LCPS_ASPNC
ID LCPS_ASPNC Reviewed; 582 AA.
AC A2QM49;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Bifunctional lycopene cyclase/phytoene synthase {ECO:0000250|UniProtKB:P37295};
DE Includes:
DE RecName: Full=Lycopene beta-cyclase {ECO:0000250|UniProtKB:P37295};
DE EC=5.5.1.19 {ECO:0000250|UniProtKB:P37295};
DE AltName: Full=Lycopene cyclase {ECO:0000250|UniProtKB:P37295};
DE Includes:
DE RecName: Full=Phytoene synthase {ECO:0000250|UniProtKB:P37295};
DE EC=2.5.1.32 {ECO:0000250|UniProtKB:P37295};
GN ORFNames=An07g00800;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the reactions from
CC geranylgeranyl diphosphate to phytoene (phytoene synthase) and lycopene
CC to beta-carotene via the intermediate gamma-carotene (lycopene
CC cyclase). {ECO:0000250|UniProtKB:P37295}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-lycopene = gamma-carotene; Xref=Rhea:RHEA:32219,
CC ChEBI:CHEBI:15948, ChEBI:CHEBI:27740; EC=5.5.1.19;
CC Evidence={ECO:0000250|UniProtKB:P37295};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=gamma-carotene = all-trans-beta-carotene;
CC Xref=Rhea:RHEA:32239, ChEBI:CHEBI:17579, ChEBI:CHEBI:27740;
CC EC=5.5.1.19; Evidence={ECO:0000250|UniProtKB:P37295};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (2E,6E,10E)-geranylgeranyl diphosphate = 15-cis-phytoene + 2
CC diphosphate; Xref=Rhea:RHEA:34475, ChEBI:CHEBI:27787,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58756; EC=2.5.1.32;
CC Evidence={ECO:0000250|UniProtKB:P37295};
CC -!- PATHWAY: Carotenoid biosynthesis; beta-carotene biosynthesis.
CC {ECO:0000250|UniProtKB:P37295}.
CC -!- PATHWAY: Carotenoid biosynthesis; phytoene biosynthesis; all-trans-
CC phytoene from geranylgeranyl diphosphate: step 1/1.
CC {ECO:0000250|UniProtKB:P37295}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the lycopene beta-
CC cyclase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phytoene/squalene
CC synthase family. {ECO:0000305}.
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DR EMBL; AM270119; CAK39303.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QM49; -.
DR PaxDb; A2QM49; -.
DR EnsemblFungi; CAK39303; CAK39303; An07g00800.
DR VEuPathDB; FungiDB:An07g00800; -.
DR HOGENOM; CLU_012965_0_0_1; -.
DR UniPathway; UPA00799; UER00773.
DR UniPathway; UPA00802; -.
DR Proteomes; UP000006706; Chromosome 4L.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046905; F:15-cis-phytoene synthase activity; IEA:UniProt.
DR GO; GO:0016767; F:geranylgeranyl-diphosphate geranylgeranyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016872; F:intramolecular lyase activity; IEA:InterPro.
DR GO; GO:0045436; F:lycopene beta cyclase activity; IEA:RHEA.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR017825; Lycopene_cyclase_dom.
DR InterPro; IPR002060; Squ/phyt_synthse.
DR Pfam; PF00494; SQS_PSY; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR TIGRFAMs; TIGR03462; CarR_dom_SF; 2.
PE 3: Inferred from homology;
KW Carotenoid biosynthesis; Isomerase; Membrane; Multifunctional enzyme;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..582
FT /note="Bifunctional lycopene cyclase/phytoene synthase"
FT /id="PRO_0000409232"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..261
FT /note="Lycopene beta-cyclase"
FT /evidence="ECO:0000250|UniProtKB:P37295"
FT REGION 268..582
FT /note="Phytoene synthase"
FT /evidence="ECO:0000250|UniProtKB:P37295"
SQ SEQUENCE 582 AA; 65647 MW; 88E8322BC29400BA CRC64;
MNQNGTRLCY SVREVPPTSF VSAPANYKRA SSHCTYTIPA ASALTVLYYP FFTAQDRCKI
CILITIAILA TLPWDSYLIR SAIWTYPPDA VVGLKILDIP IEEVFFFAIQ TYITSLTYCI
FTKPLVRPMY LRSHLERRGT RYVVATVILA LMGGGTACLL LGRRMTYLGL ILVWACPILL
FQWMMSYPFL SELPWKPTIT SICLPTLHLW FADSRAMGTG TWRIEEGTKL NFRIGGLELE
EALFFLVSNM MVVLGLVGCD YAYALQEYES LSQPASDVYI TLRKALSLLA RPLPIDASLI
SALSQAVYRL QEKSQSMFLG SALFQGQLRI DLIFLYSFCR VMDDLIDEAE DEQEARFWVT
ECRHLLDSTH RSEPHSDHFY TGKKGEEHER LRQSISYLPP SHLSNDSFDD LLKGFEIDLK
FNPQREAFPI QSEYCLDQYA GFVAGTVGVL VFDLTLFHCG HYFIQDVPRL RRAAKDMGKA
MQCQPRGDGG ATSGRKRAIA GNRGELYGYW TTAEGAERHK PGASVEDEGA FGATAKSWLA
GDVITELCHC FIQAEYVIYL VRHQNASADT LVLLSALVYR LE
