ID   CRTY_PSEVU              Reviewed;         386 AA.
AC   Q01331;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Lycopene beta-cyclase {ECO:0000303|PubMed:8422926};
DE            EC=5.5.1.19 {ECO:0000269|PubMed:8422926, ECO:0000305|PubMed:7808389};
DE   AltName: Full=Lycopene cyclase {ECO:0000303|PubMed:8422926};
GN   Name=crtY {ECO:0000303|PubMed:8422926};
OS   Pseudescherichia vulneris (Escherichia vulneris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Pseudescherichia.
OX   NCBI_TaxID=566;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=ATCC 39368 / Eho10;
RX   PubMed=7808389; DOI=10.1007/bf00302252;
RA   Hundle B., Alberti M., Nievelstein V., Beyer P., Kleinig H.,
RA   Armstrong G.A., Burke D.H., Hearst J.E.;
RT   "Functional assignment of Erwinia herbicola Eho10 carotenoid genes
RT   expressed in Escherichia coli.";
RL   Mol. Gen. Genet. 245:406-416(1994).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=ATCC 39368 / Eho10;
RX   PubMed=8422926; DOI=10.1016/0014-5793(93)81188-6;
RA   Hundle B.S., O'Brien D.A., Beyer P., Kleinig H., Hearst J.E.;
RT   "In vitro expression and activity of lycopene cyclase and beta-carotene
RT   hydroxylase from Erwinia herbicola.";
RL   FEBS Lett. 315:329-334(1993).
CC   -!- FUNCTION: Catalyzes the double cyclization reaction which converts
CC       lycopene to beta-carotene. {ECO:0000269|PubMed:8422926,
CC       ECO:0000305|PubMed:7808389}.
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:0000269|PubMed:8422926,
CC         ECO:0000305|PubMed:7808389};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55621;
CC         Evidence={ECO:0000269|PubMed:8422926, ECO:0000305|PubMed:7808389};
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; beta-carotene biosynthesis.
CC       {ECO:0000305|PubMed:7808389, ECO:0000305|PubMed:8422926}.
CC   -!- SIMILARITY: Belongs to the lycopene cyclase family. {ECO:0000305}.
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DR   EMBL; M87280; AAA64980.1; -; Genomic_DNA.
DR   PIR; S52981; S52981.
DR   AlphaFoldDB; Q01331; -.
DR   UniPathway; UPA00802; -.
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_0000079374"
FT   BINDING         3..33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   386 AA;  43341 MW;  F4A40563BFCFA980 CRC64;
     MRDLILVGGG LANGLIAWRL RQRYPQLNLL LIEAGEQPGG NHTWSFHEDD LTPGQHAWLA
     PLVAHAWPGY EVQFPDLRRR LARGYYSITS ERFAEALHQA LGENIWLNCS VSEVLPNSVR
     LANGEALLAG AVIDGRGVTA SSAMQTGYQL FLGQQWRLTQ PHGLTVPILM DATVAQQQGY
     RFVYTLPLSA DTLLIEDTRY ANVPQRDDNA LRQTVTDYAH SKGWQLAQLE REETGCLPIT
     LAGDIQALWA DAPGVPRSGM RAGLFHPTTG YSLPLAVALA DAIADSPRLG SVPLYQLTRQ
     FAERHWRRQG FFRLLNRMLF LAGREENRWR VMQRFYGLPE PTVERFYAGR LSLFDKARIL
     TGKPPVPLGE AWRAALNHFP DRRDKG