PSY1_MAIZE
ID PSY1_MAIZE Reviewed; 410 AA.
AC P49085; Q6EIC3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Phytoene synthase 1, chloroplastic {ECO:0000303|PubMed:15247400};
DE Short=ZmPSY1 {ECO:0000305};
DE EC=2.5.1.32 {ECO:0000269|PubMed:15247400};
DE Flags: Precursor;
GN Name=PSY1 {ECO:0000303|PubMed:15247400};
GN Synonyms=Y1 {ECO:0000303|PubMed:8722797};
GN ORFNames=ZEAMMB73_Zm00001d036345 {ECO:0000312|EMBL:AQK80705.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=8722797; DOI=10.1093/genetics/143.1.479;
RA Buckner B., Sanmiguel P., Janick-Buckner D., Bennetzen J.L.;
RT "The y1 gene of maize codes for phytoene synthase.";
RL Genetics 143:479-488(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=15247400; DOI=10.1104/pp.104.039818;
RA Gallagher C.E., Matthews P.D., Li F., Wurtzel E.T.;
RT "Gene duplication in the carotenoid biosynthetic pathway preceded evolution
RT of the grasses.";
RL Plant Physiol. 135:1776-1783(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RA Zhu C., Wurtzel E.T.;
RT "Zea mays phytoene synthase 1 (PSY1) mRNA, complete cds.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=23023170; DOI=10.1105/tpc.112.104174;
RA Shumskaya M., Bradbury L.M., Monaco R.R., Wurtzel E.T.;
RT "Plastid localization of the key carotenoid enzyme phytoene synthase is
RT altered by isozyme, allelic variation, and activity.";
RL Plant Cell 24:3725-3741(2012).
CC -!- FUNCTION: Catalyzes the conversion of geranylgeranyl diphosphate to
CC phytoene. Mediates the first committed step in carotenoid biosynthesis.
CC {ECO:0000269|PubMed:15247400}.
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:15247400};
CC -!- PATHWAY: Carotenoid biosynthesis; phytoene biosynthesis; all-trans-
CC phytoene from geranylgeranyl diphosphate: step 1/1. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:23023170}. Note=Forms punctuate spots in plastid
CC stroma. {ECO:0000269|PubMed:23023170}.
CC -!- TISSUE SPECIFICITY: Expressed in embryos, endosperm and seedling leaves
CC (PubMed:8722797). Expressed in leaves and endosperm (PubMed:8722797).
CC {ECO:0000269|PubMed:8722797}.
CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase family.
CC {ECO:0000305}.
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DR EMBL; U32636; AAB60314.1; -; Genomic_DNA.
DR EMBL; AY324431; AAR08445.1; -; Genomic_DNA.
DR EMBL; AY773475; AAX13806.1; -; mRNA.
DR EMBL; CM000782; AQK80705.1; -; Genomic_DNA.
DR EMBL; CM000782; AQK80706.1; -; Genomic_DNA.
DR EMBL; BT034021; ACF79026.1; -; mRNA.
DR PIR; S68307; S68307.
DR RefSeq; NP_001108124.2; NM_001114652.2.
DR AlphaFoldDB; P49085; -.
DR SMR; P49085; -.
DR STRING; 4577.GRMZM2G300348_P02; -.
DR PaxDb; P49085; -.
DR PRIDE; P49085; -.
DR EnsemblPlants; Zm00001eb271860_T001; Zm00001eb271860_P001; Zm00001eb271860.
DR GeneID; 100136882; -.
DR Gramene; Zm00001eb271860_T001; Zm00001eb271860_P001; Zm00001eb271860.
DR KEGG; zma:100136882; -.
DR MaizeGDB; 66643; -.
DR eggNOG; KOG1459; Eukaryota.
DR HOGENOM; CLU_037269_2_0_1; -.
DR OMA; WLLYAWC; -.
DR OrthoDB; 1463212at2759; -.
DR BioCyc; MetaCyc:GBWI-61910-MON; -.
DR BRENDA; 2.5.1.32; 6752.
DR UniPathway; UPA00799; UER00773.
DR Proteomes; UP000007305; Chromosome 6.
DR ExpressionAtlas; P49085; baseline and differential.
DR GO; GO:0010287; C:plastoglobule; IEA:EnsemblPlants.
DR GO; GO:0046905; F:15-cis-phytoene synthase activity; IBA:GO_Central.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:InterPro.
DR GO; GO:0016767; F:geranylgeranyl-diphosphate geranylgeranyltransferase activity; IBA:GO_Central.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IBA:GO_Central.
DR CDD; cd00683; Trans_IPPS_HH; 1.
DR Gene3D; 1.10.600.10; -; 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 Pfam; PF00494; SQS_PSY; 1.
DR SFLD; SFLDG01212; Phytoene_synthase_like; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR PROSITE; PS01044; SQUALEN_PHYTOEN_SYN_1; 1.
DR PROSITE; PS01045; SQUALEN_PHYTOEN_SYN_2; 1.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; Chloroplast; Isoprene biosynthesis; Plastid;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 63..410
FT /note="Phytoene synthase 1, chloroplastic"
FT /id="PRO_0000029858"
FT CONFLICT 66
FT /note="A -> P (in Ref. 1; AAB60314)"
FT CONFLICT 344
FT /note="T -> N (in Ref. 1; AAB60314)"
SQ SEQUENCE 410 AA; 46442 MW; D0AD0E679C1AF3D7 CRC64;
MAIILVRAAS PGLSAADSIS HQGTLQCSTL LKTKRPAARR WMPCSLLGLH PWEAGRPSPA
VYSSLAVNPA GEAVVSSEQK VYDVVLKQAA LLKRQLRTPV LDARPQDMDM PRNGLKEAYD
RCGEICEEYA KTFYLGTMLM TEERRRAIWA IYVWCRRTDE LVDGPNANYI TPTALDRWEK
RLEDLFTGRP YDMLDAALSD TISRFPIDIQ PFRDMIEGMR SDLRKTRYNN FDELYMYCYY
VAGTVGLMSV PVMGIATESK ATTESVYSAA LALGIANQLT NILRDVGEDA RRGRIYLPQD
ELAQAGLSDE DIFKGVVTNR WRNFMKRQIK RARMFFEEAE RGVTELSQAS RWPVWASLLL
YRQILDEIEA NDYNNFTKRA YVGKGKKLLA LPVAYGKSLL LPCSLRNGQT
