DOX1_ARATH
ID DOX1_ARATH Reviewed; 639 AA.
AC Q9SGH6;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Alpha-dioxygenase 1 {ECO:0000303|PubMed:12060227};
DE Short=Alpha DOX1 {ECO:0000303|PubMed:12060227};
DE EC=1.13.11.92 {ECO:0000269|PubMed:10455113};
DE AltName: Full=Fatty acid dioxygenase AlphaDOX1 {ECO:0000305};
DE AltName: Full=Pathogen-induced oxygenase {ECO:0000303|PubMed:10455113};
DE AltName: Full=Plant alpha dioxygenase 1 {ECO:0000303|PubMed:15100225};
GN Name=DOX1 {ECO:0000303|PubMed:12060227};
GN Synonyms=DIOX1 {ECO:0000305}, PADOX-1 {ECO:0000303|PubMed:15100225},
GN PIOX {ECO:0000303|PubMed:10455113};
GN OrderedLocusNames=At3g01420 {ECO:0000312|Araport:AT3G01420};
GN ORFNames=T13O15.6 {ECO:0000312|EMBL:AAF24612.1};
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 [GENOMIC DNA], FUNCTION, INDUCTION BY PATHOGENS, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=12060227; DOI=10.1046/j.1365-313x.2002.01195.x;
RA De Leon I.P., Sanz A., Hamberg M., Castresana C.;
RT "Involvement of the Arabidopsis alpha-DOX1 fatty acid dioxygenase in
RT protection against oxidative stress and cell death.";
RL Plant J. 29:61-62(2002).
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 FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10455113; DOI=10.1074/jbc.274.35.24503;
RA Hamberg M., Sanz A., Castresana C.;
RT "alpha-oxidation of fatty acids in higher plants. Identification of a
RT pathogen-inducible oxygenase (piox) as an alpha-dioxygenase and
RT biosynthesis of 2-hydroperoxylinolenic acid.";
RL J. Biol. Chem. 274:24503-24513(1999).
RN [6]
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND MUTAGENESIS OF HIS-163;
RP TYR-386; ARG-387 AND HIS-389.
RX PubMed=15100225; DOI=10.1074/jbc.m401779200;
RA Liu W., Rogge C.E., Bambai B., Palmer G., Tsai A.L., Kulmacz R.J.;
RT "Characterization of the heme environment in Arabidopsis thaliana fatty
RT acid alpha-dioxygenase-1.";
RL J. Biol. Chem. 279:29805-29815(2004).
RN [7]
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 [8]
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 [9]
RP SUBCELLULAR LOCATION.
RX PubMed=24214535; DOI=10.1104/pp.113.230185;
RA Shimada T.L., Takano Y., Shimada T., Fujiwara M., Fukao Y., Mori M.,
RA Okazaki Y., Saito K., Sasaki R., Aoki K., Hara-Nishimura I.;
RT "Leaf oil body functions as a subcellular factory for the production of a
RT phytoalexin in Arabidopsis.";
RL Plant Physiol. 164:105-118(2014).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) IN COMPLEX WITH HEME AND CALCIUM
RP ION, ACTIVE SITE, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP MUTAGENESIS OF GLN-159; HIS-318; THR-323; TYR-386; ARG-565 AND ARG-566.
RX PubMed=23373518; DOI=10.1021/bi400013k;
RA Goulah C.C., Zhu G., Koszelak-Rosenblum M., Malkowski M.G.;
RT "The crystal structure of alpha-dioxygenase provides insight into diversity
RT in the cyclooxygenase-peroxidase superfamily.";
RL Biochemistry 52:1364-1372(2013).
CC -!- FUNCTION: Alpha-dioxygenase that catalyzes the primary oxygenation step
CC of a variety of 14-20 carbon fatty acids, containing up to three
CC unsaturated bonds, into their corresponding 2R-hydroperoxides
CC (PubMed:12060227, PubMed:10455113). Involved in the production of
CC oxylipins that function in cell signaling, wound healing, and
CC protection from infection (PubMed:12060227, PubMed:10455113). Mediates
CC protection against oxidative stress and cell death, probably by
CC generating some lipid-derived molecules (PubMed:12060227). Promotes
CC local and systemic plant defense in a salicylic acid (SA)-dependent
CC manner, including the establishment of systemic acquired resistance
CC (SAR) in response to incompatible interaction (PubMed:22199234).
CC Involved in a negative regulation of abscisic acid (ABA)-mediated
CC signaling pathway (PubMed:22199234). {ECO:0000269|PubMed:10455113,
CC ECO:0000269|PubMed:12060227, ECO:0000269|PubMed:22199234}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-saturated fatty acid + O2 = a (2R)-2-hydroperoxy fatty
CC acid; Xref=Rhea:RHEA:63508, ChEBI:CHEBI:15379, ChEBI:CHEBI:83955,
CC ChEBI:CHEBI:147340; EC=1.13.11.92;
CC Evidence={ECO:0000269|PubMed:10455113};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63509;
CC Evidence={ECO:0000269|PubMed:10455113};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (R)-2-hydroperoxy-
CC (9Z,12Z,15Z)-octadecatrienoate; Xref=Rhea:RHEA:16329,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:76161;
CC EC=1.13.11.92; Evidence={ECO:0000269|PubMed:10455113};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16330;
CC Evidence={ECO:0000269|PubMed:10455113};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate + O2 = (2R)-2-hydroperoxyhexadecanoate;
CC Xref=Rhea:RHEA:63836, ChEBI:CHEBI:7896, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:149616; EC=1.13.11.92;
CC Evidence={ECO:0000269|PubMed:10455113};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63837;
CC Evidence={ECO:0000269|PubMed:10455113};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (2R,9Z,12Z)-2-
CC hydroperoxyoctadecadienoate; Xref=Rhea:RHEA:63860, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:149618; EC=1.13.11.92;
CC Evidence={ECO:0000269|PubMed:10455113};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63861;
CC Evidence={ECO:0000269|PubMed:10455113};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + O2 = (2R,9Z)-2-hydroperoxyoctadecenoate;
CC Xref=Rhea:RHEA:63868, ChEBI:CHEBI:15379, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:149623; EC=1.13.11.92;
CC Evidence={ECO:0000269|PubMed:10455113};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63869;
CC Evidence={ECO:0000269|PubMed:10455113};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:15100225, ECO:0000269|PubMed:23373518};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000269|PubMed:15100225, ECO:0000269|PubMed:23373518};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:23373518};
CC Note=Binds 1 calcium ion per subunit. {ECO:0000269|PubMed:23373518};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 uM for linolenic acid (at pH 8 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10455113};
CC KM=17 uM for linoleic acid (at pH 8 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10455113};
CC KM=13 uM for oleic acid (at pH 8 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10455113};
CC KM=14 uM for oleic acid (at pH 7.8 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:15100225};
CC KM=11 uM for palmitic acid (at pH 8 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10455113};
CC Vmax=119 nmol/min/mg enzyme with linolenic acid as substrate (at pH 8
CC and 30 degrees Celsius) {ECO:0000269|PubMed:10455113};
CC Vmax=111 nmol/min/mg enzyme with linoleic acid as substrate (at pH 8
CC and 30 degrees Celsius) {ECO:0000269|PubMed:10455113};
CC Vmax=91 nmol/min/mg enzyme with oleic acid as substrate (at pH 8 and
CC 30 degrees Celsius) {ECO:0000269|PubMed:10455113};
CC Vmax=46 nmol/min/mg enzyme with palmitic acid as substrate (at pH 8
CC and 30 degrees Celsius) {ECO:0000269|PubMed:10455113};
CC -!- SUBUNIT: Forms monomers in solution. {ECO:0000269|PubMed:23373518}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:24214535}.
CC Note=Localizes on the surface of leaf oil bodies.
CC {ECO:0000269|PubMed:24214535}.
CC -!- TISSUE SPECIFICITY: Expressed in roots (epiderm), mature flowers (e.g.
CC anthers) and senescing leaves. {ECO:0000269|PubMed:12060227,
CC ECO:0000269|PubMed:17369372}.
CC -!- INDUCTION: Induced by salicylic acid (SA) and by some chemicals
CC generating reactive oxygen species (ROS, e.g. nitric oxide (NO),
CC intracellular superoxide and singlet oxygen) such as sodium
CC nitropruside (SNP), paraquat and rose bengal (RB). Accumulates locally,
CC at the infection site, in response to both incompatible and compatible
CC bacterial pathogens (e.g. Pseudomonas syringae pv. tomato DC3000) in a
CC SA-dependent manner, with a faster response during hypersensitive
CC reactions. {ECO:0000269|PubMed:12060227}.
CC -!- DISRUPTION PHENOTYPE: Slightly higher accumulation of Pseudomonas
CC syringae pv. tomato DC3000 in infected leaves. Partially impaired
CC systemic acquired resistance (SAR) in response to incompatible
CC interaction. When associated with LOX1 disruption; hypersensitivity to
CC the growth-inhibitory effect of abscisic acid (ABA) accompanied by an
CC accumulation of ABA-inducible marker genes.
CC {ECO:0000269|PubMed:22199234}.
CC -!- SIMILARITY: Belongs to the peroxidase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00298}.
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DR EMBL; AF334402; AAL87742.1; -; Genomic_DNA.
DR EMBL; AC010870; AAF24612.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73664.1; -; Genomic_DNA.
DR EMBL; AY042787; AAK68727.1; -; mRNA.
DR EMBL; AY064666; AAL47373.1; -; mRNA.
DR RefSeq; NP_186791.1; NM_111008.3.
DR PDB; 4HHR; X-ray; 1.51 A; A=1-639.
DR PDB; 4HHS; X-ray; 1.70 A; A=1-639.
DR PDBsum; 4HHR; -.
DR PDBsum; 4HHS; -.
DR AlphaFoldDB; Q9SGH6; -.
DR SMR; Q9SGH6; -.
DR BioGRID; 6468; 2.
DR STRING; 3702.AT3G01420.1; -.
DR PeroxiBase; 3377; AtDiOx01.
DR iPTMnet; Q9SGH6; -.
DR PaxDb; Q9SGH6; -.
DR PRIDE; Q9SGH6; -.
DR ProteomicsDB; 222140; -.
DR EnsemblPlants; AT3G01420.1; AT3G01420.1; AT3G01420.
DR GeneID; 821135; -.
DR Gramene; AT3G01420.1; AT3G01420.1; AT3G01420.
DR KEGG; ath:AT3G01420; -.
DR Araport; AT3G01420; -.
DR TAIR; locus:2096697; AT3G01420.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_033051_0_0_1; -.
DR InParanoid; Q9SGH6; -.
DR OMA; AFAPWTK; -.
DR OrthoDB; 276568at2759; -.
DR PhylomeDB; Q9SGH6; -.
DR BioCyc; ARA:AT3G01420-MON; -.
DR BioCyc; MetaCyc:AT3G01420-MON; -.
DR BRENDA; 1.13.11.92; 399.
DR PRO; PR:Q9SGH6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SGH6; baseline and differential.
DR Genevisible; Q9SGH6; AT.
DR GO; GO:0012511; C:monolayer-surrounded lipid storage body; IDA:TAIR.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
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; IDA:TAIR.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:1902609; P:(R)-2-hydroxy-alpha-linolenic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0008219; P:cell death; IEP:TAIR.
DR GO; GO:0071732; P:cellular response to nitric oxide; IEP:UniProtKB.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IEP:UniProtKB.
DR GO; GO:0071446; P:cellular response to salicylic acid stimulus; IEP:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IEP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IDA:TAIR.
DR GO; GO:0001561; P:fatty acid alpha-oxidation; IDA:TAIR.
DR GO; GO:0006629; P:lipid metabolic process; TAS:TAIR.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
DR GO; GO:0009627; P:systemic acquired resistance; IMP:UniProtKB.
DR CDD; cd09818; PIOX_like; 1.
DR Gene3D; 1.10.640.10; -; 1.
DR InterPro; IPR034815; A_dioxygenase.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR Pfam; PF03098; An_peroxidase; 1.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Fatty acid biosynthesis; Fatty acid metabolism;
KW Heme; Hypersensitive response; Iron; Lipid biosynthesis; Lipid droplet;
KW Lipid metabolism; Metal-binding; Oxidoreductase; Oxylipin biosynthesis;
KW Peroxidase; Plant defense; Reference proteome.
FT CHAIN 1..639
FT /note="Alpha-dioxygenase 1"
FT /id="PRO_0000420284"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:23373518"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:23373518"
FT BINDING 168
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000269|PubMed:23373518"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:23373518"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:23373518"
FT BINDING 220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:23373518"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:23373518"
FT BINDING 389
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:23373518"
FT BINDING 486
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000269|PubMed:23373518"
FT BINDING 490
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000269|PubMed:23373518"
FT SITE 266
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT MUTAGEN 159
FT /note="Q->N,S,V: Slightly reduces oxygenase activity."
FT /evidence="ECO:0000269|PubMed:23373518"
FT MUTAGEN 163
FT /note="H->C: Reduces oxygenase activity 17-fold."
FT /evidence="ECO:0000269|PubMed:15100225"
FT MUTAGEN 163
FT /note="H->M: Reduces oxygenase activity 6-fold."
FT /evidence="ECO:0000269|PubMed:15100225"
FT MUTAGEN 163
FT /note="H->Q: Reduces oxygenase activity more than 100-
FT fold."
FT /evidence="ECO:0000269|PubMed:15100225"
FT MUTAGEN 163
FT /note="H->Y: Reduces oxygenase activity 8-fold."
FT /evidence="ECO:0000269|PubMed:15100225"
FT MUTAGEN 318
FT /note="H->A: Reduces oxygenase activity 14-fold."
FT /evidence="ECO:0000269|PubMed:23373518"
FT MUTAGEN 318
FT /note="H->Q: Reduces oxygenase activity 4-fold."
FT /evidence="ECO:0000269|PubMed:23373518"
FT MUTAGEN 323
FT /note="T->A: Reduces oxygenase activity 14-fold."
FT /evidence="ECO:0000269|PubMed:23373518"
FT MUTAGEN 323
FT /note="T->L: Abolishes oxygenase activity."
FT /evidence="ECO:0000269|PubMed:23373518"
FT MUTAGEN 386
FT /note="Y->F: Abolishes oxygenase activity."
FT /evidence="ECO:0000269|PubMed:23373518"
FT MUTAGEN 386
FT /note="Y->F: Reduces oxygenase activity more than 100-
FT fold."
FT /evidence="ECO:0000269|PubMed:15100225"
FT MUTAGEN 387
FT /note="R->H: No effect on oxygenase activity."
FT /evidence="ECO:0000269|PubMed:15100225"
FT MUTAGEN 389
FT /note="H->C,M: Reduces oxygenase activity 13-fold."
FT /evidence="ECO:0000269|PubMed:15100225"
FT MUTAGEN 565
FT /note="R->A: Slightly reduces oxygenase activity."
FT /evidence="ECO:0000269|PubMed:23373518"
FT MUTAGEN 565
FT /note="R->K: Reduces oxygenase activity 3-fold."
FT /evidence="ECO:0000269|PubMed:23373518"
FT MUTAGEN 565
FT /note="R->L: Reduces oxygenase activity 2-fold."
FT /evidence="ECO:0000269|PubMed:23373518"
FT MUTAGEN 566
FT /note="R->A,L: Abolishes oxygenase activity."
FT /evidence="ECO:0000269|PubMed:23373518"
FT MUTAGEN 566
FT /note="R->K: Reduces oxygenase activity 36-fold."
FT /evidence="ECO:0000269|PubMed:23373518"
FT HELIX 1..12
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 21..25
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 29..43
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 52..69
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:4HHR"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:4HHR"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:4HHR"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 152..165
FT /evidence="ECO:0007829|PDB:4HHR"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:4HHR"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:4HHR"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:4HHR"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4HHR"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:4HHR"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 229..235
FT /evidence="ECO:0007829|PDB:4HHR"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 270..293
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 299..320
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 322..326
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 330..341
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 346..352
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 358..361
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 380..385
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:4HHR"
FT STRAND 394..399
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:4HHR"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 419..422
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 424..434
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 436..444
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 458..461
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 479..489
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 495..501
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 510..512
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 517..526
FT /evidence="ECO:0007829|PDB:4HHR"
FT TURN 527..529
FT /evidence="ECO:0007829|PDB:4HHR"
FT TURN 531..533
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 536..542
FT /evidence="ECO:0007829|PDB:4HHR"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 553..568
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:4HHR"
FT TURN 574..576
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 579..582
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 584..592
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 596..603
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 607..611
FT /evidence="ECO:0007829|PDB:4HHR"
FT STRAND 614..616
FT /evidence="ECO:0007829|PDB:4HHR"
FT HELIX 633..635
FT /evidence="ECO:0007829|PDB:4HHR"
SQ SEQUENCE 639 AA; 73158 MW; 9AB1700BBF353E9E CRC64;
MKVITSLISS ILLKFIHKDF HEIYARMSLL DRFLLLIVHG VDKMVPWHKL PVFLGLTYLE
VRRHLHQQYN LLNVGQTPTG IRFDPANYPY RTADGKFNDP FNEGVGSQNS FFGRNCPPVD
QKSKLRRPDP MVVATKLLGR KKFIDTGKQF NMIAASWIQF MIHDWIDHLE DTHQIELVAP
KEVASKCPLS SFRFLKTKEV PTGFFEIKTG SQNIRTPWWD SSVIYGSNSK TLDRVRTYKD
GKLKISEETG LLLHDEDGLA ISGDIRNSWA GVSALQALFI KEHNAVCDAL KDEDDDLEDE
DLYRYARLVT SAVVAKIHTI DWTVQLLKTD TLLAGMRANW YGLLGKKFKD SFGHAGSSIL
GGVVGMKKPQ NHGVPYSLTE DFTSVYRMHS LLPDQLHILD IDDVPGTNKS LPLIQEISMR
DLIGRKGEET MSHIGFTKLM VSMGHQASGA LELMNYPMWL RDIVPHDPNG QARPDHVDLA
ALEIYRDRER SVPRYNEFRR SMFMIPITKW EDLTEDEEAI EVLDDVYDGD VEELDLLVGL
MAEKKIKGFA ISETAFYIFL IMATRRLEAD RFFTSDFNET IYTKKGLEWV NTTESLKDVI
DRHYPDMTDK WMNSESAFSV WDSPPLTKNP IPLYLRIPS
