ID   BCH_GENLU               Reviewed;         320 AA.
AC   B3SGL0; Q1XIT1;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Beta-carotene 3-hydroxylase, chloroplastic;
DE            Short=GenCHYB;
DE            EC=1.14.15.24 {ECO:0000250|UniProtKB:Q9SZZ8};
DE   Flags: Precursor;
GN   Name=BHY;
OS   Gentiana lutea (Yellow gentian).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Gentianaceae; Gentianeae; Gentianinae;
OC   Gentiana.
OX   NCBI_TaxID=38851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=12591618; DOI=10.1016/s0167-4781(03)00017-4;
RA   Zhu C., Yamamura S., Nishihara M., Koiwa H., Sandmann G.;
RT   "cDNAs for the synthesis of cyclic carotenoids in petals of Gentiana lutea
RT   and their regulation during flower development.";
RL   Biochim. Biophys. Acta 1625:305-308(2003).
CC   -!- FUNCTION: Nonheme diiron monooxygenase involved in the biosynthesis of
CC       xanthophylls. Specific for beta-ring hydroxylations of beta-carotene.
CC       Uses ferredoxin as an electron donor. {ECO:0000250|UniProtKB:Q9SZZ8,
CC       ECO:0000305|PubMed:12591618}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-beta-carotene + 4 H(+) + 2 O2 + 4 reduced [2Fe-2S]-
CC         [ferredoxin] = all-trans-zeaxanthin + 2 H2O + 4 oxidized [2Fe-2S]-
CC         [ferredoxin]; Xref=Rhea:RHEA:30331, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC         COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17579, ChEBI:CHEBI:27547, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738; EC=1.14.15.24;
CC         Evidence={ECO:0000250|UniProtKB:Q9SZZ8};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Up-regulated during flower development.
CC       {ECO:0000269|PubMed:12591618}.
CC   -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC       involved in iron binding.
CC   -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR   EMBL; AB027187; BAE92729.1; -; mRNA.
DR   EMBL; EF203255; ACF21782.1; -; mRNA.
DR   AlphaFoldDB; B3SGL0; -.
DR   KEGG; ag:ACF21782; -.
DR   BRENDA; 1.14.15.24; 8915.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR045019; BETA-OHASE-like.
DR   InterPro; IPR006694; Fatty_acid_hydroxylase.
DR   PANTHER; PTHR31899; PTHR31899; 1.
DR   Pfam; PF04116; FA_hydroxylase; 1.
PE   2: Evidence at transcript level;
KW   Carotenoid biosynthesis; Chloroplast; Hydrolase; Iron; Membrane;
KW   Metal-binding; NAD; Oxidoreductase; Plastid; Transit peptide;
KW   Transmembrane; Transmembrane helix.
FT   TRANSIT         1..78
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           79..320
FT                   /note="Beta-carotene 3-hydroxylase, chloroplastic"
FT                   /id="PRO_0000412809"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          165..292
FT                   /note="Fatty acid hydroxylase"
FT                   /evidence="ECO:0000255"
FT   MOTIF           177..182
FT                   /note="Histidine box-1"
FT   MOTIF           189..193
FT                   /note="Histidine box-2"
FT   MOTIF           250..255
FT                   /note="Histidine box-3"
FT   MOTIF           276..280
FT                   /note="Histidine box-4"
FT   CONFLICT        73
FT                   /note="R -> K (in Ref. 1; BAE92729)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   320 AA;  35574 MW;  B045A044BD2FD172 CRC64;
     METQFLVSGR NSNIHCRIDS ISSSSLTPKS SPVSTSTPTL VVFPPFKLVS KSLRTRSKPR
     LTVCFVLEEK ELRGKLVVAS DDDDGAGEVR KQREKEISAS AEKLAQKLAR KKSERFTYLV
     AAVMSSFGIT SMAVLSVYYR FSWQMEGGEI PLSEMFGTFA LSVGAAVGME FWARWAHEAL
     WHASLWHMHE SHHKPREGPF ELNDIFAIIN AVPAIALLSY GFFHKGLIPG LCFGAGLGIT
     VFGMAYMFVH DGLVHKRFPV GPIADVPYFR RVAAAHTLHH SDKFNGVPYG LFLGPKELEE
     VGGLQVLEME INRRTKNNQS