CRTY_HALS3
ID CRTY_HALS3 Reviewed; 237 AA.
AC B0R753;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Lycopene beta-cyclase {ECO:0000303|PubMed:12003928};
DE EC=5.5.1.19 {ECO:0000269|PubMed:12003928};
GN Name=crtY {ECO:0000303|PubMed:12003928}; OrderedLocusNames=OE_3983R;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ROLE IN BACTERIORHODOPSIN BIOGENESIS,
RP PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=12003928; DOI=10.1128/jb.184.11.2889-2897.2002;
RA Peck R.F., Johnson E.A., Krebs M.P.;
RT "Identification of a lycopene beta-cyclase required for bacteriorhodopsin
RT biogenesis in the archaeon Halobacterium salinarum.";
RL J. Bacteriol. 184:2889-2897(2002).
CC -!- FUNCTION: Catalyzes the cyclization of both ends of lycopene to form
CC beta-carotene, a retinal precursor. Is required for bacteriorhodopsin
CC biogenesis, a light-driven proton pump with a covalently bound retinal
CC cofactor. {ECO:0000269|PubMed:12003928}.
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:12003928};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55621;
CC Evidence={ECO:0000269|PubMed:12003928};
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:0000269|PubMed:12003928};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32220;
CC Evidence={ECO:0000269|PubMed:12003928};
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:12003928};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32240;
CC Evidence={ECO:0000269|PubMed:12003928};
CC -!- PATHWAY: Carotenoid biosynthesis; beta-carotene biosynthesis.
CC {ECO:0000269|PubMed:12003928}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Strains lacking this gene show undetectable
CC levels of bacteriorhodopsin, retinal, and beta-carotene and
CC accumulation of lycopene to high levels. {ECO:0000269|PubMed:12003928}.
CC -!- SIMILARITY: Belongs to the lycopene beta-cyclase family. {ECO:0000305}.
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DR EMBL; AM774415; CAP14572.1; -; Genomic_DNA.
DR RefSeq; WP_012289440.1; NC_010364.1.
DR AlphaFoldDB; B0R753; -.
DR PRIDE; B0R753; -.
DR EnsemblBacteria; CAP14572; CAP14572; OE_3983R.
DR GeneID; 5953587; -.
DR KEGG; hsl:OE_3983R; -.
DR HOGENOM; CLU_076391_0_0_2; -.
DR OMA; WYGDGAV; -.
DR UniPathway; UPA00802; -.
DR Proteomes; UP000001321; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016872; F:intramolecular lyase activity; IEA:InterPro.
DR GO; GO:0045436; F:lycopene beta cyclase activity; IDA:UniProtKB.
DR GO; GO:0016120; P:carotene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0042574; P:retinal metabolic process; IMP:UniProtKB.
DR InterPro; IPR017825; Lycopene_cyclase_dom.
DR Pfam; PF18916; Lycopene_cyc; 2.
DR TIGRFAMs; TIGR03462; CarR_dom_SF; 2.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; Cell membrane; Isomerase; Membrane; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..237
FT /note="Lycopene beta-cyclase"
FT /id="PRO_0000408500"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 237 AA; 25822 MW; 66A9A770C9BEF601 CRC64;
MTTSYLTFLA VAVGPPLVAL GVVRAARWDG DRARAAGVGI LLALALSYTT PWDNYLIATG
VWWYGEGTVV GRLWQMPIEE YLFVITQTLL TGLWVQALPL RPTAGFSPTR RDAVLGALAG
VLVGCGGAVL LTVDATFYIG AIIAWAAPVL ALQWAVGWRY LWRRRRVFAA AVLVPTLFLS
AADRYAIADG IWILAGQYTT GITVLGLPIE EGAFFFVTNV FVSQGLILYA WVLARWR
