ID   CRTB_PARSN              Reviewed;         304 AA.
AC   P54975; Q33DT6;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=15-cis-phytoene synthase;
DE            Short=PSase;
DE            EC=2.5.1.32;
GN   Name=crtB;
OS   Paracoccus sp. (strain N81106 / MBIC 01143) (Agrobacterium aurantiacum).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus; unclassified Paracoccus (in: Bacteria).
OX   NCBI_TaxID=81397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=7592436; DOI=10.1128/jb.177.22.6575-6584.1995;
RA   Misawa N., Satomi Y., Kondo K., Yokoyama A., Kajiwara S., Saito T.,
RA   Ohtani T., Miki W.;
RT   "Structure and functional analysis of a marine bacterial carotenoid
RT   biosynthesis gene cluster and astaxanthin biosynthetic pathway proposed at
RT   the gene level.";
RL   J. Bacteriol. 177:6575-6584(1995).
RN   [2]
RP   SEQUENCE REVISION TO 56; 90-92 AND 284-295.
RA   Misawa N.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Maruyama T., Inomata Y., Haga M., Ide T., Misawa N.;
RT   "Structure of the complete carotenoid biosynthesis gene cluster of
RT   Paracoccus sp. strain N81106.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of carotenoids for the
CC       production of astaxanthin. Catalyzes the condensation of two molecules
CC       of geranylgeranyl diphosphate (GGPP) to give prephytoene diphosphate
CC       (PPPP) and the subsequent rearrangement of the cyclopropylcarbinyl
CC       intermediate to yield 15-cis phytoene. {ECO:0000269|PubMed:7592436}.
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:7592436};
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; astaxanthin biosynthesis.
CC   -!- PATHWAY: Carotenoid biosynthesis; phytoene biosynthesis.
CC   -!- SIMILARITY: Belongs to the phytoene/squalene synthase family.
CC       {ECO:0000305}.
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DR   EMBL; D58420; BAA09595.2; -; Genomic_DNA.
DR   EMBL; AB206672; BAE47469.1; -; Genomic_DNA.
DR   AlphaFoldDB; P54975; -.
DR   SMR; P54975; -.
DR   UniPathway; UPA00387; -.
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   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..304
FT                   /note="15-cis-phytoene synthase"
FT                   /id="PRO_0000067430"
SQ   SEQUENCE   304 AA;  33030 MW;  A9C253BED2B90E00 CRC64;
     MSDLVLTSTE AITQGSQSFA TAAKLMPPGI RDDTVMLYAW CRHADDVIDG QALGSRPEAV
     NDPQARLDGL RADTLAALQG DGPVTPPFAA LRAVARRHDF PQAWPMDLIE GFAMDVEARD
     YRTLDDVLEY SYHVAGIVGV MMARVMGVRD DPVLDRACDL GLAFQLTNIA RDVIDDARIG
     RCYLPGDWLD QAGARVDGPV PSPELYTVIL RLLDAAELYY ASARVGLADL PPRCAWSIAA
     ALRIYRAIGL RIRKGGPEAY RQRISTSKAA KIGLLGIGGW DVARSRLPGA GVSRQGLWTR
     PHHA