LOX1_ARATH
ID LOX1_ARATH Reviewed; 859 AA.
AC Q06327; Q9FZ30;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Linoleate 9S-lipoxygenase 1 {ECO:0000303|PubMed:17369372};
DE EC=1.13.11.58 {ECO:0000269|PubMed:18949503};
DE AltName: Full=Lipoxygenase 1 {ECO:0000303|PubMed:17369372};
DE Short=AtLOX1 {ECO:0000303|PubMed:18949503};
GN Name=LOX1 {ECO:0000303|PubMed:17369372};
GN OrderedLocusNames=At1g55020 {ECO:0000312|Araport:AT1G55020};
GN ORFNames=F14C21.3, F14C21.54, T24C10.13 {ECO:0000312|EMBL:AAG00881.1};
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], INDUCTION BY ABA; JA AND PATHOGEN, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=7506426; DOI=10.1104/pp.101.2.441;
RA Melan M.A., Dong X., Endara M.E., Davis K.R., Ausubel F.M., Peterman T.K.;
RT "An Arabidopsis thaliana lipoxygenase gene can be induced by pathogens,
RT abscisic acid, and methyl jasmonate.";
RL Plant Physiol. 101:441-450(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8305494; DOI=10.1016/0005-2760(94)90244-5;
RA Melan M.A., Nemhauser J.M., Peterman T.K.;
RT "Structure and sequence of the Arabidopsis thaliana lipoxygenase 1 gene.";
RL Biochim. Biophys. Acta 1210:377-380(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
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 [6]
RP TISSUE SPECIFICITY, INDUCTION BY LIGHT, AND DEVELOPMENTAL STAGE.
RX PubMed=12232208; DOI=10.1104/pp.105.1.385;
RA Melan M.A., Enriquez A.L.D., Peterman T.K.;
RT "The LOX1 gene of Arabidopsis is temporally and spatially regulated in
RT germinating seedlings.";
RL Plant Physiol. 105:385-393(1994).
RN [7]
RP TISSUE SPECIFICITY.
RA Peterman T.K., Rattigan E.M., Enriquez A., Melan M.A.;
RT "Immunological characterization of Arabidopsis thaliana lipoxygenase:
RT Expression of the LOX1 gene product in Escherichia coli and polyclonal
RT antibody production.";
RL Plant Physiol. Biochem. 32:443-450(1994).
RN [8]
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 [9]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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 [10]
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).
RN [11]
RP FUNCTION.
RX PubMed=21481031; DOI=10.1111/j.1365-313x.2011.04608.x;
RA Lopez M.A., Vicente J., Kulasekaran S., Vellosillo T., Martinez M.,
RA Irigoyen M.L., Cascon T., Bannenberg G., Hamberg M., Castresana C.;
RT "Antagonistic role of 9-lipoxygenase-derived oxylipins and ethylene in the
RT control of oxidative stress, lipid peroxidation and plant defence.";
RL Plant J. 67:447-458(2011).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22199234; DOI=10.1093/mp/ssr105;
RA Vicente J., Cascon T., Vicedo B., Garcia-Agustin P., Hamberg M.,
RA Castresana C.;
RT "Role of 9-lipoxygenase and alpha-dioxygenase oxylipin pathways as
RT modulators of local and systemic defense.";
RL Mol. Plant 5:914-928(2012).
RN [13]
RP FUNCTION.
RX PubMed=23314084; DOI=10.1016/j.plaphy.2012.12.005;
RA Keunen E., Remans T., Opdenakker K., Jozefczak M., Gielen H., Guisez Y.,
RA Vangronsveld J., Cuypers A.;
RT "A mutant of the Arabidopsis thaliana LIPOXYGENASE1 gene shows altered
RT signalling and oxidative stress related responses after cadmium exposure.";
RL Plant Physiol. Biochem. 63:272-280(2013).
RN [14]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23526882; DOI=10.1371/journal.pbio.1001513;
RA Montillet J.L., Leonhardt N., Mondy S., Tranchimand S., Rumeau D.,
RA Boudsocq M., Garcia A.V., Douki T., Bigeard J., Lauriere C., Chevalier A.,
RA Castresana C., Hirt H.;
RT "An abscisic acid-independent oxylipin pathway controls stomatal closure
RT and immune defense in Arabidopsis.";
RL PLoS Biol. 11:e1001513-e1001513(2013).
RN [15]
RP FUNCTION, INDUCTION BY FUSARIUM GRAMINEARUM, AND DISRUPTION PHENOTYPE.
RX PubMed=26075826; DOI=10.1094/mpmi-04-15-0096-r;
RA Nalam V.J., Alam S., Keereetaweep J., Venables B., Burdan D., Lee H.,
RA Trick H.N., Sarowar S., Makandar R., Shah J.;
RT "Facilitation of Fusarium graminearum infection by 9-lipoxygenases in
RT Arabidopsis and wheat.";
RL Mol. Plant Microbe Interact. 28:1142-1152(2015).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26417008; DOI=10.1104/pp.15.00992;
RA Marcos R., Izquierdo Y., Vellosillo T., Kulasekaran S., Cascon T.,
RA Hamberg M., Castresana C.;
RT "9-Lipoxygenase-derived oxylipins activate brassinosteroid signaling to
RT promote cell wall-based defense and limit pathogen infection.";
RL Plant Physiol. 169:2324-2334(2015).
RN [17]
RP FUNCTION.
RX PubMed=28371855; DOI=10.1093/pcp/pcx036;
RA Oenel A., Fekete A., Krischke M., Faul S.C., Gresser G., Havaux M.,
RA Mueller M.J., Berger S.;
RT "Enzymatic and non-enzymatic mechanisms contribute to lipid oxidation
RT during seed aging.";
RL Plant Cell Physiol. 58:925-933(2017).
CC -!- FUNCTION: 9S-lipoxygenase that can use linoleic acid or linolenic acid
CC as substrates. Plant lipoxygenases may be involved in a number of
CC diverse aspects of plant physiology including growth and development,
CC pest resistance, and senescence or responses to wounding. Catalyzes the
CC hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene
CC structure. Function as regulators of root development by controlling
CC the emergence of lateral roots (PubMed:17369372, PubMed:18949503). 9S-
CC lypoxygenase-derived oxylipins may play an antagonistic role to
CC ethylene signaling in the control of responses involving oxidative
CC stress, lipid peroxidation and plant defense (PubMed:21481031). LOX1-
CC derived oxylipins may be involved in stress signaling from roots to
CC shoots in response to cadmium exposure (PubMed:23314084). 9S-
CC lypoxygenase-derived oxylipins are engaged during infection to control
CC the balance between salicylic acid (SA) and jasmonate (JA) signaling to
CC facilitate infection by the fungal pathogen Fusarium graminearum
CC (PubMed:26075826). 9S-lypoxygenase-derived oxylipins activate
CC brassinosteroid signaling to promote cell wall-based defense and limit
CC pathogen infection (PubMed:26417008). The LOX1-derived compound (9S)-
CC hydroperoxy-(10E,12Z,15Z)-octadecatrienoate protects plant tissues
CC against infection by the bacterial pathogen Pseudomonas syringae pv
CC tomato DC3000 (PubMed:22199234). The LOX1-derived oxylipins are
CC required to trigger stomatal closure in response to both infection by
CC the bacterial pathogen Pseudomonas syringae pv tomato DC3000, and the
CC pathogen-associated molecular pattern (PAMP) flagellin peptide flg22
CC (PubMed:23526882). Contributes to the oxidation of free fatty acids
CC during seed aging (PubMed:28371855). {ECO:0000269|PubMed:17369372,
CC ECO:0000269|PubMed:18949503, ECO:0000269|PubMed:21481031,
CC ECO:0000269|PubMed:22199234, ECO:0000269|PubMed:23314084,
CC ECO:0000269|PubMed:23526882, ECO:0000269|PubMed:26075826,
CC ECO:0000269|PubMed:26417008, ECO:0000269|PubMed:28371855}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-
CC octadecadienoate; Xref=Rhea:RHEA:30291, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:60955; EC=1.13.11.58;
CC Evidence={ECO:0000269|PubMed:18949503};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30292;
CC Evidence={ECO:0000269|PubMed:18949503};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (9S)-hydroperoxy-
CC (10E,12Z,15Z)-octadecatrienoate; Xref=Rhea:RHEA:51248,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:60962;
CC Evidence={ECO:0000269|PubMed:18949503};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51249;
CC Evidence={ECO:0000269|PubMed:18949503};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|PROSITE-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: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Seedlings, roots, leaves, and flowers (at protein
CC level) (PubMed:12232208, PubMed:17369372, PubMed:7506426, Ref.7).
CC Expressed in guard cells (PubMed:23526882).
CC {ECO:0000269|PubMed:12232208, ECO:0000269|PubMed:17369372,
CC ECO:0000269|PubMed:23526882, ECO:0000269|PubMed:7506426,
CC ECO:0000269|Ref.7}.
CC -!- DEVELOPMENTAL STAGE: Transiently expressed during germination, within 1
CC day after imbibition, especially in the epidermis and the aleurone
CC layer. Later present in the epidermis of the radicle and the adaxial
CC side of the cotyledons. In roots, confined to the pericycle cells and
CC in the lateral root primordia (LRP), and declined at the time of
CC lateral root emergence. Expression is greatly increased in leaves
CC during leaf senescence. {ECO:0000269|PubMed:11891244,
CC ECO:0000269|PubMed:12232208, ECO:0000269|PubMed:17369372}.
CC -!- INDUCTION: By pathogens (e.g. Pseudomonas syringae), wounding, abscisic
CC acid (ABA) and methyl jasmonate (MeJA). Higher levels in light than in
CC dark conditions (PubMed:12232208, PubMed:7506426). Induced by infection
CC with the fungal pathogen Fusarium graminearum (PubMed:26075826).
CC {ECO:0000269|PubMed:12232208, ECO:0000269|PubMed:26075826,
CC ECO:0000269|PubMed:7506426}.
CC -!- DISRUPTION PHENOTYPE: Increment in the number of lateral roots, and
CC moderate increase in the length of the primary root (PubMed:17369372).
CC Enhanced disease resistance to the fungal pathogen Fusarium graminearum
CC (PubMed:26075826). Enhanced susceptibility to the bacterial pathogen
CC Pseudomonas syringae pv tomato DC3000 (PubMed:22199234,
CC PubMed:23526882). The double mutant plants lox1 and lox5 exhibit
CC enhanced susceptibility to the bacterial pathogen Pseudomonas syringae
CC pv tomato DC3000 and the biotrophic powdery mildew pathogen
CC Golovinomyces cichoracearum (PubMed:26417008).
CC {ECO:0000269|PubMed:17369372, ECO:0000269|PubMed:22199234,
CC ECO:0000269|PubMed:23526882, ECO:0000269|PubMed:26075826,
CC ECO:0000269|PubMed:26417008}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; L04637; AAA32827.1; -; mRNA.
DR EMBL; U01843; AAA17036.1; -; Genomic_DNA.
DR EMBL; AC064840; AAG00881.1; -; Genomic_DNA.
DR EMBL; AC069144; AAG51123.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33175.1; -; Genomic_DNA.
DR EMBL; AY093104; AAM13103.1; -; mRNA.
DR EMBL; BT010358; AAQ56801.1; -; mRNA.
DR PIR; JQ2267; JQ2267.
DR RefSeq; NP_175900.1; NM_104376.3.
DR AlphaFoldDB; Q06327; -.
DR SMR; Q06327; -.
DR BioGRID; 27169; 1.
DR STRING; 3702.AT1G55020.1; -.
DR SwissLipids; SLP:000001762; -.
DR PaxDb; Q06327; -.
DR PRIDE; Q06327; -.
DR ProteomicsDB; 238668; -.
DR EnsemblPlants; AT1G55020.1; AT1G55020.1; AT1G55020.
DR GeneID; 841944; -.
DR Gramene; AT1G55020.1; AT1G55020.1; AT1G55020.
DR KEGG; ath:AT1G55020; -.
DR Araport; AT1G55020; -.
DR TAIR; locus:2011030; AT1G55020.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR InParanoid; Q06327; -.
DR OMA; FDSTPDE; -.
DR OrthoDB; 385042at2759; -.
DR PhylomeDB; Q06327; -.
DR BRENDA; 1.13.11.58; 399.
DR UniPathway; UPA00382; -.
DR PRO; PR:Q06327; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q06327; baseline and differential.
DR Genevisible; Q06327; AT.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0010311; P:lateral root formation; IMP:UniProtKB.
DR GO; GO:0034440; P:lipid oxidation; IDA:TAIR.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR CDD; cd01751; PLAT_LH2; 1.
DR Gene3D; 4.10.372.10; -; 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; PTHR11771; 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; SSF48484; SSF48484; 1.
DR SUPFAM; SSF49723; SSF49723; 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 Cytoplasm; Dioxygenase; Fatty acid biosynthesis; Fatty acid metabolism;
KW Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Oxylipin biosynthesis; Plant defense; Reference proteome; Stress response.
FT CHAIN 1..859
FT /note="Linoleate 9S-lipoxygenase 1"
FT /id="PRO_0000220703"
FT DOMAIN 21..161
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 164..859
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 213..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 519
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 524
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 711
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 715
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 859
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ SEQUENCE 859 AA; 98045 MW; 49378EBACD5FF579 CRC64;
MFGELRDLLT GGGNETTTKK VKGTVVLMKK NVLDFNDFNA SFLDRLHEFL GNKITLRLVS
SDVTDSENGS KGKLGKAAHL EDWITTITSL TAGESAFKVT FDYETDFGYP GAFLIRNSHF
SEFLLKSLTL EDVPGHGRVH YICNSWIYPA KHYTTDRVFF SNKTYLPHET PATLLKYREE
ELVSLRGTGE GELKEWDRVY DYAYYNDLGV PPKNPRPVLG GTQEYPYPRR GRTGRKPTKE
DPQTESRLPI TSSLDIYVPR DERFGHLKMS DFLAYALKAI AQFIQPALEA VFDDTPKEFD
SFEDVLKIYE EGIDLPNQAL IDSIVKNIPL EMLKEIFRTD GQKFLKFPVP QVIKEDKTAW
RTDEEFAREM LAGLNPVVIQ LLKEFPPKSK LDSESYGNQN STITKSHIEH NLDGLTVEEA
LEKERLFILD HHDTLMPYLG RVNTTTTKTY ASRTLLFLKD DGTLKPLVIE LSLPHPNGDK
FGAVSEVYTP GEGVYDSLWQ LAKAFVGVND SGNHQLISHW MQTHASIEPF VIATNRQLSV
LHPVFKLLEP HFRDTMNINA LARQILINGG GIFEITVFPS KYAMEMSSFI YKNHWTFPDQ
ALPAELKKRG MAVEDPEAPH GLRLRIKDYP YAVDGLEVWY AIESWVRDYI FLFYKIEEDI
QTDTELQAWW KEVREEGHGD KKSEPWWPKM QTREELVESC TIIIWVASAL HAAVNFGQYP
VAGYLPNRPT ISRQYMPKEN TPEFEELEKN PDKVFLKTIT AQLQTLLGIS LIEILSTHSS
DEVYLGQRDS KEWAAEKEAL EAFEKFGEKV KEIEKNIDER NDDETLKNRT GLVKMPYTLL
FPSSEGGVTG RGIPNSVSI
