ID   BCH_ONCHC               Reviewed;         305 AA.
AC   C3VEQ1;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Beta-carotene 3-hydroxylase, chloroplastic;
DE            Short=OgHYB;
DE            EC=1.14.15.24 {ECO:0000250|UniProtKB:Q9SZZ8};
DE   AltName: Full=Beta-carotene hydroxylase;
DE   Flags: Precursor;
GN   Name=BHY; Synonyms=HYB;
OS   Oncidium hybrid cultivar (Orchid).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Epidendroideae; Cymbidieae; Oncidiinae; Oncidium.
OX   NCBI_TaxID=141207;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=20635095; DOI=10.1007/s00425-010-1222-x;
RA   Chiou C.Y., Pan H.A., Chuang Y.N., Yeh K.W.;
RT   "Differential expression of carotenoid-related genes determines diversified
RT   carotenoid coloration in floral tissues of Oncidium cultivars.";
RL   Planta 232:937-948(2010).
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   -!- 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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in flower buds and lips. Detected in
CC       roots and leaves. {ECO:0000269|PubMed:20635095}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during floral development.
CC       {ECO:0000269|PubMed:20635095}.
CC   -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC       involved in iron binding. {ECO:0000250}.
CC   -!- MISCELLANEOUS: High expression of beta-hydroxylase (BHY) and zeaxanthin
CC       epoxidase (ZEP) results in the accumulation of violaxanthin, 9-cis-
CC       violaxanthin and neoxanthin in the yellow cultivar Gower Ramsey, while
CC       the down-regulation of BHY and ZEP results in the accumulation of beta-
CC       carotene and orange coloration in floral tissues of the cultivar
CC       Sunkist.
CC   -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR   EMBL; FJ859991; ACP27626.1; -; mRNA.
DR   AlphaFoldDB; C3VEQ1; -.
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..41
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..305
FT                   /note="Beta-carotene 3-hydroxylase, chloroplastic"
FT                   /id="PRO_0000426712"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          146..272
FT                   /note="Fatty acid hydroxylase"
FT                   /evidence="ECO:0000255"
FT   MOTIF           157..162
FT                   /note="Histidine box-1"
FT   MOTIF           169..173
FT                   /note="Histidine box-2"
FT   MOTIF           230..235
FT                   /note="Histidine box-3"
FT   MOTIF           256..260
FT                   /note="Histidine box-4"
SQ   SEQUENCE   305 AA;  34224 MW;  EFDBD00ED9B35CFA CRC64;
     MAFAMSSSLT LFQYQSFGKK PFFSRRRDFA GCSMMNPLVA RCNRATEICC VVRKDGEAES
     LVEAENDQLE EEVMKPTSID SFSVVLRSER KKAERRTYLV AAMASSLGFT FMAAAAVYYR
     FAWQMEGGAV PLTEMMGTFS LAVGSAVGME YWARWAHRAL WHTSLWHMHE SHHRPRDGPF
     ELNDVFALIN AFPAVALLAF GFFHRGFFSG LCFGAGLGIT LYGMAYMFVH DGLVHRRFPV
     GPIATVPYFQ WVAAAHQIHH ADKFNGVPYG LFLGHKELEE VGGMEALERE IKRGVKVFSS
     SPNQS