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Database: UniProt
Entry: CRTI_PARSN
LinkDB: CRTI_PARSN
Original site: CRTI_PARSN 
ID   CRTI_PARSN              Reviewed;         501 AA.
AC   P54978; Q33DT7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   13-SEP-2023, entry version 77.
DE   RecName: Full=Phytoene desaturase (lycopene-forming);
DE            EC=1.3.99.31;
DE   AltName: Full=4-step phytoene desaturase;
DE   AltName: Full=Phytoene dehydrogenase;
GN   Name=crtI;
OS   Paracoccus sp. (strain N81106 / MBIC 01143) (Agrobacterium aurantiacum).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=81397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7592436; DOI=10.1128/jb.177.22.6575-6584.1995;
RA   Misawa N., Satomi Y., Kondo K., Yokoyama A., Kajiwara S., Saito T.,
RA   Ohtani T., Miki W.;
RT   "Structure and functional analysis of a marine bacterial carotenoid
RT   biosynthesis gene cluster and astaxanthin biosynthetic pathway proposed at
RT   the gene level.";
RL   J. Bacteriol. 177:6575-6584(1995).
RN   [2]
RP   SEQUENCE REVISION TO 211.
RA   Misawa N.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Maruyama T., Inomata Y., Haga M., Ide T., Misawa N.;
RT   "Structure of the complete carotenoid biosynthesis gene cluster of
RT   Paracoccus sp. strain N81106.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This enzyme converts phytoene into lycopene via the
CC       intermediaries of phytofluene, zeta-carotene and neurosporene by the
CC       introduction of four double bonds. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=15-cis-phytoene + 4 A = 4 AH2 + all-trans-lycopene;
CC         Xref=Rhea:RHEA:15585, ChEBI:CHEBI:13193, ChEBI:CHEBI:15948,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:27787; EC=1.3.99.31;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- PATHWAY: Carotenoid biosynthesis; astaxanthin biosynthesis.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; D58420; BAA09594.2; -; Genomic_DNA.
DR   EMBL; AB206672; BAE47468.1; -; Genomic_DNA.
DR   AlphaFoldDB; P54978; -.
DR   SMR; P54978; -.
DR   UniPathway; UPA00387; -.
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; 3.
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   NCBIfam; TIGR02734; crtI_fam; 1.
DR   PANTHER; PTHR43734:SF3; B-CAROTENE KETOLASE; 1.
DR   PANTHER; PTHR43734; PHYTOENE DESATURASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00982; PHYTOENE_DH; 1.
PE   3: Inferred from homology;
KW   Carotenoid biosynthesis; FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..501
FT                   /note="Phytoene desaturase (lycopene-forming)"
FT                   /id="PRO_0000067687"
FT   BINDING         12..45
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   501 AA;  54806 MW;  944B4BF05872C1BF CRC64;
     MNAHSPAAKT AIVIGAGFGG LALAIRLQSA GIATTLVEAR DKPGGRAYVW HDQGHLFDAG
     PTVITDPDAL KELWALTGQD MARDVTLMPV SPFYRLMWPG GKVFDYVNEA DQLERQIAQF
     NPDDLEGYRR FRDYAEEVYQ EGYVKLGTVP FLKLGQMLKA APALMKLEAY KSVHAKVATF
     IKDPYLRQAF SYHTLLVGGN PFSTSSIYAL IHALERRGGV WFAKGGTNQL VAGMVALFER
     LGGQMLLNAK VARIDTDGPR ATGVTLADGR ALTADMVASN GDVMHNYRDL LGHTARGQSR
     AKSLNAKRWS MSLFVLHFGL REAPKDVAHH TILFGPRYKE LVNEIFKGPK LAEDFSLYLH
     SPCTTDPEMA PPGMSTHYVL APVPHLGRAD IDWAVEGPRY ADRILASLEE RLIPNLRANL
     TTTRIFTPSD FASELNAHHG SAFSVEPILT QSAWFRPHNR DKTIRNFYLV GAGTHPGAGI
     PGVVGSAKAT AQVMLSDLAS A
//
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