OXLA_RHOOP
ID OXLA_RHOOP Reviewed; 534 AA.
AC Q8VPD4;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=L-amino acid oxidase {ECO:0000303|PubMed:17234209, ECO:0000303|Ref.1};
DE Short=L-AAO {ECO:0000303|Ref.1};
DE Short=LAO;
DE Short=roLAAO {ECO:0000303|PubMed:17234209};
DE EC=1.4.3.2 {ECO:0000269|Ref.1};
DE Flags: Precursor;
OS Rhodococcus opacus (Nocardia opaca).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=37919;
RN [1] {ECO:0000312|EMBL:AAL14831.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND BIOTECHNOLOGY.
RC STRAIN=DSM 43250;
RX DOI=10.1016/S0141-0229(02)00072-8;
RA Geueke B., Hummel W.;
RT "A new bacterial L-amino acid oxidase with a broad substrate specificity:
RT purification and characterization.";
RL Enzyme Microb. Technol. 31:77-87(2002).
RN [2] {ECO:0007744|PDB:2JAE, ECO:0007744|PDB:2JB1, ECO:0007744|PDB:2JB2}
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 46-534 IN COMPLEX WITH FAD AND
RP SUBSTRATE, AND COFACTOR.
RX PubMed=17234209; DOI=10.1016/j.jmb.2006.11.071;
RA Faust A., Niefind K., Hummel W., Schomburg D.;
RT "The structure of a bacterial L-amino acid oxidase from Rhodococcus opacus
RT gives new evidence for the hydride mechanism for dehydrogenation.";
RL J. Mol. Biol. 367:234-248(2007).
CC -!- FUNCTION: Catalyzes an oxidative deamination of basic, hydrophobic and
CC aromatic L-amino acids, thus producing hydrogen peroxide that may
CC contribute to the diverse toxic effects of this enzyme (Ref.1). Is
CC active on most L-amino acid (39 on 43 tested) with the exception of L-
CC Thr, L-Pro, and L-Gly (Ref.1). {ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-asparagine + O2 = 2-oxosuccinamate + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:61224, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57735,
CC ChEBI:CHEBI:58048; Evidence={ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-methionine + O2 = 4-methylsulfanyl-2-oxobutanoate +
CC H2O2 + NH4(+); Xref=Rhea:RHEA:61236, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57844; Evidence={ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-phenylalanine + O2 = 3-phenylpyruvate + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:61240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-tyrosine + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:61248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242,
CC ChEBI:CHEBI:58315; Evidence={ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine + O2 = 2-oxoglutaramate + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:61260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16769, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58359; Evidence={ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-alanine + O2 = H2O2 + NH4(+) + pyruvate;
CC Xref=Rhea:RHEA:61264, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57972; Evidence={ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:60996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57427; Evidence={ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-lysine + O2 = 6-amino-2-oxohexanoate + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:14437, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:58183; Evidence={ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-arginine + O2 = 5-guanidino-2-oxopentanoate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:51404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:58489; Evidence={ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate + O2 = 2-oxoglutarate + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:20728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985; Evidence={ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-cystine + O2 = (2R)-2-amino-2-carboxylatoethyl-
CC disulfanyl-oxopropanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:61284,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:35491, ChEBI:CHEBI:144484;
CC Evidence={ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-serine + O2 = 3-hydroxypyruvate + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:61344, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17180, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:33384; Evidence={ECO:0000269|Ref.1};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:17234209, ECO:0000269|Ref.1};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:17234209,
CC ECO:0000269|Ref.1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.019 mM for L-Tyr {ECO:0000269|Ref.1};
CC KM=0.070 mM for L-Arg {ECO:0000269|Ref.1};
CC KM=0.026 mM for L-norleucine {ECO:0000269|Ref.1};
CC KM=0.034 mM for L-ornithine {ECO:0000269|Ref.1};
CC KM=0.022 mM for L-Phe {ECO:0000269|Ref.1};
CC KM=0.028 mM for L-Leu {ECO:0000269|Ref.1};
CC KM=0.039 mM for L-Met {ECO:0000269|Ref.1};
CC KM=0.026 mM for L-citrulline {ECO:0000269|Ref.1};
CC KM=0.028 mM for L-Asn {ECO:0000269|Ref.1};
CC KM=0.085 mM for L-Gln {ECO:0000269|Ref.1};
CC KM=0.274 mM for L-Ala {ECO:0000269|Ref.1};
CC KM=0.015 mM for L-Lys {ECO:0000269|Ref.1};
CC KM=5.11 mM for L-Ile {ECO:0000269|Ref.1};
CC KM=0.411 mM for L-Glu {ECO:0000269|Ref.1};
CC KM=3.73 mM for L-Val {ECO:0000269|Ref.1};
CC KM=1.36 mM for L-Ser {ECO:0000269|Ref.1};
CC Vmax=9.69 umol/min/mg enzyme toward L-Tyr {ECO:0000269|Ref.1};
CC Vmax=8.12 umol/min/mg enzyme toward L-Arg {ECO:0000269|Ref.1};
CC Vmax=7.55 umol/min/mg enzyme toward L-norleucine {ECO:0000269|Ref.1};
CC Vmax=7.48 umol/min/mg enzyme toward L-ornithine {ECO:0000269|Ref.1};
CC Vmax=6.97 umol/min/mg enzyme toward L-Phe {ECO:0000269|Ref.1};
CC Vmax=6.45 umol/min/mg enzyme toward L-Leu {ECO:0000269|Ref.1};
CC Vmax=6.43 umol/min/mg enzyme toward L-Met {ECO:0000269|Ref.1};
CC Vmax=5.47 umol/min/mg enzyme toward L-citrulline {ECO:0000269|Ref.1};
CC Vmax=5.37 umol/min/mg enzyme toward L-Asn {ECO:0000269|Ref.1};
CC Vmax=5.06 umol/min/mg enzyme toward L-Gln {ECO:0000269|Ref.1};
CC Vmax=4.27 umol/min/mg enzyme toward L-Ala {ECO:0000269|Ref.1};
CC Vmax=3.56 umol/min/mg enzyme toward L-Lys {ECO:0000269|Ref.1};
CC Vmax=2.84 umol/min/mg enzyme toward L-Ile {ECO:0000269|Ref.1};
CC Vmax=2.32 umol/min/mg enzyme toward L-Glu {ECO:0000269|Ref.1};
CC Vmax=1.93 umol/min/mg enzyme toward L-Val {ECO:0000269|Ref.1};
CC Vmax=4.36 umol/min/mg enzyme toward L-Ser {ECO:0000269|Ref.1};
CC pH dependence:
CC Optimum pH is 8-9. {ECO:0000269|Ref.1};
CC -!- SUBUNIT: Homodimer; non-covalently linked. {ECO:0000269|Ref.1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|Ref.1}. Note=Unexpectedly,
CC is not secreted into the medium. {ECO:0000269|Ref.1}.
CC -!- PTM: Predicted to be exported by the Tat system. {ECO:0000255|PROSITE-
CC ProRule:PRU00648}.
CC -!- PTM: Not glycosylated. {ECO:0000269|PubMed:17234209}.
CC -!- BIOTECHNOLOGY: Can be used for the preparation of D-amino acids by
CC resolving racemic amino acid mixtures and for the production of alpha-
CC keto acids. {ECO:0000305|Ref.1}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
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DR EMBL; AY053450; AAL14831.1; -; Genomic_DNA.
DR PDB; 2JAE; X-ray; 1.25 A; A/B=46-534.
DR PDB; 2JB1; X-ray; 1.55 A; A/B=46-534.
DR PDB; 2JB2; X-ray; 1.45 A; A/B=46-534.
DR PDB; 2JB3; X-ray; 1.85 A; A/B=46-534.
DR PDBsum; 2JAE; -.
DR PDBsum; 2JB1; -.
DR PDBsum; 2JB2; -.
DR PDBsum; 2JB3; -.
DR AlphaFoldDB; Q8VPD4; -.
DR SMR; Q8VPD4; -.
DR STRING; 37919.EP51_32830; -.
DR BRENDA; 1.4.3.2; 4353.
DR EvolutionaryTrace; Q8VPD4; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050025; F:L-glutamate oxidase activity; IEA:RHEA.
DR GO; GO:0050029; F:L-lysine oxidase activity; IEA:RHEA.
DR GO; GO:0106329; F:L-phenylalaine oxidase activity; IEA:RHEA.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein;
KW Glycoprotein; Nucleotide-binding; Oxidoreductase; Signal.
FT SIGNAL 1..45
FT /note="Tat-type signal"
FT /evidence="ECO:0000269|Ref.1"
FT CHAIN 46..534
FT /note="L-amino acid oxidase"
FT /evidence="ECO:0000305|Ref.1"
FT /id="PRO_0000448256"
FT BINDING 66..67
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17234209,
FT ECO:0007744|PDB:2JAE, ECO:0007744|PDB:2JB1,
FT ECO:0007744|PDB:2JB2, ECO:0007744|PDB:2JB3"
FT BINDING 86..88
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17234209,
FT ECO:0007744|PDB:2JAE, ECO:0007744|PDB:2JB1,
FT ECO:0007744|PDB:2JB2, ECO:0007744|PDB:2JB3"
FT BINDING 94
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17234209,
FT ECO:0007744|PDB:2JAE, ECO:0007744|PDB:2JB1,
FT ECO:0007744|PDB:2JB2, ECO:0007744|PDB:2JB3"
FT BINDING 125..128
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17234209,
FT ECO:0007744|PDB:2JAE, ECO:0007744|PDB:2JB1,
FT ECO:0007744|PDB:2JB2, ECO:0007744|PDB:2JB3"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17234209,
FT ECO:0007744|PDB:2JB1, ECO:0007744|PDB:2JB2"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17234209,
FT ECO:0007744|PDB:2JB1, ECO:0007744|PDB:2JB2"
FT BINDING 305
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17234209,
FT ECO:0007744|PDB:2JAE, ECO:0007744|PDB:2JB1,
FT ECO:0007744|PDB:2JB2, ECO:0007744|PDB:2JB3"
FT BINDING 415
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17234209,
FT ECO:0007744|PDB:2JB1, ECO:0007744|PDB:2JB2"
FT BINDING 503
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17234209,
FT ECO:0007744|PDB:2JAE, ECO:0007744|PDB:2JB1,
FT ECO:0007744|PDB:2JB2, ECO:0007744|PDB:2JB3"
FT BINDING 510..512
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17234209,
FT ECO:0007744|PDB:2JAE, ECO:0007744|PDB:2JB1,
FT ECO:0007744|PDB:2JB2, ECO:0007744|PDB:2JB3"
FT BINDING 510
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17234209,
FT ECO:0007744|PDB:2JB1, ECO:0007744|PDB:2JB2"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:2JAE"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:2JAE"
FT HELIX 135..142
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:2JAE"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:2JAE"
FT HELIX 173..194
FT /evidence="ECO:0007829|PDB:2JAE"
FT TURN 195..200
FT /evidence="ECO:0007829|PDB:2JAE"
FT HELIX 203..216
FT /evidence="ECO:0007829|PDB:2JAE"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:2JAE"
FT HELIX 252..258
FT /evidence="ECO:0007829|PDB:2JAE"
FT TURN 259..263
FT /evidence="ECO:0007829|PDB:2JAE"
FT HELIX 264..268
FT /evidence="ECO:0007829|PDB:2JAE"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:2JAE"
FT HELIX 285..294
FT /evidence="ECO:0007829|PDB:2JAE"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:2JB2"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 324..335
FT /evidence="ECO:0007829|PDB:2JAE"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:2JAE"
FT HELIX 351..358
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 365..374
FT /evidence="ECO:0007829|PDB:2JAE"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 409..417
FT /evidence="ECO:0007829|PDB:2JAE"
FT HELIX 419..425
FT /evidence="ECO:0007829|PDB:2JAE"
FT HELIX 429..444
FT /evidence="ECO:0007829|PDB:2JAE"
FT HELIX 446..449
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 450..459
FT /evidence="ECO:0007829|PDB:2JAE"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:2JAE"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 467..470
FT /evidence="ECO:0007829|PDB:2JB2"
FT HELIX 486..491
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:2JAE"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:2JAE"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:2JAE"
FT HELIX 512..531
FT /evidence="ECO:0007829|PDB:2JAE"
SQ SEQUENCE 534 AA; 57805 MW; D8D367949BB2D444 CRC64;
MAFTRRSFMK GLGATGGAGL AYGAMSTLGL APSTAAPART FQPLAAGDLI GKVKGSHSVV
VLGGGPAGLC SAFELQKAGY KVTVLEARTR PGGRVWTARG GSEETDLSGE TQKCTFSEGH
FYNVGATRIP QSHITLDYCR ELGVEIQGFG NQNANTFVNY QSDTSLSGQS VTYRAAKADT
FGYMSELLKK ATDQGALDQV LSREDKDALS EFLSDFGDLS DDGRYLGSSR RGYDSEPGAG
LNFGTEKKPF AMQEVIRSGI GRNFSFDFGY DQAMMMFTPV GGMDRIYYAF QDRIGTDNIV
FGAEVTSMKN VSEGVTVEYT AGGSKKSITA DYAICTIPPH LVGRLQNNLP GDVLTALKAA
KPSSSGKLGI EYSRRWWETE DRIYGGASNT DKDISQIMFP YDHYNSDRGV VVAYYSSGKR
QEAFESLTHR QRLAKAIAEG SEIHGEKYTR DISSSFSGSW RRTKYSESAW ANWAGSGGSH
GGAATPEYEK LLEPVDKIYF AGDHLSNAIA WQHGALTSAR DVVTHIHERV AQEA
