LYEL_HALSA
ID LYEL_HALSA Reviewed; 275 AA.
AC Q9HPD9;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Lycopene elongase/hydratase {ECO:0000305};
DE EC=2.5.1.150 {ECO:0000250|UniProtKB:M0L7V9};
GN Name=lye {ECO:0000303|PubMed:21840984}; OrderedLocusNames=VNG_1682C;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=21840984; DOI=10.1128/jb.05376-11;
RA Dummer A.M., Bonsall J.C., Cihla J.B., Lawry S.M., Johnson G.C., Peck R.F.;
RT "Bacterioopsin-mediated regulation of bacterioruberin biosynthesis in
RT Halobacterium salinarum.";
RL J. Bacteriol. 193:5658-5667(2011).
CC -!- FUNCTION: Involved in the biosynthesis of the acyclic C50 carotenoid
CC bacterioruberin (BR) (PubMed:21840984). 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:21840984). 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) (By similarity).
CC Can also catalyze the conversion of lycopene to
CC tetrahydrobisanhydrobacterioruberin (TH-BABR) (PubMed:21840984).
CC {ECO:0000250|UniProtKB:M0L7V9, ECO:0000269|PubMed:21840984}.
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:21840984};
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:0000250|UniProtKB:M0L7V9};
CC -!- ACTIVITY REGULATION: Inhibited by bacterioopsin.
CC {ECO:0000269|PubMed:21840984}.
CC -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000269|PubMed:21840984}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Loss of bacterioruberins production.
CC {ECO:0000269|PubMed:21840984}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AE004437; AAG19931.1; -; Genomic_DNA.
DR PIR; G84320; G84320.
DR RefSeq; WP_010903229.1; NC_002607.1.
DR AlphaFoldDB; Q9HPD9; -.
DR SMR; Q9HPD9; -.
DR STRING; 64091.VNG_1682C; -.
DR PaxDb; Q9HPD9; -.
DR EnsemblBacteria; AAG19931; AAG19931; VNG_1682C.
DR GeneID; 5953078; -.
DR GeneID; 62884940; -.
DR KEGG; hal:VNG_1682C; -.
DR PATRIC; fig|64091.14.peg.1283; -.
DR HOGENOM; CLU_058976_0_0_2; -.
DR InParanoid; Q9HPD9; -.
DR OMA; PANVFLY; -.
DR OrthoDB; 71004at2157; -.
DR PhylomeDB; Q9HPD9; -.
DR Proteomes; UP000000554; 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: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; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..275
FT /note="Lycopene elongase/hydratase"
FT /id="PRO_0000428794"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 275 AA; 29589 MW; 50F53001C0D7B7D3 CRC64;
MFRYLFVLSR PRFWLYLAGP VLVGVSYGAT TVGELFSAPA VVLFSYFLLP ANIYLYGIND
VFDRDVDETN PKKDGRESRY RGGAAVAVIV AVCGVFLGFV AAPLPAEAWP YLAAWFVLAT
EYSAPPLRFK TTPVLDSLSN GLYVLPAAAA YAGVSGTHPP LLAVAGGWLW AMGMHTFSAI
PDIEPDRAAG IQTTATALGA DRALAYCAGI WLLSAAVFAL VDVRFGLLLL AYPVLVFGIR
RLQVAVGRAY WWYPAVNTLV GMVFTLGGLW GVVHG
