ID   CRTI_NEUCR              Reviewed;         595 AA.
AC   P21334; Q7RVL2;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Phytoene desaturase;
DE            EC=1.3.99.30;
DE   AltName: Full=Albino-1 protein;
DE   AltName: Full=Phytoene desaturase (3,4-didehydrolycopene-forming);
DE   Flags: Precursor;
GN   Name=al-1; ORFNames=NCU00552;
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=2144609; DOI=10.1128/mcb.10.10.5064-5070.1990;
RA   Schmidhauser T.J., Lauter F.-R., Russo V.E.A., Yanofsky C.;
RT   "Cloning, sequence, and photoregulation of al-1, a carotenoid biosynthetic
RT   gene of Neurospora crassa.";
RL   Mol. Cell. Biol. 10:5064-5070(1990).
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=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   [3]
RP   FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=11017770; DOI=10.1006/fgbi.2000.1212;
RA   Hausmann A., Sandmann G.;
RT   "A single five-step desaturase is involved in the carotenoid biosynthesis
RT   pathway to beta-carotene and torulene in Neurospora crassa.";
RL   Fungal Genet. Biol. 30:147-153(2000).
RN   [4]
RP   FUNCTION.
RX   PubMed=18812228; DOI=10.1016/j.fgb.2008.09.001;
RA   Estrada A.F., Maier D., Scherzinger D., Avalos J., Al-Babili S.;
RT   "Novel apocarotenoid intermediates in Neurospora crassa mutants imply a new
RT   biosynthetic reaction sequence leading to neurosporaxanthin formation.";
RL   Fungal Genet. Biol. 45:1497-1505(2008).
CC   -!- FUNCTION: Phytoene desaturase involved in the carotenoid biosynthesis
CC       pathway. Converts phytoene into 3,4-didehydrolycopene via the
CC       intermediary of phytofluene, zeta-carotene, neurosporene and lycopene,
CC       by introducing up to five double bonds into phytoene.
CC       {ECO:0000269|PubMed:11017770, ECO:0000269|PubMed:18812228}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=15-cis-phytoene + 5 A = 5 AH2 + all-trans-3,4-
CC         didehydrolycopene; Xref=Rhea:RHEA:30975, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:27787, ChEBI:CHEBI:62474;
CC         EC=1.3.99.30;
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000269|PubMed:11017770};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=30 uM for phytoene {ECO:0000269|PubMed:11017770};
CC         KM=32 uM for lycopene {ECO:0000269|PubMed:11017770};
CC   -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: By photoinduction.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; M57465; AAA33555.1; -; Genomic_DNA.
DR   EMBL; CM002236; EAA35477.1; -; Genomic_DNA.
DR   PIR; A35919; A35919.
DR   RefSeq; XP_964713.1; XM_959620.2.
DR   AlphaFoldDB; P21334; -.
DR   SMR; P21334; -.
DR   STRING; 5141.EFNCRP00000000637; -.
DR   EnsemblFungi; EAA35477; EAA35477; NCU00552.
DR   GeneID; 3880862; -.
DR   KEGG; ncr:NCU00552; -.
DR   VEuPathDB; FungiDB:NCU00552; -.
DR   HOGENOM; CLU_019722_2_1_1; -.
DR   InParanoid; P21334; -.
DR   BioCyc; MetaCyc:MON-16128; -.
DR   UniPathway; UPA00803; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR014105; Carotenoid/retinoid_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR008150; Phytoene_DH_bac_CS.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR02734; crtI_fam; 1.
DR   PROSITE; PS00982; PHYTOENE_DH; 1.
PE   1: Evidence at protein level;
KW   Carotenoid biosynthesis; Membrane; NAD; Oxidoreductase; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..595
FT                   /note="Phytoene desaturase"
FT                   /id="PRO_0000067695"
FT   TRANSMEM        574..594
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   595 AA;  66367 MW;  0FF3DF07328ED784 CRC64;
     MAETQRPRSA IIVGAGAGGI AVAARLAKAG VDVTVLEKND FTGGRCSLIH TKAGYRFDQG
     PSLLLLPGLF RETFEDLGTT LEQEDVELLQ CFPNYNIWFS DGKRFSPTTD NATMKVEIEK
     WEGPDGFRRY LSWLAEGHQH YETSLRHVLH RNFKSILELA DPRLVVTLLM ALHPFESIWH
     RAGRYFKTDR MQRVFTFATM YMGMSPFDAP ATYSLLQYSE LAEGIWYPRG GFHKVLDALV
     KIGERMGVKY RLNTGVSQVL TDGGKNGKKP KATGVQLENG EVLNADLVVV NADLVYTYNN
     LLPKEIGGIK KYANKLNNRK ASCSSISFYW SLSGMAKELE THNIFLAEEY KESFDAIFER
     QALPDDPSFY IHVPSRVDPS AAPPDRDAVI ALVPVGHLLQ NGQPELDWPT LVSKARAGVL
     ATIQARTGLS LSPLITEEIV NTPYTWETKF NLSKGAILGL AHDFFNVLAF RPRTKAQGMD
     NAYFVGASTH PGTGVPIVLA GAKITAEQIL EETFPKNTKV PWTTNEERNS ERMRKEMDEK
     ITEEGIIMRS NSSKPGRRGS DAFEGAMEVV NLLSQRAFPL LVALMGVLYF LLFVR