LBTBC_DIESC
ID LBTBC_DIESC Reviewed; 432 AA.
AC A1XI30;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=C(50) beta-cyclic carotenoids biosynthesis protein LbtBC {ECO:0000305};
DE Includes:
DE RecName: Full=Putative C(50) carotenoid beta-cyclase subunit B {ECO:0000305};
DE EC=5.5.1.- {ECO:0000305|PubMed:17008032};
DE Includes:
DE RecName: Full=Lycopene elongase/hydratase {ECO:0000250|UniProtKB:M0L7V9};
DE EC=2.5.1.150 {ECO:0000250|UniProtKB:M0L7V9};
GN Name=lbtBC {ECO:0000303|PubMed:17008032};
OS Dietzia sp. (strain CQ4).
OC Bacteria; Actinobacteria; Corynebacteriales; Dietziaceae; Dietzia;
OC unclassified Dietzia.
OX NCBI_TaxID=370437;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND SUBUNIT.
RC STRAIN=CQ4;
RX PubMed=17008032; DOI=10.1016/j.gene.2006.08.006;
RA Tao L., Yao H., Cheng Q.;
RT "Genes from a Dietzia sp. for synthesis of C40 and C50 beta-cyclic
RT carotenoids.";
RL Gene 386:90-97(2007).
CC -!- FUNCTION: Involved in the biosynthesis of C(50) beta-cyclic carotenoids
CC (PubMed:17008032). The elongase/hydratase domain catalyzes the
CC elongation of lycopene by attaching a C(5) isoprene unit at C-2, as
CC well as the hydroxylation of the previous end of the molecule (By
CC similarity). The enzyme acts at both ends of the substrate, and
CC catalyzes the conversion of lycopene to the C(45) intermediate
CC dihydroisopentenyldehydrorhodopin (DH-IDR) and the conversion of
CC isopentenyldehydrorhodopin (IDR) to the C(50) carotenoid
CC dihydrobisanhydrobacterioruberin (DH-BABR) (By similarity). The beta-
CC cyclase domain may produce the C(50) beta-cyclic carotenoid C.p.450
CC from the C(50) carotenoid dihydrobisanhydrobacterioruberin (DH-BABR)
CC (Probable). {ECO:0000250|UniProtKB:M0L7V9, ECO:0000269|PubMed:17008032,
CC ECO:0000305|PubMed:17008032}.
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:M0L7V9};
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:17008032}.
CC -!- SUBUNIT: May form a complex with LbtA. {ECO:0000305|PubMed:17008032}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; DQ369754; ABD24402.1; -; Genomic_DNA.
DR AlphaFoldDB; A1XI30; -.
DR KEGG; ag:ABD24402; -.
DR BioCyc; MetaCyc:MON-20369; -.
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:0016872; F:intramolecular lyase activity; IEA:InterPro.
DR GO; GO:0045436; F:lycopene beta cyclase activity; IEA:UniProt.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0016120; P:carotene biosynthetic process; IEA:UniProt.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.357.140; -; 1.
DR InterPro; IPR017825; Lycopene_cyclase_dom.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR044878; UbiA_sf.
DR Pfam; PF18916; Lycopene_cyc; 1.
DR Pfam; PF01040; UbiA; 1.
DR TIGRFAMs; TIGR03462; CarR_dom_SF; 1.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; Cell membrane; Isomerase; Membrane; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..432
FT /note="C(50) beta-cyclic carotenoids biosynthesis protein
FT LbtBC"
FT /id="PRO_0000450595"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..140
FT /note="Beta-cyclase"
FT /evidence="ECO:0000305"
FT REGION 111..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..432
FT /note="Elongase/hydratase"
FT /evidence="ECO:0000305"
FT COMPBIAS 125..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 432 AA; 45929 MW; E20A54C34CD3A406 CRC64;
MTSLYTTLNL TMSIPVVAVA LLAAWRLRGP ERRRWLIGVG GALLILMILT AVFDNIMISA
GLVAYDDSLT SGIRLGVAPI EDFAYAVAAA VFVPSVWALL TASPRVGAEV GSPTVSGRGD
ALLTRAPEPG DDDEVRTPER PGTPGLLTTL FWSSRPVSWV NTAAPFALAY FLATGGFDLV
GVIGTIFFLV PYNLAMYGIN DVFDYESDLR NPRKGGVEGS VLERSRHTAT LVASAVTTVP
FLVYLVLTGT VESSLWLAAS AFAVIAYSAK GLRFKEIPFL DSLTSAFHFV SPAIVGWTIA
GAELTGGVWA CLIAFMLWGA ASQAFGAVQD VRFDREADLK SVATVLGARA AVWFALACYV
AAVVVLLAAA PWPASGAAFA ILPYLATVAA YVGVTDADAE RTNEGWKRFL VLNMLAGFCV
TQIVLWSVLV WS
