BCH1_ARATH
ID BCH1_ARATH Reviewed; 310 AA.
AC Q9SZZ8; F4JTC5; Q96297;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Beta-carotene 3-hydroxylase 1, chloroplastic;
DE Short=AtB1;
DE EC=1.14.15.24 {ECO:0000269|PubMed:8798688};
DE Flags: Precursor;
GN Name=BETA-OHASE 1; Synonyms=B1, CHY1; OrderedLocusNames=At4g25700;
GN ORFNames=L73G19.80;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
RA Giuliano G., Rosati C., Santangelo G., Nebuloso E.;
RT "Gene structure and regulation of the carotenoid biosynthesis pathway in
RT Arabidopsis thaliana.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 17-310 (ISOFORM 1), FUNCTION, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=8798688; DOI=10.1074/jbc.271.40.24544;
RA Sun Z., Gantt E., Cunningham F.X. Jr.;
RT "Cloning and functional analysis of the beta-carotene hydroxylase of
RT Arabidopsis thaliana.";
RL J. Biol. Chem. 271:24349-24352(1996).
RN [6]
RP 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 [7]
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 [8]
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 [9]
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:0000269|PubMed:8798688, 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:0000269|PubMed:8798688};
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
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=Q9SZZ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SZZ8-2; Sequence=VSP_041793, VSP_041794;
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 -!- DOMAIN: The N-terminal part of the mature protein (70-129) is probably
CC involved in the formation of a functional homodimer.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC light conditions; due to redundancy with BCH2. 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 -!- MISCELLANEOUS: A protein lacking the first 69 amino acids has a normal
CC in vitro activity, while a protein lacking 129 N-terminal amino acids
CC produces predominantly the monohydroxy intermediate beta-cryptoxanthin.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR EMBL; AF125576; AAF85797.1; -; mRNA.
DR EMBL; AF125577; AAF85798.1; -; Genomic_DNA.
DR EMBL; AL050400; CAB43701.1; -; Genomic_DNA.
DR EMBL; AL161563; CAB81380.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85098.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85099.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67497.1; -; Genomic_DNA.
DR EMBL; AF370220; AAK44035.1; -; mRNA.
DR EMBL; AY113923; AAM44971.1; -; mRNA.
DR EMBL; U58919; AAC49443.1; -; mRNA.
DR PIR; T09562; T09562.
DR RefSeq; NP_001031715.1; NM_001036638.3. [Q9SZZ8-2]
DR RefSeq; NP_001320065.1; NM_001341759.1. [Q9SZZ8-2]
DR RefSeq; NP_194300.1; NM_118702.4. [Q9SZZ8-1]
DR AlphaFoldDB; Q9SZZ8; -.
DR STRING; 3702.AT4G25700.1; -.
DR PaxDb; Q9SZZ8; -.
DR PRIDE; Q9SZZ8; -.
DR ProteomicsDB; 240645; -. [Q9SZZ8-1]
DR EnsemblPlants; AT4G25700.1; AT4G25700.1; AT4G25700. [Q9SZZ8-1]
DR EnsemblPlants; AT4G25700.2; AT4G25700.2; AT4G25700. [Q9SZZ8-2]
DR EnsemblPlants; AT4G25700.3; AT4G25700.3; AT4G25700. [Q9SZZ8-2]
DR GeneID; 828675; -.
DR Gramene; AT4G25700.1; AT4G25700.1; AT4G25700. [Q9SZZ8-1]
DR Gramene; AT4G25700.2; AT4G25700.2; AT4G25700. [Q9SZZ8-2]
DR Gramene; AT4G25700.3; AT4G25700.3; AT4G25700. [Q9SZZ8-2]
DR KEGG; ath:AT4G25700; -.
DR Araport; AT4G25700; -.
DR TAIR; locus:2131381; AT4G25700.
DR eggNOG; ENOG502QSIR; Eukaryota.
DR HOGENOM; CLU_054855_0_1_1; -.
DR InParanoid; Q9SZZ8; -.
DR OMA; TIYFRHS; -.
DR OrthoDB; 1220596at2759; -.
DR PhylomeDB; Q9SZZ8; -.
DR BioCyc; ARA:AT4G25700-MON; -.
DR BioCyc; MetaCyc:AT4G25700-MON; -.
DR BRENDA; 1.14.15.24; 399.
DR PRO; PR:Q9SZZ8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZZ8; baseline and differential.
DR Genevisible; Q9SZZ8; 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 1: Evidence at protein 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..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 52..310
FT /note="Beta-carotene 3-hydroxylase 1, chloroplastic"
FT /id="PRO_0000412804"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 145..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"
FT VAR_SEQ 216..224
FT /note="GLGITVFGI -> VSPSFIWSY (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041793"
FT VAR_SEQ 225..310
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041794"
SQ SEQUENCE 310 AA; 34361 MW; C5F2AF54EDA82C0E CRC64;
MAAGLSTAVT FKPLHRSFSS SSTDFRLRLP KSLSGFSPSL RFKRFSVCYV VEERRQNSPI
ENDERPESTS STNAIDAEYL ALRLAEKLER KKSERSTYLI AAMLSSFGIT SMAVMAVYYR
FSWQMEGGEI SMLEMFGTFA LSVGAAVGME FWARWAHRAL WHASLWNMHE SHHKPREGPF
ELNDVFAIVN AGPAIGLLSY GFFNKGLVPG LCFGAGLGIT VFGIAYMFVH DGLVHKRFPV
GPIADVPYLR KVAAAHQLHH TDKFNGVPYG LFLGPKELEE VGGNEELDKE ISRRIKSYKK
ASGSGSSSSS
