BCH2_ARATH
ID BCH2_ARATH Reviewed; 303 AA.
AC Q9LTG0; B3H4E9;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Beta-carotene 3-hydroxylase 2, chloroplastic;
DE Short=AtB2;
DE EC=1.14.15.24 {ECO:0000250|UniProtKB:Q9SZZ8};
DE Flags: Precursor;
GN Name=BETA-OHASE 2; Synonyms=B2, CHY2; OrderedLocusNames=At5g52570;
GN ORFNames=F6N7.5;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11587509; DOI=10.1023/a:1011623907959;
RA Tian L., DellaPenna D.;
RT "Characterization of a second carotenoid beta-hydroxylase gene from
RT Arabidopsis and its relationship to the LUT1 locus.";
RL Plant Mol. Biol. 47:379-388(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12782726; DOI=10.1105/tpc.011403;
RA Tian L., Magallanes-Lundback M., Musetti V., DellaPenna D.;
RT "Functional analysis of beta- and epsilon-ring carotenoid hydroxylases in
RT Arabidopsis.";
RL Plant Cell 15:1320-1332(2003).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16890225; DOI=10.1016/j.febslet.2006.07.055;
RA Fiore A., Dall'osto L., Fraser P.D., Bassi R., Giuliano G.;
RT "Elucidation of the beta-carotene hydroxylation pathway in Arabidopsis
RT thaliana.";
RL FEBS Lett. 580:4718-4722(2006).
RN [7]
RP FUNCTION.
RX PubMed=19147649; DOI=10.1093/pcp/pcp005;
RA Kim J., Smith J.J., Tian L., Dellapenna D.;
RT "The evolution and function of carotenoid hydroxylases in Arabidopsis.";
RL Plant Cell Physiol. 50:463-479(2009).
CC -!- FUNCTION: Nonheme diiron monooxygenase involved in the biosynthesis of
CC xanthophylls. Specific for beta-ring hydroxylations of beta-carotene.
CC Has also a low activity toward the beta- and epsilon-rings of alpha-
CC carotene. No activity with acyclic carotenoids such as lycopene and
CC neurosporene. Uses ferredoxin as an electron donor.
CC {ECO:0000305|PubMed:11587509, ECO:0000305|PubMed:12782726,
CC ECO:0000305|PubMed:16890225, ECO:0000305|PubMed:19147649}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LTG0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LTG0-2; Sequence=VSP_041795;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flowers, stems, roots and
CC siliques. {ECO:0000269|PubMed:11587509}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in iron binding.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC light conditions; due to the redundancy with BCH1. Bch1 and bch2 double
CC mutant has no visible phenotype, but lower levels of beta, beta-
CC xanthophylls and increased beta-carotene and lutein. Cyp97c1, bch1 and
CC bch2 triple mutant is paler and smaller than wild-type.
CC {ECO:0000269|PubMed:12782726, ECO:0000269|PubMed:16890225}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR EMBL; AB025606; BAA98075.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96235.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96236.1; -; Genomic_DNA.
DR EMBL; AY074394; AAL67090.1; -; mRNA.
DR EMBL; AY117225; AAM51300.1; -; mRNA.
DR RefSeq; NP_001119420.1; NM_001125948.1. [Q9LTG0-2]
DR RefSeq; NP_200070.1; NM_124636.4. [Q9LTG0-1]
DR AlphaFoldDB; Q9LTG0; -.
DR BioGRID; 20579; 1.
DR STRING; 3702.AT5G52570.1; -.
DR PaxDb; Q9LTG0; -.
DR PRIDE; Q9LTG0; -.
DR ProteomicsDB; 240851; -. [Q9LTG0-1]
DR EnsemblPlants; AT5G52570.1; AT5G52570.1; AT5G52570. [Q9LTG0-1]
DR EnsemblPlants; AT5G52570.2; AT5G52570.2; AT5G52570. [Q9LTG0-2]
DR GeneID; 835334; -.
DR Gramene; AT5G52570.1; AT5G52570.1; AT5G52570. [Q9LTG0-1]
DR Gramene; AT5G52570.2; AT5G52570.2; AT5G52570. [Q9LTG0-2]
DR KEGG; ath:AT5G52570; -.
DR Araport; AT5G52570; -.
DR TAIR; locus:2149599; AT5G52570.
DR eggNOG; ENOG502QSIR; Eukaryota.
DR HOGENOM; CLU_054855_0_1_1; -.
DR InParanoid; Q9LTG0; -.
DR OMA; PMDDKPE; -.
DR OrthoDB; 1220596at2759; -.
DR PhylomeDB; Q9LTG0; -.
DR BioCyc; ARA:AT5G52570-MON; -.
DR BioCyc; MetaCyc:AT5G52570-MON; -.
DR BRENDA; 1.14.15.24; 399.
DR PRO; PR:Q9LTG0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LTG0; baseline and differential.
DR Genevisible; Q9LTG0; AT.
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:0016123; P:xanthophyll biosynthetic process; IGI:TAIR.
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 Alternative splicing; Carotenoid biosynthesis; Chloroplast; Hydrolase;
KW Iron; Membrane; Metal-binding; NAD; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..303
FT /note="Beta-carotene 3-hydroxylase 2, chloroplastic"
FT /id="PRO_0000412805"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 143..270
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MOTIF 155..160
FT /note="Histidine box-1"
FT MOTIF 165..171
FT /note="Histidine box-2"
FT MOTIF 228..233
FT /note="Histidine box-3"
FT MOTIF 254..258
FT /note="Histidine box-4"
FT VAR_SEQ 144..212
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041795"
SQ SEQUENCE 303 AA; 33777 MW; C7B8C9BF8BAE34CB CRC64;
MAAGLSTIAV TLKPLNRSSF SANHPISTAV FPPSLRFNGF RRRKILTVCF VVEERKQSSP
MDDDNKPEST TSSSEILMTS RLLKKAEKKK SERFTYLIAA VMSSFGITSM AIMAVYYRFS
WQMKGGEVSV LEMFGTFALS VGAAVGMEFW ARWAHRALWH DSLWNMHESH HKPREGAFEL
NDVFAITNAV PAIGLLYYGF LNKGLVPGLC FGAGLGITMF GMAYMFVHDG LVHKRFPVGP
IANVPYLRKV AAAHQLHHTD KFKGVPYGLF LGPKEVEEVG GKEELEKEIS RRIKLYNKGS
STS
