ID   CRTB_SYNE7              Reviewed;         308 AA.
AC   P37269; Q31LQ5;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=15-cis-phytoene synthase {ECO:0000305};
DE            Short=PSase;
DE            EC=2.5.1.32 {ECO:0000269|PubMed:1537409};
GN   Name=crtB; Synonyms=pys; OrderedLocusNames=Synpcc7942_1984;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=1537409; DOI=10.1016/0014-5793(92)80310-d;
RA   Chamovitz D., Misawa D., Sandmann N., Hirshberg J.;
RT   "Molecular cloning and expression in Escherichia coli of a cyanobacterial
RT   gene coding for phytoene synthase, a carotenoid biosynthesis enzyme.";
RL   FEBS Lett. 296:305-310(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of carotenoids. Catalyzes the
CC       condensation of two molecules of geranylgeranyl diphosphate (GGPP) to
CC       give prephytoene diphosphate (PPPP) and the subsequent rearrangement of
CC       the cyclopropylcarbinyl intermediate to yield 15-cis-phytoene.
CC       {ECO:0000269|PubMed:1537409}.
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:1537409};
CC   -!- COFACTOR:
CC       Name=ATP; Xref=ChEBI:CHEBI:30616; Evidence={ECO:0000250};
CC       Note=ATP is required for the transferase activity but it does not seem
CC       to be hydrolyzed during the reaction. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Carotenoid biosynthesis; phytoene biosynthesis.
CC   -!- SIMILARITY: Belongs to the phytoene/squalene synthase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: The enzyme produces 15-cis-phytoene. The conversion to all-
CC       trans-phytoene is due to photoisomerisation.
CC       {ECO:0000250|UniProtKB:D5KXJ0}.
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DR   EMBL; X63873; CAA45350.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB58014.1; -; Genomic_DNA.
DR   PIR; S20383; S20383.
DR   RefSeq; WP_011244422.1; NC_007604.1.
DR   AlphaFoldDB; P37269; -.
DR   SMR; P37269; -.
DR   STRING; 1140.Synpcc7942_1984; -.
DR   PRIDE; P37269; -.
DR   DNASU; 3774171; -.
DR   EnsemblBacteria; ABB58014; ABB58014; Synpcc7942_1984.
DR   KEGG; syf:Synpcc7942_1984; -.
DR   eggNOG; COG1562; Bacteria.
DR   HOGENOM; CLU_037269_1_3_3; -.
DR   OMA; KLYCYRV; -.
DR   OrthoDB; 1449625at2; -.
DR   BioCyc; MetaCyc:SYNPCC7942_1984-MON; -.
DR   BioCyc; SYNEL:SYNPCC7942_1984-MON; -.
DR   UniPathway; UPA00799; -.
DR   GO; GO:0004311; F:farnesyltranstransferase activity; IEA:InterPro.
DR   GO; GO:0016767; F:geranylgeranyl-diphosphate geranylgeranyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IDA:UniProtKB.
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   SFLD; SFLDG01018; Squalene/Phytoene_Synthase_Lik; 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; Magnesium; Manganese; Metal-binding; Transferase.
FT   CHAIN           1..308
FT                   /note="15-cis-phytoene synthase"
FT                   /id="PRO_0000067437"
FT   CONFLICT        249
FT                   /note="G -> C (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        251..252
FT                   /note="RQ -> E (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   308 AA;  35891 MW;  9399E7308C4FFC18 CRC64;
     MLQMIPARPS RALASLSEAY EECRQITARY AKTFYLGTLL MPEAKRQAIW AIYVWCRRTD
     ELVDGPQAAQ TNFATLDAWE RRLERLFAGE PEDDCDVALV DTLARYPLDI QPFRDMIEGQ
     RMDLLQNRYS TFEDLYTYCY RVAGTVGLMS QPVMGIESTN SRAPWDPTTP PDPTQEALAL
     GIANQLTNIL RDVGEDARRG RIYLPQEELA QFNYSEQDLF NGVIDDRWRA FMQFQLDRAR
     DYFEQAERGI RQLSHDARWP VWASLMLYRE ILDVIEQNNY DVFRKRAYVP TWRKLCSLPV
     AMLRATVL