GenomeNet

Database: UniProt
Entry: B2LS46_NARTA
LinkDB: B2LS46_NARTA
Original site: B2LS46_NARTA 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system