HKT_AEDAE
ID HKT_AEDAE Reviewed; 400 AA.
AC Q0IG34; Q95V15;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=3-hydroxykynurenine transaminase {ECO:0000303|PubMed:11880382};
DE EC=2.6.1.63 {ECO:0000269|PubMed:11880382, ECO:0000269|PubMed:12220660};
DE AltName: Full=3-hydroxykynurenine transaminase and alanine--glyoxylate aminotransferase {ECO:0000303|PubMed:12220660};
DE Short=Ae-HKT/AGT {ECO:0000303|PubMed:12220660};
DE AltName: Full=Alanine--glyoxylate aminotransferase {ECO:0000255|PIRNR:PIRNR000524};
DE EC=2.6.1.44 {ECO:0000255|PIRNR:PIRNR000524, ECO:0000269|PubMed:11880382, ECO:0000269|PubMed:12220660};
GN Name=HKT {ECO:0000303|PubMed:11880382};
GN ORFNames=AAEL003508 {ECO:0000312|EMBL:EAT45177.1};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000312|EMBL:EAT45177.1};
RN [1] {ECO:0000312|EMBL:EAT45177.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000312|EMBL:EAT45177.1};
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [2] {ECO:0000312|EMBL:AAL29468.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-389, PROTEIN SEQUENCE OF 1-19; 108-114;
RP 121-130 AND 302-308, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Black-eyed Liverpool {ECO:0000312|EMBL:AAL29468.1};
RX PubMed=11880382; DOI=10.1074/jbc.m201202200;
RA Han Q., Fang J., Li J.;
RT "3-Hydroxykynurenine transaminase identity with alanine glyoxylate
RT transaminase. A probable detoxification protein in Aedes aegypti.";
RL J. Biol. Chem. 277:15781-15787(2002).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP SUBUNIT.
RX PubMed=12220660; DOI=10.1016/s0014-5793(02)03229-5;
RA Han Q., Li J.;
RT "Comparative characterization of Aedes 3-hydroxykynurenine
RT transaminase/alanine glyoxylate transaminase and Drosophila serine pyruvate
RT aminotransferase.";
RL FEBS Lett. 527:199-204(2002).
RN [4] {ECO:0007744|PDB:6MFB}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-386 IN COMPLEX WITH PYRIDOXAL
RP PHOSPHATE.
RA Maciel L.G., Oliveira A.A., Romao T.P., Silva Filha M.H.N.L.,
RA dos Anjos J.V., Soares T.A., Guido R.V.C.;
RT "Crystal structure of 3-hydroxykynurenine transaminase from Aedes
RT aegypti.";
RL Submitted (SEP-2018) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the pyridoxal 5'-phosphate-dependent transamination
CC of both 3-hydroxykynurenine and L-kynurenine to xanthurenic acid and
CC kynurenic acid, respectively, preferentially using the alpha-ketoacid
CC pyruvate, glyoxylate or oxaloacetate as the amino group acceptor
CC (PubMed:11880382, PubMed:12220660). The affinity and catalytic
CC efficiency for 3-hydroxykynurenine is higher than for L-kynurenine
CC (PubMed:12220660). Involved in the detoxification of cytotoxic
CC metabolite 3-hydroxykynurenine generated by the hydroxylation of L-
CC kynurenine, an intermediate in the tryptophan catabolism pathway
CC (PubMed:11880382, PubMed:12220660). Also catalyzes, although with a
CC lesser efficiency, the transamination of alanine with glyoxylate as an
CC amino group acceptor (PubMed:11880382). May play a role in the
CC detoxification of glyoxylate, a toxic plant metabolite from the diet
CC (Probable). {ECO:0000269|PubMed:11880382, ECO:0000269|PubMed:12220660,
CC ECO:0000305|PubMed:11880382, ECO:0000305|PubMed:12220660}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + L-alanine = glycine + pyruvate;
CC Xref=Rhea:RHEA:24248, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57972; EC=2.6.1.44;
CC Evidence={ECO:0000255|PIRNR:PIRNR000524, ECO:0000269|PubMed:11880382,
CC ECO:0000269|PubMed:12220660};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + L-kynurenine = glycine + H2O + kynurenate;
CC Xref=Rhea:RHEA:65896, ChEBI:CHEBI:15377, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; EC=2.6.1.63;
CC Evidence={ECO:0000269|PubMed:11880382, ECO:0000269|PubMed:12220660};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-L-kynurenine + glyoxylate = glycine + H2O +
CC xanthurenate; Xref=Rhea:RHEA:65900, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:58125,
CC ChEBI:CHEBI:71201; EC=2.6.1.63;
CC Evidence={ECO:0000269|PubMed:11880382, ECO:0000269|PubMed:12220660};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-L-kynurenine + pyruvate = H2O + L-alanine +
CC xanthurenate; Xref=Rhea:RHEA:65908, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57972, ChEBI:CHEBI:58125,
CC ChEBI:CHEBI:71201; Evidence={ECO:0000269|PubMed:11880382,
CC ECO:0000269|PubMed:12220660};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-kynurenine + pyruvate = H2O + kynurenate + L-alanine;
CC Xref=Rhea:RHEA:65916, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57959, ChEBI:CHEBI:57972, ChEBI:CHEBI:58454;
CC Evidence={ECO:0000269|PubMed:11880382, ECO:0000269|PubMed:12220660};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|PIRSR:PIRSR000524-50, ECO:0000269|Ref.4};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.7 mM for 3-hydroxykynurenine (at 50 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:11880382};
CC KM=11.2 mM for L-alanine (at 50 degrees Celsius, pH 7.0 and with
CC glyoxylate as cosubstrate) {ECO:0000269|PubMed:11880382};
CC KM=18 mM for alanine (at 50 degrees Celsius, pH 7.0 and with
CC glyoxylate as cosubstrate) {ECO:0000269|PubMed:12220660};
CC KM=22.8 mM for L,D-alanine (at 50 degrees Celsius, pH 7.0 and with
CC glyoxylate as cosubstrate) {ECO:0000269|PubMed:11880382};
CC KM=1.6 mM for glyoxylate (at 50 degrees Celsius, pH 7.0 and with
CC alanine as cosubstrate) {ECO:0000269|PubMed:12220660};
CC KM=6.2 mM for L-kynurenine (at 50 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:11880382};
CC KM=10 mM for L,D-kynurenine (at 50 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:11880382};
CC Vmax=60.6 umol/min/mg enzyme toward 3-hydroxykynurenine (at 50
CC degrees Celsius and pH 7.0) {ECO:0000269|PubMed:11880382};
CC Vmax=41 umol/min/mg enzyme toward L-alanine (at 50 degrees Celsius,
CC pH 7.0 and with glyoxylate as cosubstrate)
CC {ECO:0000269|PubMed:11880382};
CC Vmax=30 umol/min/mg enzyme toward alanine (at 50 degrees Celsius, pH
CC 7.0 and with glyoxylate as cosubstrate)
CC {ECO:0000269|PubMed:12220660};
CC Vmax=41.6 umol/min/mg enzyme toward L,D-alanine (at 50 degrees
CC Celsius, pH 7.0 and with glyoxylate as cosubstrate)
CC {ECO:0000269|PubMed:11880382};
CC Vmax=24 umol/min/mg enzyme toward glyoxylate (at 50 degrees Celsius,
CC pH 7.0 and with alanine as cosubstrate)
CC {ECO:0000269|PubMed:12220660};
CC Vmax=24 umol/min/mg enzyme toward L-kynurenine (at 50 degrees Celsius
CC and pH 7.0) {ECO:0000269|PubMed:11880382};
CC Vmax=18 umol/min/mg enzyme toward L-kynurenine (at 50 degrees Celsius
CC and pH 7.0) {ECO:0000269|PubMed:11880382};
CC Note=kcat is 2424 min(-1) for 3-hydroxykynurenine (at 50 degrees
CC Celsius and pH 7 (PubMed:11880382). kcat is 1640 min(-1) for L-
CC alanine (at 50 degrees Celsius, pH 7.0 and with glyoxylate as
CC cosubstrate) (PubMed:11880382). kcat is 1200 min(-1) for alanine (at
CC 50 degrees Celsius, pH 7.0 and with glyoxylate as cosubstrate)
CC (PubMed:12220660). kcat is 1664 min(-1) for L,D-alanine (at 50
CC degrees Celsius, pH 7.0 and with glyoxylate as cosubstrate)
CC (PubMed:11880382). kcat is 960 min(-1) for glyoxylate (at 50 degrees
CC Celsius, pH 7.0 and with alanine as cosubstrate) (PubMed:12220660).
CC kcat is 960 min(-1) for L-kynurenine (at 50 degrees Celsius and pH
CC 7.0) (PubMed:11880382). kcat is 720 min(-1) for L,D-kynurenine (at 50
CC degrees Celsius and pH 7.0) (PubMed:11880382).
CC {ECO:0000269|PubMed:11880382, ECO:0000269|PubMed:12220660};
CC pH dependence:
CC Optimum pH is 9 with 3-hydroxykynurenine and pyruvate, or L-alanine
CC and glyoxylate as substrates at 50 degrees Celsius.
CC {ECO:0000269|PubMed:11880382, ECO:0000269|PubMed:12220660};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius with 3-hydroxykynurenine
CC and pyruvate at pH 7 (PubMed:11880382, PubMed:12220660). Optimum
CC temperature is 60 degrees Celsius with L-alanine and glyoxylate at pH
CC 7 (PubMed:11880382, PubMed:12220660). {ECO:0000269|PubMed:11880382,
CC ECO:0000269|PubMed:12220660};
CC -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; kynurenate
CC from L-kynurenine: step 1/2. {ECO:0000269|PubMed:11880382,
CC ECO:0000269|PubMed:12220660}.
CC -!- SUBUNIT: Homodimer (By similarity). May form homotetramer
CC (PubMed:12220660). {ECO:0000250|UniProtKB:Q7PRG3,
CC ECO:0000269|PubMed:12220660}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:P21549}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing ovaries and larvae
CC (PubMed:11880382). Expression increases from 1- to 4-day-old larvae,
CC decreases in 5- and 6-day-old larvae and newly formed pupae, and
CC becomes undetectable in 12 h pupae (PubMed:11880382).
CC {ECO:0000269|PubMed:11880382}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000255|PIRNR:PIRNR000524}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL29468.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CH477274; EAT45177.1; -; Genomic_DNA.
DR EMBL; CH477274; EAT45178.1; -; Genomic_DNA.
DR EMBL; AF435806; AAL29468.1; ALT_FRAME; mRNA.
DR RefSeq; XP_001656923.1; XM_001656873.1.
DR RefSeq; XP_001656924.1; XM_001656874.1.
DR PDB; 6MFB; X-ray; 2.50 A; A/B/C/D=1-386.
DR PDBsum; 6MFB; -.
DR AlphaFoldDB; Q0IG34; -.
DR SMR; Q0IG34; -.
DR STRING; 7159.AAEL003508-PB; -.
DR ChEMBL; CHEMBL4739684; -.
DR GeneID; 5578354; -.
DR KEGG; aag:5578354; -.
DR VEuPathDB; VectorBase:AAEL003508; -.
DR eggNOG; KOG2862; Eukaryota.
DR HOGENOM; CLU_027686_0_0_1; -.
DR InParanoid; Q0IG34; -.
DR OMA; AHMGHVN; -.
DR OrthoDB; 984738at2759; -.
DR PhylomeDB; Q0IG34; -.
DR UniPathway; UPA00334; UER00726.
DR Proteomes; UP000008820; Unplaced.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IDA:UniProtKB.
DR GO; GO:0036137; F:kynurenine aminotransferase activity; IDA:UniProtKB.
DR GO; GO:0047315; F:kynurenine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0009436; P:glyoxylate catabolic process; IDA:UniProtKB.
DR GO; GO:0097053; P:L-kynurenine catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Direct protein sequencing; Peroxisome;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..400
FT /note="3-hydroxykynurenine transaminase"
FT /id="PRO_0000452185"
FT REGION 43..44
FT /note="Binds to and confers specificity for 3-
FT hydroxykynurenine; shared with dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:Q7PRG3"
FT BINDING 77..79
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:6MFB"
FT BINDING 154
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:6MFB"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7PRG3"
FT BINDING 204
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:6MFB"
FT BINDING 256
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:6MFB"
FT BINDING 259
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:6MFB"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7PRG3"
FT MOD_RES 205
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|PIRSR:PIRSR000524-50,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:6MFB"
FT CONFLICT 123
FT /note="G -> E (in Ref. 2; AAL29468)"
FT /evidence="ECO:0000305"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:6MFB"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:6MFB"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:6MFB"
FT HELIX 47..64
FT /evidence="ECO:0007829|PDB:6MFB"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:6MFB"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:6MFB"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:6MFB"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:6MFB"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:6MFB"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:6MFB"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:6MFB"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:6MFB"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:6MFB"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:6MFB"
FT TURN 181..186
FT /evidence="ECO:0007829|PDB:6MFB"
FT TURN 191..195
FT /evidence="ECO:0007829|PDB:6MFB"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:6MFB"
FT TURN 203..207
FT /evidence="ECO:0007829|PDB:6MFB"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:6MFB"
FT HELIX 220..228
FT /evidence="ECO:0007829|PDB:6MFB"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:6MFB"
FT HELIX 240..246
FT /evidence="ECO:0007829|PDB:6MFB"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:6MFB"
FT HELIX 262..278
FT /evidence="ECO:0007829|PDB:6MFB"
FT HELIX 280..300
FT /evidence="ECO:0007829|PDB:6MFB"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:6MFB"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:6MFB"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:6MFB"
FT HELIX 328..339
FT /evidence="ECO:0007829|PDB:6MFB"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:6MFB"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:6MFB"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:6MFB"
FT HELIX 366..383
FT /evidence="ECO:0007829|PDB:6MFB"
SQ SEQUENCE 400 AA; 44691 MW; 770F59D680DB7D8A CRC64;
MKFTPPPSSL RGPLVIPDKI MMGPGPSNCS KRVLAALNNT CLSNFHDELF QVIDEVKDGL
RYIFQTENRT TMCITGSAHT GMEALLCNLL EEGDIVLIAN NGIWAERAIN MATRYGADVR
VLGGPADKPF SMTDFKKAIE QHRPKCLFVV HGDSSSGLLQ PLEGLGKICH DYDCLLLVDA
VASLCGVPFY MDKWEIDGVY TGSQKVLGAP PGITPISISP KALEVIRSRK TPSKVFYWDL
LILGNYWGCY DEQKRYHHTV PSNLIFALRE AIAQIAEEGL EPVIRRRQEC AEQMYRGLQA
MGLEIFVKDP EYRLPTVTCI MIPKGVNWWK VSEYAMNNFS LEIQGGFGPT MGIAWRAGIM
GESSTLQRVN FYLYAFKESL KATHPDYVFE KKNGQTNGTK
