ID   CRTU_STRGR              Reviewed;         517 AA.
AC   P72449;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Carotenoid phi-ring synthase {ECO:0000305};
DE            EC=1.3.99.39 {ECO:0000269|PubMed:10395965};
DE   AltName: Full=Beta-carotene desaturase {ECO:0000305};
DE   AltName: Full=Carotenoid beta-ring:acceptor oxidoreductase/methyltranferase (phi-ring forming) {ECO:0000305};
GN   Name=crtU {ECO:0000303|PubMed:8917308};
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=JA 3933;
RX   PubMed=8917308; DOI=10.1007/bf02173971;
RA   Schumann G., Nurnberger H., Sandmann G., Kruegel H.J.;
RT   "Activation and analysis of cryptic crt genes for carotenoid biosynthesis
RT   from Streptomyces griseus.";
RL   Mol. Gen. Genet. 252:658-666(1996).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=JA 3933;
RX   PubMed=10395965; DOI=10.1016/s1388-1981(99)00075-x;
RA   Kruegel H., Krubasik P., Weber K., Saluz H.P., Sandmann G.;
RT   "Functional analysis of genes from Streptomyces griseus involved in the
RT   synthesis of isorenieratene, a carotenoid with aromatic end groups,
RT   revealed a novel type of carotenoid desaturase.";
RL   Biochim. Biophys. Acta 1439:57-64(1999).
CC   -!- FUNCTION: Involved in the biosynthesis of isorenieratene, a carotenoid
CC       with aromatic end groups (PubMed:10395965). Catalyzes the introduction
CC       of two additional double bonds into each ionone ring of beta-carotene
CC       to produce isorenieratene. The reaction includes an intramolecular
CC       methyl transfer from position C1 to position C2 of the ring
CC       (PubMed:10395965). {ECO:0000269|PubMed:10395965}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 A + a carotenoid beta-end derivative = a carotenoid phi-end
CC         derivative + 2 AH2; Xref=Rhea:RHEA:22524, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:139120, ChEBI:CHEBI:139129;
CC         EC=1.3.99.39; Evidence={ECO:0000269|PubMed:10395965};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:A2XDA1};
CC   -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000269|PubMed:10395965}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene leads to accumulation of
CC       beta-carotene. {ECO:0000269|PubMed:10395965}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; X95596; CAA64853.1; -; Genomic_DNA.
DR   SMR; P72449; -.
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; -; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Carotenoid biosynthesis; FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..517
FT                   /note="Carotenoid phi-ring synthase"
FT                   /id="PRO_0000453389"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         45
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         64..65
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         72
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         99
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         461
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         472
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
SQ   SEQUENCE   517 AA;  57105 MW;  276BB79EDAA4EA45 CRC64;
     MFARDSGRGH RHGRDRQAAV VPAPAGRARF TGDAPAVAVV GGGIAGIAAA TLLAERGVRV
     TLYEREPGLG GRLSGWPTEL TDGTTVTMSR GFHAFFRQYY NLRGLLRRVD PDLGSLTRLP
     DYPLWHGSGL RDSFARVPRT PPLSAMGFVA LSPTFGLRDL VRINPRAAVG LLDVRVPEVY
     ERLDGISATD FLDRIRFPEA AHHLAFEVFS RSFFADPREL SAAELALMFH IYFLGSSEGL
     LFDVPGEPFP AALWEPLHHY LEVHRVDVRT RTPLRQVRPR PGGGLDLTTD DRTTRYDALV
     LALDSGALRR LVAASPELGD TDWRARIARL RTAPPFLVSR LWLDRPVAHD RPGFLGTSGY
     GPLDNVSVLD RWEGEAARWA RRTRGSVVEL HAYAVAPDAD RSAVQDEALR QLHRVYPETR
     SARLLDARHE WRADCPMFPV GGYRDRPGVR SPDPAVTVAG DMVRTELPVA LMERAATSGF
     LAANALLERW GVRGQTLWTV PRAGRSAVLR RLAALAD