ID KASM_ARATH Reviewed; 461 AA. AC Q8L3X9; Q9SJB7; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 139. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial {ECO:0000303|PubMed:28202596}; DE EC=2.3.1.41 {ECO:0000269|PubMed:28202596}; DE AltName: Full=Beta-ketoacyl-ACP synthase {ECO:0000303|PubMed:14660674}; DE AltName: Full=mtKAS {ECO:0000303|PubMed:17616510}; DE Flags: Precursor; GN Name=KAS {ECO:0000303|PubMed:17616510}; GN OrderedLocusNames=At2g04540 {ECO:0000312|Araport:AT2G04540}; GN ORFNames=T1O3.5 {ECO:0000312|EMBL:AAD25826.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RC STRAIN=cv. Columbia; RX PubMed=14660674; DOI=10.1074/jbc.m308894200; RA Yasuno R., von Wettstein-Knowles P., Wada H.; RT "Identification and molecular characterization of the beta-ketoacyl-[acyl RT carrier-protein] synthase component of the Arabidopsis mitochondrial fatty RT acid synthase."; RL J. Biol. Chem. 279:8242-8251(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."; RL Nature 402:761-768(1999). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=17616510; DOI=10.1104/pp.107.104000; RA Ewald R., Kolukisaoglu U., Bauwe U., Mikkat S., Bauwe H.; RT "Mitochondrial protein lipoylation does not exclusively depend on the mtKAS RT pathway of de novo fatty acid synthesis in Arabidopsis."; RL Plant Physiol. 145:41-48(2007). RN [6] RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, PATHWAY, RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY. RC STRAIN=cv. Columbia; RX PubMed=28202596; DOI=10.1104/pp.16.01732; RA Guan X., Okazaki Y., Lithio A., Li L., Zhao X., Jin H., Nettleton D., RA Saito K., Nikolau B.J.; RT "Discovery and characterization of the 3-hydroxyacyl-ACP dehydratase RT component of the plant mitochondrial fatty acid synthase system."; RL Plant Physiol. 173:2010-2028(2017). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 31-461, AND SUBUNIT. RX PubMed=15527780; DOI=10.1016/j.febslet.2004.10.007; RA Olsen J.G., Rasmussen A.V., von Wettstein-Knowles P., Henriksen A.; RT "Structure of the mitochondrial beta-ketoacyl-[acyl carrier-protein] RT synthase from Arabidopsis and its role in fatty acid synthesis."; RL FEBS Lett. 577:170-174(2004). CC -!- FUNCTION: Catalyzes all the condensation reaction of fatty acid CC synthesis by the addition to an acyl acceptor of two carbons from CC malonyl-ACP (PubMed:17616510, PubMed:28202596). Able to elongate CC saturated acyl chains from 4 to at least 16 carbons (PubMed:17616510, CC PubMed:28202596). Uses malonyl-CoA but not acetyl-CoA as primer CC substrate (PubMed:17616510). When expressed in a heterologous system, CC reveals a bimodal distribution of products, with peaks at C8 and C14- CC C16 (PubMed:17616510). The major product of the reaction (octanoyl-ACP) CC is required for the lipoylation of essential mitochondrial proteins CC (PubMed:17616510, PubMed:28202596). Required for mitochondrial fatty CC acid synthesis (mtFAS) (PubMed:28202596). MtFAS are essential for CC photorespiration and plant development, probably by influencing CC mitochondrial membrane lipid composition and other lipid metabolic CC pathways (PubMed:28202596). {ECO:0000269|PubMed:17616510, CC ECO:0000269|PubMed:28202596}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651; CC EC=2.3.1.41; Evidence={ECO:0000269|PubMed:28202596}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837; CC Evidence={ECO:0000305|PubMed:28202596}; CC -!- CATALYTIC ACTIVITY: CC Reaction=butanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxohexanoyl-[ACP] + CC CO2 + holo-[ACP]; Xref=Rhea:RHEA:41820, Rhea:RHEA-COMP:9623, CC Rhea:RHEA-COMP:9628, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9685, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78454, ChEBI:CHEBI:78456; CC Evidence={ECO:0000269|PubMed:28202596}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41821; CC Evidence={ECO:0000305|PubMed:28202596}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + hexanoyl-[ACP] + malonyl-[ACP] = 3-oxooctanoyl-[ACP] + CC CO2 + holo-[ACP]; Xref=Rhea:RHEA:41836, Rhea:RHEA-COMP:9623, CC Rhea:RHEA-COMP:9632, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9685, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78459, ChEBI:CHEBI:78460; CC Evidence={ECO:0000269|PubMed:28202596}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41837; CC Evidence={ECO:0000305|PubMed:28202596}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + malonyl-[ACP] + octanoyl-[ACP] = 3-oxodecanoyl-[ACP] + CC CO2 + holo-[ACP]; Xref=Rhea:RHEA:41852, Rhea:RHEA-COMP:9623, CC Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9685, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78463, ChEBI:CHEBI:78464; CC Evidence={ECO:0000269|PubMed:28202596}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41853; CC Evidence={ECO:0000305|PubMed:28202596}; CC -!- CATALYTIC ACTIVITY: CC Reaction=decanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxododecanoyl-[ACP] CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41868, Rhea:RHEA-COMP:9623, CC Rhea:RHEA-COMP:9640, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9685, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78468, ChEBI:CHEBI:78469; CC Evidence={ECO:0000269|PubMed:28202596}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41869; CC Evidence={ECO:0000305|PubMed:28202596}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dodecanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxotetradecanoyl- CC [ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41884, Rhea:RHEA-COMP:9623, CC Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9685, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, CC ChEBI:CHEBI:65264, ChEBI:CHEBI:78449, ChEBI:CHEBI:78473; CC Evidence={ECO:0000269|PubMed:28202596}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41885; CC Evidence={ECO:0000305|PubMed:28202596}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + malonyl-[ACP] + tetradecanoyl-[ACP] = 3- CC oxohexadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41900, CC Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9649, CC Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78477, CC ChEBI:CHEBI:78478; Evidence={ECO:0000269|PubMed:28202596}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901; CC Evidence={ECO:0000305|PubMed:28202596}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + hexadecanoyl-[ACP] + malonyl-[ACP] = 3-oxooctadecanoyl- CC [ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41916, Rhea:RHEA-COMP:9623, CC Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9653, Rhea:RHEA-COMP:9685, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78483, ChEBI:CHEBI:78487; CC Evidence={ECO:0000269|PubMed:28202596}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41917; CC Evidence={ECO:0000305|PubMed:28202596}; CC -!- ACTIVITY REGULATION: Inhibited by cerulenin. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=19.1 uM for butanoyl-[ACP] {ECO:0000269|PubMed:28202596}; CC KM=8 uM for hexanoyl-[ACP] {ECO:0000269|PubMed:28202596}; CC KM=22.9 uM for octanoyl-[ACP] {ECO:0000269|PubMed:28202596}; CC KM=14.1 uM for decanoyl-[ACP] {ECO:0000269|PubMed:28202596}; CC KM=25.6 uM for dodecanoyl-[ACP] {ECO:0000269|PubMed:28202596}; CC KM=14 uM for tetradecanoyl-[ACP] {ECO:0000269|PubMed:28202596}; CC KM=8.2 uM for hexadecanoyl-[ACP] {ECO:0000269|PubMed:28202596}; CC Vmax=144.7 umol/min/mg enzyme with butanoyl-[ACP] as substrate CC {ECO:0000269|PubMed:28202596}; CC Vmax=193.1 umol/min/mg enzyme with hexanoyl-[ACP] as substrate CC {ECO:0000269|PubMed:28202596}; CC Vmax=444.1 umol/min/mg enzyme with octanoyl-[ACP] as substrate CC {ECO:0000269|PubMed:28202596}; CC Vmax=237.4 umol/min/mg enzyme with decanoyl-[ACP] as substrate CC {ECO:0000269|PubMed:28202596}; CC Vmax=317.6 umol/min/mg enzyme with dodecanoyl-[ACP] as substrate CC {ECO:0000269|PubMed:28202596}; CC Vmax=340.8 umol/min/mg enzyme with tetradecanoyl-[ACP] as substrate CC {ECO:0000269|PubMed:28202596}; CC Vmax=359.9 umol/min/mg enzyme with hexadecanoyl-[ACP] as substrate CC {ECO:0000269|PubMed:28202596}; CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000269|PubMed:28202596}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15527780}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14660674}. CC -!- TISSUE SPECIFICITY: Expressed at the same level in leaves, roots, CC siliques and flowers. {ECO:0000269|PubMed:14660674, CC ECO:0000269|PubMed:28202596}. CC -!- DISRUPTION PHENOTYPE: Slow growth and bleached leaf phenotype when CC grown under ambient air, but normal growth under CO(2)-enriched air CC (PubMed:17616510, PubMed:28202596). Thicker leaves due to enlarged CC mesophyll cells when grown in ambient air and associated with altered CC thylakoid membrane assembly and starch granule ultrastructure; these CC phenotypes are partly reversed when grown in 1 percent CO(2) atmosphere CC (PubMed:28202596). Highly prevents lipoylation of the H-protein subunit CC of the glycine decarboxylase (GDC) in leaves, but has only a limited CC effect on the lipoylation of the E2 subunits of pyruvate dehydrogenase CC (PDH) and alpha-ketoacid dehydrogenase (KGDH) complexes in leaves and CC even no effect in roots (PubMed:17616510, PubMed:28202596). Depleted 3- CC hydroxytetradecanoic acid levels (PubMed:28202596). CC {ECO:0000269|PubMed:17616510, ECO:0000269|PubMed:28202596}. CC -!- MISCELLANEOUS: Mitochondrial protein lipoylation in leaves does not CC exclusively depend on the lipoate biosynthesis by KAS and may occur CC independently of this pathway in roots. {ECO:0000305|PubMed:17616510}. CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP CC synthases family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD25826.1; Type=Erroneous gene model prediction; Evidence={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; AB073746; BAB91181.1; -; mRNA. DR EMBL; AC006951; AAD25826.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002685; AEC05844.1; -; Genomic_DNA. DR EMBL; AY099587; AAM20439.1; -; mRNA. DR EMBL; AY128832; AAM91232.1; -; mRNA. DR PIR; F84458; F84458. DR RefSeq; NP_178533.2; NM_126485.4. DR PDB; 1W0I; X-ray; 2.10 A; A/B=31-461. DR PDB; 2IX4; X-ray; 1.95 A; A/B=31-461. DR PDBsum; 1W0I; -. DR PDBsum; 2IX4; -. DR AlphaFoldDB; Q8L3X9; -. DR SMR; Q8L3X9; -. DR STRING; 3702.Q8L3X9; -. DR iPTMnet; Q8L3X9; -. DR PaxDb; 3702-AT2G04540-1; -. DR ProteomicsDB; 232273; -. DR EnsemblPlants; AT2G04540.1; AT2G04540.1; AT2G04540. DR GeneID; 814996; -. DR Gramene; AT2G04540.1; AT2G04540.1; AT2G04540. DR KEGG; ath:AT2G04540; -. DR Araport; AT2G04540; -. DR TAIR; AT2G04540; MTKAS. DR eggNOG; KOG1394; Eukaryota. DR HOGENOM; CLU_000022_69_2_1; -. DR InParanoid; Q8L3X9; -. DR OMA; ESTICPV; -. DR OrthoDB; 546841at2759; -. DR PhylomeDB; Q8L3X9; -. DR BioCyc; ARA:AT2G04540-MONOMER; -. DR BioCyc; MetaCyc:AT2G04540-MONOMER; -. DR BRENDA; 2.3.1.41; 399. DR UniPathway; UPA00094; -. DR EvolutionaryTrace; Q8L3X9; -. DR PRO; PR:Q8L3X9; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; Q8L3X9; baseline and differential. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0010027; P:thylakoid membrane organization; IMP:TAIR. DR CDD; cd00834; KAS_I_II; 1. DR Gene3D; 3.40.47.10; -; 2. DR InterPro; IPR017568; 3-oxoacyl-ACP_synth-2. DR InterPro; IPR000794; Beta-ketoacyl_synthase. DR InterPro; IPR018201; Ketoacyl_synth_AS. DR InterPro; IPR014031; Ketoacyl_synth_C. DR InterPro; IPR014030; Ketoacyl_synth_N. DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom. DR InterPro; IPR016039; Thiolase-like. DR NCBIfam; TIGR03150; fabF; 1. DR PANTHER; PTHR11712:SF336; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR11712; POLYKETIDE SYNTHASE-RELATED; 1. DR Pfam; PF00109; ketoacyl-synt; 1. DR Pfam; PF02801; Ketoacyl-synt_C; 1. DR PIRSF; PIRSF000447; KAS_II; 1. DR SMART; SM00825; PKS_KS; 1. DR SUPFAM; SSF53901; Thiolase-like; 2. DR PROSITE; PS00606; KS3_1; 1. DR PROSITE; PS52004; KS3_2; 1. DR Genevisible; Q8L3X9; AT. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Mitochondrion; KW Reference proteome; Transferase; Transit peptide. FT TRANSIT 1..28 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 29..461 FT /note="3-oxoacyl-[acyl-carrier-protein] synthase, FT mitochondrial" FT /id="PRO_0000000588" FT DOMAIN 30..460 FT /note="Ketosynthase family 3 (KS3)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 209 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 350 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 389 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT STRAND 33..42 FT /evidence="ECO:0007829|PDB:2IX4" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 48..56 FT /evidence="ECO:0007829|PDB:2IX4" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 67..70 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 77..85 FT /evidence="ECO:0007829|PDB:2IX4" FT STRAND 91..93 FT /evidence="ECO:0007829|PDB:2IX4" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 106..109 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 117..132 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 140..144 FT /evidence="ECO:0007829|PDB:2IX4" FT STRAND 146..154 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 157..168 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 172..174 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 179..183 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 187..196 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 208..210 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 211..225 FT /evidence="ECO:0007829|PDB:2IX4" FT STRAND 229..237 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 242..250 FT /evidence="ECO:0007829|PDB:2IX4" FT TURN 257..260 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 262..264 FT /evidence="ECO:0007829|PDB:2IX4" FT STRAND 281..289 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 290..295 FT /evidence="ECO:0007829|PDB:2IX4" FT STRAND 302..311 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 324..337 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 341..343 FT /evidence="ECO:0007829|PDB:2IX4" FT STRAND 346..348 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 355..369 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 371..374 FT /evidence="ECO:0007829|PDB:2IX4" FT STRAND 378..381 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 384..387 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 391..393 FT /evidence="ECO:0007829|PDB:2IX4" FT HELIX 394..408 FT /evidence="ECO:0007829|PDB:2IX4" FT STRAND 418..420 FT /evidence="ECO:0007829|PDB:2IX4" FT STRAND 426..428 FT /evidence="ECO:0007829|PDB:2IX4" FT STRAND 440..448 FT /evidence="ECO:0007829|PDB:2IX4" FT TURN 449..451 FT /evidence="ECO:0007829|PDB:2IX4" FT STRAND 452..459 FT /evidence="ECO:0007829|PDB:2IX4" SQ SEQUENCE 461 AA; 49379 MW; D9B02B19F5A5FB45 CRC64; MATSNLRRHL SASRLRLNRF ISTSSSYHSH RRVVVTGLGM VTPLGRGVET TWRRLIDGEC GIRGLTLDDL KMKSFDEETK LYTFDQLSSK VAAFVPYGSN PGEFDEALWL NSKAVANFIG YAVCAADEAL RDAEWLPTEE EEKERTGVSI GGGIGSICDI VEAAQLICEK RLRRLSPFFI PKILVNMASG HVSMKYGFQG PNHAAVTACA TGAHSIGDAT RMIQFGDADV MVAGGTESSI DALSVAGFSR SRALSTKFNS SPQEASRPFD CDRDGFVIGE GSGVIVLEEY EHAKRRGAKI YAELCGYGMS GDAHHITQPP EDGKGAVLAM TRALRQSGLC PNQIDYVNAH ATSTPIGDAV EARAIKTVFS EHATSGTLAF SSTKGATGHL LGAAGAVEAI FSILAIHHGV APMTLNVKNP DPIFDKRFMP LTTSKKMLVR TAMSNSFGFG GTNASLLFAS I //