ID   PAO1_MAIZE              Reviewed;         500 AA.
AC   O64411; Q546R6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Polyamine oxidase 1 {ECO:0000303|Ref.2};
DE            EC=1.5.3.14 {ECO:0000269|Ref.4};
DE            EC=1.5.3.15 {ECO:0000269|Ref.4};
DE   Flags: Precursor;
GN   Name=MPAO1 {ECO:0000303|Ref.2};
GN   Synonyms=MPAO {ECO:0000303|PubMed:16331971}, PAO
GN   {ECO:0000303|PubMed:9598979};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 29-93; 97-111; 115-147;
RP   150-152; 154-162; 164-225; 227-241; 254-266; 270-278; 292-314; 317-323;
RP   329-332; 343-352; 355-383; 385-394; 404-459; 461-471; 477-487 AND 493-496.
RC   STRAIN=cv. Paolo; TISSUE=Etiolated seedling;
RX   PubMed=9598979; DOI=10.1016/s0014-5793(98)00311-1;
RA   Tavladoraki P., Schinina M.E., Cecconi F., Di Agostino S., Manera F.,
RA   Rea G., Mariottini P., Federico R., Angelini R.;
RT   "Maize polyamine oxidase: primary structure from protein and cDNA
RT   sequencing.";
RL   FEBS Lett. 426:62-66(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Paolo;
RX   DOI=10.1016/S0981-9428(00)01170-0;
RA   Cervelli M., Tavladoraki P., Di Agostino S., Angelini R., Federico R.,
RA   Mariottini P.;
RT   "Isolation and characterization of three polyamine oxidase genes from Zea
RT   mays.";
RL   Plant Physiol. Biochem. 38:667-677(2000).
RN   [3]
RP   SUBUNIT, AND COFACTOR.
RX   DOI=10.1016/0031-9422(89)85004-6;
RA   Federico R., Alisi C., Forlani F.;
RT   "Properties of the polyamine oxidase from the cell wall of maize
RT   seedlings.";
RL   Phytochemistry 28:45-46(1989).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   DOI=10.1016/0031-9422(96)00316-0;
RA   Federico R., Ercolini L., Laurenzi M., Angelini R.;
RT   "Oxidation of acetylpolyamines by maize polyamine oxidase.";
RL   Phytochemistry 43:339-341(1996).
RN   [5]
RP   SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=12586904; DOI=10.1104/pp.011379;
RA   Cona A., Cenci F., Cervelli M., Federico R., Mariottini P., Moreno S.,
RA   Angelini R.;
RT   "Polyamine oxidase, a hydrogen peroxide-producing enzyme, is up-regulated
RT   by light and down-regulated by auxin in the outer tissues of the maize
RT   mesocotyl.";
RL   Plant Physiol. 131:803-813(2003).
RN   [6]
RP   FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP   LYS-328.
RX   PubMed=16331971; DOI=10.1021/bi050983i;
RA   Polticelli F., Basran J., Faso C., Cona A., Minervini G., Angelini R.,
RA   Federico R., Scrutton N.S., Tavladoraki P.;
RT   "Lys300 plays a major role in the catalytic mechanism of maize polyamine
RT   oxidase.";
RL   Biochemistry 44:16108-16120(2005).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), AND CRYSTALLIZATION.
RX   PubMed=10089528; DOI=10.1107/s0907444998005836;
RA   Binda C., Coda A., Angelini R., Federico R., Ascenzi P., Mattevi A.;
RT   "Crystallization and preliminary X-ray analysis of polyamine oxidase from
RT   Zea mays L.";
RL   Acta Crystallogr. D 54:1429-1431(1998).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 29-500 IN COMPLEXES WITH FAD AND
RP   SYNTHETIC INHIBITORS, GLYCOSYLATION AT ASN-105, AND DISULFIDE BOND.
RX   PubMed=10368296; DOI=10.1016/s0969-2126(99)80037-9;
RA   Binda C., Coda A., Angelini R., Federico R., Ascenzi P., Mattevi A.;
RT   "A 30-A-long U-shaped catalytic tunnel in the crystal structure of
RT   polyamine oxidase.";
RL   Structure 7:265-276(1999).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 29-500 IN COMPLEXES WITH FAD AND
RP   SYNTHETIC INHIBITORS, GLYCOSYLATION AT ASN-105, AND DISULFIDE BOND.
RX   PubMed=11258887; DOI=10.1021/bi002751j;
RA   Binda C., Angelini R., Federico R., Ascenzi P., Mattevi A.;
RT   "Structural bases for inhibitor binding and catalysis in polyamine
RT   oxidase.";
RL   Biochemistry 40:2766-2776(2001).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 29-500 IN COMPLEX WITH SPERMINE
RP   AND SPERMIDINE.
RA   Fiorillo A., Ilari A., Tavladoraki P.;
RT   "The crystal structure of the mutant Lys300Met of polyamine oxidase from
RT   Zea Mays unveils the role of Lys300 in catalysis.";
RL   Submitted (NOV-2009) to the PDB data bank.
CC   -!- FUNCTION: Flavoenzyme involved in polyamine back-conversion (Ref.4,
CC       PubMed:16331971). Catalyzes the oxidation of the secondary amino group
CC       of polyamines, such as spermine, spermidine and their acetyl
CC       derivatives (Ref.4, PubMed:16331971). Plays an important role in the
CC       regulation of polyamine intracellular concentration (Probable).
CC       {ECO:0000269|PubMed:16331971, ECO:0000269|Ref.4, ECO:0000305|Ref.4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + spermidine = 4-aminobutanal + H2O2 + propane-1,3-
CC         diamine; Xref=Rhea:RHEA:25820, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:57484, ChEBI:CHEBI:57834,
CC         ChEBI:CHEBI:58264; EC=1.5.3.14; Evidence={ECO:0000269|Ref.4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(8)-acetylspermidine + O2 = 4-acetamidobutanal + H2O2 +
CC         propane-1,3-diamine; Xref=Rhea:RHEA:25972, ChEBI:CHEBI:7386,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57484, ChEBI:CHEBI:58535; EC=1.5.3.15;
CC         Evidence={ECO:0000269|Ref.4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + spermine = H2O2 + N-(3-aminopropyl)-4-aminobutanal
CC         + propane-1,3-diamine; Xref=Rhea:RHEA:25824, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:45725,
CC         ChEBI:CHEBI:57484, ChEBI:CHEBI:58869; EC=1.5.3.14;
CC         Evidence={ECO:0000269|Ref.4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(1)-acetylspermine + O2 = H2O2 + N-(3-acetamidopropyl)-
CC         4-aminobutanal + propane-1,3-diamine; Xref=Rhea:RHEA:25996,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57484, ChEBI:CHEBI:58101, ChEBI:CHEBI:58858; EC=1.5.3.14;
CC         Evidence={ECO:0000269|Ref.4};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:16331971, ECO:0000269|Ref.3};
CC       Note=Binds 1 FAD per subunit. {ECO:0000305|Ref.3};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=38 uM for spermine {ECO:0000269|Ref.4};
CC         KM=40 uM for spermidine {ECO:0000269|Ref.4};
CC         KM=62 uM for N(1)-acetylspermine {ECO:0000269|Ref.4};
CC         KM=274 uM for N(1)-acetylspermidine {ECO:0000269|Ref.4};
CC         KM=100 uM for dioxygen {ECO:0000269|Ref.4};
CC         Vmax=6 umol/min/ug enzyme with spermine as substrate
CC         {ECO:0000269|Ref.4};
CC         Vmax=70 umol/min/ug enzyme with spermidine as substrate
CC         {ECO:0000269|Ref.4};
CC         Vmax=21 umol/min/ug enzyme with N(1)-acetylspermine as substrate
CC         {ECO:0000269|Ref.4};
CC         Vmax=2.5 umol/min/ug enzyme with N(1)-acetylspermidine as substrate
CC         {ECO:0000269|Ref.4};
CC       pH dependence:
CC         Optimum pH is 6.5. {ECO:0000269|PubMed:16331971, ECO:0000269|Ref.4};
CC   -!- PATHWAY: Amine and polyamine degradation; spermine degradation.
CC       {ECO:0000305}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|Ref.3}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000269|PubMed:12586904}. Secreted, cell wall
CC       {ECO:0000269|PubMed:12586904}.
CC   -!- INDUCTION: Induced by light (at protein level) (PubMed:12586904). Down-
CC       regulated by auxin (at protein level) (PubMed:12586904).
CC       {ECO:0000269|PubMed:12586904}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ002204; CAA05249.1; -; mRNA.
DR   EMBL; AJ251568; CAC03739.1; -; Genomic_DNA.
DR   EMBL; AJ251018; CAC04001.1; -; Genomic_DNA.
DR   PIR; T03387; T03387.
DR   RefSeq; NP_001105106.1; NM_001111636.1.
DR   PDB; 1B37; X-ray; 1.90 A; A/B/C=29-500.
DR   PDB; 1B5Q; X-ray; 1.90 A; A/B/C=29-500.
DR   PDB; 1H81; X-ray; 2.10 A; A/B/C=29-500.
DR   PDB; 1H82; X-ray; 1.90 A; A/B/C=29-500.
DR   PDB; 1H83; X-ray; 1.90 A; A/B/C=29-500.
DR   PDB; 1H84; X-ray; 2.00 A; A/B/C=29-500.
DR   PDB; 1H86; X-ray; 2.00 A; A/B/C=29-500.
DR   PDB; 3KPF; X-ray; 2.90 A; A/B=29-500.
DR   PDB; 3KU9; X-ray; 3.20 A; A/B=29-500.
DR   PDB; 3L1R; X-ray; 3.20 A; A/B=29-500.
DR   PDBsum; 1B37; -.
DR   PDBsum; 1B5Q; -.
DR   PDBsum; 1H81; -.
DR   PDBsum; 1H82; -.
DR   PDBsum; 1H83; -.
DR   PDBsum; 1H84; -.
DR   PDBsum; 1H86; -.
DR   PDBsum; 3KPF; -.
DR   PDBsum; 3KU9; -.
DR   PDBsum; 3L1R; -.
DR   AlphaFoldDB; O64411; -.
DR   SMR; O64411; -.
DR   STRING; 4577.O64411; -.
DR   BindingDB; O64411; -.
DR   ChEMBL; CHEMBL6108; -.
DR   Allergome; 955; Zea m PAO.
DR   GlyCosmos; O64411; 1 site, No reported glycans.
DR   iPTMnet; O64411; -.
DR   PaxDb; 4577-GRMZM2G034152_P01; -.
DR   GeneID; 541983; -.
DR   KEGG; zma:541983; -.
DR   eggNOG; KOG0029; Eukaryota.
DR   InParanoid; O64411; -.
DR   OrthoDB; 3032570at2759; -.
DR   BioCyc; MetaCyc:MONOMER-9461; -.
DR   BRENDA; 1.5.3.14; 6752.
DR   SABIO-RK; O64411; -.
DR   UniPathway; UPA00211; -.
DR   EvolutionaryTrace; O64411; -.
DR   PRO; PR:O64411; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; O64411; baseline and differential.
DR   GO; GO:0048046; C:apoplast; IDA:UniProtKB.
DR   GO; GO:0009505; C:plant-type cell wall; IDA:UniProtKB.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR   GO; GO:0052893; F:N1-acetylspermine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0052897; F:N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0046592; F:polyamine oxidase activity; IDA:UniProtKB.
DR   GO; GO:0052896; F:spermidine oxidase (propane-1,3-diamine-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0052900; F:spermine oxidase (propane-1,3-diamine-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006598; P:polyamine catabolic process; IDA:UniProtKB.
DR   GO; GO:0046208; P:spermine catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001613; Flavin_amine_oxidase.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   PANTHER; PTHR10742:SF313; POLYAMINE OXIDASE 2; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   PRINTS; PR00757; AMINEOXDASEF.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Apoplast; Cell wall; Direct protein sequencing;
KW   Disulfide bond; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:9598979"
FT   CHAIN           29..500
FT                   /note="Polyamine oxidase 1"
FT                   /id="PRO_0000001712"
FT   BINDING         42..43
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10368296,
FT                   ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT                   ECO:0007744|PDB:1H82"
FT   BINDING         63
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10368296,
FT                   ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT                   ECO:0007744|PDB:1H82"
FT   BINDING         71
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10368296,
FT                   ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT                   ECO:0007744|PDB:1H82"
FT   BINDING         87..88
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10368296,
FT                   ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT                   ECO:0007744|PDB:1H82"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:3KU9,
FT                   ECO:0007744|PDB:3L1R"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:3KU9,
FT                   ECO:0007744|PDB:3L1R"
FT   BINDING         265
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10368296,
FT                   ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT                   ECO:0007744|PDB:1H82"
FT   BINDING         427
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10368296,
FT                   ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT                   ECO:0007744|PDB:1H82"
FT   BINDING         458
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10368296,
FT                   ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT                   ECO:0007744|PDB:1H82"
FT   BINDING         466
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:3KU9,
FT                   ECO:0007744|PDB:3L1R"
FT   BINDING         467..468
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10368296,
FT                   ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT                   ECO:0007744|PDB:1H82"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:10368296,
FT                   ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT                   ECO:0007744|PDB:1H82"
FT   DISULFID        485..491
FT                   /evidence="ECO:0000269|PubMed:10368296,
FT                   ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT                   ECO:0007744|PDB:1H82"
FT   MUTAGEN         328
FT                   /note="K->M: Abolishes enzymatic activity."
FT                   /evidence="ECO:0000269|PubMed:16331971"
FT   STRAND          35..38
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   HELIX           42..53
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          59..62
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          64..69
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          74..77
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          80..85
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          88..96
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   HELIX           100..105
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:1B5Q"
FT   STRAND          127..131
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   HELIX           134..156
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   HELIX           168..176
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          178..181
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   HELIX           185..194
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   HELIX           196..199
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   TURN            203..205
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          206..208
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   TURN            209..211
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   HELIX           215..220
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          222..227
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   HELIX           235..242
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   TURN            249..251
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          259..262
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          265..270
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          275..279
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          284..292
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   HELIX           296..300
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          303..308
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   HELIX           312..320
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          321..324
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          326..332
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          345..349
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          352..357
FT                   /evidence="ECO:0007829|PDB:3KU9"
FT   STRAND          359..362
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   TURN            364..366
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          367..369
FT                   /evidence="ECO:0007829|PDB:3KPF"
FT   STRAND          372..378
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   HELIX           379..386
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   HELIX           390..404
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          406..408
FT                   /evidence="ECO:0007829|PDB:3KU9"
FT   STRAND          414..417
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   TURN            421..423
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   TURN            425..427
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          428..433
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   HELIX           440..447
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   STRAND          453..455
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   HELIX           458..460
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   TURN            462..466
FT                   /evidence="ECO:0007829|PDB:1B37"
FT   HELIX           468..488
FT                   /evidence="ECO:0007829|PDB:1B37"
SQ   SEQUENCE   500 AA;  56344 MW;  00BB4BAF7A2E41CB CRC64;
     MSSSPSFGLL AVAALLLALS LAQHGSLAAT VGPRVIVVGA GMSGISAAKR LSEAGITDLL
     ILEATDHIGG RMHKTNFAGI NVELGANWVE GVNGGKMNPI WPIVNSTLKL RNFRSDFDYL
     AQNVYKEDGG VYDEDYVQKR IELADSVEEM GEKLSATLHA SGRDDMSILA MQRLNEHQPN
     GPATPVDMVV DYYKFDYEFA EPPRVTSLQN TVPLATFSDF GDDVYFVADQ RGYEAVVYYL
     AGQYLKTDDK SGKIVDPRLQ LNKVVREIKY SPGGVTVKTE DNSVYSADYV MVSASLGVLQ
     SDLIQFKPKL PTWKVRAIYQ FDMAVYTKIF LKFPRKFWPE GKGREFFLYA SSRRGYYGVW
     QEFEKQYPDA NVLLVTVTDE ESRRIEQQSD EQTKAEIMQV LRKMFPGKDV PDATDILVPR
     WWSDRFYKGT FSNWPVGVNR YEYDQLRAPV GRVYFTGEHT SEHYNGYVHG AYLSGIDSAE
     ILINCAQKKM CKYHVQGKYD
//