AOSL_PLEHO
ID AOSL_PLEHO Reviewed; 1066 AA.
AC O16025;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Allene oxide synthase-lipoxygenase protein {ECO:0000303|PubMed:10559269};
DE Includes:
DE RecName: Full=Allene oxide synthase;
DE Short=AOS;
DE EC=4.2.1.- {ECO:0000269|PubMed:10559269, ECO:0000269|PubMed:29909837, ECO:0000269|PubMed:9302294};
DE AltName: Full=Hydroperoxidehydrase;
DE Includes:
DE RecName: Full=Arachidonate 8-lipoxygenase;
DE EC=1.13.11.40 {ECO:0000269|PubMed:10559269, ECO:0000269|PubMed:9302294};
OS Plexaura homomalla (Black sea rod).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Octocorallia; Alcyonacea;
OC Holaxonia; Plexauridae; Plexaura.
OX NCBI_TaxID=47982;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9302294; DOI=10.1126/science.277.5334.1994;
RA Koljak R., Boutaud O., Shieh B.-H., Samel N., Brash A.R.;
RT "Identification of a naturally occurring peroxidase-lipoxygenase fusion
RT protein.";
RL Science 277:1994-1996(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=10559269; DOI=10.1074/jbc.274.47.33764;
RA Boutaud O., Brash A.R.;
RT "Purification and catalytic activities of the two domains of the allene
RT oxide synthase-lipoxygenase fusion protein of the coral Plexaura
RT homomalla.";
RL J. Biol. Chem. 274:33764-33770(1999).
RN [3]
RP HEME-BINDING.
RX PubMed=11329294; DOI=10.1021/bi002121h;
RA Abraham B.D., Sono M., Boutaud O., Shriner A., Dawson J.H., Brash A.R.,
RA Gaffney B.J.;
RT "Characterization of the coral allene oxide synthase active site with UV-
RT visible absorption, magnetic circular dichroism, and electron paramagnetic
RT resonance spectroscopy: evidence for tyrosinate ligation to the ferric
RT enzyme heme iron.";
RL Biochemistry 40:2251-2259(2001).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29909837; DOI=10.1016/bs.mie.2018.02.019;
RA Brash A.R.;
RT "Catalase-Related Allene Oxide Synthase, on a Biosynthetic Route to Fatty
RT Acid Cyclopentenones: Expression and Assay of the Enzyme and Preparation of
RT the 8R-HPETE Substrate.";
RL Methods Enzymol. 605:51-68(2018).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 373-1066 IN COMPLEX WITH CALCIUM
RP AND IRON IONS, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND MUTAGENESIS
RP OF ASP-411; TRP-413; GLU-419 AND TRP-449.
RX PubMed=16162493; DOI=10.1074/jbc.m506675200;
RA Oldham M.L., Brash A.R., Newcomer M.E.;
RT "Insights from the X-ray crystal structure of coral 8R-lipoxygenase:
RT calcium activation via a C2-like domain and a structural basis of product
RT chirality.";
RL J. Biol. Chem. 280:39545-39552(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-374 IN COMPLEX WITH HEME, AND
RP SUBUNIT.
RX PubMed=15625113; DOI=10.1073/pnas.0406352102;
RA Oldham M.L., Brash A.R., Newcomer M.E.;
RT "The structure of coral allene oxide synthase reveals a catalase adapted
RT for metabolism of a fatty acid hydroperoxide.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:297-302(2005).
CC -!- FUNCTION: Bifunctional enzyme which is responsible for allene oxide
CC biosynthesis via a two-step reaction; first the lipoxygenase reaction
CC that converts polyunsaturated fatty acids such as arachidonate
CC ((5Z,8Z,11Z,14Z)-eicosatetraenoate) into a (8R)-hydroperoxide
CC intermediate ((8R)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate)
CC followed by the allene oxide synthase reaction that converts the
CC hydroperoxide intermediate ((8R)-hydroperoxy-(5Z,9E,11Z,14Z)-
CC eicosatetraenoate) into the allene oxide (8,9-epoxy-(5Z,9E,11Z,14Z)-
CC eicosatetraenoate) (PubMed:9302294, PubMed:10559269). Shows preference
CC for C20 or C22 highly polyunsaturated fatty acids and no activity with
CC C18 fatty acids in vitro (PubMed:10559269). Fatty acid allene oxides
CC are intermediates in the formation of cyclopentenones or hydrolytic
CC products in marine systems, most notably the prostanoid-related
CC clavulones (PubMed:29909837). {ECO:0000269|PubMed:10559269,
CC ECO:0000269|PubMed:9302294, ECO:0000303|PubMed:29909837}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (8R)-hydroperoxy-
CC (5Z,9E,11Z,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:14985,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57447;
CC EC=1.13.11.40; Evidence={ECO:0000269|PubMed:10559269,
CC ECO:0000269|PubMed:9302294};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14986;
CC Evidence={ECO:0000269|PubMed:10559269, ECO:0000269|PubMed:9302294};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8R)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate = 8,9-
CC epoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:51344,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57447, ChEBI:CHEBI:134054;
CC Evidence={ECO:0000269|PubMed:10559269, ECO:0000269|PubMed:29909837,
CC ECO:0000269|PubMed:9302294};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51345;
CC Evidence={ECO:0000269|PubMed:10559269, ECO:0000269|PubMed:29909837,
CC ECO:0000269|PubMed:9302294};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 = (8R)-hydroperoxy-
CC (5Z,9E,11Z,14Z,17Z)-eicosapentaenoate; Xref=Rhea:RHEA:51412,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:58562, ChEBI:CHEBI:134079;
CC Evidence={ECO:0000305|PubMed:10559269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51413;
CC Evidence={ECO:0000305|PubMed:10559269};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = 10-
CC hydroperoxy-(4Z,7Z,11E,13Z,16Z,19Z)-docosahexaenoate;
CC Xref=Rhea:RHEA:51340, ChEBI:CHEBI:15379, ChEBI:CHEBI:77016,
CC ChEBI:CHEBI:134057; Evidence={ECO:0000269|PubMed:10559269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51341;
CC Evidence={ECO:0000269|PubMed:10559269};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8Z,11Z,14Z)-eicosatrienoate + O2 = (8R)-hydroperoxy-
CC (9E,11Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:51324,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:71589, ChEBI:CHEBI:134051;
CC Evidence={ECO:0000305|PubMed:10559269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51325;
CC Evidence={ECO:0000305|PubMed:10559269};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8Z,11Z,14Z)-eicosatrienoate + O2 = 10-hydroperoxy-
CC (8Z,11Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:51328,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:71589, ChEBI:CHEBI:134052;
CC Evidence={ECO:0000269|PubMed:10559269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51329;
CC Evidence={ECO:0000269|PubMed:10559269};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8Z,11Z,14Z)-eicosatrienoate + O2 = 11-hydroperoxy-
CC (8Z,12E,14Z)-eicosatrienoate; Xref=Rhea:RHEA:51332,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:71589, ChEBI:CHEBI:134053;
CC Evidence={ECO:0000269|PubMed:10559269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51333;
CC Evidence={ECO:0000269|PubMed:10559269};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 2 calcium ions per subunit.;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Note=Binds 1 Fe cation per subunit.;
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 1 heme group per subunit.;
CC -!- ACTIVITY REGULATION: Lipoxygenase activity is stimulated by calcium,
CC sodium, lithium and potassium ions. Calcium binding promotes
CC interaction with membranes and thus facilitates access to substrates.
CC {ECO:0000269|PubMed:10559269, ECO:0000269|PubMed:16162493}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=45.28 uM for arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate)
CC {ECO:0000269|PubMed:10559269};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:10559269};
CC -!- PATHWAY: Lipid metabolism; arachidonate metabolism.
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC -!- SUBUNIT: Dimer. {ECO:0000305|PubMed:15625113,
CC ECO:0000305|PubMed:16162493}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726,
CC ECO:0000269|PubMed:16162493}. Membrane {ECO:0000269|PubMed:16162493};
CC Peripheral membrane protein {ECO:0000269|PubMed:16162493}. Note=Calcium
CC binding promotes binding to membranes.
CC -!- SIMILARITY: In the C-terminal section; belongs to the lipoxygenase
CC family. {ECO:0000305}.
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DR EMBL; AF003692; AAC47743.1; -; mRNA.
DR PIR; T30903; T30903.
DR PDB; 1U5U; X-ray; 2.00 A; A/B=1-374.
DR PDB; 2FNQ; X-ray; 3.20 A; A/B=374-1066.
DR PDB; 3DY5; X-ray; 3.51 A; A/C=1-1066.
DR PDB; 3FG1; X-ray; 1.85 A; A/B/C/D=374-1066.
DR PDB; 3FG3; X-ray; 1.90 A; A/B/C/D=374-1066.
DR PDB; 3FG4; X-ray; 2.31 A; A/B/C/D=374-1066.
DR PDB; 4QWT; X-ray; 2.00 A; A/B/C/D=374-1066.
DR PDBsum; 1U5U; -.
DR PDBsum; 2FNQ; -.
DR PDBsum; 3DY5; -.
DR PDBsum; 3FG1; -.
DR PDBsum; 3FG3; -.
DR PDBsum; 3FG4; -.
DR PDBsum; 4QWT; -.
DR AlphaFoldDB; O16025; -.
DR SMR; O16025; -.
DR SwissLipids; SLP:000001660; -.
DR PeroxiBase; 5626; PhoKatLox01.
DR PRIDE; O16025; -.
DR KEGG; ag:AAC47743; -.
DR BRENDA; 1.13.11.40; 4917.
DR UniPathway; UPA00199; -.
DR UniPathway; UPA00383; -.
DR EvolutionaryTrace; O16025; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009978; F:allene oxide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0047677; F:arachidonate 8(R)-lipoxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR InterPro; IPR020834; LipOase_CS.
DR InterPro; IPR020833; LipOase_Fe_BS.
DR InterPro; IPR001885; LipOase_mml.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR PANTHER; PTHR11771; PTHR11771; 1.
DR Pfam; PF00305; Lipoxygenase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PRINTS; PR00087; LIPOXYGENASE.
DR PRINTS; PR00467; MAMLPOXGNASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF48484; SSF48484; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR SUPFAM; SSF56634; SSF56634; 1.
DR PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cytoplasm; Dioxygenase; Fatty acid biosynthesis;
KW Fatty acid metabolism; Heme; Iron; Lipid biosynthesis; Lipid metabolism;
KW Lyase; Membrane; Metal-binding; Multifunctional enzyme; Oxidoreductase;
KW Oxylipin biosynthesis.
FT CHAIN 1..1066
FT /note="Allene oxide synthase-lipoxygenase protein"
FT /id="PRO_0000220724"
FT DOMAIN 374..490
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 491..1066
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 1..371
FT /note="Allene oxide synthase"
FT REGION 372..1066
FT /note="Arachidonate 8-lipoxygenase"
FT BINDING 353
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 387
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:16162493"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:16162493"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:16162493"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:16162493"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:16162493"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:16162493"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:16162493"
FT BINDING 452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:16162493"
FT BINDING 454
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:16162493"
FT BINDING 757
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT BINDING 762
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT BINDING 943
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT BINDING 947
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT BINDING 1066
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT MUTAGEN 411
FT /note="D->A: Reduces stimulation of LOX-activity by calcium
FT and membrane binding. Abolishes stimulation of LOX-activity
FT by calcium and membrane binding; when associated with A-
FT 419."
FT /evidence="ECO:0000269|PubMed:16162493"
FT MUTAGEN 413
FT /note="W->A: Reduces stimulation of LOX-activity by calcium
FT and membrane binding."
FT /evidence="ECO:0000269|PubMed:16162493"
FT MUTAGEN 419
FT /note="E->A: Reduces stimulation of LOX-activity by calcium
FT and membrane binding. Abolishes stimulation of LOX-activity
FT by calcium and membrane binding; when associated with A-
FT 411."
FT /evidence="ECO:0000269|PubMed:16162493"
FT MUTAGEN 449
FT /note="W->A: Reduces LOX-activity in the absence of
FT membranes and increases activity in the presence of
FT liposomes. May alter protein structure."
FT /evidence="ECO:0000269|PubMed:16162493"
FT HELIX 7..15
FT /evidence="ECO:0007829|PDB:1U5U"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:1U5U"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:1U5U"
FT HELIX 38..59
FT /evidence="ECO:0007829|PDB:1U5U"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1U5U"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1U5U"
FT STRAND 69..79
FT /evidence="ECO:0007829|PDB:1U5U"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1U5U"
FT STRAND 96..107
FT /evidence="ECO:0007829|PDB:1U5U"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1U5U"
FT STRAND 117..128
FT /evidence="ECO:0007829|PDB:1U5U"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:1U5U"
FT HELIX 147..153
FT /evidence="ECO:0007829|PDB:1U5U"
FT HELIX 160..166
FT /evidence="ECO:0007829|PDB:1U5U"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:1U5U"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:1U5U"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1U5U"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1U5U"
FT STRAND 207..219
FT /evidence="ECO:0007829|PDB:1U5U"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:1U5U"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:1U5U"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:1U5U"
FT HELIX 253..264
FT /evidence="ECO:0007829|PDB:1U5U"
FT STRAND 267..277
FT /evidence="ECO:0007829|PDB:1U5U"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:1U5U"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:1U5U"
FT STRAND 301..311
FT /evidence="ECO:0007829|PDB:1U5U"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:1U5U"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:1U5U"
FT HELIX 344..362
FT /evidence="ECO:0007829|PDB:1U5U"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:1U5U"
FT STRAND 374..382
FT /evidence="ECO:0007829|PDB:3FG1"
FT STRAND 394..400
FT /evidence="ECO:0007829|PDB:3FG1"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:3FG1"
FT STRAND 423..431
FT /evidence="ECO:0007829|PDB:3FG1"
FT STRAND 434..443
FT /evidence="ECO:0007829|PDB:3FG1"
FT STRAND 455..464
FT /evidence="ECO:0007829|PDB:3FG1"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:3FG4"
FT STRAND 471..485
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 499..515
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 534..536
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 539..541
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 545..568
FT /evidence="ECO:0007829|PDB:3FG1"
FT TURN 569..571
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 577..584
FT /evidence="ECO:0007829|PDB:3FG1"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:3FG1"
FT TURN 594..600
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 602..611
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 632..635
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 636..638
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 645..651
FT /evidence="ECO:0007829|PDB:3FG1"
FT STRAND 654..658
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 660..662
FT /evidence="ECO:0007829|PDB:3FG1"
FT STRAND 698..703
FT /evidence="ECO:0007829|PDB:3FG1"
FT STRAND 709..719
FT /evidence="ECO:0007829|PDB:3FG1"
FT STRAND 721..724
FT /evidence="ECO:0007829|PDB:2FNQ"
FT HELIX 734..754
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 755..761
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 762..775
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 781..790
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 793..803
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 810..814
FT /evidence="ECO:0007829|PDB:3FG1"
FT TURN 816..820
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 821..830
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 835..838
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 840..846
FT /evidence="ECO:0007829|PDB:3FG1"
FT TURN 852..854
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 859..882
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 886..891
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 893..905
FT /evidence="ECO:0007829|PDB:3FG1"
FT STRAND 911..913
FT /evidence="ECO:0007829|PDB:2FNQ"
FT HELIX 925..939
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 941..947
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 950..954
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 957..959
FT /evidence="ECO:0007829|PDB:3FG1"
FT STRAND 970..973
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 977..983
FT /evidence="ECO:0007829|PDB:3FG1"
FT HELIX 987..1000
FT /evidence="ECO:0007829|PDB:3FG1"
FT STRAND 1009..1011
FT /evidence="ECO:0007829|PDB:2FNQ"
FT HELIX 1021..1046
FT /evidence="ECO:0007829|PDB:3FG1"
FT STRAND 1048..1050
FT /evidence="ECO:0007829|PDB:3FG4"
FT HELIX 1057..1059
FT /evidence="ECO:0007829|PDB:3FG1"
FT STRAND 1060..1063
FT /evidence="ECO:0007829|PDB:3FG1"
SQ SEQUENCE 1066 AA; 121783 MW; DD26886BD1EE95D7 CRC64;
MTWKNFGFEI FGEKYGQEEL EKRIKDEHTP PPDSPVFGGL KLKLKKEKFK TLFTLGTTLK
GFRRATHTVG TGGIGEITIV NDPKFPEHEF FTAGRTFPAR LRHANLKYPD DAGADARSFS
IKFADSDSDG PLDIVMNTGE ANIFWNSPSL EDFVPVEEGD AAEEYVYKNP YYYYNLVEAL
RRAPDTFAHL YYYSQVTMPF KAKDGKVRYC RYRALPGDVD IKEEDESGRL TEEEQRKIWI
FSRHENEKRP DDYLRKEYVE RLQKGPVNYR LQIQIHEASP DDTATIFHAG ILWDKETHPW
FDLAKVSIKT PLSPDVLEKT AFNIANQPAS LGLLEAKSPE DYNSIGELRV AVYTWVQHLR
KLKIGSLVPA GQNAIYNVEV ETGDREHAGT DATITIRITG AKGRTDYLKL DKWFHNDFEA
GSKEQYTVQG FDVGDIQLIE LHSDGGGYWS GDPDWFVNRV IIISSTQDRV YSFPCFRWVI
KDMVLFPGEA TLPFNEVPAI VSEQRQKELE QRKLTYQWDY VSDDMPGNIK AKTHDDLPRD
VQFTDEKSRS YQESRKAALV NLGIGSLFTM FENWDSYDDY HILYRNWILG GTPNMADRWH
EDRWFGYQFL NGANPVILTR CDALPSNFPV TNEHVNASLD RGKNLDEEIK DGHIYIVDFK
VLVGAKSYGG PVLEDIGYKV PDHLKHDEAD IRYCAAPLAL FYVNKLGHLM PIAIQINQEP
GPENPIWTPH EENEHDWMMA KFWLGVAESN FHQLNTHLLR THLTTESFAL STWRNLASAH
PVFKLLQPHI YGVLAIDTIG RKELIGSGGI VDQSLSLGGG GHVTFMEKCF KEVNLQDYHL
PNALKKRGVD DPSKLPGFYY RDDGLALWEA IETFIGEIIA IFYKNDDDVK RDNEIQSWIY
DVHKNGWRVN PGHQDHGVPA SFESREQLKE VLTSLVFTFS CQHAAVNFSQ KDHYGFTPNA
PAVLRHPPPK KKGEATLQSI LSTLPSKSQA AKAIATVYIL TKFSEDERYL GNYSATAWED
KDALDAINRF QDKLEDISKK IKQRNENLEV PYIYLLPERI PNGTAI
