PIOX_CAPAN
ID PIOX_CAPAN Reviewed; 643 AA.
AC A0A2G3AC72; Q93X71;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Alpha-dioxygenase 1 {ECO:0000303|PubMed:11807143};
DE Short=Ca-COX1 {ECO:0000303|PubMed:11807143};
GN ORFNames=T459_06886 {ECO:0000312|EMBL:PHT91773.1};
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RC TISSUE=Leaf;
RX PubMed=11807143; DOI=10.1093/jexbot/53.367.383;
RA Kim Y.C., Yi S.Y., Mang H.G., Seo Y.S., Kim W.T., Choi D.;
RT "Pathogen-induced expression of cyclo-oxygenase homologue in hot pepper
RT (Capsicum annuum cv. Pukang).";
RL J. Exp. Bot. 53:383-385(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CM334;
RX PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA Bennetzen J.L., Choi D.;
RT "New reference genome sequences of hot pepper reveal the massive evolution
RT of plant disease-resistance genes by retroduplication.";
RL Genome Biol. 18:R210.1-R210.11(2017).
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 (Probable). Involved in the production of oxylipins that function in
CC cell signaling, wound healing, and protection from infection
CC (Probable). The lipid-derived signaling pathway is involved in the
CC initial response of hot pepper plants to pathogen infection (Probable).
CC {ECO:0000305|PubMed:11807143}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q9SGH6};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000250|UniProtKB:Q9SGH6};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q9SGH6};
CC Note=Binds 1 calcium ion per subunit. {ECO:0000250|UniProtKB:Q9SGH6};
CC -!- INDUCTION: Induced by infection with the bacterial pathogen Xanthomonas
CC campestris pv glycine 8ra. {ECO:0000269|PubMed:11807143}.
CC -!- SIMILARITY: Belongs to the peroxidase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00298}.
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DR EMBL; AY040869; AAK85133.1; -; mRNA.
DR EMBL; AYRZ02000002; PHT91773.1; -; Genomic_DNA.
DR STRING; 4072.A0A2G3AC72; -.
DR PeroxiBase; 6270; CanDiOx01.
DR EnsemblPlants; PHT91773; PHT91773; T459_06886.
DR Gramene; PHT91773; PHT91773; T459_06886.
DR OMA; AFAPWTK; -.
DR Proteomes; UP000189700; Genome assembly.
DR Proteomes; UP000222542; Chromosome 2.
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; IBA:GO_Central.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
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:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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 2: Evidence at transcript level;
KW Calcium; Dioxygenase; Fatty acid biosynthesis; Fatty acid metabolism; Heme;
KW Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Oxylipin biosynthesis; Peroxidase; Plant defense; Reference proteome.
FT CHAIN 1..643
FT /note="Alpha-dioxygenase 1"
FT /id="PRO_0000455384"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 172
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 392
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 BINDING 489
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 493
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT SITE 269
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT CONFLICT 221
FT /note="S -> P (in Ref. 1; AAK85133)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="A -> S (in Ref. 1; AAK85133)"
FT /evidence="ECO:0000305"
FT CONFLICT 538..549
FT /note="DLLVGMSAEKKI -> EFVSGNVCGEKD (in Ref. 1; AAK85133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 643 AA; 74007 MW; 6DC3E17A938CDA6D CRC64;
MSFIMSSLRN LFLSPLRSFI QKDFHDAFDS MTLLDKLLFM MVHFVDKLIL WHRLPVFLGL
AYLAARRHLH QEYNLINVGR TPTGVRSNPE DYPYRTADGK YNDPFNEGAG SQFSFFGRNV
MPVDQHDKLK KPDPMVVATK LLARKNFMDT GKQFNMIAAS WIQFMIHDWI DHLEDTHQIE
LRAPEEVASE CPLKSFKFYK SKKTPTGFYE IKTGYLNRRT SWWDGSAIYG SNTEALKKVR
TFEDGKLKLS ADGLLEQDEN GNIISGDVRN PWAGLLALQA LFIQEHNLVC DTLKKEYPKL
EDEDLYRHAR LVTSAVIAKV HTIDWTVELL KTDTLLAGMR ANWYGLLGKK FKDTFGHVGG
SSLGGFVGMK KPENHGVPYS LTEEFVSVYR MHQLLPDTLQ LRNIDATPGP NKSLPLTNEI
PMEDLIGGKG EENLSRIGYT KQMVSMGHQA CGALELMNYP IWMRDLIPQD VDGNDRPDHI
DLAALEIYRD RERSVARYNE FRRRMLQIPI SKWEDLTDDE EAIKMLREVY GDDVEELDLL
VGMSAEKKIK GFAISETAFF IFLIMASRRL EADKFFTSNY NEETYTKKGL EWVNTTESLK
DVLDRHYPEM TGKWMNSNSA FSVWDSSPEP HNPIPIYFRV PQQ
