ID   C1AB44_GEMAT            Unreviewed;       487 AA.
AC   C1AB44;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Phytoene dehydrogenase {ECO:0000313|EMBL:BAH39450.1};
DE            EC=1.14.99.- {ECO:0000313|EMBL:BAH39450.1};
GN   Name=crtI {ECO:0000313|EMBL:BAH39450.1};
GN   OrderedLocusNames=GAU_2408 {ECO:0000313|EMBL:BAH39450.1};
OS   Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC
OS   100505).
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatimonas.
OX   NCBI_TaxID=379066 {ECO:0000313|EMBL:BAH39450.1, ECO:0000313|Proteomes:UP000002209};
RN   [1] {ECO:0000313|Proteomes:UP000002209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505
RC   {ECO:0000313|Proteomes:UP000002209};
RA   Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., Oguchi A.,
RA   Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., Yokoyama H.,
RA   Tanikawa S., Hanada S., Kamagata Y., Fujita N.;
RT   "Complete genome sequence of Gemmatimonas aurantiaca T-27 that represents a
RT   novel phylum Gemmatimonadetes.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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|ARBA:ARBA00006046, ECO:0000256|RuleBase:RU362075}.
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DR   EMBL; AP009153; BAH39450.1; -; Genomic_DNA.
DR   RefSeq; WP_015894219.1; NC_012489.1.
DR   AlphaFoldDB; C1AB44; -.
DR   STRING; 379066.GAU_2408; -.
DR   KEGG; gau:GAU_2408; -.
DR   eggNOG; COG1233; Bacteria.
DR   HOGENOM; CLU_019722_2_1_0; -.
DR   OrthoDB; 9814556at2; -.
DR   Proteomes; UP000002209; Chromosome.
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   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 {ECO:0000256|ARBA:ARBA00022746,
KW   ECO:0000256|RuleBase:RU362075};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362075,
KW   ECO:0000313|EMBL:BAH39450.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002209}.
FT   DOMAIN          11..481
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   487 AA;  54115 MW;  6300E24E5BAF6B02 CRC64;
     MRIVVIGSGF GGLAAAIRLQ AQGHSVTIVE KLDQPGGRAC VFHQDGFTFD AGPTIITAPW
     VLDELFALTG RHTADFVSLV RLDPFYNIRF EDGSVFRYNG DKDALREQVR MFAPGDEAGY
     LTFREKAAAI FDAGMPLIDQ PFDTIGSMVK AVPALLRTRA DRSVAAMANA YLADERLRQV
     FSFHPLLVGG NPFRASSMYA LIHKLEQQWG VLFCMGGTGA LVQGLVRAFE ELGGTMRYEH
     EVADVPVVNG RATGVRCVNG VHLDADAVVC NGDVVQAYRT LIKPEHHPRT PARRLERMRH
     SMSLFVIYFG TNRQYDNIAH HEILMGPRYR ELLEDIFERK ILADDFSLYL HRPTATDPSL
     APPGCDAWYV LSPVPHLGSG TDWERVSERY RDRIMGYLEE RYLPGLSQHL VTERRVDPRY
     FEGTLNSYLG SAFGPEPVLT QSAWFRPHNR DRDIGNLYFC GAGTHPGAGL PGVISSGKIV
     AGMIGRS
//