CRTI_STRGR
ID CRTI_STRGR Reviewed; 507 AA.
AC P54981; P54971; P72447;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Phytoene dehydrogenase;
DE EC=1.3.99.-;
DE AltName: Full=Phytoene desaturase;
GN Name=crtI; Synonyms=crtE;
OS Streptomyces griseus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ISP 5395;
RA Hoshi K.;
RT "Molecular cloning and sequence analysis of crtI gene of Streptomyces
RT setonii.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JA 3933;
RX PubMed=8917308; DOI=10.1007/bf02173971;
RA Schumann G., Nurnberger H., Sandmann G., Kruegel H.J.;
RT "Activation and analysis of cryptic crt genes for carotenoid biosynthesis
RT from Streptomyces griseus.";
RL Mol. Gen. Genet. 252:658-666(1996).
CC -!- FUNCTION: This enzyme converts phytoene into zeta-carotene via the
CC intermediary of phytofluene by the symmetrical introduction of two
CC double bonds at the C-11 and C-11' positions of phytoene.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; D55723; BAA09537.1; -; Genomic_DNA.
DR EMBL; L37405; AAA91950.1; -; Genomic_DNA.
DR EMBL; X95596; CAA64850.1; -; Genomic_DNA.
DR AlphaFoldDB; P54981; -.
DR SMR; P54981; -.
DR PRIDE; P54981; -.
DR BioCyc; MetaCyc:MON-20342; -.
DR UniPathway; UPA00803; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR014105; Carotenoid/retinoid_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR008150; Phytoene_DH_bac_CS.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR02734; crtI_fam; 1.
DR PROSITE; PS00982; PHYTOENE_DH; 1.
PE 3: Inferred from homology;
KW Carotenoid biosynthesis; FAD; Flavoprotein; NAD; Oxidoreductase.
FT CHAIN 1..507
FT /note="Phytoene dehydrogenase"
FT /id="PRO_0000067692"
FT BINDING 12..45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT CONFLICT 33
FT /note="R -> S (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 39..41
FT /note="RED -> QEG (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 52..53
FT /note="SG -> TD (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="I -> V (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="D -> E (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="R -> P (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="A -> D (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="E -> Q (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="T -> A (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="L -> F (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="A -> V (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="S -> A (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 246..247
FT /note="VL -> SF (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="R -> S (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 272..274
FT /note="HIP -> RIA (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="T -> S (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="T -> A (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="D -> N (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="N -> S (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="R -> E (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="T -> S (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="G -> S (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="A -> S (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="E -> V (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="R -> G (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="E -> Q (in Ref. 1; BAA09537)"
FT /evidence="ECO:0000305"
FT CONFLICT 493..507
FT /note="RIARAPRSAPGGSSA -> PPFRDPAREVLSHDRP (in Ref. 1;
FT BAA09537)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 54509 MW; FBB97F7FE696B2AC CRC64;
MITVKGPVDH VVVVGAGLAG LAAALHLLGA GRRVTVVERE DVPGGRAGLL ESGGFRIDTG
PTVLTMPDLV EDAFAAVGER MADRLELIRL APAYRARFAD GSQLDVHTDG AAMEAAVEEF
AGARQAVGYR RLRIWLERLY RVQMRRFIDT NFDSPLQLAH PDLARLAALG GFGRLDARIG
HFVSDERLRR VFSFQALYAG VPPARALAAY AVIAYMDTVA GVYFPRGGMH ALPRAMADAA
SDAGAVLRYG QRVTRLERSG DRVTAVVTDQ EHIPCDAVVL TPDLPVSYRL LGRTPHRPLP
LRHSPSAVIL HTGTDRTWPD LAHHTISFGA AWKNTFHELT RTGRLMSDPS LLITRPTATD
PSLAPPGKHL HYVLAPCPNT EVGPGVREWR ELGPRYRDEL LAELERREMP GLGAAIEEEG
LVTPVDWTAQ GHAAGTPFSV AHTFPQTGPF RPRNLVRGTV NAVLAGCGTT PGVGVPTVLI
SGKLAAERIT GPRIARAPRS APGGSSA
