ID B9VUW2_BRARP Unreviewed; 565 AA.
AC B9VUW2;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Phytoene dehydrogenase {ECO:0000256|RuleBase:RU368016};
DE EC=1.3.5.5 {ECO:0000256|RuleBase:RU368016};
OS Brassica rapa subsp. pekinensis (Chinese cabbage) (Brassica pekinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=51351 {ECO:0000313|EMBL:ACM68700.1};
RN [1] {ECO:0000313|EMBL:ACM68700.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang L.G., Zhang H.M., Wu Y.X., Zhang Y.L.;
RT "Cloning and sequence analysis of the phytoene desaturase cDNA of Chinese
RT cabbage.";
RL Submitted (JAN-2009) 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|RuleBase:RU368016}. Membrane
CC {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}.
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; FJ606826; ACM68700.1; -; mRNA.
DR AlphaFoldDB; B9VUW2; -.
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:SF38; PHYTOENE DEHYDROGENASE; 1.
DR PANTHER; PTHR42923; 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|RuleBase:RU368016};
KW Chloroplast {ECO:0000256|RuleBase:RU368016};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368016};
KW Oxidoreductase {ECO:0000256|RuleBase:RU368016};
KW Plastid {ECO:0000256|RuleBase:RU368016}.
FT DOMAIN 101..543
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 565 AA; 63153 MW; F3BED69DC9DF0711 CRC64;
MVVFGNVSAA NLPYQNGFLK AISSGGCDLM GHRSFKISTS FKTRTRRRRS AGPLQVVCVD
IPRPELENTV NFLEAASLSA SFRSAPRPAK PLKVVIAGAG LAGLSTAKYL ADAGHKPLLL
EARDVLEGKI AAWKDADGDW YETGLHIFFG AYPNVQNLFG ELGINDRLQW KEHSMIFAMP
SKPGEFSRFD FPDVLPAPLN GIWAILRNNE MLTWPEKIKF AIGLLPAMVG GQAYVEAQDG
LSVEQWMRKQ GVPDRVTDEV FIAMSKALNF INPDELSMQC ILIALNRFLQ EKHGSKMAFL
DGNPPERLCM PIVEHIRSLG GEVRLNSRIR KIELEDDGTV KSFLLTDGTT IQGDAYVFAT
PVDILKLLLP DSWKEIPYFK RLEKLVGVPV INVHIWVDKK LKNTYDHLLF SRSNLLSVYA
DMSLTCKEYY DPNRSMLELV FAPAEEWISR SDSDIIDATM KELERLFPDE IAADQSKAKI
LKYHVVKTPR SVYKTIPDCE PCRPLQRSPI KGFYLAGDYT KQKYLASMEG AVLSGKFCSQ
SILQDYELLA ASSGPQKLSE TTLST
//