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CRTEB_CORGL
ID   CRTEB_CORGL             Reviewed;         287 AA.
AC   Q8NSP8; Q6M7E4;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Lycopene elongase/hydratase {ECO:0000305};
DE            EC=2.5.1.149 {ECO:0000250|UniProtKB:Q93QX2};
GN   Name=crtEb {ECO:0000303|PubMed:22963379};
GN   OrderedLocusNames=Cgl0620 {ECO:0000312|EMBL:BAB98013.1};
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=22963379; DOI=10.1186/1471-2180-12-198;
RA   Heider S.A., Peters-Wendisch P., Wendisch V.F.;
RT   "Carotenoid biosynthesis and overproduction in Corynebacterium
RT   glutamicum.";
RL   BMC Microbiol. 12:198-198(2012).
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:22963379). 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. The enzyme acts at both ends of the substrate, forming the C(50)
CC       carotenoid flavuxanthin via the C(45) intermediate nonaflavuxanthin (By
CC       similarity). {ECO:0000250|UniProtKB:Q93QX2,
CC       ECO:0000269|PubMed:22963379}.
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:0000250|UniProtKB:Q93QX2};
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:0000250|UniProtKB:Q93QX2};
CC   -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000269|PubMed:22963379}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Mutant accumulates lycopene and cannot produce
CC       neither flavuxanthin nor decaprenoxanthin.
CC       {ECO:0000269|PubMed:22963379}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; BA000036; BAB98013.1; -; Genomic_DNA.
DR   RefSeq; NP_599855.1; NC_003450.3.
DR   RefSeq; WP_011013770.1; NC_006958.1.
DR   AlphaFoldDB; Q8NSP8; -.
DR   STRING; 196627.cg0717; -.
DR   KEGG; cgl:Cgl0620; -.
DR   PATRIC; fig|196627.13.peg.610; -.
DR   eggNOG; COG0382; Bacteria.
DR   HOGENOM; CLU_058976_1_0_11; -.
DR   OMA; PANVFLY; -.
DR   Proteomes; UP000000582; 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   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   Cell membrane; Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..287
FT                   /note="Lycopene elongase/hydratase"
FT                   /id="PRO_0000450584"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
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;  31705 MW;  E16831C77874C2CA CRC64;
     MMEKIRLILL SSRPISWINT AYPFGLAYLL NAGEIDWLFW LGIVFFLIPY NIAMYGINDV
     FDYESDMRNP RKGGVEGAVL PKSSHSTLLW ASAISTIPFL VILFIFGTWM SSLWLTLSVL
     AVIAYSAPKL RFKERPFIDA LTSSTHFTSP ALIGATITGT SPSAAMWIAL GSFFLWGMAS
     QILGAVQDVN ADREANLSSI ATVIGARGAI RLSVVLYLLA AVLVTTLPNP AWIIGIAILT
     YVFNAARFWN ITDASCEQAN RSWKVFLWLN YFVGAVITIL LIAIHQI
 
 
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