ID   CRTS2_ONCHC             Reviewed;         587 AA.
AC   Q52QW2;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Prolycopene isomerase 2, chloroplastic;
DE            Short=CrtISO2;
DE            EC=5.2.1.13;
DE   AltName: Full=Carotenoid isomerase 2;
DE   AltName: Full=OcrtISO24;
DE   Flags: Precursor;
GN   Name=CRTISO2;
OS   Oncidium hybrid cultivar (Orchid).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Epidendroideae; Cymbidieae; Oncidiinae; Oncidium.
OX   NCBI_TaxID=141207;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Gower Ramsey;
RX   PubMed=16151849; DOI=10.1007/s00425-005-0113-z;
RA   Hieber A.D., Mudalige-Jayawickrama R.G., Kuehnle A.R.;
RT   "Color genes in the orchid Oncidium Gower Ramsey: identification,
RT   expression, and potential genetic instability in an interspecific cross.";
RL   Planta 223:521-531(2006).
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   -!- TISSUE SPECIFICITY: Up-regulated in the flower buds and flower lip
CC       tissue, while it is weakly expressed in leaves.
CC       {ECO:0000269|PubMed:16151849}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       CrtISO subfamily. {ECO:0000305}.
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DR   EMBL; AY973634; AAX84689.1; -; mRNA.
DR   AlphaFoldDB; Q52QW2; -.
DR   SMR; Q52QW2; -.
DR   UniPathway; UPA00803; -.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046608; F:carotenoid isomerase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
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..50
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           51..587
FT                   /note="Prolycopene isomerase 2, chloroplastic"
FT                   /id="PRO_0000225674"
SQ   SEQUENCE   587 AA;  64873 MW;  2ED798DA110FEAFC CRC64;
     MLCLSLNSSS TSPPKLPLHH SFSRRGIRSW VRSPCVQRKK LGFWSSPKAV LSAVSGAGSE
     AGKVEEAEEY DAIVIGSGIG GLVAATQLAV KGARVLVLEK YVIPGGSSGF FQRDGFTFDV
     GSSVMFGFSD KGNLNLITQA LEAVDCKLRT IPDPTTVHFH LPDNLSIRVH REYDMFISEL
     VNYFPHEKEG IRRFYNECWK IFNSLNSLEL KSLEEPMYLF GQFFRKPVEC LTLAFYLPQN
     AGDIARKFIK DPQLLSFIDA ECFIVSTVKA LHTPMINASM VLCDRHFGGI NYPVGGVGGI
     AKALANGLVN KGSKLLYKAN VTKILLKDGK AVGVKLSNGR EFFAKTVISN ATRWDTFGKL
     LKVEDIPQEE KNFKKIYLKA PSFLSIHMGV KAFVLPPDTD CHHFILEDNW GRLELPYGSI
     FLSIPTVLDP SLAPEGHHIF HIFTTSSIEN WEGLSHKEYE EKKELVADEI ITRLEKKLFP
     GLKDSVVLKE VGTPKTHRRF LARDSGTYGP MPRKVPKGLL GMPFNTTAIN GLYCVGDSCF
     PGQGVIAVAF SGVMCAHRVA ADLGFEKKAP VLDAALLRLL GWLRTVA