GLYOX_BACSU
ID GLYOX_BACSU Reviewed; 369 AA.
AC O31616;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Glycine oxidase {ECO:0000303|PubMed:11744710, ECO:0000303|PubMed:9827558};
DE Short=GO {ECO:0000303|PubMed:11744710};
DE EC=1.4.3.19 {ECO:0000269|PubMed:11744710, ECO:0000269|PubMed:19864430, ECO:0000269|PubMed:9827558};
GN Name=thiO {ECO:0000303|PubMed:12627963};
GN Synonyms=goxB {ECO:0000303|PubMed:9827558},
GN yjbR {ECO:0000303|PubMed:9827558}; OrderedLocusNames=BSU11670;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=MT-2;
RX PubMed=9827558; DOI=10.1016/s0014-5793(98)01313-1;
RA Nishiya Y., Imanaka T.;
RT "Purification and characterization of a novel glycine oxidase from Bacillus
RT subtilis.";
RL FEBS Lett. 438:263-266(1998).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, AND ACTIVITY
RP REGULATION.
RX PubMed=11744710; DOI=10.1074/jbc.m111095200;
RA Job V., Marcone G.L., Pilone M.S., Pollegioni L.;
RT "Glycine oxidase from Bacillus subtilis. Characterization of a new
RT flavoprotein.";
RL J. Biol. Chem. 277:6985-6993(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH FAD AND
RP N-ACETYLGLYCINE, FUNCTION IN THIAMINE BIOSYNTHESIS, PATHWAY, DISRUPTION
RP PHENOTYPE, AND SUBUNIT.
RX PubMed=12627963; DOI=10.1021/bi026916v;
RA Settembre E.C., Dorrestein P.C., Park J.-H., Augustine A.M., Begley T.P.,
RA Ealick S.E.;
RT "Structural and mechanistic studies on ThiO, a glycine oxidase essential
RT for thiamin biosynthesis in Bacillus subtilis.";
RL Biochemistry 42:2971-2981(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH GLYCOLATE AND FAD,
RP AND SUBUNIT.
RX PubMed=15105420; DOI=10.1074/jbc.m401224200;
RA Moertl M., Diederichs K., Welte W., Molla G., Motteran L., Andriolo G.,
RA Pilone M.S., Pollegioni L.;
RT "Structure-function correlation in glycine oxidase from Bacillus
RT subtilis.";
RL J. Biol. Chem. 279:29718-29727(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF MUTANT SER-51/ARG-54/ALA-244 IN
RP COMPLEX WITH GLYCOLATE AND FAD, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, KINETIC PARAMETERS, SUBUNIT, BIOTECHNOLOGY, AND MUTAGENESIS OF
RP GLY-51; ALA-54 AND HIS-244.
RX PubMed=19864430; DOI=10.1074/jbc.m109.051631;
RA Pedotti M., Rosini E., Molla G., Moschetti T., Savino C., Vallone B.,
RA Pollegioni L.;
RT "Glyphosate resistance by engineering the flavoenzyme glycine oxidase.";
RL J. Biol. Chem. 284:36415-36423(2009).
CC -!- FUNCTION: Catalyzes the FAD-dependent oxidative deamination of various
CC amines and D-amino acids to yield the corresponding alpha-keto acids,
CC ammonia/amine, and hydrogen peroxide. Oxidizes sarcosine (N-
CC methylglycine), N-ethylglycine and glycine (PubMed:9827558,
CC PubMed:11744710, PubMed:19864430). Can also oxidize the herbicide
CC glyphosate (N-phosphonomethylglycine) (PubMed:19864430). Displays lower
CC activities on D-alanine, D-valine, D-proline and D-methionine
CC (PubMed:9827558, PubMed:11744710). Does not act on L-amino acids and
CC other D-amino acids (PubMed:9827558). Is essential for thiamine
CC biosynthesis since the oxidation of glycine catalyzed by ThiO generates
CC the glycine imine intermediate (dehydroglycine) required for the
CC biosynthesis of the thiazole ring of thiamine pyrophosphate
CC (PubMed:12627963). {ECO:0000269|PubMed:11744710,
CC ECO:0000269|PubMed:12627963, ECO:0000269|PubMed:19864430,
CC ECO:0000269|PubMed:9827558}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + H2O + O2 = glyoxylate + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:11532, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305; EC=1.4.3.19;
CC Evidence={ECO:0000269|PubMed:11744710, ECO:0000269|PubMed:19864430,
CC ECO:0000269|PubMed:9827558};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-ethylglycine + O2 = ethylamine + glyoxylate + H2O2;
CC Xref=Rhea:RHEA:12472, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:36655, ChEBI:CHEBI:57440,
CC ChEBI:CHEBI:566789; EC=1.4.3.19;
CC Evidence={ECO:0000269|PubMed:11744710, ECO:0000269|PubMed:19864430,
CC ECO:0000269|PubMed:9827558};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + sarcosine = glyoxylate + H2O2 + methylamine;
CC Xref=Rhea:RHEA:15165, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:36655, ChEBI:CHEBI:57433,
CC ChEBI:CHEBI:59338; EC=1.4.3.19;
CC Evidence={ECO:0000269|PubMed:11744710, ECO:0000269|PubMed:19864430,
CC ECO:0000269|PubMed:9827558};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-alanine + H2O + O2 = H2O2 + NH4(+) + pyruvate;
CC Xref=Rhea:RHEA:22688, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57416; EC=1.4.3.19;
CC Evidence={ECO:0000269|PubMed:11744710, ECO:0000269|PubMed:19864430,
CC ECO:0000269|PubMed:9827558};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyphosate + H2O + O2 = aminomethylphosphonate + glyoxylate +
CC H(+) + H2O2; Xref=Rhea:RHEA:52740, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:36655, ChEBI:CHEBI:133673, ChEBI:CHEBI:133674;
CC Evidence={ECO:0000269|PubMed:19864430};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:11744710};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:11744710};
CC -!- ACTIVITY REGULATION: Is competitively inhibited by glycolate.
CC {ECO:0000269|PubMed:11744710}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.22 mM for sarcosine (at pH 8.0) {ECO:0000269|PubMed:9827558};
CC KM=0.66 mM for N-ethylglycine (at pH 8.0)
CC {ECO:0000269|PubMed:9827558};
CC KM=0.99 mM for glycine (at pH 8.0) {ECO:0000269|PubMed:9827558};
CC KM=46 mM for D-proline (at pH 8.0) {ECO:0000269|PubMed:9827558};
CC KM=81 mM for D-alanine (at pH 8.0) {ECO:0000269|PubMed:9827558};
CC KM=0.7 mM for glycine (at pH 8.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:19864430};
CC KM=87 mM for glyphosate (at pH 8.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:19864430};
CC Note=kcat is 1.3 sec(-1) with glycine as substrate. kcat is 1.6 sec(-
CC 1) with sarcosine as substrate. kcat is 1.4 sec(-1) with N-
CC ethylglycine as substrate. kcat is 1.3 sec(-1) with D-proline as
CC substrate. kcat is 1.1 sec(-1) with D-alanine as substrate (at pH
CC 8.0) (PubMed:9827558). kcat is 0.60 sec(-1) with glycine as
CC substrate. kcat is 0.91 sec(-1) with glyphosate as substrate (at pH
CC 8.5 and 37 degrees Celsius) (PubMed:19864430).
CC {ECO:0000269|PubMed:19864430, ECO:0000269|PubMed:9827558};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:9827558};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:9827558};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000269|PubMed:12627963}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12627963,
CC ECO:0000269|PubMed:15105420, ECO:0000269|PubMed:19864430,
CC ECO:0000269|PubMed:9827558}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have an absolute
CC requirement for the thiazole alcohol for growth.
CC {ECO:0000269|PubMed:12627963}.
CC -!- BIOTECHNOLOGY: Introducing the gene coding for the glycine oxidase
CC mutant Ser-51/Arg-54/Ala-244 in plants may be an effective alternative
CC mechanism for glyphosate tolerance in transgenic crops. In addition,
CC transgenic plants that are able to oxidize glyphosate may represent an
CC innovative bioremediation system for the soil treated with this
CC herbicide. {ECO:0000305|PubMed:19864430}.
CC -!- SIMILARITY: Belongs to the DAO family. ThiO subfamily. {ECO:0000305}.
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DR EMBL; AL009126; CAB13024.1; -; Genomic_DNA.
DR PIR; B69845; B69845.
DR RefSeq; NP_389049.1; NC_000964.3.
DR RefSeq; WP_003245044.1; NZ_JNCM01000035.1.
DR PDB; 1NG3; X-ray; 2.60 A; A/B=1-369.
DR PDB; 1NG4; X-ray; 2.30 A; A/B=1-369.
DR PDB; 1RYI; X-ray; 1.80 A; A/B/C/D=1-367.
DR PDB; 3IF9; X-ray; 2.60 A; A/B/C/D=1-369.
DR PDBsum; 1NG3; -.
DR PDBsum; 1NG4; -.
DR PDBsum; 1RYI; -.
DR PDBsum; 3IF9; -.
DR AlphaFoldDB; O31616; -.
DR SMR; O31616; -.
DR STRING; 224308.BSU11670; -.
DR DrugBank; DB02713; Acetylamino-Acetic Acid.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR PaxDb; O31616; -.
DR PRIDE; O31616; -.
DR EnsemblBacteria; CAB13024; CAB13024; BSU_11670.
DR GeneID; 939377; -.
DR KEGG; bsu:BSU11670; -.
DR PATRIC; fig|224308.179.peg.1256; -.
DR eggNOG; COG0665; Bacteria.
DR InParanoid; O31616; -.
DR OMA; GCGTLWL; -.
DR PhylomeDB; O31616; -.
DR BioCyc; BSUB:BSU11670-MON; -.
DR BioCyc; MetaCyc:BSU11670-MON; -.
DR BRENDA; 1.4.3.19; 658.
DR SABIO-RK; O31616; -.
DR UniPathway; UPA00060; -.
DR EvolutionaryTrace; O31616; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0043799; F:glycine oxidase activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IDA:UniProtKB.
DR GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012727; Gly_oxidase_ThiO.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR02352; thiamin_ThiO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; FAD; Flavoprotein; Herbicide resistance;
KW Oxidoreductase; Reference proteome; Thiamine biosynthesis.
FT CHAIN 1..369
FT /note="Glycine oxidase"
FT /id="PRO_0000162773"
FT BINDING 14..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12627963,
FT ECO:0000269|PubMed:15105420, ECO:0000269|PubMed:19864430"
FT BINDING 34..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12627963,
FT ECO:0000269|PubMed:15105420, ECO:0000269|PubMed:19864430"
FT BINDING 42..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12627963,
FT ECO:0000269|PubMed:15105420, ECO:0000269|PubMed:19864430"
FT BINDING 47..49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12627963,
FT ECO:0000269|PubMed:15105420, ECO:0000269|PubMed:19864430"
FT BINDING 174
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12627963,
FT ECO:0000269|PubMed:15105420, ECO:0000269|PubMed:19864430"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12627963"
FT BINDING 327..333
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12627963,
FT ECO:0000269|PubMed:15105420, ECO:0000269|PubMed:19864430"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12627963"
FT MUTAGEN 51
FT /note="G->R: 130-fold decrease in catalytic efficiency on
FT glycine and 28-fold increase in that on glyphosate."
FT /evidence="ECO:0000269|PubMed:19864430"
FT MUTAGEN 51
FT /note="G->S: 60-fold decrease in catalytic efficiency on
FT glycine and 210-fold increase in that on glyphosate; when
FT associated with R-54 and A-244."
FT /evidence="ECO:0000269|PubMed:19864430"
FT MUTAGEN 54
FT /note="A->R: 20-fold decrease in catalytic efficiency on
FT glycine and 34-fold increase in that on glyphosate. 60-fold
FT decrease in catalytic efficiency on glycine and 210-fold
FT increase in that on glyphosate; when associated with S-51
FT and A-244."
FT /evidence="ECO:0000269|PubMed:19864430"
FT MUTAGEN 244
FT /note="H->A: 2-fold decrease in catalytic efficiency on
FT glycine and similar catalytic efficiency on glyphosate. 60-
FT fold decrease in catalytic efficiency on glycine and 210-
FT fold increase in that on glyphosate; when associated with
FT S-51 and R-54."
FT /evidence="ECO:0000269|PubMed:19864430"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:1RYI"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:1RYI"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1RYI"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1RYI"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:1RYI"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:1RYI"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:1RYI"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:1RYI"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:1RYI"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:1RYI"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:1RYI"
FT HELIX 102..109
FT /evidence="ECO:0007829|PDB:1RYI"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:1RYI"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1RYI"
FT HELIX 122..128
FT /evidence="ECO:0007829|PDB:1RYI"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:1RYI"
FT HELIX 150..163
FT /evidence="ECO:0007829|PDB:1RYI"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1RYI"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:1RYI"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:1RYI"
FT STRAND 191..200
FT /evidence="ECO:0007829|PDB:1RYI"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:1RYI"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:1RYI"
FT STRAND 220..230
FT /evidence="ECO:0007829|PDB:1RYI"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:3IF9"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:1RYI"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:1RYI"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:1RYI"
FT HELIX 272..285
FT /evidence="ECO:0007829|PDB:1RYI"
FT HELIX 287..291
FT /evidence="ECO:0007829|PDB:1RYI"
FT STRAND 292..304
FT /evidence="ECO:0007829|PDB:1RYI"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:1RYI"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:1RYI"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:1RYI"
FT TURN 331..334
FT /evidence="ECO:0007829|PDB:1RYI"
FT HELIX 335..346
FT /evidence="ECO:0007829|PDB:1RYI"
FT HELIX 353..358
FT /evidence="ECO:0007829|PDB:1RYI"
SQ SEQUENCE 369 AA; 40937 MW; 7A9466117AC0A76A CRC64;
MKRHYEAVVI GGGIIGSAIA YYLAKENKNT ALFESGTMGG RTTSAAAGML GAHAECEERD
AFFDFAMHSQ RLYKGLGEEL YALSGVDIRQ HNGGMFKLAF SEEDVLQLRQ MDDLDSVSWY
SKEEVLEKEP YASGDIFGAS FIQDDVHVEP YFVCKAYVKA AKMLGAEIFE HTPVLHVERD
GEALFIKTPS GDVWANHVVV ASGVWSGMFF KQLGLNNAFL PVKGECLSVW NDDIPLTKTL
YHDHCYIVPR KSGRLVVGAT MKPGDWSETP DLGGLESVMK KAKTMLPAIQ NMKVDRFWAG
LRPGTKDGKP YIGRHPEDSR ILFAAGHFRN GILLAPATGA LISDLIMNKE VNQDWLHAFR
IDRKEAVQI
