CRTB_ENTAG
ID CRTB_ENTAG Reviewed; 295 AA.
AC D5KXJ0;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=15-cis-phytoene synthase {ECO:0000305};
DE EC=2.5.1.32 {ECO:0000269|PubMed:12641468};
DE AltName: Full=Phytoene synthase;
DE Short=PSase;
GN Name=crtB;
OS Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea; Pantoea agglomerans group.
OX NCBI_TaxID=549;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=206;
RA Galinousky D.V.;
RT "Sequencing of the bacterial phytoene synthase gene and comparing with psy-
RT gene of plants.";
RL Vestsi Natsyianalnai Akademii Navuk Belarusi Ser. Biyalagichnykh Navuk
RL 1:30-34(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP ACTIVITY REGULATION.
RX PubMed=12641468; DOI=10.1021/bi0206614;
RA Iwata-Reuyl D., Math S.K., Desai S.B., Poulter C.D.;
RT "Bacterial phytoene synthase: molecular cloning, expression, and
RT characterization of Erwinia herbicola phytoene synthase.";
RL Biochemistry 42:3359-3365(2003).
CC -!- FUNCTION: Involved in the biosynthesis of carotenoids. Catalyzes
CC stereoselectively the condensation of two molecules of geranylgeranyl
CC diphosphate (GGPP) to give prephytoene diphosphate (PPPP) and the
CC subsequent rearrangement of the cyclopropylcarbinyl intermediate to
CC yield 15-cis-phytoene. {ECO:0000269|PubMed:12641468}.
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:12641468};
CC -!- COFACTOR:
CC Name=ATP; Xref=ChEBI:CHEBI:30616;
CC Evidence={ECO:0000269|PubMed:12641468};
CC Note=ATP is required for the transferase activity but it does not seem
CC to be hydrolyzed during the reaction. {ECO:0000269|PubMed:12641468};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12641468};
CC -!- ACTIVITY REGULATION: Significant inhibition is seen at GGPP
CC concentrations above 100 uM. {ECO:0000269|PubMed:12641468}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.2. {ECO:0000269|PubMed:12641468};
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:0000305|PubMed:12641468}.
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DR EMBL; GU721093; ADD97675.1; -; Genomic_DNA.
DR AlphaFoldDB; D5KXJ0; -.
DR SMR; D5KXJ0; -.
DR STRING; 549.BW31_02395; -.
DR KEGG; ag:ADD97675; -.
DR eggNOG; COG1562; Bacteria.
DR UniPathway; UPA00799; -.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:InterPro.
DR GO; GO:0016767; F:geranylgeranyl-diphosphate geranylgeranyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; 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; -; 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; Manganese; Metal-binding; Transferase.
FT CHAIN 1..295
FT /note="15-cis-phytoene synthase"
FT /id="PRO_0000423168"
SQ SEQUENCE 295 AA; 32786 MW; 7F366B6FFF83956C CRC64;
MEVGSKSFAT ASKLFDAKTR RSVLMLYAWC RHCDDVIDDQ VLGFSNDTPS LQSAEQRLAQ
LEMKTRQPMR IQMHEPAFAA FQEVAMAHDI LPAYAFDHLA GFAMDVHETR YQTLDDTLRY
CYHVAGVVGL MMAQIMGVRD NATLDRACDL GLAFQLTNIA RDIVEDAEAG RCYLPAAWLA
EEGLTRENLA DPQNRKALSR VARRLVETAE PYYRSASAGL PGLPLRSAWA IATAQQVYRK
IGMKVVQAGS QAWEQRQSTS TPEKLALLVA ASGQAVTSRV ARHAPRSADL WQRPV