AMYA1_ASPOR
ID AMYA1_ASPOR Reviewed; 499 AA.
AC P0C1B3; P10529; P11763; Q00250; Q2U6K7;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Alpha-amylase A type-1/2;
DE EC=3.2.1.1 {ECO:0000305};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE AltName: Full=Taka-amylase A;
DE Short=TAA;
DE Flags: Precursor;
GN Name=amy1; Synonyms=amyI, Taa-G1; ORFNames=AO090023000944;
GN and
GN Name=amy2; Synonyms=amyII, Taa-G2; ORFNames=AO090120000196;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (AMY1 AND AMY2).
RC STRAIN=DSM 63303;
RX PubMed=2785629; DOI=10.1111/j.1365-2958.1989.tb00097.x;
RA Wirsel S., Lachmund A., Wildhardt G., Ruttkowski E.;
RT "Three alpha-amylase genes of Aspergillus oryzae exhibit identical intron-
RT exon organization.";
RL Mol. Microbiol. 3:3-14(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2789162; DOI=10.1016/0378-1119(89)90096-6;
RA Genes M.J., Dove M.J., Seligy V.L.;
RT "Aspergillus oryzae has two nearly identical Taka-amylase genes, each
RT containing eight introns.";
RL Gene 79:107-117(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Tada S., Iimura Y., Gomi K., Takahashi K., Hara S., Yoshizawa K.;
RT "Cloning and nucleotide sequence of the genomic Taka-amylase A gene of
RT Aspergillus oryzae.";
RL Agric. Biol. Chem. 53:593-599(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AMY1 AND AMY2).
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [5]
RP PROTEIN SEQUENCE OF 22-499.
RX DOI=10.2183/pjab.58.208;
RA Toda H., Kondo K., Narita K.;
RT "The complete amino acid sequence of Taka-amylase A.";
RL Proc. Jpn. Acad., B, Phys. Biol. Sci. 58:208-212(1982).
RN [6]
RP PROTEIN SEQUENCE OF 206-225.
RX PubMed=4733850; DOI=10.1093/oxfordjournals.jbchem.a130210;
RA Isemura S., Ikenaka T.;
RT "The amino acid sequences of glycopeptides obtained from Taka-amylase A
RT with trypsin and chymotrypsin.";
RL J. Biochem. 74:1-10(1973).
RN [7]
RP PROTEIN SEQUENCE OF 434-499.
RA Narita K.;
RT "Amino acid sequence of the C-terminal sixty-six residues of Taka-amylase
RT A.";
RL Proc. Jpn. Acad. 51:285-290(1975).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 22-499 IN COMPLEX WITH CALCIUM,
RP COFACTOR, AND DISULFIDE BONDS.
RX PubMed=6156152; DOI=10.1093/oxfordjournals.jbchem.a132896;
RA Matsuura Y., Kusunoki M., Harada W., Tanaka N., Iga Y., Yasuoka N.,
RA Toda H., Narita K., Kakudo M.;
RT "Molecular structure of taka-amylase A. I. Backbone chain folding at 3-A
RT resolution.";
RL J. Biochem. 87:1555-1558(1980).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
RX PubMed=6609921; DOI=10.1093/oxfordjournals.jbchem.a134659;
RA Matsuura Y., Kusunoki M., Harada W., Kakudo M.;
RT "Structure and possible catalytic residues of Taka-amylase A.";
RL J. Biochem. 95:697-702(1984).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH CALCIUM AND
RP ACARBOSE, COFACTOR, DISULFIDE BONDS, AND ACTIVE SITE.
RX PubMed=9283074; DOI=10.1021/bi970539i;
RA Brzozowski A.M., Davies G.J.;
RT "Structure of the Aspergillus oryzae alpha-amylase complexed with the
RT inhibitor acarbose at 2.0-A resolution.";
RL Biochemistry 36:10837-10845(1997).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 22-499 IN COMPLEX WITH MALTOSE
RP AND CALCIUM IONS, GLYCOSYLATION AT ASN-218, AND DISULFIDE BONDS.
RX PubMed=16880540; DOI=10.1107/s1744309106024729;
RA Vujicic-Zagar A., Dijkstra B.W.;
RT "Monoclinic crystal form of Aspergillus niger alpha-amylase in complex with
RT maltose at 1.8 angstroms resolution.";
RL Acta Crystallogr. F 62:716-721(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:16880540, ECO:0000269|PubMed:6609921,
CC ECO:0000269|PubMed:9283074};
CC Note=Binds 2 calcium ions per subunit (PubMed:6609921, PubMed:9283074,
CC PubMed:16880540). Calcium is inhibitory at high concentrations.
CC {ECO:0000269|PubMed:16880540, ECO:0000269|PubMed:6609921,
CC ECO:0000269|PubMed:9283074, ECO:0000305};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16880540,
CC ECO:0000269|PubMed:9283074}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- BIOTECHNOLOGY: Used in the brewing industry to increase the
CC fermentability of beer worts (including those made from unmalted
CC cereals), in the starch industry to make high maltose and high DE
CC syrups (starch saccharification), in the alcohol industry to reduce
CC fermentation time, in the cereal food industry for flour
CC supplementation and improvement of chilled and frozen dough, and in the
CC forestry industry for low-temperature modification of starch. Sold
CC under the name Fungamyl by Novozymes.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X12725; CAA31218.1; -; Genomic_DNA.
DR EMBL; X12726; CAA31219.1; -; Genomic_DNA.
DR EMBL; D00434; BAA00336.1; -; Genomic_DNA.
DR EMBL; AP007157; BAE59434.1; -; Genomic_DNA.
DR EMBL; AP007166; BAE62808.1; -; Genomic_DNA.
DR PIR; JK0201; JK0201.
DR PIR; JT0466; JT0466.
DR PIR; S04548; ALAS1.
DR RefSeq; XP_001821436.1; XM_001821384.2.
DR RefSeq; XP_001823941.1; XM_001823889.2.
DR PDB; 2GUY; X-ray; 1.59 A; A=22-499.
DR PDB; 2GVY; X-ray; 1.80 A; A/B=22-499.
DR PDB; 2TAA; X-ray; 3.00 A; A/B/C=22-499.
DR PDB; 3KWX; X-ray; 2.40 A; A=22-499.
DR PDB; 3VX0; X-ray; 1.50 A; A=22-499.
DR PDB; 3VX1; X-ray; 2.20 A; A=22-499.
DR PDB; 6TAA; X-ray; 2.10 A; A=22-499.
DR PDB; 6XSJ; X-ray; 1.40 A; A/B=1-499.
DR PDB; 6XSV; X-ray; 1.65 A; A=1-499.
DR PDB; 6YQ7; X-ray; 1.58 A; A/B=1-499.
DR PDB; 7TAA; X-ray; 1.98 A; A=22-499.
DR PDBsum; 2GUY; -.
DR PDBsum; 2GVY; -.
DR PDBsum; 2TAA; -.
DR PDBsum; 3KWX; -.
DR PDBsum; 3VX0; -.
DR PDBsum; 3VX1; -.
DR PDBsum; 6TAA; -.
DR PDBsum; 6XSJ; -.
DR PDBsum; 6XSV; -.
DR PDBsum; 6YQ7; -.
DR PDBsum; 7TAA; -.
DR AlphaFoldDB; P0C1B3; -.
DR SMR; P0C1B3; -.
DR STRING; 510516.P0C1B3; -.
DR Allergome; 86; Asp o 21.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GlyConnect; 25; 1 N-Linked glycan (1 site).
DR EnsemblFungi; BAE59434; BAE59434; AO090023000944.
DR EnsemblFungi; BAE62808; BAE62808; AO090120000196.
DR GeneID; 5993438; -.
DR GeneID; 5996200; -.
DR KEGG; aor:AO090023000944; -.
DR KEGG; aor:AO090120000196; -.
DR VEuPathDB; FungiDB:AO090023000944; -.
DR VEuPathDB; FungiDB:AO090120000196; -.
DR HOGENOM; CLU_006462_7_2_1; -.
DR OMA; AHNWLFT; -.
DR EvolutionaryTrace; P0C1B3; -.
DR Proteomes; UP000006564; Chromosome 3.
DR Proteomes; UP000006564; Chromosome 5.
DR GO; GO:0030428; C:cell septum; IDA:AspGD.
DR GO; GO:0030287; C:cell wall-bounded periplasmic space; IDA:AspGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:AspGD.
DR GO; GO:0032163; C:hyphal septin band; IDA:AspGD.
DR GO; GO:0031521; C:spitzenkorper; IDA:AspGD.
DR GO; GO:0004556; F:alpha-amylase activity; IGI:AspGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016052; P:carbohydrate catabolic process; IGI:AspGD.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR013777; A-amylase-like.
DR InterPro; IPR015340; A_amylase_C_dom.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF09260; DUF1966; 1.
DR PIRSF; PIRSF001024; Alph-amyl_fung; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|Ref.5"
FT CHAIN 22..499
FT /note="Alpha-amylase A type-1/2"
FT /id="PRO_0000001349"
FT ACT_SITE 227
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:9283074"
FT ACT_SITE 251
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:9283074"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:9283074"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:9283074"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16880540,
FT ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:9283074"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16880540,
FT ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16880540,
FT ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:9283074"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:9283074"
FT BINDING 230..231
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:9283074"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16880540,
FT ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:9283074"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:9283074"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:9283074"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:9283074"
FT SITE 318
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:9283074"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16880540"
FT /id="CAR_000125"
FT DISULFID 51..59
FT /evidence="ECO:0000269|PubMed:16880540,
FT ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074,
FT ECO:0007744|PDB:7TAA"
FT DISULFID 171..185
FT /evidence="ECO:0000269|PubMed:16880540,
FT ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074,
FT ECO:0007744|PDB:7TAA"
FT DISULFID 261..304
FT /evidence="ECO:0000269|PubMed:16880540,
FT ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074,
FT ECO:0007744|PDB:7TAA"
FT DISULFID 461..496
FT /evidence="ECO:0000269|PubMed:16880540,
FT ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074,
FT ECO:0007744|PDB:7TAA"
FT CONFLICT 93..94
FT /note="TT -> DC (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="H -> T (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="Q -> T (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="D -> Y (in Ref. 3; BAA00336)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="P -> L (in Ref. 3; BAA00336)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="G -> V (in Ref. 3; BAA00336)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="I -> L (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 406..409
FT /note="WPIY -> PYI (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 443..444
FT /note="Missing (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="G -> Q (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="G -> S (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="V -> VGTTV (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 465..466
FT /note="Missing (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 469..471
FT /note="DGN -> BGB (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="S -> SD (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6YQ7"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:6XSJ"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 118..130
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:2TAA"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 202..219
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 237..244
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 261..265
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 290..303
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 329..341
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 342..349
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:6XSJ"
FT TURN 361..364
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:6YQ7"
FT HELIX 378..396
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 406..411
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 414..421
FT /evidence="ECO:0007829|PDB:6XSJ"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:3VX0"
FT STRAND 426..431
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 440..444
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 454..457
FT /evidence="ECO:0007829|PDB:6XSJ"
FT TURN 458..461
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:6TAA"
FT STRAND 472..476
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 482..486
FT /evidence="ECO:0007829|PDB:6XSJ"
FT HELIX 487..490
FT /evidence="ECO:0007829|PDB:6XSJ"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:3KWX"
SQ SEQUENCE 499 AA; 54810 MW; E407AE50DD071B52 CRC64;
MMVAWWSLFL YGLQVAAPAL AATPADWRSQ SIYFLLTDRF ARTDGSTTAT CNTADQKYCG
GTWQGIIDKL DYIQGMGFTA IWITPVTAQL PQTTAYGDAY HGYWQQDIYS LNENYGTADD
LKALSSALHE RGMYLMVDVV ANHMGYDGAG SSVDYSVFKP FSSQDYFHPF CFIQNYEDQT
QVEDCWLGDN TVSLPDLDTT KDVVKNEWYD WVGSLVSNYS IDGLRIDTVK HVQKDFWPGY
NKAAGVYCIG EVLDGDPAYT CPYQNVMDGV LNYPIYYPLL NAFKSTSGSM DDLYNMINTV
KSDCPDSTLL GTFVENHDNP RFASYTNDIA LAKNVAAFII LNDGIPIIYA GQEQHYAGGN
DPANREATWL SGYPTDSELY KLIASANAIR NYAISKDTGF VTYKNWPIYK DDTTIAMRKG
TDGSQIVTIL SNKGASGDSY TLSLSGAGYT AGQQLTEVIG CTTVTVGSDG NVPVPMAGGL
PRVLYPTEKL AGSKICSSS
