ID   CRTEB_CORGT             Reviewed;         287 AA.
AC   Q93QX2;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Lycopene elongase/hydratase {ECO:0000305};
DE            EC=2.5.1.149 {ECO:0000269|PubMed:11432736};
GN   Name=crtEb {ECO:0000303|PubMed:11432736};
OS   Corynebacterium glutamicum (Brevibacterium saccharolyticum).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1718;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP   AND DISRUPTION PHENOTYPE.
RC   STRAIN=MJ233;
RX   PubMed=11432736; DOI=10.1046/j.1432-1327.2001.02275.x;
RA   Krubasik P., Kobayashi M., Sandmann G.;
RT   "Expression and functional analysis of a gene cluster involved in the
RT   synthesis of decaprenoxanthin reveals the mechanisms for C50 carotenoid
RT   formation.";
RL   Eur. J. Biochem. 268:3702-3708(2001).
CC   -!- FUNCTION: Catalyzes the elongation of the C(40) carotenoid all-trans-
CC       lycopene to the acyclic C(50) carotenoid flavuxanthin during
CC       decaprenoxanthin biosynthesis (PubMed:11432736). Acts as a bifunctional
CC       enzyme that catalyzes the elongation of lycopene by attaching a C(5)
CC       isoprene unit at C-2, as well as the hydroxylation of the new isoprene
CC       unit (Probable). The enzyme acts at both ends of the substrate, forming
CC       the C(50) carotenoid flavuxanthin via the C(45) intermediate
CC       nonaflavuxanthin (PubMed:11432736). {ECO:0000269|PubMed:11432736,
CC       ECO:0000305|PubMed:11432736}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + all-trans-lycopene + dimethylallyl diphosphate + H2O = AH2
CC         + diphosphate + nonaflavuxanthin; Xref=Rhea:RHEA:56124,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15948,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623,
CC         ChEBI:CHEBI:139514; EC=2.5.1.149;
CC         Evidence={ECO:0000269|PubMed:11432736};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + dimethylallyl diphosphate + H2O + nonaflavuxanthin = AH2 +
CC         diphosphate + flavuxanthin; Xref=Rhea:RHEA:56128, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57623, ChEBI:CHEBI:139514, ChEBI:CHEBI:139515;
CC         EC=2.5.1.149; Evidence={ECO:0000269|PubMed:11432736};
CC   -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000269|PubMed:11432736}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Disruption mutant accumulates lycopene and shows
CC       altered carotenoid biosynthesis. {ECO:0000269|PubMed:11432736}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AF159510; AAK64302.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q93QX2; -.
DR   BioCyc; MetaCyc:MON-20367; -.
DR   BRENDA; 2.5.1.149; 960.
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   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   Cell membrane; Membrane; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..287
FT                   /note="Lycopene elongase/hydratase"
FT                   /id="PRO_0000450583"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   287 AA;  31674 MW;  3FD29E1C6DDA5F0A CRC64;
     MMEKIRLILL SSRPISWVNT AYPFGLAYLL NAGEIDWLFW LGIVFFLIPY NIAMYGINDV
     FDYESDIRNP RKGGVEGAVL PKSSHSTLLW ASAISTIPFL VILFIFGTWM SSLWLTISVL
     AVIAYSAPKL RFKERPFIDA LTSSTHFTSP ALIGATITGT SPSAAMWIAL GSFFLWGMAS
     QILGAVQDVN ADREANLSSI ATVIGARGAI RLSVVLYLLA AVLVTTLPNP AWIIGIAILT
     YVFDAARFWN ITDASCEQAN RSWKVFLWLN YFVGAVITIL LIAIHQI