LYEL_HALVD
ID LYEL_HALVD Reviewed; 301 AA.
AC D4GTV9;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 47.
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=HVO_2527;
GN ORFNames=C498_07923;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
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).
RN [3]
RP FUNCTION, AND PATHWAY.
RC STRAIN=DS2 / DS70;
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 (By similarity). 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) (By similarity).
CC {ECO:0000250|UniProtKB:M0L7V9, ECO:0000250|UniProtKB:Q9HPD9,
CC 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:0000250|UniProtKB:Q9HPD9};
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 -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000269|PubMed:21840984}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- MISCELLANEOUS: H.volcanii does not produce any known rhodopsins and
CC unlike in H.salinarum, Lye is not regulated by bacterioopsin.
CC {ECO:0000305|PubMed:21840984}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CP001956; ADE02704.1; -; Genomic_DNA.
DR EMBL; AOHU01000045; ELY32674.1; -; Genomic_DNA.
DR RefSeq; WP_004042521.1; NZ_AOHU01000045.1.
DR AlphaFoldDB; D4GTV9; -.
DR SMR; D4GTV9; -.
DR STRING; 309800.C498_07923; -.
DR EnsemblBacteria; ADE02704; ADE02704; HVO_2527.
DR EnsemblBacteria; ELY32674; ELY32674; C498_07923.
DR GeneID; 8926613; -.
DR KEGG; hvo:HVO_2527; -.
DR PATRIC; fig|309800.29.peg.1542; -.
DR eggNOG; arCOG00478; Archaea.
DR HOGENOM; CLU_058976_0_0_2; -.
DR OMA; PANVFLY; -.
DR OrthoDB; 71004at2157; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; 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 3: Inferred from homology;
KW Carotenoid biosynthesis; Cell membrane; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..301
FT /note="Lycopene elongase/hydratase"
FT /id="PRO_0000428795"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 301 AA; 31969 MW; 79EBCFF8F467F6C4 CRC64;
MSADMAAQSE SGEGGDDGRA DGGLGDRLVY LAVLSRPRFW LYLAGPVVVG VAAAASALAD
LFGLEPVALF AYFLVPANVF LYGVNDVFDA DVDEANPKKD DREARWRGDP VNTVVVAASG
LLGVGLFAVA PRVAWPWLAA HFFLAVEYSA PPFRFKTTPL LDSVSNGLYV LPGVAAYAAV
SGSNPPMLAV AGAWLWTMGM HTFSAIPDIE PDREAGIRTT ATALGERRTY WYCAATWVLA
AVAFAAVDLR LGALLAAYPV VVLGIVAAGV DVDRAYWWYP VINTVVGMLI TLGALWRLVN
G
