ID   CRTB_THET2              Reviewed;         289 AA.
AC   P37270;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Phytoene synthase;
DE            Short=PSase;
DE            EC=2.5.1.-;
GN   Name=crtB; OrderedLocusNames=TT_P0057;
OS   Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OG   Plasmid pTT27.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=262724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=8215386; DOI=10.1128/aem.59.9.3150-3153.1993;
RA   Hoshino T., Fujii R., Nakahara T.;
RT   "Molecular cloning and sequence analysis of the crtB gene of Thermus
RT   thermophilus HB27, an extreme thermophile producing carotenoid pigments.";
RL   Appl. Environ. Microbiol. 59:3150-3153(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-163 / DSM 7039 / HB27; PLASMID=pTT27;
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA   Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA   Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA   Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL   Nat. Biotechnol. 22:547-553(2004).
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 phytoene (Probable).
CC       {ECO:0000305|PubMed:8215386}.
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}.
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DR   EMBL; AB001637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AE017222; AAS82387.1; -; Genomic_DNA.
DR   AlphaFoldDB; P37270; -.
DR   SMR; P37270; -.
DR   STRING; 262724.TT_P0057; -.
DR   EnsemblBacteria; AAS82387; AAS82387; TT_P0057.
DR   KEGG; tth:TT_P0057; -.
DR   eggNOG; COG1562; Bacteria.
DR   HOGENOM; CLU_037269_1_3_0; -.
DR   OMA; KLYCYRV; -.
DR   UniPathway; UPA00799; -.
DR   Proteomes; UP000000592; Plasmid pTT27.
DR   GO; GO:0004311; F:farnesyltranstransferase activity; IEA:InterPro.
DR   GO; GO:0016767; F:geranylgeranyl-diphosphate geranylgeranyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; ISS: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   3: Inferred from homology;
KW   Carotenoid biosynthesis; Magnesium; Manganese; Metal-binding; Plasmid;
KW   Transferase.
FT   CHAIN           1..289
FT                   /note="Phytoene synthase"
FT                   /id="PRO_0000067439"
SQ   SEQUENCE   289 AA;  31964 MW;  3E58C1141902D3C5 CRC64;
     MKMPASMEPD WKALLRVLRA HSATFYLGSL LFPKEARKGA WAVYAACRLG DEAVDGEGGG
     PEALEAWWAG VERAYRGRPL AEWEKGLAWA LERWDIPFEA FLHMREGFLT DLGPVRLGTE
     AELLRYCYQV AGTVGRMMAP IAGGGKEAEA RAVKLGQAMQ LTNILRDVGE DLERDRVYLP
     LDLLRAHGVE VEDLRAGRVT PGYRALMAHL EGKARALYRE GLAGLGHLKV GRAAIALAAL
     QYRGILDKLR LSGYDNLGRR AHLKAWERAL LLPKAFLAAR FPPRPEGSP