LCPS_NEUCR
ID LCPS_NEUCR Reviewed; 602 AA.
AC P37295; Q7RVN3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Bifunctional lycopene cyclase/phytoene synthase {ECO:0000303|PubMed:11862485};
DE AltName: Full=Protein albino-2;
DE Includes:
DE RecName: Full=Lycopene beta-cyclase {ECO:0000303|PubMed:11862485};
DE EC=5.5.1.19 {ECO:0000269|PubMed:11862485, ECO:0000269|PubMed:16928467};
DE AltName: Full=Carotene cyclase {ECO:0000303|PubMed:11862485};
DE AltName: Full=Lycopene cyclase {ECO:0000303|PubMed:11862485};
DE Includes:
DE RecName: Full=Phytoene synthase {ECO:0000303|PubMed:8163509};
DE EC=2.5.1.32 {ECO:0000269|PubMed:11862485, ECO:0000269|PubMed:16928467};
GN Name=al-2 {ECO:0000303|PubMed:8163509}; ORFNames=B22I21.230, NCU00585;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=8163509; DOI=10.1016/s0021-9258(17)32680-7;
RA Schmidhauser T.J., Lauter F.-R., Schumacher M., Zhou W., Russo V.E.A.,
RA Yanofsky C.;
RT "Characterization of al-2, the phytoene synthase gene of Neurospora crassa.
RT Cloning, sequence analysis, and photoregulation.";
RL J. Biol. Chem. 269:12060-12066(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TRP-189 AND LYS-208.
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=11862485; DOI=10.1007/s00438-001-0626-5;
RA Arrach N., Schmidhauser T.J., Avalos J.;
RT "Mutants of the carotene cyclase domain of al-2 from Neurospora crassa.";
RL Mol. Genet. Genomics 266:914-921(2002).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16928467; DOI=10.1016/j.bbalip.2006.06.002;
RA Sandmann G., Zhu C., Krubasik P., Fraser P.D.;
RT "The biotechnological potential of the al-2 gene from Neurospora crassa for
RT the production of monocyclic keto hydroxy carotenoids.";
RL Biochim. Biophys. Acta 1761:1085-1092(2006).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the reactions from
CC geranylgeranyl diphosphate to phytoene (phytoene synthase) and from
CC lycopene to beta-carotene via the intermediate gamma-carotene and from
CC 3,4-didehydrolycopene to torulene (lycopene cyclase). Torulene is
CC further processed to the acidic carotenoid neurosporaxanthin. The
CC cyclase preferentially catalyzes single cyclizations at only one end of
CC the substrate to produce monocyclic carotenoids.
CC {ECO:0000269|PubMed:11862485, ECO:0000269|PubMed:16928467}.
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:0000269|PubMed:11862485, ECO:0000269|PubMed:16928467};
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:0000269|PubMed:11862485,
CC ECO:0000269|PubMed:16928467};
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:0000269|PubMed:11862485, ECO:0000269|PubMed:16928467};
CC -!- PATHWAY: Carotenoid biosynthesis; beta-carotene biosynthesis.
CC {ECO:0000269|PubMed:11862485, ECO:0000269|PubMed:16928467}.
CC -!- PATHWAY: Carotenoid biosynthesis; phytoene biosynthesis; all-trans-
CC phytoene from geranylgeranyl diphosphate: step 1/1.
CC {ECO:0000269|PubMed:11862485, ECO:0000269|PubMed:16928467}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: By blue light.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L27652; AAA19428.1; -; Genomic_DNA.
DR EMBL; BX842641; CAE76609.1; -; Genomic_DNA.
DR EMBL; CM002236; EAA36489.3; -; Genomic_DNA.
DR PIR; A53583; A53583.
DR RefSeq; XP_965725.3; XM_960632.3.
DR AlphaFoldDB; P37295; -.
DR SMR; P37295; -.
DR STRING; 5141.EFNCRP00000000733; -.
DR EnsemblFungi; EAA36489; EAA36489; NCU00585.
DR GeneID; 3881954; -.
DR KEGG; ncr:NCU00585; -.
DR VEuPathDB; FungiDB:NCU00585; -.
DR HOGENOM; CLU_012965_0_0_1; -.
DR InParanoid; P37295; -.
DR BioCyc; MetaCyc:MON-16129; -.
DR UniPathway; UPA00799; UER00773.
DR UniPathway; UPA00802; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046905; F:15-cis-phytoene synthase activity; IDA:UniProtKB.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:InterPro.
DR GO; GO:0016767; F:geranylgeranyl-diphosphate geranylgeranyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016872; F:intramolecular lyase activity; IEA:InterPro.
DR GO; GO:0045436; F:lycopene beta cyclase activity; IDA:UniProtKB.
DR GO; GO:0016120; P:carotene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00683; Trans_IPPS_HH; 1.
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 InterPro; IPR019845; Squalene/phytoene_synthase_CS.
DR InterPro; IPR044843; Trans_IPPS_bact-type.
DR InterPro; IPR033904; Trans_IPPS_HH.
DR Pfam; PF00494; SQS_PSY; 1.
DR SFLD; SFLDG01212; Phytoene_synthase_like; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR TIGRFAMs; TIGR03462; CarR_dom_SF; 2.
DR PROSITE; PS01044; SQUALEN_PHYTOEN_SYN_1; 1.
DR PROSITE; PS01045; SQUALEN_PHYTOEN_SYN_2; 1.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; Isomerase; Membrane; Multifunctional enzyme;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..602
FT /note="Bifunctional lycopene cyclase/phytoene synthase"
FT /id="PRO_0000067440"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..241
FT /note="Lycopene beta-cyclase"
FT /evidence="ECO:0000305|PubMed:8163509"
FT REGION 248..602
FT /note="Phytoene synthase"
FT /evidence="ECO:0000305|PubMed:8163509"
FT MUTAGEN 189
FT /note="W->R: In JA26; Abolishes lycopene cyclase activity
FT and accumulates a polar precursor carotenoid of
FT neurosporaxanthin."
FT /evidence="ECO:0000269|PubMed:11862485"
FT MUTAGEN 208
FT /note="K->E: In JA28; Abolishes lycopene cyclase activity
FT and accumulates a polar precursor carotenoid of
FT neurosporaxanthin."
FT /evidence="ECO:0000269|PubMed:11862485"
SQ SEQUENCE 602 AA; 68928 MW; DDFFBD725007E5C2 CRC64;
MYDYAFVHLK FTVPAAVLLT AIAYPILNRI HLIQTGFLVV VAFTAALPWD AYLIKHKVWS
YPPEAIVGPR LLGIPFEELF FFVIQTYITA LVYILFNKPV LHALHLNNQQ NPPAWMRVVK
VTGQVVLVAL SVWGWNAAQV HQETSYLGLI LVWACPFLLA IWTLAGRFIL SLPWYATVLP
MFLPTFYLWA VDEFALHRGT WSIGSGTKLD FCLFGKLDIE EATFFLVTNM LIVGGMAAFD
QYLAVIYAFP TLFPKVNRYP TTHMLLQSRL INTSRYDLER IEGLREAVER LRLKSRSFYL
ANSLFSGRLR IDLILLYSFC RLADDLVDDA KSRREVLSWT AKLNHFLDLH YKDADATEDP
KKKAERIDAY IKTAFPPCAY QALHLLPTHI LPPKPLYDLI KGFEMDSQFT FHGTSDSTDL
QYPIADDKDL ENYAIYVAGT VGELCIALII YHCLPDMSDT QKRELETAAC RMGIALQYVN
IARDIVVDAR IGRVYLPTTW LKKEGLTHKM VLENPEGPEV IERMRRRLLE NAFELYGGAR
PEMQRIPSEA RGPMIGAVEN YMAIGRVLRE RKEGTVFVRM EGRATVPKRR RLSTLLRALY
EQ
