ID   BCH_HAELA               Reviewed;         322 AA.
AC   Q9SPK6;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Beta-carotene 3-hydroxylase, chloroplastic;
DE            EC=1.14.15.24 {ECO:0000250|UniProtKB:Q9SZZ8};
DE   Flags: Precursor; Fragment;
GN   Name=CRTZ;
OS   Haematococcus lacustris (Green alga) (Haematococcus pluvialis).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Haematococcaceae; Haematococcus.
OX   NCBI_TaxID=44745;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=10524195; DOI=10.1016/s0167-4781(99)00088-3;
RA   Linden H.;
RT   "Carotenoid hydroxylase from Haematococcus pluvialis: cDNA sequence,
RT   regulation and functional complementation.";
RL   Biochim. Biophys. Acta 1446:203-212(1999).
RN   [2]
RP   INDUCTION BY LIGHT.
RX   PubMed=12856941; DOI=10.1023/a:1023948929665;
RA   Steinbrenner J., Linden H.;
RT   "Light induction of carotenoid biosynthesis genes in the green alga
RT   Haematococcus pluvialis: regulation by photosynthetic redox control.";
RL   Plant Mol. Biol. 52:343-356(2003).
CC   -!- FUNCTION: Nonheme diiron monooxygenase involved in the biosynthesis of
CC       astaxanthin. Hydroxylates beta-ring of beta-carotene and catalyzes the
CC       conversion of canthaxanthin to astaxanthin. Uses ferredoxin as an
CC       electron donor. {ECO:0000250|UniProtKB:Q9SZZ8,
CC       ECO:0000305|PubMed:10524195}.
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: Not detected in vegetative cells. Up-regulated
CC       during cyst cell formation. {ECO:0000269|PubMed:10524195}.
CC   -!- INDUCTION: Up-regulated by moderate light in correlation with the redox
CC       state of the photosynthetic electron transport.
CC       {ECO:0000269|PubMed:12856941}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF162276; AAD54243.1; -; mRNA.
DR   AlphaFoldDB; Q9SPK6; -.
DR   KEGG; ag:AAD54243; -.
DR   BioCyc; MetaCyc:MON-19182; -.
DR   BRENDA; 1.14.15.24; 2522.
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..68
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           69..322
FT                   /note="Beta-carotene 3-hydroxylase, chloroplastic"
FT                   /id="PRO_0000412808"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          164..286
FT                   /note="Fatty acid hydroxylase"
FT                   /evidence="ECO:0000255"
FT   MOTIF           177..182
FT                   /note="Histidine box-1"
FT   MOTIF           191..195
FT                   /note="Histidine box-2"
FT   MOTIF           252..257
FT                   /note="Histidine box-3"
FT   MOTIF           278..282
FT                   /note="Histidine box-4"
FT   NON_TER         1
SQ   SEQUENCE   322 AA;  34987 MW;  45100BA5ECBA13EC CRC64;
     TFHKPVSGAS ALPHIGPPPH LHRSFAATTM LSKLQSISVK ARRVELARDI TRPKVCLHAQ
     RCSLVRLRVA APQTEEALGT VQAAGAGDEH SADVALQQLD RAIAERRARR KREQLSYQAA
     AIAASIGVSG IAIFATYLRF AMHMTVGGAV PWGEVAGTLL LVVGGALGME MYARYAHKAI
     WHESPLGWLL HKSHHTPRTG PFEANDLFAI INGLPAMLLC TFGFWLPNVL GAACFGAGLG
     ITLYGMAYMF VHDGLVHRRF PTGPIAGLPY MKRLTVAHQL HHSGKYGGAP WGMFLGPQEL
     QHIPGAAEEV ERLVLELDWS KR