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Database: UniProt
Entry: Q6J213_CHLRE
LinkDB: Q6J213_CHLRE
Original site: Q6J213_CHLRE 
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}.
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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
//
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