ID PSY_ARATH Reviewed; 422 AA. AC P37271; O22375; Q8LE86; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2003, sequence version 2. DT 27-MAR-2024, entry version 165. DE RecName: Full=Phytoene synthase 1, chloroplastic {ECO:0000303|PubMed:8016277, ECO:0000303|Ref.2}; DE EC=2.5.1.32 {ECO:0000269|PubMed:25675505}; DE Flags: Precursor; GN Name=PSY1 {ECO:0000303|PubMed:8016277}; GN Synonyms=PSY {ECO:0000303|Ref.2}; GN OrderedLocusNames=At5g17230 {ECO:0000312|Araport:AT5G17230}; GN ORFNames=MKP11.8 {ECO:0000312|EMBL:BAB10510.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Columbia; TISSUE=Etiolated seedling; RX PubMed=8016277; DOI=10.1104/pp.104.4.1471; RA Scolnik P.A., Bartley G.E.; RT "Nucleotide sequence of an Arabidopsis cDNA for phytoene synthase."; RL Plant Physiol. 104:1471-1472(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Columbia; RA Castrignano F., Giuliano G.; RT "Sequence of the phytoene synthase gene of Arabidopsis."; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=9330910; DOI=10.1093/dnares/4.3.215; RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., RA Miyajima N., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence RT features of the 1.6 Mb regions covered by twenty physically assigned P1 RT clones."; RL DNA Res. 4:215-230(1997). RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [7] RP INTERACTION WITH OR, AND SUBCELLULAR LOCATION. RX PubMed=26224804; DOI=10.1104/pp.15.00971; RA Yuan H., Owsiany K., Sheeja T.E., Zhou X., Rodriguez C., Li Y., Welsch R., RA Chayut N., Yang Y., Thannhauser T.W., Parthasarathy M.V., Xu Q., Deng X., RA Fei Z., Schaffer A., Katzir N., Burger J., Tadmor Y., Li L.; RT "A single amino acid substitution in an ORANGE protein promotes carotenoid RT overaccumulation in Arabidopsis."; RL Plant Physiol. 169:421-431(2015). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH OR AND ORLIKE, AND RP SUBCELLULAR LOCATION. RX PubMed=25675505; DOI=10.1073/pnas.1420831112; RA Zhou X., Welsch R., Yang Y., Alvarez D., Riediger M., Yuan H., Fish T., RA Liu J., Thannhauser T.W., Li L.; RT "Arabidopsis OR proteins are the major posttranscriptional regulators of RT phytoene synthase in controlling carotenoid biosynthesis."; RL Proc. Natl. Acad. Sci. U.S.A. 112:3558-3563(2015). CC -!- FUNCTION: Catalyzes the reaction from prephytoene diphosphate to CC phytoene. {ECO:0000269|PubMed:25675505}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 (2E,6E,10E)-geranylgeranyl diphosphate = 15-cis-phytoene + 2 CC diphosphate; Xref=Rhea:RHEA:34475, ChEBI:CHEBI:27787, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58756; EC=2.5.1.32; CC Evidence={ECO:0000269|PubMed:25675505}; CC -!- PATHWAY: Carotenoid biosynthesis; phytoene biosynthesis; all-trans- CC phytoene from geranylgeranyl diphosphate: step 1/1. {ECO:0000305}. CC -!- SUBUNIT: Monomer (By similarity). Interacts with OR (PubMed:26224804, CC PubMed:25675505). Interacts with ORLIKE (PubMed:25675505). CC {ECO:0000250, ECO:0000269|PubMed:25675505, CC ECO:0000269|PubMed:26224804}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane CC {ECO:0000269|PubMed:25675505, ECO:0000269|PubMed:26224804}; Peripheral CC membrane protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences.; CC Name=1; CC IsoId=P37271-1; Sequence=Displayed; CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase family. CC {ECO:0000305}. 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; L25812; AAA32836.1; -; mRNA. DR EMBL; AF009954; AAB65697.1; -; Genomic_DNA. DR EMBL; AB005238; BAB10510.1; -; Genomic_DNA. DR EMBL; CP002688; AED92399.1; -; Genomic_DNA. DR EMBL; CP002688; AED92400.1; -; Genomic_DNA. DR EMBL; CP002688; ANM69856.1; -; Genomic_DNA. DR EMBL; BT000450; AAN17427.1; -; mRNA. DR EMBL; BT002084; AAN72095.1; -; mRNA. DR EMBL; AY085565; AAM62787.1; -; mRNA. DR RefSeq; NP_001031895.1; NM_001036818.2. [P37271-1] DR RefSeq; NP_001331504.1; NM_001343484.1. [P37271-1] DR RefSeq; NP_197225.1; NM_121729.3. [P37271-1] DR AlphaFoldDB; P37271; -. DR SMR; P37271; -. DR BioGRID; 16863; 3. DR STRING; 3702.P37271; -. DR PaxDb; 3702-AT5G17230-3; -. DR ProteomicsDB; 248672; -. [P37271-1] DR EnsemblPlants; AT5G17230.1; AT5G17230.1; AT5G17230. [P37271-1] DR EnsemblPlants; AT5G17230.2; AT5G17230.2; AT5G17230. [P37271-1] DR EnsemblPlants; AT5G17230.4; AT5G17230.4; AT5G17230. [P37271-1] DR GeneID; 831587; -. DR Gramene; AT5G17230.1; AT5G17230.1; AT5G17230. [P37271-1] DR Gramene; AT5G17230.2; AT5G17230.2; AT5G17230. [P37271-1] DR Gramene; AT5G17230.4; AT5G17230.4; AT5G17230. [P37271-1] DR KEGG; ath:AT5G17230; -. DR Araport; AT5G17230; -. DR TAIR; AT5G17230; PSY. DR eggNOG; KOG1459; Eukaryota. DR InParanoid; P37271; -. DR OMA; YSTRAQK; -. DR PhylomeDB; P37271; -. DR BioCyc; ARA:AT5G17230-MONOMER; -. DR BioCyc; MetaCyc:AT5G17230-MONOMER; -. DR BRENDA; 2.5.1.32; 399. DR UniPathway; UPA00799; UER00773. DR PRO; PR:P37271; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; P37271; baseline and differential. DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB. DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:InterPro. DR GO; GO:0016767; F:geranylgeranyl-diphosphate geranylgeranyltransferase activity; IDA:UniProtKB. DR GO; GO:0016117; P:carotenoid biosynthetic process; IDA:UniProtKB. DR CDD; cd00683; Trans_IPPS_HH; 1. DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1. DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf. DR InterPro; IPR002060; Squ/phyt_synthse. DR InterPro; IPR019845; Squalene/phytoene_synthase_CS. DR InterPro; IPR044843; Trans_IPPS_bact-type. DR InterPro; IPR033904; Trans_IPPS_HH. DR PANTHER; PTHR31480; BIFUNCTIONAL LYCOPENE CYCLASE/PHYTOENE SYNTHASE; 1. DR PANTHER; PTHR31480:SF2; PHYTOENE SYNTHASE, CHLOROPLASTIC; 1. DR Pfam; PF00494; SQS_PSY; 1. DR SFLD; SFLDG01212; Phytoene_synthase_like; 1. DR SFLD; SFLDG01018; Squalene/Phytoene_Synthase_Lik; 1. DR SUPFAM; SSF48576; Terpenoid synthases; 1. DR PROSITE; PS01044; SQUALEN_PHYTOEN_SYN_1; 1. DR PROSITE; PS01045; SQUALEN_PHYTOEN_SYN_2; 1. DR Genevisible; P37271; AT. PE 1: Evidence at protein level; KW Alternative splicing; Carotenoid biosynthesis; Chloroplast; KW Isoprene biosynthesis; Membrane; Plastid; Reference proteome; Transferase; KW Transit peptide. FT TRANSIT 1..70 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 71..422 FT /note="Phytoene synthase 1, chloroplastic" FT /id="PRO_0000029852" FT CONFLICT 60 FT /note="R -> M (in Ref. 6; AAM62787)" FT /evidence="ECO:0000305" FT CONFLICT 128 FT /note="L -> LV (in Ref. 1; AAA32836)" FT /evidence="ECO:0000305" FT CONFLICT 143 FT /note="A -> P (in Ref. 1; AAA32836)" FT /evidence="ECO:0000305" SQ SEQUENCE 422 AA; 47487 MW; C44F0A512F2DD31E CRC64; MSSSVAVLWV ATSSLNPDPM NNCGLVRVLE SSRLFSPCQN QRLNKGKKKQ IPTWSSSFVR NRSRRIGVVS SSLVASPSGE IALSSEEKVY NVVLKQAALV NKQLRSSSYD LDVKKPQDVV LPGSLSLLGE AYDRCGEVCA EYAKTFYLGT LLMTPERRKA IWAIYVWCRR TDELVDGPNA SHITPMALDR WEARLEDLFR GRPFDMLDAA LADTVARYPV DIQPFRDMIE GMRMDLKKSR YQNFDDLYLY CYYVAGTVGL MSVPVMGIDP KSKATTESVY NAALALGIAN QLTNILRDVG EDARRGRVYL PQDELAQAGL SDEDIFAGKV TDKWRNFMKM QLKRARMFFD EAEKGVTELS AASRWPVWAS LLLYRRILDE IEANDYNNFT KRAYVGKVKK IAALPLAYAK SVLKTSSSRL SI //