. DR Bgee; ENSSSCG00000031174; Expressed in kidney and 44 other cell types or tissues. DR ExpressionAtlas; P00636; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. 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; EXP: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:0006002; P:fructose 6-phosphate metabolic process; ISS:UniProtKB. 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 CDD; cd00354; FBPase; 1. DR FunFam; 3.30.540.10:FF:000037; Fructose-1,6-bisphosphatase 1; 1. DR FunFam; 3.40.190.80:FF:000001; Fructose-1,6-bisphosphatase class 1; 1. DR Gene3D; 3.40.190.80; -; 1. DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 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 NCBIfam; NF006778; PRK09293.1-1; 1. DR PANTHER; PTHR11556:SF11; FRUCTOSE-1,6-BISPHOSPHATASE 1; 1. DR PANTHER; PTHR11556; FRUCTOSE-1,6-BISPHOSPHATASE-RELATED; 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 SUPFAM; SSF56655; Carbohydrate phosphatase; 1. DR PROSITE; PS00124; FBPASE; 1. 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; -. 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 HELIX 238..241 FT /evidence="ECO:0007829|PDB:1NUW" 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 HELIX 278..282 FT /evidence="ECO:0007829|PDB:1NUW" FT HELIX 283..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 HELIX 306..308 FT /evidence="ECO:0007829|PDB:1FSA" 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 //