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Database: UniProt
Entry: A0A0E0CWA2_9ORYZ
LinkDB: A0A0E0CWA2_9ORYZ
Original site: A0A0E0CWA2_9ORYZ 
ID   A0A0E0CWA2_9ORYZ        Unreviewed;       582 AA.
AC   A0A0E0CWA2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Phytoene dehydrogenase {ECO:0000256|RuleBase:RU368016};
DE            EC=1.3.5.5 {ECO:0000256|RuleBase:RU368016};
OS   Oryza meridionalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI03G05990.1};
RN   [1] {ECO:0000313|EnsemblPlants:OMERI03G05990.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI03G05990.1};
RA   Wing R.A., Panaud O., Henry R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OMERI03G05990.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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   AlphaFoldDB; A0A0E0CWA2; -.
DR   EnsemblPlants; OMERI03G05990.1; OMERI03G05990.1; OMERI03G05990.
DR   Gramene; OMERI03G05990.1; OMERI03G05990.1; OMERI03G05990.
DR   HOGENOM; CLU_022687_1_0_1; -.
DR   UniPathway; UPA00803; -.
DR   Proteomes; UP000008021; Chromosome 3.
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:0050660; F:flavin adenine dinucleotide binding; IEA:UniProt.
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   3: Inferred from homology;
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008021}.
FT   DOMAIN          161..573
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   582 AA;  65015 MW;  60D7387925356A64 CRC64;
     MVVSSVCANH HFCMRRQTRS SPAALPKHSC VLICQIRSEY NFRSCFSMDT GCLSSMNITG
     TSQARSFAGQ LPTHRCFASG SIQALKSSQH VSFGVKSLVL RNKGKGFRRR LGALQVVCQD
     FPRPPLENTI NFLEAGQLSS FFRNSEQPTK PLQVVIAGAG LAGLSTAKYL ADAGHKPILL
     EARDVLGGKL LGRMKMEIGM KLGFISFNLF GELGINDRLQ WKEHSMIFAM PNKPGEFSRF
     DFPETLPAPL NGIWAILRNN EMLTWPEKVK FALGLLPAMV GGQAYVEAQD GLTVSEWMKK
     QGVPDRVNDE VFIAMSKALN FINPDELSMQ CILIALNRFL QEKHGSKMAF LDGNPPERLC
     MPIVDHVRSL GGEVRLNSRI QKIELNPDGT VKHFALTDGT QITGDAYVFA TPEWKEISYF
     KKLEKLVGVP VINVHIWFDR KLKNTYDHLL FSRSSLLSEY YDPNRSMLEL VFAPAEEWVG
     RSDTEIIEAT MQELAKLFPD EIAADQSKAK ILKYHVVKTP RSVYKTIPDC EPCRPLQRSP
     IEGFYLAGDY TKQKYLASME GAVLSGKFCA QSIVESEVPV AS
//
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