ID   CRIT_STRCO              Reviewed;         564 AA.
AC   Q9ACU1;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Bifunctional protein CrtB/UppS;
DE   Includes:
DE     RecName: Full=Phytoene synthase;
DE              EC=2.5.1.32;
DE   Includes:
DE     RecName: Full=Isoprenyl transferase;
DE              EC=2.5.1.-;
GN   Name=crtB/uppS3; OrderedLocusNames=SCP1.212;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OG   Plasmid SCP1.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Catalyzes the reaction from prephytoene diphosphate to
CC       phytoene. {ECO:0000250}.
CC   -!- FUNCTION: Catalyzes the condensation of isopentenyl diphosphate (IPP)
CC       with allylic pyrophosphates generating different type of terpenoids.
CC       {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Carotenoid biosynthesis; phytoene biosynthesis; all-trans-
CC       phytoene from geranylgeranyl diphosphate: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the phytoene/squalene
CC       synthase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the UPP synthase
CC       family. {ECO:0000305}.
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DR   EMBL; AL589148; CAC36733.1; -; Genomic_DNA.
DR   RefSeq; NP_639818.1; NC_003903.1.
DR   RefSeq; WP_011039510.1; NC_003903.1.
DR   AlphaFoldDB; Q9ACU1; -.
DR   SMR; Q9ACU1; -.
DR   GeneID; 1095290; -.
DR   KEGG; sco:SCP1.212; -.
DR   PATRIC; fig|100226.15.peg.8152; -.
DR   HOGENOM; CLU_035230_0_0_11; -.
DR   InParanoid; Q9ACU1; -.
DR   OMA; EWRERAH; -.
DR   UniPathway; UPA00799; UER00773.
DR   Proteomes; UP000001973; Plasmid SCP1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0008834; F:di-trans,poly-cis-decaprenylcistransferase activity; IBA:GO_Central.
DR   GO; GO:0016767; F:geranylgeranyl-diphosphate geranylgeranyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR   GO; GO:0002094; F:polyprenyltransferase activity; IBA:GO_Central.
DR   GO; GO:0033850; F:Z-farnesyl diphosphate synthase activity; IBA:GO_Central.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016094; P:polyprenol biosynthetic process; IBA:GO_Central.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd00475; Cis_IPPS; 1.
DR   Gene3D; 1.10.600.10; -; 1.
DR   Gene3D; 3.40.1180.10; -; 1.
DR   HAMAP; MF_01139; ISPT; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR002060; Squ/phyt_synthse.
DR   InterPro; IPR019845; Squalene/phytoene_synthase_CS.
DR   InterPro; IPR001441; UPP_synth-like.
DR   InterPro; IPR018520; UPP_synth-like_CS.
DR   InterPro; IPR036424; UPP_synth-like_sf.
DR   PANTHER; PTHR10291; PTHR10291; 1.
DR   Pfam; PF01255; Prenyltransf; 1.
DR   Pfam; PF00494; SQS_PSY; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
DR   SUPFAM; SSF64005; SSF64005; 1.
DR   TIGRFAMs; TIGR00055; uppS; 1.
DR   PROSITE; PS01045; SQUALEN_PHYTOEN_SYN_2; 1.
DR   PROSITE; PS01066; UPP_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Carotenoid biosynthesis; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Magnesium; Metal-binding;
KW   Multifunctional enzyme; Peptidoglycan synthesis; Plasmid;
KW   Reference proteome; Transferase.
FT   CHAIN           1..564
FT                   /note="Bifunctional protein CrtB/UppS"
FT                   /id="PRO_0000123687"
FT   ACT_SITE        329
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        377
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         330..333
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         334
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         346
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         374..376
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         378
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         380
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         497
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         502..504
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         515
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   564 AA;  62105 MW;  88B1A330C1CC46C6 CRC64;
     MVRDWSACGS LLLVMTVAKD RGGPAVAGSG GGVESPELRA AYEVCEAEAR QFAVELWAAA
     ETLPVETRPS LYAIASWSAY TDRIIDEGPL EGREERLAQW SADTLADLRA GHSSHPLRRA
     LVDTVRRWGL AEALIEEHLD SARADCAAVP VFETFKDQRR YLRGCSGALA ELWVPLLEPR
     GPEAFRLMSV LGEACQVADL FEDLPDDLAA GRCYLPRQDL RGLGLDVDDL RRGEREEALN
     AFVDAQLAHW RGLLEETVLA PSTVGARYQI FVHTLLLGAQ MHFDEVTLLR SRVLTQGLES
     LVTGDGRMSR RAARPGPGPV PGHIAVIADG NRRWAEARGL LADQGHRAGI RAVLRLVNAA
     QRTGIRHVTV YMFSTENWYR SQGEVAALFG AFADWFARGA QTVHELGVRV RWSGRRDRLE
     ESLASSFELL ESMTANNDKL TLTICLDYGG REELAAAARA LAAEAVAGTI RPEQIGMAEV
     ARHLYVPEMP DVDLLVRTCE QRISNFLPWH LAYAELVFDP APWPDFDLAR LRDAVDSYAG
     RERRFGGDAE LPAQAGNLEP ARNG