ID R1EE55_BOTPV Unreviewed; 936 AA.
AC R1EE55;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Bifunctional lycopene cyclase/phytoene synthase {ECO:0000256|ARBA:ARBA00018909};
DE EC=5.5.1.19 {ECO:0000256|ARBA:ARBA00012242};
DE AltName: Full=Phytoene desaturase {ECO:0000256|ARBA:ARBA00013293};
DE AltName: Full=Phytoene desaturase (3,4-didehydrolycopene-forming) {ECO:0000256|ARBA:ARBA00034551};
GN ORFNames=UCRNP2_7258 {ECO:0000313|EMBL:EOD46013.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD46013.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
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:0000256|ARBA:ARBA00029335};
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:0000256|ARBA:ARBA00029313};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
CC -!- PATHWAY: Carotenoid biosynthesis; beta-carotene biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005089}.
CC -!- PATHWAY: Carotenoid biosynthesis; phytoene biosynthesis; all-trans-
CC phytoene from geranylgeranyl diphosphate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005172}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006046, ECO:0000256|RuleBase:RU362075}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phytoene/squalene
CC synthase family. {ECO:0000256|ARBA:ARBA00008406}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the lycopene beta-
CC cyclase family. {ECO:0000256|ARBA:ARBA00008247}.
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DR EMBL; KB916504; EOD46013.1; -; Genomic_DNA.
DR RefSeq; XP_007586514.1; XM_007586452.1.
DR AlphaFoldDB; R1EE55; -.
DR STRING; 1287680.R1EE55; -.
DR KEGG; npa:UCRNP2_7258; -.
DR eggNOG; KOG4254; Eukaryota.
DR HOGENOM; CLU_292389_0_0_1; -.
DR OrthoDB; 5490570at2759; -.
DR UniPathway; UPA00799; UER00773.
DR UniPathway; UPA00802; -.
DR Proteomes; UP000013521; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:UniProt.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 2.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR014105; Carotenoid/retinoid_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR017825; Lycopene_cyclase_dom.
DR InterPro; IPR008150; Phytoene_DH_bac_CS.
DR InterPro; IPR002060; Squ/phyt_synthse.
DR InterPro; IPR019845; Squalene/phytoene_synthase_CS.
DR NCBIfam; TIGR03462; CarR_dom_SF; 2.
DR NCBIfam; TIGR02734; crtI_fam; 1.
DR PANTHER; PTHR43734; PHYTOENE DESATURASE; 1.
DR PANTHER; PTHR43734:SF1; PHYTOENE DESATURASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF00494; SQS_PSY; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF48576; Terpenoid synthases; 1.
DR PROSITE; PS00982; PHYTOENE_DH; 1.
DR PROSITE; PS01045; SQUALEN_PHYTOEN_SYN_2; 1.
PE 3: Inferred from homology;
KW Carotenoid biosynthesis {ECO:0000256|ARBA:ARBA00022746,
KW ECO:0000256|RuleBase:RU362075}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362075};
KW Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 414..693
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT REGION 915..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..936
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 936 AA; 105012 MW; 9EC7E2737B45EE28 CRC64;
MGYDYALVHL KYTVPPALAL TLLYRPLLTR LDVYKILFLI AVVSTIPWDS YLIRTRVWTY
PAYVILGPTL FDIPAEELFF FVIQTYNTSL LYLLLSKPVF FPVYLRAEGG KSNALQGRKP
SWRKYQWTGQ AVLALGIGLS LRMVQVGGRG TYIGLIILWA FPFLLLLWSL AYQFILAIPR
SSSTWPIVVP TLYLWIVDTL ALRRGTWVIE AGTKLGIHLW PGLEIEEAFF FLVTNTLIVF
GLIAFDNALT ILYTWRLRID LILLYSFCRV ADDLIDNASD CKEAREWIRK LRMYLDLSYK
GSEEGTLLQD YVEIKFPPEA QSALRFLPTS YLSRSRMGVA LQYVNISRDI AVDAQIQRVY
IPVDWLGEKE LTPAAVIKNP QDAVHSRPSS TPKLSAMDEK ARQKTAVVIG AGVGGVATAA
RLAKAGYQVT VVEKNDFTGG RCSLIEHNGF RFDQGPSLLL LPNLFAEAFH DLGTSLEAEG
VHLLKCEPNY NLWFGDGHSF ELSTDLARMK REIERWEGKD GFERYLRFLQ EAHRHYELSV
THVLKRNFTT LLSMARWSFL KHLLELHPFE SIYSRASKYF WTERLRRVFT FGSMYMGMSP
FDAPGTYSLL QYTELAEGIW YPEGGFHKVV DALVKVGQKL GVEYRLSTPV SHIALSPDQR
RATGVVLASG ETLHADVVVN NSDLVYAYNN LLPQTPYARS LTRKPASCSS ISFYWSLSRT
VPELRAHNIF LADSYRTSFD SIFKHQQIPA EPSFYVNVPS RIDASAAPPG HDAVVVLVPV
GHLVSTTPST SSASTAAGQD WQRMRALARA TVLDTIRART GADLAPLIRH ERVNDPAAWR
DAFNLDRGAI LGLSHDFFNV LSFRPKTRHP SIRGLYFVGA STHPGTGVPI CLAGSKVTVE
QVVGDGGGEA VVWGHGGTGK KREREGIDRV EGGTRC
//
