LYEL_HALJT
ID LYEL_HALJT Reviewed; 294 AA.
AC M0L7V9; A0A0A1GNW8;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Lycopene elongase/hydratase {ECO:0000305};
DE EC=2.5.1.150 {ECO:0000269|PubMed:25712483};
GN Name=lyeJ {ECO:0000303|PubMed:25712483};
GN Synonyms=c0506 {ECO:0000303|PubMed:25712483};
GN ORFNames=C444_12922 {ECO:0000312|EMBL:EMA29702.1};
OS Haloarcula japonica (strain ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032
OS / NCIMB 13157 / TR-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=1227453;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1;
RX PubMed=25712483; DOI=10.1128/jb.02523-14;
RA Yang Y., Yatsunami R., Ando A., Miyoko N., Fukui T., Takaichi S.,
RA Nakamura S.;
RT "Complete biosynthetic pathway of the C50 carotenoid bacterioruberin from
RT lycopene in the extremely halophilic archaeon Haloarcula japonica.";
RL J. Bacteriol. 197:1614-1623(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- FUNCTION: Involved in the biosynthesis of the acyclic C50 carotenoid
CC bacterioruberin (BR) (PubMed:25712483). Acts as a bifunctional
CC elongase/hydratase that catalyzes the elongation of lycopene by
CC attaching a C(5) isoprene unit at C-2, as well as the hydroxylation of
CC the previous end of the molecule (PubMed:25712483). The enzyme acts at
CC both ends of the substrate, and catalyzes the conversion of lycopene to
CC the C(45) intermediate dihydroisopentenyldehydrorhodopin (DH-IDR) and
CC the conversion of isopentenyldehydrorhodopin (IDR) to the C(50)
CC carotenoid dihydrobisanhydrobacterioruberin (DH-BABR)
CC (PubMed:25712483). Can also catalyze the conversion of lycopene to
CC tetrahydrobisanhydrobacterioruberin (TH-BABR) (Probable).
CC {ECO:0000269|PubMed:25712483, ECO:0000305|PubMed:25712483}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-lycopene + dimethylallyl diphosphate + H2O =
CC dihydroisopentenyldehydrorhodopin + diphosphate;
CC Xref=Rhea:RHEA:58188, ChEBI:CHEBI:15377, ChEBI:CHEBI:15948,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:87163;
CC EC=2.5.1.150; Evidence={ECO:0000269|PubMed:25712483};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + H2O + isopentenyldehydrorhodopin =
CC dihydrobisanhydrobacterioruberin + diphosphate; Xref=Rhea:RHEA:58192,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623,
CC ChEBI:CHEBI:87161, ChEBI:CHEBI:87162; EC=2.5.1.150;
CC Evidence={ECO:0000269|PubMed:25712483};
CC -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000269|PubMed:25712483}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Mutant produces lycopene, but not C(45) and C(50)
CC carotenoids. {ECO:0000269|PubMed:25712483}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; LC008543; BAP82510.1; -; Genomic_DNA.
DR EMBL; AOLY01000037; EMA29702.1; -; Genomic_DNA.
DR RefSeq; WP_004593285.1; NZ_AOLY01000037.1.
DR AlphaFoldDB; M0L7V9; -.
DR SMR; M0L7V9; -.
DR STRING; 1227453.C444_12922; -.
DR EnsemblBacteria; EMA29702; EMA29702; C444_12922.
DR KEGG; ag:BAP82510; -.
DR PATRIC; fig|1227453.3.peg.2544; -.
DR eggNOG; arCOG00478; Archaea.
DR OrthoDB; 71004at2157; -.
DR BRENDA; 2.5.1.150; 13658.
DR Proteomes; UP000011524; Unassembled WGS sequence.
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:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.357.140; -; 1.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR044878; UbiA_sf.
DR Pfam; PF01040; UbiA; 1.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; Cell membrane; Membrane; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..294
FT /note="Lycopene elongase/hydratase"
FT /id="PRO_0000450594"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 294 AA; 32067 MW; 523A0CC4BFF7AD88 CRC64;
MPELPTDRLT AVIPPEETLL GYLLRLSRPR FWLYLGGPVI VGVSYAADGP GELFSPLAIA
LFLYFTIPGN VFLYGVNDIF DADIDEHNPK KDDGREVSYR GDSAVTAIVV ASGALALLFA
LVLPTLGIVA LLAWMALSVE YSAPPLRFKT TPFLDSISNG LYILPGVIGY AAIEGVAPPA
TAVVGAWLWA MGMHTFSAIP DIEPDREAGI QTTATFLGES NTYYYCVMCW LMAAFVFNFT
HWVFGVLLLV YPGLVFGILG VGVDIDEAYW WYPAINTVVG MVFTLIALWV MLYG
