ID CRTY_PANAN Reviewed; 382 AA.
AC P21687;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 13-SEP-2023, entry version 78.
DE RecName: Full=Lycopene beta-cyclase {ECO:0000303|PubMed:2254247};
DE EC=5.5.1.19 {ECO:0000269|PubMed:11943208, ECO:0000269|PubMed:20178989, ECO:0000269|PubMed:8898919, ECO:0000305|PubMed:2254247};
DE AltName: Full=Lycopene cyclase {ECO:0000303|PubMed:2254247};
GN Name=crtY {ECO:0000303|PubMed:2254247};
OS Pantoea ananas (Erwinia uredovora).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=553;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=ATCC 19321 / DSM 30080 / NCPPB 800 / NRRL B-14773 / 20D3;
RX PubMed=2254247; DOI=10.1128/jb.172.12.6704-6712.1990;
RA Misawa N., Nakagawa M., Kobayashi K., Yamano S., Izawa Y., Nakamura K.,
RA Harashima K.;
RT "Elucidation of the Erwinia uredovora carotenoid biosynthetic pathway by
RT functional analysis of gene products expressed in Escherichia coli.";
RL J. Bacteriol. 172:6704-6712(1990).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8898919; DOI=10.1111/j.1432-1033.1996.0291t.x;
RA Takaichi S., Sandmann G., Schnurr G., Satomi Y., Suzuki A., Misawa N.;
RT "The carotenoid 7,8-dihydro-psi end group can be cyclized by the lycopene
RT cyclases from the bacterium Erwinia uredovora and the higher plant Capsicum
RT annuum.";
RL Eur. J. Biochem. 241:291-296(1996).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=11943208; DOI=10.1016/s0014-5793(02)02453-5;
RA Hornero-Mendez D., Britton G.;
RT "Involvement of NADPH in the cyclization reaction of carotenoid
RT biosynthesis.";
RL FEBS Lett. 515:133-136(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF GLU-199.
RX PubMed=20178989; DOI=10.1074/jbc.m109.091843;
RA Yu Q., Schaub P., Ghisla S., Al-Babili S., Krieger-Liszkay A., Beyer P.;
RT "The lycopene cyclase CrtY from Pantoea ananatis (formerly Erwinia
RT uredovora) catalyzes an FADred-dependent non-redox reaction.";
RL J. Biol. Chem. 285:12109-12120(2010).
CC -!- FUNCTION: Catalyzes the double cyclization reaction which converts
CC lycopene to beta-carotene (PubMed:2254247, PubMed:11943208,
CC PubMed:20178989). Also catalyzes the double cyclization reaction which
CC converts neurosporene to 7,8-dihydro-beta-carotene via monocyclic beta-
CC zeacarotene (PubMed:8898919). May also convert zeta-carotene to
CC bicyclic 7,8,7',8'-tetrahydro-beta-carotene (PubMed:8898919).
CC {ECO:0000269|PubMed:11943208, ECO:0000269|PubMed:20178989,
CC ECO:0000269|PubMed:2254247, ECO:0000269|PubMed:8898919}.
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:11943208,
CC ECO:0000269|PubMed:20178989, ECO:0000269|PubMed:8898919,
CC ECO:0000305|PubMed:2254247};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55621;
CC Evidence={ECO:0000269|PubMed:11943208, ECO:0000269|PubMed:20178989,
CC ECO:0000269|PubMed:8898919, ECO:0000305|PubMed:2254247};
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:0000305|PubMed:20178989};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32220;
CC Evidence={ECO:0000305|PubMed:20178989};
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:0000269|PubMed:20178989};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32240;
CC Evidence={ECO:0000269|PubMed:20178989};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-neurosporene = beta-zeacarotene;
CC Xref=Rhea:RHEA:67976, ChEBI:CHEBI:16833, ChEBI:CHEBI:27533;
CC EC=5.5.1.19; Evidence={ECO:0000269|PubMed:8898919};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67977;
CC Evidence={ECO:0000269|PubMed:8898919};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-zeacarotene = 7,8-dihydro-beta-carotene;
CC Xref=Rhea:RHEA:67980, ChEBI:CHEBI:27533, ChEBI:CHEBI:80427;
CC Evidence={ECO:0000269|PubMed:8898919};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67981;
CC Evidence={ECO:0000269|PubMed:8898919};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:20178989};
CC -!- ACTIVITY REGULATION: Activity is increased in the presence of NAD(P)H
CC (PubMed:11943208, PubMed:20178989). NADPH is not involved directly in
CC the cyclization reaction, but must play an indirect role, e.g. as an
CC allosteric activator (PubMed:11943208). {ECO:0000269|PubMed:11943208,
CC ECO:0000269|PubMed:20178989}.
CC -!- PATHWAY: Carotenoid biosynthesis; beta-carotene biosynthesis.
CC {ECO:0000305|PubMed:2254247}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:20178989}. Note=Membrane-bound.
CC {ECO:0000269|PubMed:20178989}.
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; D90087; BAA14126.1; -; Genomic_DNA.
DR PIR; C37802; C37802.
DR AlphaFoldDB; P21687; -.
DR ChEMBL; CHEMBL2285356; -.
DR DrugCentral; P21687; -.
DR BioCyc; MetaCyc:MONOMER-14938; -.
DR UniPathway; UPA00802; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR008461; CrtY.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR010108; Lycopene_cyclase_b/e.
DR NCBIfam; TIGR01790; carotene-cycl; 1.
DR NCBIfam; TIGR01789; lycopene_cycl; 1.
DR Pfam; PF05834; Lycopene_cycl; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; Cell inner membrane; Cell membrane; FAD;
KW Flavoprotein; Isomerase; Membrane; NAD; NADP.
FT CHAIN 1..382
FT /note="Lycopene beta-cyclase"
FT /id="PRO_0000079375"
FT BINDING 6..36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305"
FT MUTAGEN 199
FT /note="E->A: Loss of activity. Still binds FAD."
FT /evidence="ECO:0000269|PubMed:20178989"
SQ SEQUENCE 382 AA; 43047 MW; 62A94222A9EB6D45 CRC64;
MQPHYDLILV GAGLANGLIA LRLQQQQPDM RILLIDAAPQ AGGNHTWSFH HDDLTESQHR
WIAPLVVHHW PDYQVRFPTR RRKLNSGYFC ITSQRFAEVL QRQFGPHLWM DTAVAEVNAE
SVRLKKGQVI GARAVIDGRG YAANSALSVG FQAFIGQEWR LSHPHGLSSP IIMDATVDQQ
NGYRFVYSLP LSPTRLLIED THYIDNATLD PECARQNICD YAAQQGWQLQ TLLREEQGAL
PITLSGNADA FWQQRPLACS GLRAGLFHPT TGYSLPLAVA VADRLSALDV FTSASIHHAI
THFARERWQQ QGFFRMLNRM LFLAGPADSR WRVMQRFYGL PEDLIARFYA GKLTLTDRLR
ILSGKPPVPV LAALQAIMTT HR
//
