BCH1_CAPAN
ID BCH1_CAPAN Reviewed; 315 AA.
AC O49815; A0A1U8FZA1; D7P8N7;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Beta-carotene hydroxylase 1, chloroplastic {ECO:0000305};
DE EC=1.14.15.24 {ECO:0000269|PubMed:9555077};
DE Flags: Precursor;
GN Name=CA1 {ECO:0000303|PubMed:9555077};
GN Synonyms=CrtZ-2 {ECO:0000312|EMBL:ADH04291.1};
GN ORFNames=LOC107863219, T459_09470 {ECO:0000312|EMBL:PHT87364.1};
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL
RP STAGE, ACTIVITY REGULATION, MOTIF, AND MUTAGENESIS OF HIS-171; HIS-176;
RP HIS-183; HIS-186; HIS-187; HIS-244; HIS-249; HIS-270; HIS-273 AND HIS-274.
RX PubMed=9555077; DOI=10.1016/s0005-2760(98)00029-0;
RA Bouvier F., Keller Y., d'Harlingue A., Camara B.;
RT "Xanthophyll biosynthesis: molecular and functional characterization of
RT carotenoid hydroxylases from pepper fruits (Capsicum annuum L.).";
RL Biochim. Biophys. Acta 1391:320-328(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Pericarp;
RX PubMed=20582146; DOI=10.1016/j.plantsci.2010.04.014;
RA Guzman I., Hamby S., Romero J., Bosland P.W., O'Connell M.A.;
RT "Variability of carotenoid biosynthesis in orange colored Capsicum spp.";
RL Plant Sci. 179:49-59(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=23124390; DOI=10.1007/s00122-012-2001-9;
RA Borovsky Y., Tadmor Y., Bar E., Meir A., Lewinsohn E., Paran I.;
RT "Induced mutation in beta-CAROTENE HYDROXYLASE results in accumulation of
RT beta-carotene and conversion of red to orange color in pepper fruit.";
RL Theor. Appl. Genet. 126:557-565(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24441736; DOI=10.1038/ng.2877;
RA Kim S., Park M., Yeom S.I., Kim Y.M., Lee J.M., Lee H.A., Seo E., Choi J.,
RA Cheong K., Kim K.T., Jung K., Lee G.W., Oh S.K., Bae C., Kim S.B.,
RA Lee H.Y., Kim S.Y., Kim M.S., Kang B.C., Jo Y.D., Yang H.B., Jeong H.J.,
RA Kang W.H., Kwon J.K., Shin C., Lim J.Y., Park J.H., Huh J.H., Kim J.S.,
RA Kim B.D., Cohen O., Paran I., Suh M.C., Lee S.B., Kim Y.K., Shin Y.,
RA Noh S.J., Park J., Seo Y.S., Kwon S.Y., Kim H.A., Park J.M., Kim H.J.,
RA Choi S.B., Bosland P.W., Reeves G., Jo S.H., Lee B.W., Cho H.T., Choi H.S.,
RA Lee M.S., Yu Y., Do Choi Y., Park B.S., van Deynze A., Ashrafi H., Hill T.,
RA Kim W.T., Pai H.S., Ahn H.K., Yeam I., Giovannoni J.J., Rose J.K.,
RA Soerensen I., Lee S.J., Kim R.W., Choi I.Y., Choi B.S., Lim J.S., Lee Y.H.,
RA Choi D.;
RT "Genome sequence of the hot pepper provides insights into the evolution of
RT pungency in Capsicum species.";
RL Nat. Genet. 46:270-278(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Zunla-1;
RX PubMed=24591624; DOI=10.1073/pnas.1400975111;
RA Qin C., Yu C., Shen Y., Fang X., Chen L., Min J., Cheng J., Zhao S., Xu M.,
RA Luo Y., Yang Y., Wu Z., Mao L., Wu H., Ling-Hu C., Zhou H., Lin H.,
RA Gonzalez-Morales S., Trejo-Saavedra D.L., Tian H., Tang X., Zhao M.,
RA Huang Z., Zhou A., Yao X., Cui J., Li W., Chen Z., Feng Y., Niu Y., Bi S.,
RA Yang X., Li W., Cai H., Luo X., Montes-Hernandez S., Leyva-Gonzalez M.A.,
RA Xiong Z., He X., Bai L., Tan S., Tang X., Liu D., Liu J., Zhang S.,
RA Chen M., Zhang L., Zhang L., Zhang Y., Liao W., Zhang Y., Wang M., Lv X.,
RA Wen B., Liu H., Luan H., Zhang Y., Yang S., Wang X., Xu J., Li X., Li S.,
RA Wang J., Palloix A., Bosland P.W., Li Y., Krogh A., Rivera-Bustamante R.F.,
RA Herrera-Estrella L., Yin Y., Yu J., Hu K., Zhang Z.;
RT "Whole-genome sequencing of cultivated and wild peppers provides insights
RT into Capsicum domestication and specialization.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:5135-5140(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CM334;
RX PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA Bennetzen J.L., Choi D.;
RT "New reference genome sequences of hot pepper reveal the massive evolution
RT of plant disease-resistance genes by retroduplication.";
RL Genome Biol. 18:R210.1-R210.11(2017).
CC -!- FUNCTION: Nonheme diiron monooxygenase involved in the biosynthesis of
CC xanthophylls. Specific for beta-ring hydroxylations of beta-carotene.
CC Produces beta-cryptoxanthin and zeaxanthin. Uses ferredoxin as an
CC electron donor. {ECO:0000269|PubMed:9555077}.
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:0000269|PubMed:9555077};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30332;
CC Evidence={ECO:0000269|PubMed:9555077};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-beta-carotene + 2 H(+) + O2 + 2 reduced [2Fe-2S]-
CC [ferredoxin] = beta-cryptoxanthin + H2O + 2 oxidized [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:30323, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, ChEBI:CHEBI:10362, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17579, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738; Evidence={ECO:0000269|PubMed:9555077};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30324;
CC Evidence={ECO:0000269|PubMed:9555077};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-cryptoxanthin + 2 H(+) + O2 + 2 reduced [2Fe-2S]-
CC [ferredoxin] = all-trans-zeaxanthin + H2O + 2 oxidized [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:30327, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, ChEBI:CHEBI:10362, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:27547, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738; Evidence={ECO:0000269|PubMed:9555077};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30328;
CC Evidence={ECO:0000269|PubMed:9555077};
CC -!- ACTIVITY REGULATION: Inhibited by o-phenanthroline and 8-
CC hydroxyquinoline. {ECO:0000269|PubMed:9555077}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during chloroplast to chromoplast
CC transition stage. {ECO:0000269|PubMed:9555077}.
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; Y09225; CAA70427.1; -; mRNA.
DR EMBL; GU122940; ADH04291.1; -; Genomic_DNA.
DR EMBL; GU122946; ADH04297.1; -; Genomic_DNA.
DR EMBL; GU122945; ADH04296.1; -; Genomic_DNA.
DR EMBL; GU122944; ADH04295.1; -; Genomic_DNA.
DR EMBL; GU122943; ADH04294.1; -; Genomic_DNA.
DR EMBL; GU122942; ADH04293.1; -; Genomic_DNA.
DR EMBL; GU122941; ADH04292.1; -; Genomic_DNA.
DR EMBL; JQ031264; AFA50498.1; -; mRNA.
DR EMBL; AYRZ02000003; PHT87364.1; -; Genomic_DNA.
DR RefSeq; NP_001311784.1; NM_001324855.1.
DR AlphaFoldDB; O49815; -.
DR STRING; 4072.D7P8N7; -.
DR SwissLipids; SLP:000001508; -.
DR EnsemblPlants; PHT87364; PHT87364; T459_09470.
DR GeneID; 107863219; -.
DR Gramene; PHT87364; PHT87364; T459_09470.
DR KEGG; ag:CAA70427; -.
DR KEGG; cann:107863219; -.
DR OMA; GMEFWAI; -.
DR OrthoDB; 1220596at2759; -.
DR BRENDA; 1.14.15.24; 1169.
DR Proteomes; UP000189700; Genome assembly.
DR Proteomes; UP000222542; Chromosome 3.
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:0052611; F:beta-carotene 3-hydroxylase activity; IEA:RHEA.
DR GO; GO:0052610; F:beta-cryptoxanthin hydroxylase activity; IEA:RHEA.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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 1: Evidence at protein level;
KW Carotenoid biosynthesis; Chloroplast; Hydrolase; Iron; Membrane;
KW Metal-binding; NAD; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..58
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 59..315
FT /note="Beta-carotene hydroxylase 1, chloroplastic"
FT /id="PRO_0000412806"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 159..286
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MOTIF 171..176
FT /note="Histidine box-1"
FT /evidence="ECO:0000305|PubMed:9555077"
FT MOTIF 183..187
FT /note="Histidine box-2"
FT /evidence="ECO:0000305|PubMed:9555077"
FT MOTIF 244..249
FT /note="Histidine box-3"
FT /evidence="ECO:0000305|PubMed:9555077"
FT MOTIF 270..274
FT /note="Histidine box-4"
FT /evidence="ECO:0000305|PubMed:9555077"
FT MUTAGEN 171
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9555077"
FT MUTAGEN 176
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9555077"
FT MUTAGEN 183
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9555077"
FT MUTAGEN 186
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9555077"
FT MUTAGEN 187
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9555077"
FT MUTAGEN 244
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9555077"
FT MUTAGEN 249
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9555077"
FT MUTAGEN 270
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9555077"
FT MUTAGEN 273
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9555077"
FT MUTAGEN 274
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9555077"
FT CONFLICT 211..212
FT /note="LL -> FF (in Ref. 1; CAA70427)"
FT CONFLICT 225
FT /note="L -> I (in Ref. 1; CAA70427)"
FT CONFLICT 259
FT /note="N -> K (in Ref. 1; CAA70427)"
FT CONFLICT 298
FT /note="L -> I (in Ref. 1; CAA70427)"
FT CONFLICT 312
FT /note="S -> L (in Ref. 1; CAA70427)"
SQ SEQUENCE 315 AA; 35318 MW; 8B5E8361FA6D143D CRC64;
MAAEISISAS SRAICLQRNP FPAPKYFATA PPLLFFSPLT CNLDAILRSR RKPRLAACFV
LKDDKLYTAQ SGKQSDTEAI GDEIEVETNE EKSLAVRLAE KFARKKSERF TYLVAAVMSS
LGITSMAVIS VYYRFSWQME GGEMPFSEMF CTFALAFGAA IGMEYWARWA HRALWHASLW
HMHESHHRPR EGPFELNDIF AIINAVPAIA LLSFGFNHKG LIPGLCFGAG LGITVFGMAY
MFVHDGLVHK RFPVGPIANV PYFQRVAAAH QLHHSDKFDG VPYGLFLGPK ELEEVGVLEE
LEKEVNRRIK SSKRL
