ID LOX2_ARATH Reviewed; 896 AA. AC P38418; Q0WLR8; Q56WG6; Q8GW45; Q8W4E4; Q9M1U5; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 24-JAN-2024, entry version 186. DE RecName: Full=Lipoxygenase 2, chloroplastic; DE Short=AtLOX2; DE EC=1.13.11.12 {ECO:0000269|PubMed:18949503}; DE Flags: Precursor; GN Name=LOX2; OrderedLocusNames=At3g45140; ORFNames=T14D3.80; 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]. RX PubMed=8290626; DOI=10.1104/pp.103.4.1133; RA Bell E., Mullet J.E.; RT "Characterization of an Arabidopsis lipoxygenase gene responsive to methyl RT jasmonate and wounding."; RL Plant Physiol. 103:1133-1137(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."; RL Nature 408:820-822(2000). 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-125. RC STRAIN=cv. Columbia; RX PubMed=11910074; DOI=10.1126/science.1071006; RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., RA Shinagawa A., Shinozaki K.; RT "Functional annotation of a full-length Arabidopsis cDNA collection."; RL Science 296:141-145(2002). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 454-896. RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., RA Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [7] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=7567995; DOI=10.1073/pnas.92.19.8675; RA Bell E., Creelman R.A., Mullet J.E.; RT "A chloroplast lipoxygenase is required for wound-induced jasmonic acid RT accumulation in Arabidopsis."; RL Proc. Natl. Acad. Sci. U.S.A. 92:8675-8679(1995). RN [8] RP INDUCTION BY WOUNDING. RX PubMed=11090221; DOI=10.1105/tpc.12.11.2237; RA Wang C., Zien C.A., Afitlhile M., Welti R., Hildebrand D.F., Wang X.; RT "Involvement of phospholipase D in wound-induced accumulation of jasmonic RT acid in arabidopsis."; RL Plant Cell 12:2237-2246(2000). RN [9] RP INTERACTION WITH EIF4E2, AND SUBCELLULAR LOCATION. RX PubMed=11117257; DOI=10.1023/a:1006494628892; RA Freire M.A., Tourneur C., Granier F., Camonis J., El Amrani A., RA Browning K.S., Robaglia C.; RT "Plant lipoxygenase 2 is a translation initiation factor-4E-binding RT protein."; RL Plant Mol. Biol. 44:129-140(2000). RN [10] RP INDUCTION BY APHIDS AND WOUNDING. RX PubMed=11161062; DOI=10.1104/pp.125.2.1074; RA Moran P.J., Thompson G.A.; RT "Molecular responses to aphid feeding in Arabidopsis in relation to plant RT defense pathways."; RL Plant Physiol. 125:1074-1085(2001). RN [11] RP INDUCTION BY JASMONATE. RX PubMed=11874572; DOI=10.1046/j.0960-7412.2001.01241.x; RA Jensen A.B., Raventos D., Mundy J.; RT "Fusion genetic analysis of jasmonate-signalling mutants in Arabidopsis."; RL Plant J. 29:595-606(2002). RN [12] RP DEVELOPMENTAL STAGE. RX PubMed=11891244; DOI=10.1104/pp.010843; RA He Y., Fukushige H., Hildebrand D.F., Gan S.; RT "Evidence supporting a role of jasmonic acid in Arabidopsis leaf RT senescence."; RL Plant Physiol. 128:876-884(2002). RN [13] RP INDUCTION BY NITRIC OXIDE. RX PubMed=14716563; DOI=10.1007/s00425-003-1178-1; RA Huang X., Stettmaier K., Michel C., Hutzler P., Mueller M.J., Durner J.; RT "Nitric oxide is induced by wounding and influences jasmonic acid signaling RT in Arabidopsis thaliana."; RL Planta 218:938-946(2004). RN [14] RP INDUCTION BY LEAF VOLATILES. RX PubMed=15879447; DOI=10.1093/pcp/pci122; RA Kishimoto K., Matsui K., Ozawa R., Takabayashi J.; RT "Volatile C6-aldehydes and allo-ocimene activate defense genes and induce RT resistance against Botrytis cinerea in Arabidopsis thaliana."; RL Plant Cell Physiol. 46:1093-1102(2005). RN [15] RP INDUCTION BY MYZUS PERSICAE AND BREVICORYNE BRASSICAE. RX PubMed=17545220; DOI=10.1093/jxb/erm043; RA Kusnierczyk A., Winge P., Midelfart H., Armbruster W.S., Rossiter J.T., RA Bones A.M.; RT "Transcriptional responses of Arabidopsis thaliana ecotypes with different RT glucosinolate profiles after attack by polyphagous Myzus persicae and RT oligophagous Brevicoryne brassicae."; RL J. Exp. Bot. 58:2537-2552(2007). RN [16] RP INDUCTION BY BACTERIAL PATHOGENS. RX PubMed=17313166; DOI=10.1094/mpmi-20-2-0146; RA Jakob K., Kniskern J.M., Bergelson J.; RT "The role of pectate lyase and the jasmonic acid defense response in RT Pseudomonas viridiflava virulence."; RL Mol. Plant Microbe Interact. 20:146-158(2007). RN [17] RP TISSUE SPECIFICITY. RX PubMed=17369372; DOI=10.1105/tpc.106.046052; RA Vellosillo T., Martinez M., Lopez M.A., Vicente J., Cascon T., Dolan L., RA Hamberg M., Castresana C.; RT "Oxylipins produced by the 9-lipoxygenase pathway in Arabidopsis regulate RT lateral root development and defense responses through a specific signaling RT cascade."; RL Plant Cell 19:831-846(2007). RN [18] RP REPRESSION BY WRKY62. RX PubMed=17510065; DOI=10.1093/pcp/pcm058; RA Mao P., Duan M., Wei C., Li Y.; RT "WRKY62 transcription factor acts downstream of cytosolic NPR1 and RT negatively regulates jasmonate-responsive gene expression."; RL Plant Cell Physiol. 48:833-842(2007). RN [19] RP INDUCTION BY CATERPILLAR. RX PubMed=18487634; DOI=10.1093/jxb/ern108; RA Weech M.-H., Chapleau M., Pan L., Ide C., Bede J.C.; RT "Caterpillar saliva interferes with induced Arabidopsis thaliana defence RT responses via the systemic acquired resistance pathway."; RL J. Exp. Bot. 59:2437-2448(2008). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. RX PubMed=18431481; DOI=10.1371/journal.pone.0001994; RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., RA van Wijk K.J.; RT "Sorting signals, N-terminal modifications and abundance of the chloroplast RT proteome."; RL PLoS ONE 3:E1994-E1994(2008). RN [21] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=18949503; DOI=10.1007/s11745-008-3245-7; RA Bannenberg G., Martinez M., Hamberg M., Castresana C.; RT "Diversity of the enzymatic activity in the lipoxygenase gene family of RT Arabidopsis thaliana."; RL Lipids 44:85-95(2009). CC -!- FUNCTION: 13S-lipoxygenase that can use linolenic acid as substrates. CC Plant lipoxygenases may be involved in a number of diverse aspects of CC plant physiology including growth and development, pest resistance, and CC senescence or responses to wounding. Catalyzes the hydroperoxidation of CC lipids containing a cis,cis-1,4-pentadiene structure. Required for the CC wound-induced synthesis of jasmonic acid (JA) in leaves. CC {ECO:0000269|PubMed:18949503, ECO:0000269|PubMed:7567995}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)- CC octadecadienoate; Xref=Rhea:RHEA:22780, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:30245, ChEBI:CHEBI:57466; EC=1.13.11.12; CC Evidence={ECO:0000269|PubMed:18949503}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22781; CC Evidence={ECO:0000269|PubMed:18949503}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (13S)-hydroperoxy- CC (9Z,11E,15Z)-octadecatrienoate; Xref=Rhea:RHEA:34495, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:58757; CC EC=1.13.11.12; Evidence={ECO:0000269|PubMed:18949503}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34496; CC Evidence={ECO:0000269|PubMed:18949503}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00726}; CC Note=Binds 1 Fe cation per subunit. Iron is tightly bound. CC {ECO:0000255|PROSITE-ProRule:PRU00726}; CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE- CC ProRule:PRU00726}. CC -!- SUBUNIT: Interacts with EIF4E2. {ECO:0000269|PubMed:11117257}. CC -!- INTERACTION: CC P38418; O04663: EIF(ISO)4E; NbExp=7; IntAct=EBI-1770437, EBI-1770425; CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast CC {ECO:0000269|PubMed:18431481}. Cytoplasm. Note=The unprocessed form is CC cytoplasmic whereas the cleaved form is chloroplastic. CC -!- TISSUE SPECIFICITY: In leaves and inflorescences but not abundant in CC seeds, roots and stems. {ECO:0000269|PubMed:17369372}. CC -!- DEVELOPMENTAL STAGE: Expression is sharply reduced in leaves during CC leaf senescence. {ECO:0000269|PubMed:11891244}. CC -!- INDUCTION: By methyl jasmonate (MeJA) and wounding, probably through CC nitric oxide-mediated (NO) induction. Slightly locally induced upon CC herbivors infestation such as aphids (Myzus persicae and Brevicoryne CC brassicae), or caterpillar (Spodoptera exigua). Induced by leaf- CC volatiles generated by herbivors-mediated wounding such as (E)-2- CC hexenal, (Z)-3-hexenal, (Z)-3-hexenol or allo-ocimene (2,6- CC dimethyl-2,4,6-octatriene). Increased levels by bacterial pathogens CC (e.g. P.viridiflava and P.syringae pv. tomato). Repressed by WRKY62. CC {ECO:0000269|PubMed:11090221, ECO:0000269|PubMed:11161062, CC ECO:0000269|PubMed:11874572, ECO:0000269|PubMed:14716563, CC ECO:0000269|PubMed:15879447, ECO:0000269|PubMed:17313166, CC ECO:0000269|PubMed:17510065, ECO:0000269|PubMed:17545220, CC ECO:0000269|PubMed:18487634}. CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB72152.1; 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; L23968; AAA32749.1; -; mRNA. DR EMBL; AL138649; CAB72152.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002686; AEE77997.1; -; Genomic_DNA. DR EMBL; AY062611; AAL32689.1; -; mRNA. DR EMBL; AK119093; BAC43666.1; -; mRNA. DR EMBL; AK222075; BAD94917.1; -; mRNA. DR EMBL; AK230124; BAF01939.1; -; mRNA. DR PIR; JQ2391; JQ2391. DR PIR; T47454; T47454. DR RefSeq; NP_566875.1; NM_114383.3. DR AlphaFoldDB; P38418; -. DR SMR; P38418; -. DR BioGRID; 8970; 5. DR IntAct; P38418; 4. DR STRING; 3702.P38418; -. DR iPTMnet; P38418; -. DR PaxDb; 3702-AT3G45140-1; -. DR ProteomicsDB; 238417; -. DR EnsemblPlants; AT3G45140.1; AT3G45140.1; AT3G45140. DR GeneID; 823650; -. DR Gramene; AT3G45140.1; AT3G45140.1; AT3G45140. DR KEGG; ath:AT3G45140; -. DR Araport; AT3G45140; -. DR TAIR; AT3G45140; LOX2. DR eggNOG; ENOG502QQSP; Eukaryota. DR HOGENOM; CLU_004282_0_0_1; -. DR InParanoid; P38418; -. DR OrthoDB; 462210at2759; -. DR PhylomeDB; P38418; -. DR BioCyc; ARA:AT3G45140-MONOMER; -. DR BioCyc; MetaCyc:AT3G45140-MONOMER; -. DR BRENDA; 1.13.11.12; 399. DR UniPathway; UPA00382; -. DR PRO; PR:P38418; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; P38418; baseline and differential. DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB. DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR. DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR. DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; HDA:TAIR. DR GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003729; F:mRNA binding; IDA:TAIR. DR GO; GO:1901149; F:salicylic acid binding; HDA:TAIR. DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IMP:TAIR. DR GO; GO:0009695; P:jasmonic acid biosynthetic process; IMP:TAIR. DR GO; GO:0034440; P:lipid oxidation; IDA:TAIR. DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB. DR GO; GO:0009620; P:response to fungus; IEP:TAIR. DR GO; GO:0080027; P:response to herbivore; IEP:UniProtKB. DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR. DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB. DR CDD; cd01751; PLAT_LH2; 1. DR Gene3D; 3.10.450.60; -; 1. DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1. 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; IPR001246; LipOase_plant. DR InterPro; IPR042057; Lipoxy_PLAT/LH2. DR InterPro; IPR027433; Lipoxygenase_dom_3. DR InterPro; IPR001024; PLAT/LH2_dom. DR InterPro; IPR036392; PLAT/LH2_dom_sf. DR PANTHER; PTHR11771; LIPOXYGENASE; 1. DR PANTHER; PTHR11771:SF89; LIPOXYGENASE 2, CHLOROPLASTIC; 1. DR Pfam; PF00305; Lipoxygenase; 1. DR Pfam; PF01477; PLAT; 1. DR PRINTS; PR00087; LIPOXYGENASE. DR PRINTS; PR00468; PLTLPOXGNASE. DR SMART; SM00308; LH2; 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. DR SWISS-2DPAGE; P38418; -. DR Genevisible; P38418; AT. PE 1: Evidence at protein level; KW Chloroplast; Cytoplasm; Dioxygenase; Fatty acid biosynthesis; KW Fatty acid metabolism; Iron; Lipid biosynthesis; Lipid metabolism; KW Metal-binding; Oxidoreductase; Oxylipin biosynthesis; Plastid; KW Reference proteome; Transit peptide. FT TRANSIT 1..56 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 57..896 FT /note="Lipoxygenase 2, chloroplastic" FT /id="PRO_0000018326" FT DOMAIN 79..199 FT /note="PLAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152" FT DOMAIN 202..896 FT /note="Lipoxygenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT REGION 175..232 FT /note="EIF4E2 binding" FT BINDING 554 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 559 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 746 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 750 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 896 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT CONFLICT 119..125 FT /note="ITVEDYA -> EYTFFFL (in Ref. 5; BAC43666)" FT /evidence="ECO:0000305" FT CONFLICT 613 FT /note="W -> C (in Ref. 4; AAL32689)" FT /evidence="ECO:0000305" FT CONFLICT 646 FT /note="L -> V (in Ref. 6; BAF01939)" FT /evidence="ECO:0000305" FT CONFLICT 731 FT /note="L -> F (in Ref. 6; BAF01939)" FT /evidence="ECO:0000305" SQ SEQUENCE 896 AA; 102046 MW; F32822205C8F9F22 CRC64; MYCRESLSSL QTLNVAKSLS SLFPKQSALI NPISAGRRNN LPRPNLRRRC KVTASRANIE QEGNTVKEPI QNIKVKGYIT AQEEFLEGIT WSRGLDDIAD IRGRSLLVEL ISAKTDQRIT VEDYAQRVWA EAPDEKYECE FEMPEDFGPV GAIKIQNQYH RQLFLKGVEL KLPGGSITFT CESWVAPKSV DPTKRIFFSD KSYLPSQTPE PLKKYRKEEL ETLQGKNREE VGEFTKFERI YDYDVYNDVG DPDNDPELAR PVIGGLTHPY PRRCKTGRKP CETDPSSEQR YGGEFYVPRD EEFSTAKGTS FTGKAVLAAL PSIFPQIESV LLSPQEPFPH FKAIQNLFEE GIQLPKDAGL LPLLPRIIKA LGEAQDDILQ FDAPVLINRD RFSWLRDDEF ARQTLAGLNP YSIQLVEEWP LISKLDPAVY GDPTSLITWE IVEREVKGNM TVDEALKNKR LFVLDYHDLL LPYVNKVREL NNTTLYASRT LFFLSDDSTL RPVAIELTCP PNINKPQWKQ VFTPGYDATS CWLWNLAKTH AISHDAGYHQ LISHWLRTHA CTEPYIIAAN RQLSAMHPIY RLLHPHFRYT MEINARARQS LVNGGGIIET CFWPGKYALE LSSAVYGKLW RFDQEGLPAD LIKRGLAEED KTAEHGVRLT IPDYPFANDG LILWDAIKEW VTDYVKHYYP DEELITSDEE LQGWWSEVRN IGHGDKKDEP WWPVLKTQDD LIGVVTTIAW VTSGHHAAVN FGQYGYGGYF PNRPTTTRIR MPTEDPTDEA LKEFYESPEK VLLKTYPSQK QATLVMVTLD LLSTHSPDEE YIGEQQEASW ANEPVINAAF ERFKGKLQYL EGVIDERNVN ITLKNRAGAG VVKYELLKPT SEHGVTGMGV PYSISI //