ID B2LS46_NARTA Unreviewed; 574 AA.
AC B2LS46;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 41.
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 Name=zds {ECO:0000313|EMBL:ACB87206.1};
OS Narcissus tazetta subsp. chinensis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC Amaryllidoideae; Narcissus.
OX NCBI_TaxID=391288 {ECO:0000313|EMBL:ACB87206.1};
RN [1] {ECO:0000313|EMBL:ACB87206.1}
RP NUCLEOTIDE SEQUENCE.
RA Pan D., Jiang L., Lin L.;
RT "Cloning of Full-Length cDNA Encoding for Zeta-Carotene Desaturase (zds) in
RT Narcissus tazetta L. var. chinensis Roem.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; EU573238; ACB87206.1; -; mRNA.
DR AlphaFoldDB; B2LS46; -.
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; 3.50.50.60; 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 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 74..538
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 574 AA; 63728 MW; D1FA9744E6A52F32 CRC64;
MASFTCLIHS SSFGVGGKKV KKNRMIQSKL FSIRSALDTK VSDMSVNAPK GLFPPEPEHY
RGPKLKVAII GAGLAGMSTA VELLDQGHEV DIYESRQFIG GKVGSFVDKR GNHIEMGLHV
FFGCYNNLFR LMKKVGADEN LLVKDHTHTF VNRGGEIGEL DFRFPMGAPL HGIRAFLTTN
QLKPYDEARN AVALALSPVV RALIDPNGAM QDIRNLDNIS FSDWFLSKGG TRTSIQRMWD
PVAYALGFID CDNISARCML TIFSLFATKT EASLLRMLKG SPDAYLSGPI RKYITDKGGR
FHLRWGCREI LYDESSNGDT YITGIAMSKA TNKKLVKADV YVAACDVPGI KRLIPSEWRE
WDLFDNIYKL DGVPVVTVQL RYNGWVTELQ DLEKSRQLRR AVGLDNLLYT PDADFSCFAD
LALSSPEDYY IEGQGSLKQA VLTPGDPYMP LPNDAIIERV RKQVLDLFPS SQGLEVLWSS
VVKIGQSLYR EGPGKDPFRP DQKTPVKNFF LAGSYTKQDY IDSMEGATLS GRQAAAYICS
AGEELAALRK KIAADHPEQL INEDSNISDE LSLV
//