GLCDH_SACSO
ID GLCDH_SACSO Reviewed; 366 AA.
AC O93715;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Glucose 1-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02127};
DE Short=GDH {ECO:0000255|HAMAP-Rule:MF_02127};
DE Short=GlcDH {ECO:0000255|HAMAP-Rule:MF_02127};
DE EC=1.1.1.47 {ECO:0000255|HAMAP-Rule:MF_02127, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:3827812};
DE AltName: Full=Aldose 1-dehydrogenase [NAD(P)(+)] {ECO:0000305|PubMed:12824170};
DE EC=1.1.1.359 {ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:3827812};
DE AltName: Full=Galactose 1-dehydrogenase {ECO:0000305|PubMed:12824170};
DE EC=1.1.1.120 {ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:3827812};
DE EC=1.1.1.48 {ECO:0000269|PubMed:12824170};
GN Name=gdh {ECO:0000312|EMBL:CAA09918.1};
OS Saccharolobus solfataricus (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=2287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, AND SUBUNIT.
RC STRAIN=ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1;
RX PubMed=12824170; DOI=10.1074/jbc.m305818200;
RA Lamble H.J., Heyer N.I., Bull S.D., Hough D.W., Danson M.J.;
RT "Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus
RT revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate
RT aldolase.";
RL J. Biol. Chem. 278:34066-34072(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=3827812; DOI=10.1042/bj2390517;
RA Giardina P., de Biasi M.G., de Rosa M., Gambacorta A., Buonocore V.;
RT "Glucose dehydrogenase from the thermoacidophilic archaebacterium
RT Sulfolobus solfataricus.";
RL Biochem. J. 239:517-522(1986).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF WILD-TYPE IN COMPLEXES WITH NADP
RP AND ZINC AND MUTANT ALA-41 IN COMPLEXES WITH BETA-D-GLUCOSE OR D-XYLOSE;
RP NADP AND ZINC, SUBUNIT, KINETIC PARAMETERS, COFACTOR, CATALYTIC MECHANISM,
RP AND MUTAGENESIS OF THR-41.
RC STRAIN=ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1;
RX PubMed=16556607; DOI=10.1074/jbc.m601334200;
RA Milburn C.C., Lamble H.J., Theodossis A., Bull S.D., Hough D.W.,
RA Danson M.J., Taylor G.L.;
RT "The structural basis of substrate promiscuity in glucose dehydrogenase
RT from the hyperthermophilic archaeon Sulfolobus solfataricus.";
RL J. Biol. Chem. 281:14796-14804(2006).
CC -!- FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to
CC D-gluconate via gluconolactone. Displays broad substrate specificity
CC since it is able to catalyze the oxidation of a number of alternative
CC aldose sugars, such as D-galactose, D-xylose and L-arabinose, to the
CC corresponding glyconate. Can utilize both NAD(+) and NADP(+) as
CC electron acceptor. Physiologically, seems to be involved in the
CC degradation of both glucose and galactose through a non-phosphorylative
CC variant of the Entner-Doudoroff pathway. {ECO:0000269|PubMed:12824170,
CC ECO:0000269|PubMed:3827812}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose + NAD(+) = D-glucono-1,5-lactone + H(+) + NADH;
CC Xref=Rhea:RHEA:14293, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16217, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.47;
CC Evidence={ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:3827812};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose + NAD(+) = D-glucono-1,5-lactone + H(+) + NADH;
CC Xref=Rhea:RHEA:14293, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16217, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.359; Evidence={ECO:0000269|PubMed:12824170,
CC ECO:0000269|PubMed:3827812};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH;
CC Xref=Rhea:RHEA:14405, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16217, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.47;
CC Evidence={ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:3827812};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH;
CC Xref=Rhea:RHEA:14405, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16217, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.359; Evidence={ECO:0000269|PubMed:12824170,
CC ECO:0000269|PubMed:3827812};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose + NAD(+) = D-galactono-1,4-lactone + H(+) + NADH;
CC Xref=Rhea:RHEA:21296, ChEBI:CHEBI:4139, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15895, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.48;
CC Evidence={ECO:0000269|PubMed:12824170};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose + NADP(+) = D-galactono-1,5-lactone + H(+) +
CC NADPH; Xref=Rhea:RHEA:18625, ChEBI:CHEBI:4139, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15945, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.359; Evidence={ECO:0000269|PubMed:12824170,
CC ECO:0000269|PubMed:3827812};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose + NADP(+) = D-galactono-1,5-lactone + H(+) +
CC NADPH; Xref=Rhea:RHEA:18625, ChEBI:CHEBI:4139, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15945, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.120; Evidence={ECO:0000269|PubMed:12824170,
CC ECO:0000269|PubMed:3827812};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldopyranose + NAD(+) = aldono-1,5-lactone + H(+) + NADH;
CC Xref=Rhea:RHEA:15917, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:140379, ChEBI:CHEBI:140380;
CC EC=1.1.1.359; Evidence={ECO:0000269|PubMed:12824170,
CC ECO:0000269|PubMed:3827812};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldopyranose + NADP(+) = aldono-1,5-lactone + H(+) + NADPH;
CC Xref=Rhea:RHEA:36587, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:140379, ChEBI:CHEBI:140380;
CC EC=1.1.1.359; Evidence={ECO:0000269|PubMed:12824170,
CC ECO:0000269|PubMed:3827812};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16556607};
CC Note=Binds 2 Zn(2+) ions per subunit. One of the zinc atoms is
CC essential for catalytic activity while the other has a structural
CC function. {ECO:0000269|PubMed:16556607};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA in vitro.
CC {ECO:0000269|PubMed:3827812}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.0 mM for D-glucose (in the presence of NAD(+), at 70 degrees
CC Celsius and pH 8) {ECO:0000269|PubMed:3827812};
CC KM=1.50 mM for D-glucose (in the presence of NAD(+), at 70 degrees
CC Celsius and pH 7.5) {ECO:0000269|PubMed:12824170};
CC KM=0.44 mM for D-glucose (in the presence of NADP(+), at 70 degrees
CC Celsius and pH 8) {ECO:0000269|PubMed:3827812};
CC KM=1.30 mM for D-glucose (in the presence of NADP(+), at 70 degrees
CC Celsius and pH 7.5) {ECO:0000269|PubMed:12824170};
CC KM=0.57 mM for D-galactose (in the presence of NAD(+), at 70 degrees
CC Celsius and pH 7.5) {ECO:0000269|PubMed:12824170};
CC KM=22 mM for D-galactose (in the presence of NADP(+), at 70 degrees
CC Celsius and pH 8) {ECO:0000269|PubMed:3827812};
CC KM=0.44 mM for D-galactose (in the presence of NADP(+), at 70 degrees
CC Celsius and pH 7.5) {ECO:0000269|PubMed:12824170};
CC KM=0.25 mM for D-xylose (in the presence of NAD(+), at 70 degrees
CC Celsius and pH 7.5) {ECO:0000269|PubMed:16556607};
CC KM=0.18 mM for D-xylose (in the presence of NADP(+), at 70 degrees
CC Celsius and pH 7.5) {ECO:0000269|PubMed:16556607};
CC KM=1.2 mM for NAD(+) (at 70 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:3827812};
CC KM=0.03 mM for NADP(+) (at 70 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:3827812};
CC Vmax=110 umol/min/mg enzyme for the oxidation of D-glucose by NAD(+)
CC (at 70 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12824170};
CC Vmax=70 umol/min/mg enzyme for the oxidation of D-glucose by NADP(+)
CC (at 70 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12824170};
CC Vmax=90 umol/min/mg enzyme for the oxidation of D-galactose by NAD(+)
CC (at 70 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12824170};
CC Vmax=55 umol/min/mg enzyme for the oxidation of D-galactose by
CC NADP(+) (at 70 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:12824170};
CC Vmax=90 umol/min/mg enzyme for the oxidation of D-xylose by NAD(+)
CC (at 70 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:16556607};
CC Vmax=65 umol/min/mg enzyme for the oxidation of D-xylose by NADP(+)
CC (at 70 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:16556607};
CC pH dependence:
CC Optimum pH is 9. {ECO:0000269|PubMed:3827812};
CC Temperature dependence:
CC Optimum temperature is 77 degrees Celsius. At 37 degrees Celsius,
CC shows about 20% activity as compared with the maximal value.
CC {ECO:0000269|PubMed:3827812};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12824170,
CC ECO:0000269|PubMed:16556607, ECO:0000269|PubMed:3827812}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Glucose 1-dehydrogenase subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_02127}.
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DR EMBL; AJ012093; CAA09918.1; -; Genomic_DNA.
DR PIR; T44937; T44937.
DR RefSeq; WP_009992653.1; NZ_LT549890.1.
DR PDB; 2CD9; X-ray; 1.80 A; A/B=1-366.
DR PDB; 2CDA; X-ray; 2.28 A; A/B=1-366.
DR PDB; 2CDB; X-ray; 1.60 A; A/B/C/D=1-366.
DR PDB; 2CDC; X-ray; 1.50 A; A/B/C/D=1-366.
DR PDBsum; 2CD9; -.
DR PDBsum; 2CDA; -.
DR PDBsum; 2CDB; -.
DR PDBsum; 2CDC; -.
DR AlphaFoldDB; O93715; -.
DR SMR; O93715; -.
DR GeneID; 44128727; -.
DR OMA; NWGHEDI; -.
DR OrthoDB; 43162at2157; -.
DR BioCyc; MetaCyc:MON-4842; -.
DR BRENDA; 1.1.1.359; 6163.
DR BRENDA; 1.1.1.47; 6163.
DR SABIO-RK; O93715; -.
DR EvolutionaryTrace; O93715; -.
DR GO; GO:0047640; F:aldose 1-dehydrogenase activity; IEA:RHEA.
DR GO; GO:0047910; F:galactose 1-dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0019151; F:galactose 1-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005534; F:galactose binding; IDA:UniProtKB.
DR GO; GO:0047934; F:glucose 1-dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0047935; F:glucose 1-dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0047936; F:glucose 1-dehydrogenase [NAD(P)] activity; IDA:UniProtKB.
DR GO; GO:0005536; F:glucose binding; IDA:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
DR GO; GO:0070401; F:NADP+ binding; IDA:UniProtKB.
DR GO; GO:0033222; F:xylose binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0033498; P:galactose catabolic process via D-galactonate; IDA:UniProtKB.
DR GO; GO:0019595; P:non-phosphorylated glucose catabolic process; IDA:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
DR HAMAP; MF_02127; Glucose_DH; 1.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR026583; Glc_1-DH_arc.
DR InterPro; IPR031640; Glu_dehyd_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF16912; Glu_dehyd_C; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW Metal-binding; NAD; NADP; Nucleotide-binding; Oxidoreductase; Zinc.
FT CHAIN 1..366
FT /note="Glucose 1-dehydrogenase"
FT /id="PRO_0000414839"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16556607"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16556607"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16556607"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16556607"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:16556607"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:16556607"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:16556607"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:16556607"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16556607"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16556607"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16556607"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16556607"
FT BINDING 189..192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16556607"
FT BINDING 211..213
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16556607"
FT BINDING 277..279
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16556607"
FT BINDING 305..307
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16556607"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16556607"
FT BINDING 354
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16556607"
FT MUTAGEN 41
FT /note="T->A: Large decrease in catalytic activity and
FT substrate affinity."
FT /evidence="ECO:0000269|PubMed:16556607"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:2CDC"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 27..38
FT /evidence="ECO:0007829|PDB:2CDC"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2CDC"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:2CDC"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2CDC"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:2CDC"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:2CDC"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:2CDC"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:2CDC"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:2CDC"
FT HELIX 149..165
FT /evidence="ECO:0007829|PDB:2CDC"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:2CDC"
FT HELIX 190..203
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:2CDC"
FT HELIX 217..226
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:2CDC"
FT HELIX 238..244
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:2CDC"
FT HELIX 259..264
FT /evidence="ECO:0007829|PDB:2CDC"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 268..276
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:2CDC"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:2CDC"
FT HELIX 310..326
FT /evidence="ECO:0007829|PDB:2CDC"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:2CDC"
FT HELIX 344..352
FT /evidence="ECO:0007829|PDB:2CDC"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:2CDC"
SQ SEQUENCE 366 AA; 40891 MW; 59D4AC33B447D3EB CRC64;
MKAIIVKPPN AGVQVKDVDE KKLDSYGKIK IRTIYNGICG TDREIVNGKL TLSTLPKGKD
FLVLGHEAIG VVEESYHGFS QGDLVMPVNR RGCGICRNCL VGRPDFCETG EFGEAGIHKM
DGFMREWWYD DPKYLVKIPK SIEDIGILAQ PLADIEKSIE EILEVQKRVP VWTCDDGTLN
CRKVLVVGTG PIGVLFTLLF RTYGLEVWMA NRREPTEVEQ TVIEETKTNY YNSSNGYDKL
KDSVGKFDVI IDATGADVNI LGNVIPLLGR NGVLGLFGFS TSGSVPLDYK TLQEIVHTNK
TIIGLVNGQK PHFQQAVVHL ASWKTLYPKA AKMLITKTVS INDEKELLKV LREKEHGEIK
IRILWE
