ID T1SI66_CAMSI Unreviewed; 582 AA.
AC T1SI66;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Phytoene dehydrogenase {ECO:0000256|RuleBase:RU368016};
DE EC=1.3.5.5 {ECO:0000256|RuleBase:RU368016};
OS Camellia sinensis (Tea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Theaceae; Camellia.
OX NCBI_TaxID=4442 {ECO:0000313|EMBL:AGT45481.1};
RN [1] {ECO:0000313|EMBL:AGT45481.1}
RP NUCLEOTIDE SEQUENCE.
RA Deng T., Wu Y., Liu S., Li Y., Li J., Huang J., Liu Z.;
RT "Molecular cloning and characterization of the full-length cDNA encoding
RT the phytoene desaturase gene from Camellia sinensis.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts phytoene into zeta-carotene via the intermediary of
CC phytofluene by the symmetrical introduction of two double bonds at the
CC C-11 and C-11' positions of phytoene with a concomitant isomerization
CC of two neighboring double bonds at the C9 and C9' positions from trans
CC to cis. {ECO:0000256|RuleBase:RU368016}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=15-cis-phytoene + 2 a plastoquinone = 9,9',15-tri-cis-zeta-
CC carotene + 2 a plastoquinol; Xref=Rhea:RHEA:30287, Rhea:RHEA-
CC COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:17757, ChEBI:CHEBI:27787,
CC ChEBI:CHEBI:48717, ChEBI:CHEBI:62192; EC=1.3.5.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001534,
CC ECO:0000256|RuleBase:RU368016};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU368016};
CC -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004900, ECO:0000256|RuleBase:RU368016}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU368016}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|RuleBase:RU368016}. Plastid, chromoplast
CC {ECO:0000256|ARBA:ARBA00004260, ECO:0000256|RuleBase:RU368016}.
CC Membrane {ECO:0000256|RuleBase:RU368016}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU368016}.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006046, ECO:0000256|RuleBase:RU368016}.
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DR EMBL; KC915039; AGT45481.1; -; mRNA.
DR AlphaFoldDB; T1SI66; -.
DR UniPathway; UPA00803; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009509; C:chromoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016166; F:phytoene dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR014102; Phytoene_desaturase.
DR NCBIfam; TIGR02731; phytoene_desat; 1.
DR PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR PANTHER; PTHR42923:SF3; PROTOPORPHYRINOGEN OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 2: Evidence at transcript level;
KW Carotenoid biosynthesis {ECO:0000256|ARBA:ARBA00022746,
KW ECO:0000256|RuleBase:RU368016};
KW Chloroplast {ECO:0000256|RuleBase:RU368016};
KW Chromoplast {ECO:0000256|ARBA:ARBA00022904};
KW Membrane {ECO:0000256|RuleBase:RU368016};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU368016}; Plastid {ECO:0000256|RuleBase:RU368016}.
FT DOMAIN 120..561
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 582 AA; 64955 MW; B58E50F0E09B9DF4 CRC64;
MSQFGQVSTI SVSGQNNGIS VWNPKSTWGC GCSFGSGPAK ALSFRGSDSM GHRFKIPNAY
AVGTRPRKDV CPLKVVCIDY PRPDLESTVN FLEAAYLSST FRTSRRPDKP LKVVIAGAGL
AGLSTAKYLA DAGHKPVLLE ARDVLGGKVA AWKDDDGDWY ETGLHIFFGA YPNVQNLFGE
LGINDRLQWK EHSMIFAMPN KPGEFSRFDF PEVLPAPLNG IWAILKNNEM LTWPEKIKFA
IGLIPAILGG QAYVEAQDVL SVKDWMRKQG IPDRVTTEVF IAMSKALNFI NPDELSMQCI
LIALNRFLQE KHGSKMAFLD GNPPERLCRP IVDHIQSLGG EVQLNSRIKK IELNKDGTVK
SFLLNNGNAI EGDAYVFATP VDILKLLLPE DWKEIPYFRK LEILVGVPVI NVHIWFDRKL
RNTYDHLLFS RSPLLSVYAD MSVACKEYYD PNRSMLELVF APAEEWISCS DEEIIDATMK
ELAKLFPDEI SADQSKAKIL KYHVVKTPRS VYKTVPNCEP CRPLQRSPVE GFYLSGDYTK
QKYLASMEGA VLSGKLCAQA IVQDYEKLVA REQGKLAEAS VV
//
