PAOX_ARTGO
ID PAOX_ARTGO Reviewed; 638 AA.
AC P46881;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Phenylethylamine oxidase;
DE EC=1.4.3.21 {ECO:0000250|UniProtKB:P12807};
DE AltName: Full=Primary amine oxidase;
DE Flags: Precursor;
OS Arthrobacter globiformis.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=1665;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 8010 / DSM 20124 / BCRC 10598 / JCM 1332 / KCTC 9101 / NBRC
RC 12137 / NCIMB 8907 / NRRL B-2979 / 168;
RX PubMed=8147851; DOI=10.1006/bbrc.1994.1343;
RA Tanizawa K., Matsuzaki R., Shimizu E., Yorifuji T., Fukui T.;
RT "Cloning and sequencing of phenylethylamine oxidase from Arthrobacter
RT globiformis and implication of Tyr-382 as the precursor to its covalently
RT bound quinone cofactor.";
RL Biochem. Biophys. Res. Commun. 199:1096-1102(1994).
RN [2] {ECO:0007744|PDB:1AV4, ECO:0007744|PDB:1AVK, ECO:0007744|PDB:1AVL}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH COPPER AND
RP SUBSTRATE, TOPAQUINONE AT TYR-382, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=9405045; DOI=10.1021/bi971797i;
RA Wilce M.C., Dooley D.M., Freeman H.C., Guss J.M., Matsunami H.,
RA McIntire W.S., Ruggiero C.E., Tanizawa K., Yamaguchi H.;
RT "Crystal structures of the copper-containing amine oxidase from
RT Arthrobacter globiformis in the holo and apo forms: implications for the
RT biogenesis of topaquinone.";
RL Biochemistry 36:16116-16133(1997).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58001; EC=1.4.3.21;
CC Evidence={ECO:0000250|UniProtKB:P12807};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:9405045};
CC Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:9405045};
CC -!- COFACTOR:
CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC Evidence={ECO:0000269|PubMed:9405045};
CC Note=Contains 1 topaquinone per subunit. {ECO:0000269|PubMed:9405045};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9405045}.
CC -!- INDUCTION: By phenethylamine.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000269|PubMed:9405045}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
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DR EMBL; U03517; AAA18114.1; -; Unassigned_DNA.
DR PIR; JC2139; JC2139.
DR PDB; 1AV4; X-ray; 2.20 A; A=1-638.
DR PDB; 1AVK; X-ray; 2.20 A; A=1-638.
DR PDB; 1AVL; X-ray; 2.80 A; A=1-638.
DR PDB; 1IQX; X-ray; 2.00 A; A/B=1-638.
DR PDB; 1IQY; X-ray; 1.80 A; A/B=1-638.
DR PDB; 1IU7; X-ray; 1.80 A; A/B=1-638.
DR PDB; 1IVU; X-ray; 1.90 A; A/B=1-638.
DR PDB; 1IVV; X-ray; 2.10 A; A/B=1-638.
DR PDB; 1IVW; X-ray; 1.80 A; A/B=1-638.
DR PDB; 1IVX; X-ray; 2.20 A; A/B=1-638.
DR PDB; 1RJO; X-ray; 1.67 A; A=3-638.
DR PDB; 1SIH; X-ray; 1.73 A; A=3-638.
DR PDB; 1SII; X-ray; 1.70 A; A=3-638.
DR PDB; 1UI7; X-ray; 2.00 A; A/B=1-638.
DR PDB; 1UI8; X-ray; 1.80 A; A/B=1-638.
DR PDB; 1W4N; X-ray; 1.65 A; A/B=3-638.
DR PDB; 1W5Z; X-ray; 1.86 A; A=3-638.
DR PDB; 1W6C; X-ray; 2.20 A; A=3-638.
DR PDB; 1W6G; X-ray; 1.55 A; A=3-638.
DR PDB; 1WMN; X-ray; 1.80 A; A/B=1-638.
DR PDB; 1WMO; X-ray; 1.80 A; A/B=1-638.
DR PDB; 1WMP; X-ray; 2.00 A; A/B=1-638.
DR PDB; 2BT3; X-ray; 1.73 A; A=3-638.
DR PDB; 2CFD; X-ray; 1.60 A; A/B=3-638.
DR PDB; 2CFG; X-ray; 1.55 A; A/B=3-638.
DR PDB; 2CFK; X-ray; 1.80 A; A=3-638.
DR PDB; 2CFL; X-ray; 1.80 A; A=3-638.
DR PDB; 2CFW; X-ray; 1.74 A; A=3-638.
DR PDB; 2CG0; X-ray; 1.80 A; A=3-638.
DR PDB; 2CG1; X-ray; 1.67 A; A=3-638.
DR PDB; 2CWT; X-ray; 1.82 A; A/B=1-638.
DR PDB; 2CWU; X-ray; 1.85 A; A/B=1-638.
DR PDB; 2CWV; X-ray; 1.85 A; A/B=1-638.
DR PDB; 2D1W; X-ray; 1.74 A; A/B=1-638.
DR PDB; 2E2T; X-ray; 2.05 A; A=1-638.
DR PDB; 2E2U; X-ray; 1.68 A; A/B=1-628.
DR PDB; 2E2V; X-ray; 1.80 A; A/B=1-628.
DR PDB; 2YX9; X-ray; 1.68 A; A/B=1-638.
DR PDB; 2ZL8; X-ray; 1.73 A; A/B=1-638.
DR PDB; 3AMO; X-ray; 2.10 A; A/B=1-638.
DR PDB; 3KII; X-ray; 1.90 A; A/B=3-638.
DR PDB; 3KN4; X-ray; 2.05 A; A=3-638.
DR PDB; 3WA2; X-ray; 1.08 A; X=9-629.
DR PDB; 3WA3; X-ray; 1.55 A; A/B=9-629.
DR PDB; 3X3X; X-ray; 1.57 A; A/B=9-628.
DR PDB; 3X3Y; X-ray; 1.50 A; A/B=9-628.
DR PDB; 3X3Z; X-ray; 1.51 A; A/B=9-628.
DR PDB; 3X40; X-ray; 1.85 A; A/B=9-628.
DR PDB; 3X41; X-ray; 1.87 A; A/B=9-628.
DR PDB; 3X42; X-ray; 1.88 A; A/B=9-629.
DR PDB; 5ZOU; X-ray; 1.68 A; A/B=9-628.
DR PDB; 5ZOW; X-ray; 1.78 A; A/B=9-628.
DR PDB; 5ZOX; X-ray; 1.69 A; A/B=9-628.
DR PDB; 5ZOY; X-ray; 1.70 A; A/B=9-628.
DR PDB; 5ZOZ; X-ray; 1.70 A; A/B=9-628.
DR PDB; 5ZP0; X-ray; 1.74 A; A/B=9-628.
DR PDB; 5ZP1; X-ray; 1.67 A; A/B=9-628.
DR PDB; 5ZP2; X-ray; 1.75 A; A/B=9-628.
DR PDB; 5ZP3; X-ray; 1.78 A; A/B=9-628.
DR PDB; 5ZP4; X-ray; 1.80 A; A/B=9-628.
DR PDB; 5ZP5; X-ray; 1.77 A; A/B=9-628.
DR PDB; 5ZP6; X-ray; 1.69 A; A/B=9-628.
DR PDB; 5ZP7; X-ray; 1.63 A; A/B=9-628.
DR PDB; 5ZP8; X-ray; 1.66 A; A/B=9-628.
DR PDB; 5ZP9; X-ray; 1.70 A; A/B=9-628.
DR PDB; 5ZPA; X-ray; 1.69 A; A/B=9-628.
DR PDB; 5ZPB; X-ray; 1.79 A; A/B=9-628.
DR PDB; 5ZPC; X-ray; 1.74 A; A/B=9-628.
DR PDB; 5ZPD; X-ray; 1.67 A; A/B=9-628.
DR PDB; 5ZPE; X-ray; 1.69 A; A/B=9-628.
DR PDB; 5ZPF; X-ray; 1.76 A; A/B=9-628.
DR PDB; 5ZPG; X-ray; 1.65 A; A/B=9-628.
DR PDB; 5ZPH; X-ray; 1.72 A; A/B=9-628.
DR PDB; 5ZPI; X-ray; 1.75 A; A/B=9-628.
DR PDB; 5ZPJ; X-ray; 1.65 A; A/B=9-628.
DR PDB; 5ZPK; X-ray; 1.65 A; A/B=9-628.
DR PDB; 5ZPL; X-ray; 1.60 A; A/B=9-628.
DR PDB; 5ZPM; X-ray; 1.65 A; A/B=9-628.
DR PDB; 5ZPN; X-ray; 1.60 A; A/B=9-628.
DR PDB; 5ZPO; X-ray; 1.73 A; A/B=9-628.
DR PDB; 5ZPP; X-ray; 1.81 A; A/B=9-628.
DR PDB; 5ZPQ; X-ray; 1.85 A; A/B=9-628.
DR PDB; 5ZPR; X-ray; 1.92 A; A/B=9-628.
DR PDB; 5ZPS; X-ray; 1.75 A; A/B=9-628.
DR PDB; 5ZPT; X-ray; 1.90 A; A/B=9-628.
DR PDB; 6L9C; Other; 1.14 A; X=9-629.
DR PDB; 7F8K; X-ray; 2.20 A; A=1-638.
DR PDBsum; 1AV4; -.
DR PDBsum; 1AVK; -.
DR PDBsum; 1AVL; -.
DR PDBsum; 1IQX; -.
DR PDBsum; 1IQY; -.
DR PDBsum; 1IU7; -.
DR PDBsum; 1IVU; -.
DR PDBsum; 1IVV; -.
DR PDBsum; 1IVW; -.
DR PDBsum; 1IVX; -.
DR PDBsum; 1RJO; -.
DR PDBsum; 1SIH; -.
DR PDBsum; 1SII; -.
DR PDBsum; 1UI7; -.
DR PDBsum; 1UI8; -.
DR PDBsum; 1W4N; -.
DR PDBsum; 1W5Z; -.
DR PDBsum; 1W6C; -.
DR PDBsum; 1W6G; -.
DR PDBsum; 1WMN; -.
DR PDBsum; 1WMO; -.
DR PDBsum; 1WMP; -.
DR PDBsum; 2BT3; -.
DR PDBsum; 2CFD; -.
DR PDBsum; 2CFG; -.
DR PDBsum; 2CFK; -.
DR PDBsum; 2CFL; -.
DR PDBsum; 2CFW; -.
DR PDBsum; 2CG0; -.
DR PDBsum; 2CG1; -.
DR PDBsum; 2CWT; -.
DR PDBsum; 2CWU; -.
DR PDBsum; 2CWV; -.
DR PDBsum; 2D1W; -.
DR PDBsum; 2E2T; -.
DR PDBsum; 2E2U; -.
DR PDBsum; 2E2V; -.
DR PDBsum; 2YX9; -.
DR PDBsum; 2ZL8; -.
DR PDBsum; 3AMO; -.
DR PDBsum; 3KII; -.
DR PDBsum; 3KN4; -.
DR PDBsum; 3WA2; -.
DR PDBsum; 3WA3; -.
DR PDBsum; 3X3X; -.
DR PDBsum; 3X3Y; -.
DR PDBsum; 3X3Z; -.
DR PDBsum; 3X40; -.
DR PDBsum; 3X41; -.
DR PDBsum; 3X42; -.
DR PDBsum; 5ZOU; -.
DR PDBsum; 5ZOW; -.
DR PDBsum; 5ZOX; -.
DR PDBsum; 5ZOY; -.
DR PDBsum; 5ZOZ; -.
DR PDBsum; 5ZP0; -.
DR PDBsum; 5ZP1; -.
DR PDBsum; 5ZP2; -.
DR PDBsum; 5ZP3; -.
DR PDBsum; 5ZP4; -.
DR PDBsum; 5ZP5; -.
DR PDBsum; 5ZP6; -.
DR PDBsum; 5ZP7; -.
DR PDBsum; 5ZP8; -.
DR PDBsum; 5ZP9; -.
DR PDBsum; 5ZPA; -.
DR PDBsum; 5ZPB; -.
DR PDBsum; 5ZPC; -.
DR PDBsum; 5ZPD; -.
DR PDBsum; 5ZPE; -.
DR PDBsum; 5ZPF; -.
DR PDBsum; 5ZPG; -.
DR PDBsum; 5ZPH; -.
DR PDBsum; 5ZPI; -.
DR PDBsum; 5ZPJ; -.
DR PDBsum; 5ZPK; -.
DR PDBsum; 5ZPL; -.
DR PDBsum; 5ZPM; -.
DR PDBsum; 5ZPN; -.
DR PDBsum; 5ZPO; -.
DR PDBsum; 5ZPP; -.
DR PDBsum; 5ZPQ; -.
DR PDBsum; 5ZPR; -.
DR PDBsum; 5ZPS; -.
DR PDBsum; 5ZPT; -.
DR PDBsum; 6L9C; -.
DR PDBsum; 7F8K; -.
DR AlphaFoldDB; P46881; -.
DR SMR; P46881; -.
DR DrugBank; DB02511; 2-Hydroxy-5-({1-[(2-Naphthyloxy)Methyl]-3-Oxoprop-1-Enyl}Amino)Tyrosine.
DR DrugBank; DB02537; 2-Hydroxy-5-({1-[(4-Methylphenoxy)Methyl]-3-Oxoprop-1-Enyl}Amino)-L-Tyrosine.
DR DrugBank; DB06988; 2-HYDROXY-5-{[(1E)-2-PHENYLETHYLIDENE]AMINO}-L-TYROSINE.
DR DrugBank; DB04334; 6-hydroxydopa quinone.
DR KEGG; ag:AAA18114; -.
DR BRENDA; 1.4.3.21; 444.
DR EvolutionaryTrace; P46881; -.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008131; F:primary amine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009308; P:amine metabolic process; IEA:InterPro.
DR Gene3D; 2.70.98.20; -; 1.
DR InterPro; IPR000269; Cu_amine_oxidase.
DR InterPro; IPR015798; Cu_amine_oxidase_C.
DR InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR PANTHER; PTHR10638; PTHR10638; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR SUPFAM; SSF49998; SSF49998; 1.
DR SUPFAM; SSF54416; SSF54416; 2.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Disulfide bond;
KW Metal-binding; Oxidoreductase; TPQ.
FT PROPEP 1..2
FT /id="PRO_0000035681"
FT CHAIN 3..638
FT /note="Phenylethylamine oxidase"
FT /id="PRO_0000035682"
FT ACT_SITE 298
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT ACT_SITE 382
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 296..307
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 379..384
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 431
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:9405045,
FT ECO:0007744|PDB:1AV4, ECO:0007744|PDB:1AVL,
FT ECO:0007744|PDB:1IU7, ECO:0007744|PDB:1IVU,
FT ECO:0007744|PDB:1IVV, ECO:0007744|PDB:1IVW,
FT ECO:0007744|PDB:1IVX, ECO:0007744|PDB:1RJO,
FT ECO:0007744|PDB:1SIH, ECO:0007744|PDB:1SII,
FT ECO:0007744|PDB:1UI8, ECO:0007744|PDB:1W4N,
FT ECO:0007744|PDB:1W5Z, ECO:0007744|PDB:1W6C,
FT ECO:0007744|PDB:1W6G, ECO:0007744|PDB:2BT3,
FT ECO:0007744|PDB:2CFD, ECO:0007744|PDB:2CFG,
FT ECO:0007744|PDB:2CFK, ECO:0007744|PDB:2CFL,
FT ECO:0007744|PDB:2CFW, ECO:0007744|PDB:2CG0,
FT ECO:0007744|PDB:2CG1, ECO:0007744|PDB:2CWT,
FT ECO:0007744|PDB:2CWU, ECO:0007744|PDB:2CWV,
FT ECO:0007744|PDB:2D1W, ECO:0007744|PDB:2E2T,
FT ECO:0007744|PDB:2E2U, ECO:0007744|PDB:2E2V,
FT ECO:0007744|PDB:2YX9, ECO:0007744|PDB:2ZL8,
FT ECO:0007744|PDB:3AMO, ECO:0007744|PDB:3KII,
FT ECO:0007744|PDB:3KN4, ECO:0007744|PDB:3WA2,
FT ECO:0007744|PDB:3WA3"
FT BINDING 433
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:9405045,
FT ECO:0007744|PDB:1AV4, ECO:0007744|PDB:1AVL,
FT ECO:0007744|PDB:1IU7, ECO:0007744|PDB:1IVU,
FT ECO:0007744|PDB:1IVV, ECO:0007744|PDB:1IVW,
FT ECO:0007744|PDB:1IVX, ECO:0007744|PDB:1RJO,
FT ECO:0007744|PDB:1SIH, ECO:0007744|PDB:1SII,
FT ECO:0007744|PDB:1UI8, ECO:0007744|PDB:1W4N,
FT ECO:0007744|PDB:1W5Z, ECO:0007744|PDB:1W6C,
FT ECO:0007744|PDB:1W6G, ECO:0007744|PDB:2BT3,
FT ECO:0007744|PDB:2CFD, ECO:0007744|PDB:2CFG,
FT ECO:0007744|PDB:2CFK, ECO:0007744|PDB:2CFL,
FT ECO:0007744|PDB:2CFW, ECO:0007744|PDB:2CG0,
FT ECO:0007744|PDB:2CG1, ECO:0007744|PDB:2CWT,
FT ECO:0007744|PDB:2CWU, ECO:0007744|PDB:2CWV,
FT ECO:0007744|PDB:2D1W, ECO:0007744|PDB:2E2T,
FT ECO:0007744|PDB:2E2U, ECO:0007744|PDB:2E2V,
FT ECO:0007744|PDB:2YX9, ECO:0007744|PDB:2ZL8,
FT ECO:0007744|PDB:3AMO, ECO:0007744|PDB:3KII,
FT ECO:0007744|PDB:3KN4, ECO:0007744|PDB:3WA2,
FT ECO:0007744|PDB:3WA3"
FT BINDING 592
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:9405045,
FT ECO:0007744|PDB:1AV4, ECO:0007744|PDB:1AVL,
FT ECO:0007744|PDB:1IU7, ECO:0007744|PDB:1IVU,
FT ECO:0007744|PDB:1IVV, ECO:0007744|PDB:1IVW,
FT ECO:0007744|PDB:1IVX, ECO:0007744|PDB:1RJO,
FT ECO:0007744|PDB:1SIH, ECO:0007744|PDB:1SII,
FT ECO:0007744|PDB:1UI8, ECO:0007744|PDB:1W4N,
FT ECO:0007744|PDB:1W5Z, ECO:0007744|PDB:1W6C,
FT ECO:0007744|PDB:1W6G, ECO:0007744|PDB:2BT3,
FT ECO:0007744|PDB:2CFD, ECO:0007744|PDB:2CFG,
FT ECO:0007744|PDB:2CFK, ECO:0007744|PDB:2CFL,
FT ECO:0007744|PDB:2CFW, ECO:0007744|PDB:2CG0,
FT ECO:0007744|PDB:2CG1, ECO:0007744|PDB:2CWT,
FT ECO:0007744|PDB:2CWU, ECO:0007744|PDB:2CWV,
FT ECO:0007744|PDB:2D1W, ECO:0007744|PDB:2E2T,
FT ECO:0007744|PDB:2E2U, ECO:0007744|PDB:2E2V,
FT ECO:0007744|PDB:2YX9, ECO:0007744|PDB:2ZL8,
FT ECO:0007744|PDB:3AMO, ECO:0007744|PDB:3KII,
FT ECO:0007744|PDB:3KN4, ECO:0007744|PDB:3WA2,
FT ECO:0007744|PDB:3WA3"
FT MOD_RES 382
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000269|PubMed:9405045"
FT DISULFID 317..343
FT /evidence="ECO:0000269|PubMed:9405045,
FT ECO:0007744|PDB:1AV4, ECO:0007744|PDB:1AVL,
FT ECO:0007744|PDB:1IQX, ECO:0007744|PDB:1IQY,
FT ECO:0007744|PDB:1IU7, ECO:0007744|PDB:1IVW,
FT ECO:0007744|PDB:1IVX, ECO:0007744|PDB:1RJO,
FT ECO:0007744|PDB:1UI8, ECO:0007744|PDB:1WMN,
FT ECO:0007744|PDB:1WMO, ECO:0007744|PDB:2CWT"
FT MUTAGEN 382
FT /note="Y->F: Loss of activity."
FT HELIX 17..29
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1WMO"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:3WA2"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:3WA2"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:3WA2"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:3WA2"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:3WA2"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:3WA2"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:3X3Y"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3KN4"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3WA3"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:3WA2"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:3WA2"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:3X3Y"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:3WA2"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:3WA2"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 254..264
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 267..284
FT /evidence="ECO:0007829|PDB:3WA2"
FT TURN 289..293
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:3X3Y"
FT HELIX 298..302
FT /evidence="ECO:0007829|PDB:3WA2"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:3WA2"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 342..356
FT /evidence="ECO:0007829|PDB:3WA2"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 363..379
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 382..391
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 396..404
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 417..423
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 426..429
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 431..441
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 448..457
FT /evidence="ECO:0007829|PDB:3WA2"
FT TURN 462..464
FT /evidence="ECO:0007829|PDB:1AV4"
FT STRAND 470..476
FT /evidence="ECO:0007829|PDB:3WA2"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:3WA2"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 494..503
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 509..516
FT /evidence="ECO:0007829|PDB:3WA2"
FT HELIX 529..533
FT /evidence="ECO:0007829|PDB:3WA2"
FT HELIX 535..538
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 539..545
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 563..566
FT /evidence="ECO:0007829|PDB:3X3Y"
FT HELIX 567..571
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 578..580
FT /evidence="ECO:0007829|PDB:5ZOY"
FT STRAND 582..592
FT /evidence="ECO:0007829|PDB:3WA2"
FT HELIX 596..598
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 599..615
FT /evidence="ECO:0007829|PDB:3WA2"
FT STRAND 617..619
FT /evidence="ECO:0007829|PDB:3WA2"
FT TURN 621..624
FT /evidence="ECO:0007829|PDB:3WA2"
SQ SEQUENCE 638 AA; 70646 MW; 1800396BA7A983F2 CRC64;
MTPSTIQTAS PFRLASAGEI SEVQGILRTA GLLGPEKRIA YLGVLDPARG AGSEAEDRRF
RVFIHDVSGA RPQEVTVSVT NGTVISAVEL DTAATGELPV LEEEFEVVEQ LLATDERWLK
ALAARNLDVS KVRVAPLSAG VFEYAEERGR RILRGLAFVQ DFPEDSAWAH PVDGLVAYVD
VVSKEVTRVI DTGVFPVPAE HGNYTDPELT GPLRTTQKPI SITQPEGPSF TVTGGNHIEW
EKWSLDVGFD VREGVVLHNI AFRDGDRLRP IINRASIAEM VVPYGDPSPI RSWQNYFDTG
EYLVGQYANS LELGCDCLGD ITYLSPVISD AFGNPREIRN GICMHEEDWG ILAKHSDLWS
GINYTRRNRR MVISFFTTIG NYDYGFYWYL YLDGTIEFEA KATGVVFTSA FPEGGSDNIS
QLAPGLGAPF HQHIFSARLD MAIDGFTNRV EEEDVVRQTM GPGNERGNAF SRKRTVLTRE
SEAVREADAR TGRTWIISNP ESKNRLNEPV GYKLHAHNQP TLLADPGSSI ARRAAFATKD
LWVTRYADDE RYPTGDFVNQ HSGGAGLPSY IAQDRDIDGQ DIVVWHTFGL THFPRVEDWP
IMPVDTVGFK LRPEGFFDRS PVLDVPANPS QSGSHCHG
