BCH2_CAPAN
ID BCH2_CAPAN Reviewed; 308 AA.
AC O49814; A0A1U8H3T3; A0A2G2Z953;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Beta-carotene hydroxylase 2, chloroplastic {ECO:0000305};
DE EC=1.14.15.24 {ECO:0000269|PubMed:9555077};
DE Flags: Precursor;
GN Name=CA2 {ECO:0000303|PubMed:9555077};
GN ORFNames=LOC107873401, T459_16578 {ECO:0000312|EMBL:PHT78526.1};
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, AND MOTIF.
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 [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 [3]
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:0000250|UniProtKB:O49815}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
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 -!- SEQUENCE CAUTION:
CC Sequence=CAA70888.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; Y09722; CAA70888.1; ALT_SEQ; mRNA.
DR EMBL; AYRZ02000006; PHT78526.1; -; Genomic_DNA.
DR RefSeq; XP_016575733.1; XM_016720247.1.
DR AlphaFoldDB; O49814; -.
DR STRING; 4072.A0A1U8H3T3; -.
DR SwissLipids; SLP:000001509; -.
DR EnsemblPlants; PHT78526; PHT78526; T459_16578.
DR GeneID; 107873401; -.
DR Gramene; PHT78526; PHT78526; T459_16578.
DR KEGG; ag:CAA70888; -.
DR KEGG; cann:107873401; -.
DR OMA; TIYFRHS; -.
DR OrthoDB; 1220596at2759; -.
DR BRENDA; 1.14.15.24; 1169.
DR Proteomes; UP000189700; Chromosome 6.
DR Proteomes; UP000222542; Chromosome 6.
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..59
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 60..308
FT /note="Beta-carotene hydroxylase 2, chloroplastic"
FT /id="PRO_0000412807"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 152..279
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MOTIF 164..169
FT /note="Histidine box-1"
FT /evidence="ECO:0000305|PubMed:9555077"
FT MOTIF 176..180
FT /note="Histidine box-2"
FT /evidence="ECO:0000305|PubMed:9555077"
FT MOTIF 237..242
FT /note="Histidine box-3"
FT /evidence="ECO:0000305|PubMed:9555077"
FT MOTIF 263..267
FT /note="Histidine box-4"
FT /evidence="ECO:0000305|PubMed:9555077"
SQ SEQUENCE 308 AA; 34656 MW; 4BB6DE5438E07562 CRC64;
MAAARISFSS TSRTSYYRHS PFLGPKPTPT TPSVYPITPF SPNLGSILRC RRRPSFTVCF
VLEDDKFKTQ FEAGEEDIEM KIEEQISATR LAEKLARKKS ERFTYLVAAV MSSFGITSMA
VMAVYYRFYW QMEGGEVPFS EMFGTFALSV GAAVGMEFWA RWAHKALWHA SLWHMHESHH
KPREGPFELN DVFAIINAVP AIALLDYGFF HKGLIPGLCF GAGLGITVFG MAYMFVHDGL
VHKRFPVGPV ANVPYLRKVA AAHSLHHSEK FNGVPYGLFL GPKELEEVGG LEELEKEVNR
RTRYIKGS
