ID Q93Y81_CITPA Unreviewed; 570 AA.
AC Q93Y81;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 69.
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};
OS Citrus paradisi (Grapefruit).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=37656 {ECO:0000313|EMBL:AAK51557.1};
RN [1] {ECO:0000313|EMBL:AAK51557.1}
RP NUCLEOTIDE SEQUENCE.
RA Costa M.C., Moreira C.D., Otoni W.C., Moore G.A.;
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAK51557.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21594623; DOI=10.1007/s11033-011-0814-2;
RA Costa M.G., Moreira C.D., Melton J.R., Otoni W.C., Moore G.A.;
RT "Characterization and developmental expression of genes encoding the early
RT carotenoid biosynthetic enzymes in Citrus paradisi Macf.";
RL Mol. Biol. Rep. 0:0-0(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; AF372617; AAK51557.1; -; mRNA.
DR AlphaFoldDB; Q93Y81; -.
DR UniPathway; UPA00803; -.
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:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 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 2: Evidence at transcript level;
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}.
FT DOMAIN 70..534
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 570 AA; 62985 MW; 03BB1B7E0895633D CRC64;
MGSSVLFPAT SVTGVSWSRV QEKCPRFCVR ASLDANVSDM SVNAPKGLFP PEPEHYRGPK
LKVAIIGAGL AGMSTAVELL DQGHEVDIYE SRSFIGGKVG SFVDKRGNHI EMGLHVFFGC
YNNLFRLMKK VGADKNLLVK DHTHTFVNKG GEIGELDFRF PIGAPLHGIR AFLSTNQLKT
YDKARNALAL ALSPVVKALV DPDGALKDIR DLDSISFSDW FLSKGGTRMS IQRMWDPVAY
ALGFIDCDNI SARCMLTIFA LFATKTETSL LRMLKGSPDV YLSGPIRKYI TDKGGRFHLR
WGCREILYDK AANAETYVKG LAMSKATDKE VVQADACVAA CDVPGIKRLL PSSWREMKFF
NNIYALVGVP VVTVQLRYNG WVTELQGLER SRQLRRALGL DNLLYTPDAD FSCFADLALT
SPEDYYREGQ GSLLQCVLTP GDPYMPLPND EIIRRVAKQV LALFPSSQGL EVIWSSVVKI
GQSLYREGPG KDPFRPDQKT PVKNFFLAGS YTKQDYIDSM EGATLSGRQA SAYICNAGEE
LVALRKQLAA FESQEQMEAP TTTNDELSLV
//
