ID D8RV23_SELML Unreviewed; 556 AA.
AC D8RV23;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Phytoene dehydrogenase {ECO:0000256|RuleBase:RU368016};
DE EC=1.3.5.5 {ECO:0000256|RuleBase:RU368016};
GN ORFNames=SELMODRAFT_232430 {ECO:0000313|EMBL:EFJ23885.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ23885.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
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; GL377591; EFJ23885.1; -; Genomic_DNA.
DR RefSeq; XP_002975100.1; XM_002975054.1.
DR AlphaFoldDB; D8RV23; -.
DR STRING; 88036.D8RV23; -.
DR EnsemblPlants; EFJ23885; EFJ23885; SELMODRAFT_232430.
DR Gramene; EFJ23885; EFJ23885; SELMODRAFT_232430.
DR KEGG; smo:SELMODRAFT_232430; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_022687_1_0_1; -.
DR InParanoid; D8RV23; -.
DR OMA; THCFFGA; -.
DR UniPathway; UPA00803; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
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; 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 SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
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|RuleBase:RU368016};
KW Plastid {ECO:0000256|RuleBase:RU368016};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514}.
FT DOMAIN 107..549
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 556 AA; 61276 MW; 6C6BBE88675FEBA3 CRC64;
MSNLAQTGES SLLCGTAKEA LSSCDTGRRT GSSLDGCDAP VFSSTSLLPA IAEPRARGNS
RVVCKDYPRP EIDSTVNFLE AAALSASLRN APRPSEPLKI VIAGAGLAGL STAKYVADAG
HIPIVLEARD VLGGKVAAWK DKDGDWYETG LHIFFGAYPN VQNLFGELGI NDRLQWKEHS
MIFARPDKPG EFSRFDFPEL PAPFNGVLAI LKNNEMLTWP EKIRFAIGLL PAIVGGQKYV
EAQDNLTVKE WMIKQGVPER VNDEVFIAMS KALNFINPDE LSMQCVLIAL NRFLQESHGS
KMAFLDGNPP ERLCTPIVDH FSKLGGEVRL NSQLQKIVVN DDGRVKHFAL TDGSIVEGDV
YVSAMPVDIL KLLLPESWKE MPYFKKLSKL VGVPVINVHI WFDRKLKNTY DHLLFSRSPL
LSVYADMSTT CKEYADPNKS MLELVFAPAD KWIARSEEDI LDATMQELAK LFPDEIAADG
SKAKVLKYHI VKTPRQASVY KTVPDCEPCR PLQRSPLRGF YLAGDFTKQK YLASMEGAVL
SGKLCAMSIV QASGVC
//