ID   CRTSO_DAUCA             Reviewed;         615 AA.
AC   Q2VEX9;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Prolycopene isomerase, chloroplastic;
DE            Short=CrtISO;
DE            EC=5.2.1.13;
DE   AltName: Full=Carotenoid isomerase;
DE   Flags: Precursor;
GN   Name=CRTISO;
OS   Daucus carota (Wild carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Sativum;
RA   Just B.J., Santos C.A.F., Fonseca M.E.N., Oloizia B.B., Simon P.W.;
RT   "Carotenoid biosynthesis structural genes in carrot (Daucus carota L.): STS
RT   markers, molecular mapping, and sequencing.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Carotene cis-trans-isomerase that converts 7,9,9'-tri-cis-
CC       neurosporene to 9'-cis-neurosporene and 7,9,9',7'-tetra-cis-lycopene
CC       (also known as prolycopene) into all-trans-lycopene. Isomerization
CC       requires redox-active components, suggesting that isomerization is
CC       achieved by a reversible redox reaction acting at specific double
CC       bonds. Isomerizes adjacent cis-double bonds at C7 and C9 pairwise into
CC       the trans-configuration, but is incapable of isomerizing single cis-
CC       double bonds at C9 and C9' (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7,7',9,9'-tetra-cis-lycopene = all-trans-lycopene;
CC         Xref=Rhea:RHEA:30971, ChEBI:CHEBI:15948, ChEBI:CHEBI:62466;
CC         EC=5.2.1.13;
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000250};
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       CrtISO subfamily. {ECO:0000305}.
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DR   EMBL; DQ192188; ABB52069.1; -; mRNA.
DR   RefSeq; NP_001316099.1; NM_001329170.1.
DR   AlphaFoldDB; Q2VEX9; -.
DR   SMR; Q2VEX9; -.
DR   PRIDE; Q2VEX9; -.
DR   GeneID; 108219304; -.
DR   OrthoDB; 873686at2759; -.
DR   UniPathway; UPA00803; -.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046608; F:carotenoid isomerase activity; IEA:EnsemblPlants.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009662; P:etioplast organization; IEA:EnsemblPlants.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR014101; CrtISO.
DR   InterPro; IPR045892; CrtISO-like.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR46313; PTHR46313; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR02730; carot_isom; 1.
PE   2: Evidence at transcript level;
KW   Carotenoid biosynthesis; Chloroplast; FAD; Flavoprotein; Isomerase;
KW   Membrane; NAD; NADP; Plastid; Transit peptide.
FT   TRANSIT         1..62
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           63..615
FT                   /note="Prolycopene isomerase, chloroplastic"
FT                   /id="PRO_0000225671"
SQ   SEQUENCE   615 AA;  67989 MW;  DB59C845ADC431E3 CRC64;
     MSTSIFETPL PRSDLFLCSN SLLSQNYKLF DNSRSFGLKS LRPRCQKDGL LYPKPLNFGF
     CRVSRRKRKP NFVLNSVLSV DKELESDETV GLGRSREYDA IVIGSGIGGL VAATQLAVKG
     AKVLVLEKYL IPGGSSGYYE RDGFTFDVGS SVMFGFSDKG NLNLITQALA AVGCKMEVIP
     DPSTVHFHLP SNLSVLVHRE YNEFFSELTS KFPHEKEGIF KFYGECWKIF NALNSLELKS
     LEEPIYLFGQ FFKKPMECLT LAYYLPQNAG DIARKFIKDP EVLSFIDAEC FIVSTVNALK
     TPMINASMVL CDRHYGGINY PVGGVGGIAK SLAKGLVDQG SEIQYKANVK SIIVENGKAV
     GVRLANGNEI FAKNIISNAT RWDTFGKLLK QDELPKEEEN FQKLYIKAPS FLSIHLGVKS
     DVLPPDTDCH HFVLEDDWSN LEVPYGSIFL SIPTVLDSSL APEGNHILHI FTTSSIEDWQ
     GMSQKDYEKK KELVADEIIS RLEKKLFPGL QSSIVLKEVG TPKTHRRYLA RDSGTYGPMP
     QGTPKGLLGM PFNTTAIDGL YCVGDSCFPG QGVIAVAFSG VMCAHRVAAD LGLEQKSPIL
     DAALLRLLGW FRTLA