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Database: UniProt
Entry: F4GZW7_CELFA
LinkDB: F4GZW7_CELFA
Original site: F4GZW7_CELFA 
ID   F4GZW7_CELFA            Unreviewed;       591 AA.
AC   F4GZW7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=Phytoene desaturase {ECO:0000313|EMBL:AEE47283.1};
GN   OrderedLocusNames=Celf_3169 {ECO:0000313|EMBL:AEE47283.1};
OS   Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 /
OS   NCIMB 8980 / NCTC 7547).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=590998 {ECO:0000313|EMBL:AEE47283.1, ECO:0000313|Proteomes:UP000008460};
RN   [1] {ECO:0000313|EMBL:AEE47283.1, ECO:0000313|Proteomes:UP000008460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 /
RC   NCTC 7547 {ECO:0000313|Proteomes:UP000008460};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA   Woyke T.;
RT   "Complete sequence of Cellulomonas fimi ATCC 484.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000256|ARBA:ARBA00004829,
CC       ECO:0000256|RuleBase:RU362075}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       {ECO:0000256|RuleBase:RU362075}.
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DR   EMBL; CP002666; AEE47283.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4GZW7; -.
DR   STRING; 590998.Celf_3169; -.
DR   KEGG; cfi:Celf_3169; -.
DR   eggNOG; COG1233; Bacteria.
DR   HOGENOM; CLU_019722_2_1_11; -.
DR   OMA; INYPKGG; -.
DR   Proteomes; UP000008460; Chromosome.
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; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR014105; Carotenoid/retinoid_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
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   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Carotenoid biosynthesis {ECO:0000256|ARBA:ARBA00022746,
KW   ECO:0000256|RuleBase:RU362075};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362075};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008460}.
FT   DOMAIN          46..557
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   591 AA;  63105 MW;  C659859ED0102E1A CRC64;
     MTTTAPRAGG SDAPPAGRTP RSRAATGTAA QPGDGPGRVV VVGGGIGGLM TAALLARGGA
     QVTLLERHER LGGRMGTLTV DGFRFDTGPS WYFMPEVFAH AFALLGERVE DHLDLVPLDP
     AYRLFTEPQT PGGRAEGFDL VADAEQNWAT FEALEPGAGE AVRRYAQDAS LAYRTALDHF
     LWTTFQRPDR LLSAPVVRRS GTLVDLLTHT LAEKVERTVQ HPVLRQALGY HAVFLGSSPY
     RVPALYSLMS HLDLVDGVRY PRGGMYTVIE ALERLAVREG VEIRTGADVV EIDVEPAPRT
     ARTPRRTGVA RGVRLATGEL VEADVVVSGA DRHHTETALL DPRHSDHPAP TWERSGPGIS
     ALLVMAGVRG ALPELAHHSL FFTRDWPGNF ADILGDGRST PADRLRVPEV ASVYASRTTA
     TDPTAAPPGH ENLFLLVPFP ADASLGDGAP GSPERDEVER HADRFLDQVG AWAGIDDLRG
     RVVTRHVVAP ADFARDLSAW RGTALGMEHT LAQSAMFRPG DASARVPNLL HVGGGTVPGV
     GLPMCLISAE LVAKRLLGET STRPLPAPLR PGFLDAARPA GVWSAVRAGR A
//
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