F16PA_ECOLI
ID F16PA_ECOLI Reviewed; 332 AA.
AC P0A993; P09200; Q2M674;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Fructose-1,6-bisphosphatase class 1 {ECO:0000255|HAMAP-Rule:MF_01855, ECO:0000305};
DE Short=FBPase class 1 {ECO:0000255|HAMAP-Rule:MF_01855, ECO:0000305};
DE EC=3.1.3.11 {ECO:0000255|HAMAP-Rule:MF_01855, ECO:0000269|PubMed:16670087, ECO:0000269|PubMed:6327623};
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 {ECO:0000255|HAMAP-Rule:MF_01855, ECO:0000305};
GN Name=fbp {ECO:0000303|PubMed:6327623}; Synonyms=fdp;
GN OrderedLocusNames=b4232, JW4191;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2843822; DOI=10.1093/nar/16.17.8707;
RA Hamilton W.D.O., Harrison D.A., Dyer T.A.;
RT "Sequence of the Escherichia coli fructose-1,6-bisphosphatase gene.";
RL Nucleic Acids Res. 16:8707-8707(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 43-62; 220-229; 239-249; 254-269 AND 297-308.
RX PubMed=3008716; DOI=10.1016/0006-291x(86)90005-7;
RA Marcus F., Gontero B., Harrsch P.B., Rittenhouse J.;
RT "Amino acid sequence homology among fructose-1,6-bisphosphatases.";
RL Biochem. Biophys. Res. Commun. 135:374-381(1986).
RN [6]
RP CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=6327623; DOI=10.1128/jb.158.3.1048-1053.1984;
RA Sedivy J.M., Daldal F., Fraenkel D.G.;
RT "Fructose bisphosphatase of Escherichia coli: cloning of the structural
RT gene (fbp) and preparation of a chromosomal deletion.";
RL J. Bacteriol. 158:1048-1053(1984).
RN [7]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [8] {ECO:0007744|PDB:2GQ1}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH SULFATE IONS,
RP PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT,
RP COFACTOR, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=16670087; DOI=10.1074/jbc.m602553200;
RA Hines J.K., Fromm H.J., Honzatko R.B.;
RT "Novel allosteric activation site in Escherichia coli fructose-1,6-
RT bisphosphatase.";
RL J. Biol. Chem. 281:18386-18393(2006).
RN [9] {ECO:0007744|PDB:2OWZ, ECO:0007744|PDB:2OX3}
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) IN COMPLEXES WITH
RP FRUCTOSE-6-PHOSPHATE; CITRATE AND PHOSPHOENOLPYRUVATE, ACTIVITY REGULATION,
RP AND SUBUNIT.
RX PubMed=17314096; DOI=10.1074/jbc.m611104200;
RA Hines J.K., Fromm H.J., Honzatko R.B.;
RT "Structures of activated fructose-1,6-bisphosphatase from Escherichia coli.
RT Coordinate regulation of bacterial metabolism and the conservation of the
RT R-state.";
RL J. Biol. Chem. 282:11696-11704(2007).
RN [10] {ECO:0007744|PDB:2Q8M}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH
RP FRUCTOSE-1,6-BISPHOSPHATE; MAGNESIUM IONS; AMP AND
RP BETA-D-GLUCOSE-6-PHOSPHATE, SUBUNIT, COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=17567577; DOI=10.1074/jbc.m703580200;
RA Hines J.K., Kruesel C.E., Fromm H.J., Honzatko R.B.;
RT "Structure of inhibited fructose-1,6-bisphosphatase from Escherichia coli:
RT distinct allosteric inhibition sites for AMP and glucose 6-phosphate and
RT the characterization of a gluconeogenic switch.";
RL J. Biol. Chem. 282:24697-24706(2007).
RN [11] {ECO:0007744|PDB:2QVR}
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) IN COMPLEX WITH
RP FRUCTOSE-2,6-BISPHOSPHATE; MAGNESIUM IONS AND CITRATE, AND ACTIVITY
RP 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 -!- 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:0000255|HAMAP-Rule:MF_01855,
CC ECO:0000269|PubMed:16670087, ECO:0000269|PubMed:6327623};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01855,
CC ECO:0000269|PubMed:16670087, ECO:0000269|PubMed:17567577};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01855, ECO:0000269|PubMed:16670087,
CC ECO:0000269|PubMed:17567577};
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. Activated by three-carbon
CC carboxylic acids, phosphorylated three-carbon carboxylic acids and
CC sulfate. Strongly activated by phosphoenolpyruvate and citrate.
CC Inhibited by AMP, which affects the turnover of bound substrate and not
CC the affinity for substrate. Allosterically inhibited by glucose 6-
CC phosphate. AMP and glucose 6-phosphate act synergistically as
CC allosteric inhibitors. Phosphoenolpyruvate antagonizes inhibition by
CC AMP and glucose 6-phosphate. Fructose 2,6-bisphosphate acts as
CC competitive inhibitor. {ECO:0000269|PubMed:16670087,
CC ECO:0000269|PubMed:17314096, ECO:0000269|PubMed:17567577,
CC ECO:0000269|PubMed:17933867}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.7 uM for fructose 1,6-biphosphate {ECO:0000269|PubMed:16670087};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_01855}.
CC -!- SUBUNIT: Homotetramer. Phosphoenolpyruvate stabilizes the homotetramer.
CC {ECO:0000269|PubMed:16670087, ECO:0000269|PubMed:17314096,
CC ECO:0000269|PubMed:17567577, ECO:0000269|PubMed:17933867}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01855,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000255|HAMAP-
CC Rule:MF_01855, ECO:0000305}.
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DR EMBL; X12545; CAA31062.1; -; mRNA.
DR EMBL; U14003; AAA97129.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77189.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78232.1; -; Genomic_DNA.
DR PIR; S01383; PAEC.
DR RefSeq; NP_418653.1; NC_000913.3.
DR RefSeq; WP_000853753.1; NZ_STEB01000013.1.
DR PDB; 2GQ1; X-ray; 1.45 A; A=1-332.
DR PDB; 2OWZ; X-ray; 2.18 A; A=1-332.
DR PDB; 2OX3; X-ray; 2.18 A; A=1-332.
DR PDB; 2Q8M; X-ray; 2.05 A; A/B=1-332.
DR PDB; 2QVR; X-ray; 2.18 A; A=1-332.
DR PDBsum; 2GQ1; -.
DR PDBsum; 2OWZ; -.
DR PDBsum; 2OX3; -.
DR PDBsum; 2Q8M; -.
DR PDBsum; 2QVR; -.
DR AlphaFoldDB; P0A993; -.
DR SMR; P0A993; -.
DR BioGRID; 4259316; 21.
DR STRING; 511145.b4232; -.
DR SWISS-2DPAGE; P0A993; -.
DR jPOST; P0A993; -.
DR PaxDb; P0A993; -.
DR PRIDE; P0A993; -.
DR EnsemblBacteria; AAC77189; AAC77189; b4232.
DR EnsemblBacteria; BAE78232; BAE78232; BAE78232.
DR GeneID; 66671851; -.
DR GeneID; 948753; -.
DR KEGG; ecj:JW4191; -.
DR KEGG; eco:b4232; -.
DR PATRIC; fig|1411691.4.peg.2470; -.
DR EchoBASE; EB0279; -.
DR eggNOG; COG0158; Bacteria.
DR HOGENOM; CLU_039977_2_2_6; -.
DR InParanoid; P0A993; -.
DR OMA; YIPENCP; -.
DR PhylomeDB; P0A993; -.
DR BioCyc; EcoCyc:F16B-MON; -.
DR BioCyc; MetaCyc:F16B-MON; -.
DR BRENDA; 3.1.3.11; 2026.
DR SABIO-RK; P0A993; -.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; P0A993; -.
DR PRO; PR:P0A993; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006000; P:fructose metabolic process; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IMP:EcoCyc.
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; Allosteric enzyme; Carbohydrate metabolism; Cytoplasm;
KW Direct protein sequencing; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..332
FT /note="Fructose-1,6-bisphosphatase class 1"
FT /id="PRO_0000200492"
FT BINDING 3..5
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000305|PubMed:17314096,
FT ECO:0000305|PubMed:17933867, ECO:0007744|PDB:2OWZ,
FT ECO:0007744|PDB:2QVR"
FT BINDING 3..5
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000305|PubMed:17314096,
FT ECO:0007744|PDB:2OX3"
FT BINDING 19..23
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:17567577,
FT ECO:0007744|PDB:2Q8M"
FT BINDING 30
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000305|PubMed:17314096,
FT ECO:0000305|PubMed:17933867, ECO:0007744|PDB:2OWZ,
FT ECO:0007744|PDB:2QVR"
FT BINDING 30
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000305|PubMed:17314096,
FT ECO:0007744|PDB:2OX3"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855,
FT ECO:0000269|PubMed:17567577"
FT BINDING 104..105
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:17567577,
FT ECO:0007744|PDB:2Q8M"
FT BINDING 110
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855,
FT ECO:0000269|PubMed:17567577"
FT BINDING 110
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855,
FT ECO:0000269|PubMed:17567577, ECO:0000269|PubMed:17933867"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855,
FT ECO:0000269|PubMed:17567577"
FT BINDING 113..116
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855,
FT ECO:0000305|PubMed:17314096, ECO:0000305|PubMed:17567577"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855,
FT ECO:0000269|PubMed:17567577, ECO:0000269|PubMed:17933867"
FT BINDING 187
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000305|PubMed:17314096,
FT ECO:0000305|PubMed:17933867, ECO:0007744|PDB:2OWZ,
FT ECO:0007744|PDB:2QVR"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855,
FT ECO:0000305|PubMed:17314096, ECO:0000305|PubMed:17567577"
FT BINDING 222
FT /ligand="beta-D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58247"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000305|PubMed:17567577,
FT ECO:0007744|PDB:2Q8M"
FT BINDING 225
FT /ligand="beta-D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58247"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000305|PubMed:17567577,
FT ECO:0007744|PDB:2Q8M"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855,
FT ECO:0000305|PubMed:17314096, ECO:0000305|PubMed:17567577"
FT BINDING 257..259
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855,
FT ECO:0000305|PubMed:17314096, ECO:0000305|PubMed:17567577"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855,
FT ECO:0000305|PubMed:17314096, ECO:0000305|PubMed:17567577"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855,
FT ECO:0000269|PubMed:17567577, ECO:0000269|PubMed:17933867"
FT HELIX 4..10
FT /evidence="ECO:0007829|PDB:2GQ1"
FT TURN 11..14
FT /evidence="ECO:0007829|PDB:2GQ1"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:2GQ1"
FT HELIX 19..40
FT /evidence="ECO:0007829|PDB:2GQ1"
FT TURN 41..48
FT /evidence="ECO:0007829|PDB:2QVR"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:2QVR"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2QVR"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:2GQ1"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:2GQ1"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:2GQ1"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:2GQ1"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:2GQ1"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:2GQ1"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2GQ1"
FT STRAND 154..173
FT /evidence="ECO:0007829|PDB:2GQ1"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:2GQ1"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:2GQ1"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:2GQ1"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:2GQ1"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:2GQ1"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:2GQ1"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:2GQ1"
FT HELIX 243..253
FT /evidence="ECO:0007829|PDB:2GQ1"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:2GQ1"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:2GQ1"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:2GQ1"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:2GQ1"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:2GQ1"
FT STRAND 289..296
FT /evidence="ECO:0007829|PDB:2GQ1"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:2GQ1"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:2GQ1"
FT HELIX 316..328
FT /evidence="ECO:0007829|PDB:2GQ1"
SQ SEQUENCE 332 AA; 36834 MW; 4F0FC8109491D78F CRC64;
MKTLGEFIVE KQHEFSHATG ELTALLSAIK LGAKIIHRDI NKAGLVDILG ASGAENVQGE
VQQKLDLFAN EKLKAALKAR DIVAGIASEE EDEIVVFEGC EHAKYVVLMD PLDGSSNIDV
NVSVGTIFSI YRRVTPVGTP VTEEDFLQPG NKQVAAGYVV YGSSTMLVYT TGCGVHAFTY
DPSLGVFCLC QERMRFPEKG KTYSINEGNY IKFPNGVKKY IKFCQEEDKS TNRPYTSRYI
GSLVADFHRN LLKGGIYLYP STASHPDGKL RLLYECNPMA FLAEQAGGKA SDGKERILDI
IPETLHQRRS FFVGNDHMVE DVERFIREFP DA
