ID   CRTY_PARSN              Reviewed;         386 AA.
AC   P54974; Q33DT8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Lycopene beta-cyclase {ECO:0000305};
DE            EC=5.5.1.19 {ECO:0000305|PubMed:7592436};
DE   AltName: Full=Lycopene cyclase {ECO:0000303|PubMed:7592436};
GN   Name=crtY {ECO:0000303|PubMed:7592436};
OS   Paracoccus sp. (strain N81106 / MBIC 01143) (Agrobacterium aurantiacum).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus; unclassified Paracoccus (in: Bacteria).
OX   NCBI_TaxID=81397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RX   PubMed=7592436; DOI=10.1128/jb.177.22.6575-6584.1995;
RA   Misawa N., Satomi Y., Kondo K., Yokoyama A., Kajiwara S., Saito T.,
RA   Ohtani T., Miki W.;
RT   "Structure and functional analysis of a marine bacterial carotenoid
RT   biosynthesis gene cluster and astaxanthin biosynthetic pathway proposed at
RT   the gene level.";
RL   J. Bacteriol. 177:6575-6584(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Maruyama T., Inomata Y., Haga M., Ide T., Misawa N.;
RT   "Structure of the complete carotenoid biosynthesis gene cluster of
RT   Paracoccus sp. strain N81106.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the double cyclization reaction which converts
CC       lycopene to beta-carotene. {ECO:0000305|PubMed:7592436}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a carotenoid psi-end group = a carotenoid beta-end derivative;
CC         Xref=Rhea:RHEA:55620, ChEBI:CHEBI:139114, ChEBI:CHEBI:139120;
CC         EC=5.5.1.19; Evidence={ECO:0000305|PubMed:7592436};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55621;
CC         Evidence={ECO:0000305|PubMed:7592436};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-lycopene = gamma-carotene; Xref=Rhea:RHEA:32219,
CC         ChEBI:CHEBI:15948, ChEBI:CHEBI:27740; EC=5.5.1.19;
CC         Evidence={ECO:0000250|UniProtKB:P21687};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32220;
CC         Evidence={ECO:0000250|UniProtKB:P21687};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=gamma-carotene = all-trans-beta-carotene;
CC         Xref=Rhea:RHEA:32239, ChEBI:CHEBI:17579, ChEBI:CHEBI:27740;
CC         EC=5.5.1.19; Evidence={ECO:0000250|UniProtKB:P21687};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32240;
CC         Evidence={ECO:0000250|UniProtKB:P21687};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P21687};
CC   -!- PATHWAY: Carotenoid biosynthesis; astaxanthin biosynthesis.
CC       {ECO:0000305|PubMed:7592436}.
CC   -!- SIMILARITY: Belongs to the lycopene cyclase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D58420; BAA09593.1; -; Genomic_DNA.
DR   EMBL; AB206672; BAE47467.1; -; Genomic_DNA.
DR   AlphaFoldDB; P54974; -.
DR   UniPathway; UPA00387; -.
DR   GO; GO:0045436; F:lycopene beta cyclase activity; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR008461; CrtY.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR010108; Lycopene_cyclase_b/e.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR01790; carotene-cycl; 1.
DR   TIGRFAMs; TIGR01789; lycopene_cycl; 1.
PE   1: Evidence at protein level;
KW   Carotenoid biosynthesis; FAD; Flavoprotein; Isomerase; NAD; NADP.
FT   CHAIN           1..386
FT                   /note="Lycopene beta-cyclase"
FT                   /id="PRO_0000079373"
FT   BINDING         4..34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   386 AA;  42202 MW;  E14C41E688AF78AC CRC64;
     MTHDVLLAGA GLANGLIALA LRAARPDLRV LLLDHAAGPS DGHTWSCHDP DLSPDWLARL
     KPLRRANWPD QEVRFPRHAR RLATGYGSLD GAALADAVVR SGAEIRWDSD IALLDAQGAT
     LSCGTRIEAG AVLDGRGAQP SRHLTVGFQK FVGVEIETDR PHGVPRPMIM DATVTQQDGY
     RFIYLLPFSP TRILIEDTRY SDGGDLDDDA LAAASHDYAR QQGWTGAEVR RERGILPIAL
     AHDAAGFWAD HAAGPVPVGL RAGFFHPVTG YSLPYAAQVA DVVAGLSGPP GTDALRGAIR
     DYAIDRARRD RFLRLLNRML FRGCAPDRRY TLLQRFYRMP HGLIERFYAG RLSVADQLRI
     VTGKPPIPLG TAIRCLPERP LLKENA