ID C7T0M6_FRAAN Unreviewed; 569 AA.
AC C7T0M6;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 42.
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:ACR61394.1};
OS Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Potentilleae; Fragariinae;
OC Fragaria.
OX NCBI_TaxID=3747 {ECO:0000313|EMBL:ACR61394.1};
RN [1] {ECO:0000313|EMBL:ACR61394.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhu H., Li Y., Wen Q.;
RL Submitted (AUG-2009) 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; FJ795343; ACR61394.1; -; mRNA.
DR AlphaFoldDB; C7T0M6; -.
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 72..536
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 569 AA; 62828 MW; 7722A8DE1F7D336A CRC64;
MASWVLLPVA PLTSRCLVAP VRSQRSSSIC ARSSLDTNVS DMSVNAPKGL FPPEPEHYRG
PKLKVAIIGA GLAGMSTAVE LLDQGHEVDI YESRPFIGGK VGSFVDKRGN HIEMGLHVFF
GCYSNLFRLM KKVGAEENLL VKDHTHTFVN KGGQIGELDF RFPIGAPIHG ILAFLSTNQI
KTYDKARNAL ALALSPVVKA LVDPDGALSD VRDLDSISFS DWFMSKGGTR TSIQRMWDPV
AYALGFIDCD NISARCMLTI FTLFATKTEA SLLRMLKGSP DVYLSGPIRK YIIDKGGRFY
LRWGCREILY DKSADGETYV AGLAMSKATN KQTVKADAYV AACDVPGIKR LLPSQWREWE
FFNNIYELVG VPVVTVQLRY DGWVTEMQDL ERSRQLKQAL GLDNLLYTPD ADFSCFADLA
LASPEDYYIE GQGSLLQCVL TPGDPYMPLP NEEIIAKVTK QVLTLFPSSQ GLEVTWSSVV
KIGQSLYREG PGKDPFRPDQ KTPVKNFFLA GSYTKQDYID SMEGATLSGR RASAYICNAG
EDLVQLRKKL ASQEGYTKAS NTTDELSLV
//