ID A0A1S3CQH4_CUCME Unreviewed; 591 AA.
AC A0A1S3CQH4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=9-cis-epoxycarotenoid dioxygenase {ECO:0000256|ARBA:ARBA00039007};
DE EC=1.13.11.51 {ECO:0000256|ARBA:ARBA00039007};
GN Name=LOC103503120 {ECO:0000313|RefSeq:XP_008465499.1};
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008465499.1};
RN [1] {ECO:0000313|Proteomes:UP000089565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT "The genome of melon (Cucumis melo L.).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN [2] {ECO:0000313|RefSeq:XP_008465499.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9'-cis-neoxanthin + O2 = (3S,5R,6R)-3,5-dihydroxy-6,7-
CC didehydro-5,6-dihydro-12'-apo-beta-caroten-12'-al + 2-cis,4-trans-
CC xanthoxin; Xref=Rhea:RHEA:19677, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32304, ChEBI:CHEBI:34596, ChEBI:CHEBI:35306;
CC EC=1.13.11.51; Evidence={ECO:0000256|ARBA:ARBA00036784};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-cis-violaxanthin + O2 = (3S,5R,6S)-5,6-epoxy-3-hydroxy-5,6-
CC dihydro-12'-apo-beta-caroten-12'-al + 2-cis,4-trans-xanthoxin;
CC Xref=Rhea:RHEA:16541, ChEBI:CHEBI:15379, ChEBI:CHEBI:32304,
CC ChEBI:CHEBI:34597, ChEBI:CHEBI:35305; EC=1.13.11.51;
CC Evidence={ECO:0000256|ARBA:ARBA00035929};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 9-cis-epoxycarotenoid + O2 = 2-cis,4-trans-xanthoxin + a
CC 12'-apo-carotenal; Xref=Rhea:RHEA:23328, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32304, ChEBI:CHEBI:51972, ChEBI:CHEBI:51973;
CC EC=1.13.11.51; Evidence={ECO:0000256|ARBA:ARBA00036011};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|PIRSR:PIRSR604294-1};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604294-1};
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family.
CC {ECO:0000256|ARBA:ARBA00006787}.
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DR RefSeq; XP_008465499.1; XM_008467277.2.
DR AlphaFoldDB; A0A1S3CQH4; -.
DR GeneID; 103503120; -.
DR KEGG; cmo:103503120; -.
DR eggNOG; KOG1285; Eukaryota.
DR InParanoid; A0A1S3CQH4; -.
DR OrthoDB; 318119at2759; -.
DR Proteomes; UP000089565; Unplaced.
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; IEA:InterPro.
DR InterPro; IPR004294; Carotenoid_Oase.
DR PANTHER; PTHR10543:SF26; 9-CIS-EPOXYCAROTENOID DIOXYGENASE NCED3, CHLOROPLASTIC; 1.
DR PANTHER; PTHR10543; BETA-CAROTENE DIOXYGENASE; 1.
DR Pfam; PF03055; RPE65; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964,
KW ECO:0000313|RefSeq:XP_008465499.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR604294-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR604294-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000089565}.
FT REGION 43..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 289
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 338
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 403
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 577
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 591 AA; 65544 MW; 620922D36EA8BF71 CRC64;
MASSSFLKSP FSSSMPDKTL SNYTSRRLLS VSSSLHTPSI IQIPKHSHTT FPSPLKTSIP
KPPPLSTTPP LSGSEDWNFL QRAAAMALDA VENALISAER KHSLPKTADP AVQIAGNFAP
VPEQPVRKGL PVIGKVPECI RGVYVRNGAN PLHEPVSGHH LFDGDGMVHA VEFSEAGGVS
YACRFTETQR LVQERAYGRP VFPKAIGELH GHSGIARLML FYARGLFGLV DHNQGIGVAN
AGLVYFNGRL LAMSEDDLPY QIRVTPAGDL KTVGRFDFDG QLKSTMIAHP KLDPVSGEMF
ALSYDVIQKP YLKYFKFSPE GEKSPDVEIP LPQPTMMHDF AITEKYVVIP DQQVVFKLPE
MIRGGSPVVY DKEKTSRFGI LDKNAADANA IKWIEAPDCF CFHLWNAWEE PETNEIVVIG
SCMTPPDSIF NECEENLKSV LSEIRLNLST GKSTRRPIIS ETEQVNLEAG MVNRNLLGRK
TQFSYLALAE PWPKVSGFAK VDLFTGEIKK YLYGEQRYGG EPLFLPREGA EAEDDGHILA
FVHDEKEWKS ELQIVNAMTL ELEATVKLPS RVPYGFHGTF ISSEDLQKQI R
//
