ID G6PD_LEUME Reviewed; 486 AA.
AC P11411;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 09-APR-2025, entry version 158.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00966};
DE Short=G6PD {ECO:0000255|HAMAP-Rule:MF_00966};
DE EC=1.1.1.363 {ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:11106479, ECO:0000269|PubMed:1304341, ECO:0000269|PubMed:4396688, ECO:0000269|PubMed:9485426};
DE AltName: Full=Glucose-6-phosphate dehydrogenase (NAD(P)(+)) {ECO:0000305};
GN Name=zwf {ECO:0000255|HAMAP-Rule:MF_00966};
OS Leuconostoc mesenteroides.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=1245;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12291;
RX PubMed=2071589; DOI=10.1016/s0021-9258(18)98798-3;
RA Lee W.T., Flynn T.G., Lyons C., Levy H.R.;
RT "Cloning of the gene and amino acid sequence for glucose 6-phosphate
RT dehydrogenase from Leuconostoc mesenteroides.";
RL J. Biol. Chem. 266:13028-13034(1991).
RN [2]
RP PROTEIN SEQUENCE OF 147-188.
RX PubMed=3100332; DOI=10.1016/0014-5793(87)81445-x;
RA Bhadbhade M.M., Adams M.J., Flynn T.G., Levy H.R.;
RT "Sequence identity between a lysine-containing peptide from Leuconostoc
RT mesenteroides glucose-6-phosphate dehydrogenase and an active site peptide
RT from human erythrocyte glucose-6-phosphate dehydrogenase.";
RL FEBS Lett. 211:243-246(1987).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=4396688; DOI=10.1016/s0021-9258(19)77187-7;
RA Olive C., Geroch M.E., Levy H.R.;
RT "Glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides. Kinetic
RT studies.";
RL J. Biol. Chem. 246:2047-2057(1971).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-22.
RX PubMed=1304341; DOI=10.1002/pro.5560010304;
RA Lee W.T., Levy H.R.;
RT "Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase
RT participates in substrate binding through charge-charge interaction.";
RL Protein Sci. 1:329-334(1992).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF THR-15; LYS-22; ARG-47;
RP GLN-48; PRO-150; TYR-180; LYS-183; LYS-344; ASP-375 AND TYR-416.
RX PubMed=11106479; DOI=10.1021/bi0014610;
RA Vought V., Ciccone T., Davino M.H., Fairbairn L., Lin Y., Cosgrove M.S.,
RA Adams M.J., Levy H.R.;
RT "Delineation of the roles of amino acids involved in the catalytic
RT functions of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase.";
RL Biochemistry 39:15012-15021(2000).
RN [6] {ECO:0007744|PDB:1DPG}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=7881907; DOI=10.1016/s0969-2126(94)00110-3;
RA Rowland P., Basak A.K., Gover S., Levy H.R., Adams M.J.;
RT "The three-dimensional structure of glucose 6-phosphate dehydrogenase from
RT Leuconostoc mesenteroides refined at 2.0-A resolution.";
RL Structure 2:1073-1087(1994).
RN [7] {ECO:0007744|PDB:2DPG}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT ASN-241 IN COMPLEX WITH
RP NADP, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE
RP SITE, AND MUTAGENESIS OF ASP-178; HIS-179 AND HIS-241.
RX PubMed=9485426; DOI=10.1021/bi972069y;
RA Cosgrove M.S., Naylor C., Paludan S., Adams M.J., Levy H.R.;
RT "On the mechanism of the reaction catalyzed by glucose 6-phosphate
RT dehydrogenase.";
RL Biochemistry 37:2759-2767(1998).
RN [8] {ECO:0007744|PDB:1E77, ECO:0007744|PDB:1E7M, ECO:0007744|PDB:1E7Y}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS ASN-178 AND CYS-366 IN
RP COMPLEXES WITH NAD; NADP AND GLUCOSE 6-PHOSPHATE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=11106478; DOI=10.1021/bi0014608;
RA Cosgrove M.S., Gover S., Naylor C.E., Vandeputte-Rutten L., Adams M.J.,
RA Levy H.R.;
RT "An examination of the role of Asp-177 in the His-Asp catalytic dyad of
RT Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: X-ray
RT structure and pH dependence of kinetic parameters of the D177N mutant
RT enzyme.";
RL Biochemistry 39:15002-15011(2000).
RN [9] {ECO:0007744|PDB:1H93, ECO:0007744|PDB:1H94, ECO:0007744|PDB:1H9A, ECO:0007744|PDB:1H9B}
RP X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) IN COMPLEXES WITH NAD AND NADP.
RX PubMed=11320304; DOI=10.1107/s0907444901003420;
RA Naylor C.E., Gover S., Basak A.K., Cosgrove M.S., Levy H.R., Adams M.J.;
RT "NADP+ and NAD+ binding to the dual coenzyme specific enzyme Leuconostoc
RT mesenteroides glucose 6-phosphate dehydrogenase: different interdomain
RT hinge angles are seen in different binary and ternary complexes.";
RL Acta Crystallogr. D 57:635-648(2001).
CC -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6-
CC phosphogluconolactone. Can utilize either NADP(+) or NAD(+).
CC {ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:11106479,
CC ECO:0000269|PubMed:1304341, ECO:0000269|PubMed:4396688,
CC ECO:0000269|PubMed:9485426}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + NAD(+) = 6-phospho-D-glucono-1,5-
CC lactone + NADH + H(+); Xref=Rhea:RHEA:38215, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57955,
CC ChEBI:CHEBI:61548; EC=1.1.1.363;
CC Evidence={ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:11106479,
CC ECO:0000269|PubMed:1304341, ECO:0000269|PubMed:4396688,
CC ECO:0000269|PubMed:9485426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-
CC lactone + NADPH + H(+); Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:61548; EC=1.1.1.363;
CC Evidence={ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:11106479,
CC ECO:0000269|PubMed:1304341, ECO:0000269|PubMed:4396688,
CC ECO:0000269|PubMed:9485426};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=114 uM for glucose 6-phosphate (with NADP)
CC {ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:9485426};
CC KM=69 uM for glucose 6-phosphate (with NAD)
CC {ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:9485426};
CC KM=8 uM for NADP {ECO:0000269|PubMed:11106478,
CC ECO:0000269|PubMed:9485426};
CC KM=160 uM for NAD {ECO:0000269|PubMed:11106478,
CC ECO:0000269|PubMed:9485426};
CC pH dependence:
CC Optimum pH is 5.4-8.9. {ECO:0000269|PubMed:11106478,
CC ECO:0000269|PubMed:9485426};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 1/3. {ECO:0000255|HAMAP-Rule:MF_00966}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11106478,
CC ECO:0000269|PubMed:9485426}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00966}.
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DR EMBL; M64446; AAA25265.1; -; Genomic_DNA.
DR PIR; A39864; A39864.
DR PDB; 1DPG; X-ray; 2.00 A; A/B=2-486.
DR PDB; 1E77; X-ray; 2.69 A; A=2-486.
DR PDB; 1E7M; X-ray; 2.54 A; A=2-486.
DR PDB; 1E7Y; X-ray; 2.48 A; A=2-486.
DR PDB; 1H93; X-ray; 2.20 A; A=2-486.
DR PDB; 1H94; X-ray; 2.50 A; A=2-486.
DR PDB; 1H9A; X-ray; 2.16 A; A=2-486.
DR PDB; 1H9B; X-ray; 2.40 A; A=2-486.
DR PDB; 2DPG; X-ray; 2.50 A; A=2-486.
DR PDBsum; 1DPG; -.
DR PDBsum; 1E77; -.
DR PDBsum; 1E7M; -.
DR PDBsum; 1E7Y; -.
DR PDBsum; 1H93; -.
DR PDBsum; 1H94; -.
DR PDBsum; 1H9A; -.
DR PDBsum; 1H9B; -.
DR PDBsum; 2DPG; -.
DR AlphaFoldDB; P11411; -.
DR SMR; P11411; -.
DR STRING; 1245.ARA02_09055; -.
DR BindingDB; P11411; -.
DR ChEMBL; CHEMBL1741173; -.
DR DrugBank; DB04122; beta-D-glucose 6-phosphate.
DR DrugBank; DB02338; NADPH.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR KEGG; ag:AAA25265; -.
DR BioCyc; MetaCyc:MONOMER-13060; -.
DR BRENDA; 1.1.1.363; 839.
DR SABIO-RK; P11411; -.
DR UniPathway; UPA00115; UER00408.
DR EvolutionaryTrace; P11411; -.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:TreeGrafter.
DR Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00966; G6PD; 1.
DR InterPro; IPR001282; G6P_DH.
DR InterPro; IPR019796; G6P_DH_AS.
DR InterPro; IPR022675; G6P_DH_C.
DR InterPro; IPR022674; G6P_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00871; zwf; 1.
DR PANTHER; PTHR23429:SF0; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE; 1.
DR PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PIRSF; PIRSF000110; G6PD; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW Glucose metabolism; NAD; NADP; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..486
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000068125"
FT ACT_SITE 241
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966,
FT ECO:0000269|PubMed:9485426"
FT BINDING 13..20
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966,
FT ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:11320304,
FT ECO:0000269|PubMed:9485426"
FT BINDING 47
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966,
FT ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:11320304,
FT ECO:0000269|PubMed:9485426"
FT BINDING 86..87
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966,
FT ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:11320304,
FT ECO:0000269|PubMed:9485426"
FT BINDING 149
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966,
FT ECO:0000269|PubMed:11320304"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11106478"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11106478"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11106478"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11106478"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11106478"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11106478"
FT MUTAGEN 15
FT /note="T->A: Decreases catalytic efficiency toward glucose
FT 6-phosphate."
FT /evidence="ECO:0000269|PubMed:11106479"
FT MUTAGEN 15
FT /note="T->S: Decreases catalytic efficiency toward glucose
FT 6-phosphate (with NAD)."
FT /evidence="ECO:0000269|PubMed:11106479"
FT MUTAGEN 22
FT /note="K->E: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:11106479,
FT ECO:0000269|PubMed:1304341"
FT MUTAGEN 22
FT /note="K->Q: Strongly decreases catalytic efficiency toward
FT glucose 6-phosphate."
FT /evidence="ECO:0000269|PubMed:11106479,
FT ECO:0000269|PubMed:1304341"
FT MUTAGEN 22
FT /note="K->R: Decreases catalytic efficiency toward glucose
FT 6-phosphate."
FT /evidence="ECO:0000269|PubMed:11106479,
FT ECO:0000269|PubMed:1304341"
FT MUTAGEN 47
FT /note="R->A: Decreases catalytic efficiency toward glucose
FT 6-phosphate."
FT /evidence="ECO:0000269|PubMed:11106479"
FT MUTAGEN 48
FT /note="Q->A,E: Decreases catalytic efficiency toward
FT glucose 6-phosphate."
FT /evidence="ECO:0000269|PubMed:11106479"
FT MUTAGEN 150
FT /note="P->G,V: Strongly decreases catalytic efficiency
FT toward glucose 6-phosphate."
FT /evidence="ECO:0000269|PubMed:11106479"
FT MUTAGEN 178
FT /note="D->N: Strongly decreases catalytic efficiency toward
FT glucose 6-phosphate."
FT /evidence="ECO:0000269|PubMed:9485426"
FT MUTAGEN 179
FT /note="H->N: Strongly decreases catalytic efficiency toward
FT glucose 6-phosphate."
FT /evidence="ECO:0000269|PubMed:9485426"
FT MUTAGEN 180
FT /note="Y->F: Decreases catalytic efficiency toward glucose
FT 6-phosphate."
FT /evidence="ECO:0000269|PubMed:11106479"
FT MUTAGEN 183
FT /note="K->Q,R: Strongly decreases catalytic efficiency
FT toward glucose 6-phosphate."
FT /evidence="ECO:0000269|PubMed:11106479"
FT MUTAGEN 241
FT /note="H->N: Strongly decreases catalytic efficiency toward
FT glucose 6-phosphate."
FT /evidence="ECO:0000269|PubMed:9485426"
FT MUTAGEN 344
FT /note="K->Q,R: Strongly decreases catalytic efficiency
FT toward glucose 6-phosphate."
FT /evidence="ECO:0000269|PubMed:11106479"
FT MUTAGEN 375
FT /note="D->Q: Strongly decreases catalytic efficiency toward
FT glucose 6-phosphate."
FT /evidence="ECO:0000269|PubMed:11106479"
FT MUTAGEN 416
FT /note="Y->F: Decreases catalytic efficiency toward glucose
FT 6-phosphate."
FT /evidence="ECO:0000269|PubMed:11106479"
FT CONFLICT 154..156
FT /note="SYD -> HYI (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="L -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:1DPG"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 17..21
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 38..48
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 92..106
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:1DPG"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 184..188
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 189..194
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:1DPG"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 208..216
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:1H9A"
FT HELIX 225..236
FT /evidence="ECO:0007829|PDB:1DPG"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 259..270
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 278..284
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:1H9A"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 333..343
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 345..352
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 369..377
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 379..387
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 395..403
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 406..411
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 415..425
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:1H94"
FT HELIX 434..452
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:1DPG"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:1DPG"
FT HELIX 469..476
FT /evidence="ECO:0007829|PDB:1DPG"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:1DPG"
SQ SEQUENCE 486 AA; 54441 MW; AA43433F83ED091D CRC64;
MVSEIKTLVT FFGGTGDLAK RKLYPSVFNL YKKGYLQKHF AIVGTARQAL NDDEFKQLVR
DSIKDFTDDQ AQAEAFIEHF SYRAHDVTDA ASYAVLKEAI EEAADKFDID GNRIFYMSVA
PRFFGTIAKY LKSEGLLADT GYNRLMIEKP FGTSYDTAAE LQNDLENAFD DNQLFRIDHY
LGKEMVQNIA ALRFGNPIFD AAWNKDYIKN VQVTLSEVLG VEERAGYYDT AGALLDMIQN
HTMQIVGWLA MEKPESFTDK DIRAAKNAAF NALKIYDEAE VNKYFVRAQY GAGDSADFKP
YLEELDVPAD SKNNTFIAGE LQFDLPRWEG VPFYVRSGKR LAAKQTRVDI VFKAGTFNFG
SEQEAQEAVL SIIIDPKGAI ELKLNAKSVE DAFNTRTIDL GWTVSDEDKK NTPEPYERMI
HDTMNGDGSN FADWNGVSIA WKFVDAISAV YTADKAPLET YKSGSMGPEA SDKLLAANGD
AWVFKG
//