ID Q6J213_CHLRE Unreviewed; 564 AA.
AC Q6J213;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 115.
DE RecName: Full=Phytoene dehydrogenase {ECO:0000256|RuleBase:RU368016};
DE EC=1.3.5.5 {ECO:0000256|RuleBase:RU368016};
GN Name=PDS {ECO:0000313|EMBL:AAT38476.1};
GN ORFNames=CHLRE_12g509650v5 {ECO:0000313|EMBL:PNW74792.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055 {ECO:0000313|EMBL:AAT38476.1};
RN [1] {ECO:0000313|EMBL:AAT38476.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15579683; DOI=10.1534/genetics.104.030635;
RA McCarthy S.S., Kobayashi M.C., Niyogi K.K.;
RT "White mutants of Chlamydomonas reinhardtii are defective in phytoene
RT synthase.";
RL Genetics 168:1249-1257(2004).
RN [2] {ECO:0000313|EMBL:PNW74792.1, ECO:0000313|Proteomes:UP000006906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906}, and CC-503 cw92 mt+
RC {ECO:0000313|EMBL:PNW74792.1};
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [3] {ECO:0000313|EMBL:PNW74792.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CC-503 cw92 mt+ {ECO:0000313|EMBL:PNW74792.1};
RG Chlamydomonas Annotation Team;
RG JGI Annotation Team;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Grigoriev I.V., Rokhsar D.S.;
RT "WGS assembly of Chlamydomonas reinhardtii.";
RL Submitted (JUL-2017) 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|ARBA:ARBA00001974,
CC 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}.
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; AY604703; AAT38476.1; -; mRNA.
DR EMBL; CM008973; PNW74792.1; -; Genomic_DNA.
DR RefSeq; XP_001690859.1; XM_001690807.1.
DR STRING; 3055.Q6J213; -.
DR PaxDb; 3055-EDP05305; -.
DR EnsemblPlants; PNW74792; PNW74792; CHLRE_12g509650v5.
DR GeneID; 5716547; -.
DR Gramene; PNW74792; PNW74792; CHLRE_12g509650v5.
DR KEGG; cre:CHLRE_12g509650v5; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_022687_1_0_1; -.
DR OMA; HSMIFNQ; -.
DR OrthoDB; 3597164at2759; -.
DR BRENDA; 1.3.99.29; 1318.
DR UniPathway; UPA00803; -.
DR Proteomes; UP000006906; Chromosome 12.
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:0016491; F:oxidoreductase activity; IBA:GO_Central.
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; IPR001613; Flavin_amine_oxidase.
DR InterPro; IPR014102; Phytoene_desaturase.
DR NCBIfam; TIGR02731; phytoene_desat; 1.
DR PANTHER; PTHR42923:SF41; 15-CIS-PHYTOENE DESATURASE, CHLOROPLASTIC/CHROMOPLASTIC-RELATED; 1.
DR PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
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 Chromoplast {ECO:0000256|ARBA:ARBA00022904};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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:UP000006906};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 543..562
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 83..522
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 564 AA; 62837 MW; 61A1A7296C21F9E5 CRC64;
MQTQVKPSSS RQANLVAKGA SCPRVAVRRV AGRRALEVVA RDYPRPAFET AETFQEAKAL
SSKLKDAPRP AKPLKVVIAG AGLAGLSAAK YLSDAGHHPI VLEGRDVLGG KVAAWKDEDG
DWYETGLHIF FGAYPNMMNV FKELNIEERL QWKEHSMIFA MPDSPGEFSR FDFPDIPAPF
NGVFAILRNN QMLTWPEKIQ FAIGLLPAII FGQKYVEEQD HLSVTQWMRQ QGVPDRVNEE
VFIAMAKALA FIDPDRLSMT VVLTALNRFL QERHGSKMAF LDGAPPERLC QPMVDHFTAR
GGELKMNARV KDIVLNDDGS VKHYKLTTGE VVEGDLYMSA MPVDILKLLV PDQWKPNPYF
SQLKELEGVP VINIHIWFDR KLTTVDHLLF SRSPLLSVYA DMSTTCKEYY DTEKSMLELV
FAPAKDWIGR SDEDIIAATM TELERLFPTE IKADQSLAKI RKYKVIKTPL SVYESRAGRE
AFRPSQRTPI KNFFLAGDFT KQKYLASMEG AIFSGKLAAE QIVNDYNYKG VAPPARSSSS
PELVAASALL AVAAVGAGLV GFGR
//