PDH1_LEUMG
ID PDH1_LEUMG Reviewed; 602 AA.
AC Q3L245;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Pyranose dehydrogenase 1 {ECO:0000303|PubMed:18097667};
DE Short=PDH 1 {ECO:0000303|PubMed:18097667};
DE EC=1.1.99.29 {ECO:0000269|PubMed:18083263, ECO:0000269|Ref.3, ECO:0000269|Ref.4};
DE AltName: Full=Pyranose:quinone oxidoreductase 1 {ECO:0000303|Ref.4};
DE Flags: Precursor;
GN Name=pdh1 {ECO:0000303|PubMed:18097667};
OS Leucoagaricus meleagris (Western flat-topped agaric) (Agaricus meleagris).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=201219;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND INDUCTION.
RC STRAIN=CCBAS 907;
RX PubMed=18097667; DOI=10.1007/s00294-007-0171-9;
RA Kittl R., Sygmund C., Halada P., Volc J., Divne C., Haltrich D.,
RA Peterbauer C.K.;
RT "Molecular cloning of three pyranose dehydrogenase-encoding genes from
RT Agaricus meleagris and analysis of their expression by real-time RT-PCR.";
RL Curr. Genet. 53:117-127(2008).
RN [2]
RP PROTEIN SEQUENCE OF 26-35, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION, AND MASS
RP SPECTROMETRY.
RC STRAIN=CCBAS 907;
RX PubMed=18083263; DOI=10.1016/j.jbiotec.2007.10.013;
RA Sygmund C., Kittl R., Volc J., Halada P., Kubatova E., Haltrich D.,
RA Peterbauer C.K.;
RT "Characterization of pyranose dehydrogenase from Agaricus meleagris and its
RT application in the C-2 specific conversion of D-galactose.";
RL J. Biotechnol. 133:334-342(2008).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=CCBAS 907;
RX DOI=10.1016/j.tetlet.2004.09.149;
RA Sedmera P., Halada P., Peterbauer C., Volc J.;
RT "A new enzyme catalysis: 3,4-dioxidation of some aryl beta-D-
RT glycopyranosides by fungal pyranose dehydrogenase.";
RL Tetrahedron Lett. 45:8677-8680(2004).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=CCBAS 907;
RX DOI=10.1016/j.molcatb.2006.04.004;
RA Sedmera P., Halada P., Kubatova E., Haltrich D., Prikrylova V., Volc J.;
RT "New biotransformations of some reducing sugars to the corresponding
RT (di)dehydro(glycosyl) aldoses or aldonic acids using fungal pyranose
RT dehydrogenase.";
RL J. Mol. Catal., B Enzym. 41:32-42(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH FAD, GLYCOSYLATION
RP AT ASN-100 AND ASN-344, COFACTOR, AND ACTIVE SITE.
RX PubMed=23326459; DOI=10.1371/journal.pone.0053567;
RA Tan T.C., Spadiut O., Wongnate T., Sucharitakul J., Krondorfer I.,
RA Sygmund C., Haltrich D., Chaiyen P., Peterbauer C.K., Divne C.;
RT "The 1.6 A crystal structure of pyranose dehydrogenase from Agaricus
RT meleagris rationalizes substrate specificity and reveals a flavin
RT intermediate.";
RL PLoS ONE 8:E53567-E53567(2013).
CC -!- FUNCTION: Catalyzes the single-oxidation or sequential double oxidation
CC reaction of carbohydrates primarily at carbon-2 and/or carbon-3 with
CC the concomitant reduction of the flavin. The enzyme exhibits a broad
CC sugar substrate specificity, oxidizing different aldopyranoses to the
CC corresponding C-1, C-2, C-3 or C-1,2, C-2,3 and C-3,4 (di)dehydro
CC sugars with substrate-specific regioselectivity. Accepts only a narrow
CC range of electron acceptors such as substituted benzoquinones and
CC complexed metal ions and reacts extremely slowly with O(2) as acceptor.
CC May play a role in the natural recycling of plant matter by oxidizing
CC all major monosaccharides in lignocellulose and by reducing quinone
CC compounds or reactive radical species generated during lignin
CC depolymerization. {ECO:0000269|PubMed:18083263, ECO:0000269|Ref.3,
CC ECO:0000269|Ref.4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-2-ulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={ECO:0000269|PubMed:18083263,
CC ECO:0000269|Ref.3, ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-3-ulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={ECO:0000269|PubMed:18083263,
CC ECO:0000269|Ref.3, ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-2,3-diulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={ECO:0000269|PubMed:18083263,
CC ECO:0000269|Ref.3, ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a pyranoside + acceptor = a pyranosid-3-ulose + reduced
CC acceptor.; EC=1.1.99.29; Evidence={ECO:0000269|PubMed:18083263,
CC ECO:0000269|Ref.3, ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a pyranoside + acceptor = a pyranosid-3,4-diulose + reduced
CC acceptor.; EC=1.1.99.29; Evidence={ECO:0000269|PubMed:18083263,
CC ECO:0000269|Ref.3, ECO:0000269|Ref.4};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:18083263, ECO:0000269|PubMed:23326459};
CC Note=Binds 1 FAD covalently per subunit. {ECO:0000269|PubMed:18083263,
CC ECO:0000269|PubMed:23326459};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.82 mM for D-glucose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:18083263};
CC KM=6.82 mM for cellobiose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:18083263};
CC KM=8.61 mM for D-maltose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:18083263};
CC KM=156 mM for maltotriose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:18083263};
CC KM=108 mM for D-mannose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:18083263};
CC KM=1.05 mM for D-galactose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:18083263};
CC KM=137 mM for L-sorbose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:18083263};
CC KM=59.7 mM for D-ribose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:18083263};
CC KM=79.1 mM for D-talose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:18083263};
CC KM=1.93 mM for D-xylose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:18083263};
CC KM=0.54 mM for L-arabinose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:18083263};
CC KM=10.8 mM for xylobiose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:18083263};
CC KM=153 mM for D-fructose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:18083263};
CC KM=134 mM for lactose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:18083263};
CC KM=0.13 mM for ferricenium (at pH 8.5 with D-glucose as substrate)
CC {ECO:0000269|PubMed:18083263};
CC KM=1.82 mM for 1,4-benzoquinone (at pH 3.0 with D-glucose as
CC substrate) {ECO:0000269|PubMed:18083263};
CC KM=0.55 mM for 2-chloro-1,4-benzoquinone (at pH 5.0 with D-glucose as
CC substrate) {ECO:0000269|PubMed:18083263};
CC KM=0.92 mM for 2,5-dichloro-1,4-benzoquinone (at pH 5.0 with D-
CC glucose as substrate) {ECO:0000269|PubMed:18083263};
CC KM=0.18 mM for methyl-1,4-benzoquinone (at pH 8.0 with D-glucose as
CC substrate) {ECO:0000269|PubMed:18083263};
CC KM=0.22 mM for 3,5-di-tert-butyl-benzoquinone (at pH 6.0 with D-
CC glucose as substrate) {ECO:0000269|PubMed:18083263};
CC KM=0.14 mM for 2,6-dichloroindophenol (at pH 4.0 with D-glucose as
CC substrate) {ECO:0000269|PubMed:18083263};
CC Vmax=41.4 umol/min/mg enzyme for D-glucose (with ferricenium ion
CC (Fc(+)) as electron acceptor) {ECO:0000269|PubMed:18083263};
CC Vmax=34.5 umol/min/mg enzyme for cellobiose (with ferricenium ion
CC (Fc(+)) as electron acceptor) {ECO:0000269|PubMed:18083263};
CC Vmax=38.9 umol/min/mg enzyme for D-maltose (with ferricenium ion
CC (Fc(+)) as electron acceptor) {ECO:0000269|PubMed:18083263};
CC Vmax=21.3 umol/min/mg enzyme for maltotriose (with ferricenium ion
CC (Fc(+)) as electron acceptor) {ECO:0000269|PubMed:18083263};
CC Vmax=26.4 umol/min/mg enzyme for D-mannose (with ferricenium ion
CC (Fc(+)) as electron acceptor) {ECO:0000269|PubMed:18083263};
CC Vmax=43.7 umol/min/mg enzyme for D-galactose (with ferricenium ion
CC (Fc(+)) as electron acceptor) {ECO:0000269|PubMed:18083263};
CC Vmax=14.1 umol/min/mg enzyme for L-sorbose (with ferricenium ion
CC (Fc(+)) as electron acceptor) {ECO:0000269|PubMed:18083263};
CC Vmax=28.2 umol/min/mg enzyme for D-ribose (with ferricenium ion
CC (Fc(+)) as electron acceptor) {ECO:0000269|PubMed:18083263};
CC Vmax=19.2 umol/min/mg enzyme for D-talose (with ferricenium ion
CC (Fc(+)) as electron acceptor) {ECO:0000269|PubMed:18083263};
CC Vmax=39.1 umol/min/mg enzyme for D-xylose (with ferricenium ion
CC (Fc(+)) as electron acceptor) {ECO:0000269|PubMed:18083263};
CC Vmax=33.5 umol/min/mg enzyme for L-arabinose (with ferricenium ion
CC (Fc(+)) as electron acceptor) {ECO:0000269|PubMed:18083263};
CC Vmax=45.4 umol/min/mg enzyme for xylobiose (with ferricenium ion
CC (Fc(+)) as electron acceptor) {ECO:0000269|PubMed:18083263};
CC Vmax=14.9 umol/min/mg enzyme for D-fructose (with ferricenium ion
CC (Fc(+)) as electron acceptor) {ECO:0000269|PubMed:18083263};
CC Vmax=35.6 umol/min/mg enzyme for lactose (with ferricenium ion
CC (Fc(+)) as electron acceptor) {ECO:0000269|PubMed:18083263};
CC Vmax=93.9 umol/min/mg enzyme for ferricenium (at pH 8.5 with D-
CC glucose as substrate) {ECO:0000269|PubMed:18083263};
CC Vmax=68.5 umol/min/mg enzyme for 1,4-benzoquinone (at pH 3.0 with D-
CC glucose as substrate) {ECO:0000269|PubMed:18083263};
CC Vmax=13.6 umol/min/mg enzyme for 2-chloro-1,4-benzoquinone (at pH 5.0
CC with D-glucose as substrate) {ECO:0000269|PubMed:18083263};
CC Vmax=2.78 umol/min/mg enzyme for 2,5-dichloro-1,4-benzoquinone (at pH
CC 5.0 with D-glucose as substrate) {ECO:0000269|PubMed:18083263};
CC Vmax=2.7 umol/min/mg enzyme for methyl-1,4-benzoquinone (at pH 8.0
CC with D-glucose as substrate) {ECO:0000269|PubMed:18083263};
CC Vmax=95.6 umol/min/mg enzyme for 3,5-di-tert-butyl-benzoquinone (at
CC pH 6.0 with D-glucose as substrate) {ECO:0000269|PubMed:18083263};
CC Vmax=56.3 umol/min/mg enzyme for 2,6-dichloroindophenol (at pH 4.0
CC with D-glucose as substrate) {ECO:0000269|PubMed:18083263};
CC pH dependence:
CC Optimum pH is 9 with ferricenium ion (Fc(+)) as electron acceptor.
CC The enzyme is stable from pH 4 to pH 10.
CC {ECO:0000269|PubMed:18083263};
CC Temperature dependence:
CC Optimum temperature is 63 degrees Celsius with ferricenium ion
CC (Fc(+)) as electron acceptor. {ECO:0000269|PubMed:18083263};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18083263}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18083263}.
CC -!- INDUCTION: Induced by carbon starvation. {ECO:0000269|PubMed:18097667}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:18083263}.
CC -!- MASS SPECTROMETRY: Mass=66547; Method=MALDI; Note=Mass of the N-
CC glycosylated protein.; Evidence={ECO:0000269|PubMed:18083263};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AY753306; AAW82996.1; -; Genomic_DNA.
DR EMBL; AY753307; AAW82997.1; -; mRNA.
DR PDB; 4H7U; X-ray; 1.60 A; A=1-602.
DR PDBsum; 4H7U; -.
DR AlphaFoldDB; Q3L245; -.
DR SMR; Q3L245; -.
DR CAZy; AA3; Auxiliary Activities 3.
DR iPTMnet; Q3L245; -.
DR BRENDA; 1.1.99.29; 7355.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0033718; F:pyranose dehydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing; FAD;
KW Flavoprotein; Glycoprotein; Oxidoreductase; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:18083263"
FT CHAIN 26..602
FT /note="Pyranose dehydrogenase 1"
FT /id="PRO_0000431287"
FT ACT_SITE 537
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:23326459"
FT ACT_SITE 581
FT /evidence="ECO:0000269|PubMed:23326459"
FT MOD_RES 128
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000269|PubMed:23326459"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23326459"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23326459"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:4H7U"
FT TURN 107..111
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 188..195
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 202..213
FT /evidence="ECO:0007829|PDB:4H7U"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:4H7U"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 324..329
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:4H7U"
FT TURN 339..342
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 349..357
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 366..376
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 413..424
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 443..453
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 482..499
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:4H7U"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 508..513
FT /evidence="ECO:0007829|PDB:4H7U"
FT TURN 514..517
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 521..531
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 564..568
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:4H7U"
FT STRAND 574..576
FT /evidence="ECO:0007829|PDB:4H7U"
FT HELIX 583..600
FT /evidence="ECO:0007829|PDB:4H7U"
SQ SEQUENCE 602 AA; 64684 MW; EC7A73CABCA75DBE CRC64;
MLPRVTKLNS RLLSLALLGI QIARGAITYQ HPDDLPSGVD YDFIVAGGGT AGLVVASRLS
ENSNWKVLVI EAGPSNKDAF VTRVPGLAST LGAGSPIDWN YTTIPQDGLD GRSLDYPRAK
ILGGCSTHNG MVYTRGSKDD WNSWAGIIGD QGLGWDSILP AIKKAEKFTQ DFTDQSVKGH
IDPSVHGFDG KLSVSAAYSN ISFNDLLFET TKELNAEFPF KLDMNDGKPI GLGWTQYTID
NHAERSSSAT SYLESTGDNV HVLVNTLVTR VLSASGNGTD FRKVEFAVDA NSPKKQLEAK
KEVIVAGGVI ASPQILMNSG IGERKVLQAV GIDTLIDNPS VGKNLSDQGA TSVMFDTTLP
STDFDVDAAL TEWTNSHTGP LARGARLNHL TFVRLPDDKL NGQDPSSGKN SPHIEFQFAQ
ITPQVPTLGV PKQAPLPAAN SYRLLLQLAV VNLYSISRGS ISLSDNNPFT YPLIDLNMFK
EDIDIAILRE GIRSAGRMFS SKAFKNSVNK FVYPPADATS DEDLDAFLRS STFSYVHGVG
TLSMSPKGAS WGVVNPDFKV KGTSGLRVVD ASVIPHAPAA HTQLPVYAFA EYASALIAKS
YN
