ID D7L2Z6_ARALL Unreviewed; 561 AA.
AC D7L2Z6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Zeta-carotene desaturase {ECO:0000256|RuleBase:RU362008};
DE EC=1.3.5.6 {ECO:0000256|RuleBase:RU362008};
DE AltName: Full=9,9'-di-cis-zeta-carotene desaturase {ECO:0000256|RuleBase:RU362008};
GN ORFNames=ARALYDRAFT_477758 {ECO:0000313|EMBL:EFH58637.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- FUNCTION: Catalyzes the conversion of zeta-carotene to lycopene via the
CC intermediary of neurosporene. It carries out two consecutive
CC desaturations (introduction of double bonds) at positions C-7 and C-7'.
CC {ECO:0000256|RuleBase:RU362008}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9,9'-di-cis-zeta-carotene + 2 a quinone = 7,7',9,9'-tetra-cis-
CC lycopene + 2 a quinol; Xref=Rhea:RHEA:30955, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:48716, ChEBI:CHEBI:62466, ChEBI:CHEBI:132124; EC=1.3.5.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000914,
CC ECO:0000256|RuleBase:RU362008};
CC -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004900, ECO:0000256|RuleBase:RU362008}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|RuleBase:RU362008}. Plastid, chromoplast
CC {ECO:0000256|RuleBase:RU362008}.
CC -!- SIMILARITY: Belongs to the zeta carotene desaturase family.
CC {ECO:0000256|ARBA:ARBA00010192, ECO:0000256|RuleBase:RU362008}.
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DR EMBL; GL348715; EFH58637.1; -; Genomic_DNA.
DR RefSeq; XP_002882378.1; XM_002882332.1.
DR AlphaFoldDB; D7L2Z6; -.
DR STRING; 81972.D7L2Z6; -.
DR EnsemblPlants; fgenesh2_kg.3__459__AT3G04870.2; fgenesh2_kg.3__459__AT3G04870.2; fgenesh2_kg.3__459__AT3G04870.2.
DR Gramene; fgenesh2_kg.3__459__AT3G04870.2; fgenesh2_kg.3__459__AT3G04870.2; fgenesh2_kg.3__459__AT3G04870.2.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_022687_1_1_1; -.
DR OrthoDB; 348089at2759; -.
DR UniPathway; UPA00803; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009509; C:chromoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0052887; F:7,9,9'-tricis-neurosporene:quinone oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016719; F:9,9'-di-cis-zeta-carotene desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0052886; F:9,9'-dicis-carotene:quinone oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0052889; P:9,9'-di-cis-zeta-carotene desaturation to 7,9,7',9'-tetra-cis-lycopene; IEA:EnsemblPlants.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1901177; P:lycopene biosynthetic process; IEA:EnsemblPlants.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR014103; Zeta_caro_desat.
DR NCBIfam; TIGR02732; zeta_caro_desat; 1.
DR PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR PANTHER; PTHR42923:SF41; ZETA-CAROTENE DESATURASE, CHLOROPLASTIC_CHROMOPLASTIC; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Carotenoid biosynthesis {ECO:0000256|RuleBase:RU362008};
KW Chloroplast {ECO:0000256|RuleBase:RU362008};
KW Chromoplast {ECO:0000256|RuleBase:RU362008};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362008}; Plastid {ECO:0000256|RuleBase:RU362008};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT DOMAIN 69..533
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 561 AA; 62034 MW; 328C01A229DBF064 CRC64;
MASSIVFAAT PATGFLSQPS LKSRRFYVNS SLDSDVSDMS VNAPKGLFPP EPVPYKGPKL
KVAIIGAGLA GMSTAVELLD QGHEVDIYDS RTFIGGKVGS FVDRRGNHIE MGLHVFFGCY
NNLFRLMKKV GADKNLLVKD HTHTFINKDG TVGELDFRFS VGAPIHGIRA FLVTNQLKPY
DKLRNSLALA LSPVVKALVD PDGAMRDIRN LDSISFSDWF LSKGGTRASI QRMWDPVAYA
LGFIDCDNMS ARCMLTIFSL FATKTEASLL RMLKGSPDVY LSGPIKQYIT DRGGRIHLRW
GCREILYDKS ADGETYVTGL AISKATNKKI VKADVYVAAC DVPGIKRLLP KEWRESRFFN
DIYELEGVPV VTVQLRYNGW VTELQDIELS RQLKRAVGLD NLLYTPDADF SCFADLALAS
PADYYIEGQG TLLQCVLTPG DPYMRMPNDK IIEKVAMQVT ELFPSSRSLE VTWSSVVKIA
QSLYREAPGK DPFRPDQKTP IKNFFLAGSY TKQDYIDSME GATLSGRQAS SYICDTGEEL
AELNKKLSSS ATAVPDELSL V
//
