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 28-JUN-2023, entry version 120. 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; Malacalcyonacea; OC 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}. 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; 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 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:0034440; P:lipid oxidation; IEA:InterPro. DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW. DR CDD; cd08151; AOS; 1. DR Gene3D; 3.10.450.60; -; 1. DR Gene3D; 2.40.180.10; Catalase core domain; 1. 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; LIPOXYGENASE; 1. DR PANTHER; PTHR11771:SF153; LIPOXYGENASE DOMAIN-CONTAINING PROTEIN; 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; SSF56634; Heme-dependent catalase-like; 1. DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1. DR SUPFAM; SSF48484; Lipoxigenase; 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 FT A-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 FT A-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 //