LUT1_ARATH
ID LUT1_ARATH Reviewed; 539 AA.
AC Q6TBX7; Q56ZY1; Q8RWV4; Q9SCP8;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Carotene epsilon-monooxygenase, chloroplastic;
DE EC=1.14.14.158;
DE AltName: Full=Cytochrome P450 97C1;
DE AltName: Full=Protein LUTEIN DEFICIENT 1;
DE Flags: Precursor;
GN Name=CYP97C1; Synonyms=LUT1; OrderedLocusNames=At3g53130; ORFNames=T4D2.60;
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], AND DISRUPTION PHENOTYPE.
RX PubMed=14709673; DOI=10.1073/pnas.2237237100;
RA Tian L., Musetti V., Kim J., Magallanes-Lundback M., DellaPenna D.;
RT "The Arabidopsis LUT1 locus encodes a member of the cytochrome p450 family
RT that is required for carotenoid epsilon-ring hydroxylation activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:402-407(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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].
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 [LARGE SCALE MRNA] OF 240-539.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=18466360; DOI=10.1111/j.1399-3054.2008.01124.x;
RA Perez-Bueno M.L., Horton P.;
RT "The role of lutein in the acclimation of higher plant chloroplast
RT membranes to suboptimal conditions.";
RL Physiol. Plantarum 134:227-236(2008).
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).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [11]
RP FUNCTION.
RX PubMed=19939422; DOI=10.1016/j.phytochem.2009.10.011;
RA Kim J.E., Cheng K.M., Craft N.E., Hamberger B., Douglas C.J.;
RT "Over-expression of Arabidopsis thaliana carotenoid hydroxylases
RT individually and in combination with a beta-carotene ketolase provides
RT insight into in vivo functions.";
RL Phytochemistry 71:168-178(2010).
RN [12]
RP FUNCTION.
RX PubMed=22513258; DOI=10.1186/1471-2229-12-50;
RA Fiore A., Dall'Osto L., Cazzaniga S., Diretto G., Giuliano G., Bassi R.;
RT "A quadruple mutant of Arabidopsis reveals a beta-carotene hydroxylation
RT activity for LUT1/CYP97C1 and a regulatory role of xanthophylls on
RT determination of the PSI/PSII ratio.";
RL BMC Plant Biol. 12:50-50(2012).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 70-539 IN COMPLEX WITH HEME, AND
RP COFACTOR.
RX PubMed=32513704; DOI=10.1073/pnas.2001806117;
RA Niu G., Guo Q., Wang J., Zhao S., He Y., Liu L.;
RT "Structural basis for plant lutein biosynthesis from alpha-carotene.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:14150-14157(2020).
CC -!- FUNCTION: Heme-containing cytochrome P450 involved in the biosynthesis
CC of xanthophylls. Specific for epsilon- and beta-ring hydroxylation of
CC alpha-carotene. Has only a low activity toward the beta-rings of beta-
CC carotene. The preferred substrate in planta is not alpha-carotene but
CC the epsilon-ring of zeinoxanthin (PubMed:12782726, PubMed:16890225,
CC PubMed:19147649, PubMed:19939422). Possesses a major beta-carotene
CC hydroxylase activity in planta when depleted in its preferred substrate
CC alpha-carotene (PubMed:22513258). {ECO:0000269|PubMed:12782726,
CC ECO:0000269|PubMed:16890225, ECO:0000269|PubMed:19147649,
CC ECO:0000269|PubMed:19939422, ECO:0000269|PubMed:22513258}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-carotene + O2 + reduced [NADPH--hemoprotein reductase] =
CC alpha-cryptoxanthin + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:30399, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:10223, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:28425, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.158;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + reduced [NADPH--hemoprotein reductase] + zeinoxanthin =
CC H(+) + H2O + lutein + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:57352, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:28838, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:65244; EC=1.14.14.158;
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:32513704};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but lacks lutein and
CC accumulates high levels of zeinoxanthin and beta-xanthophylls. Triple
CC mutant cyp97c1, bch1 and bch2 is paler and smaller than wild-type.
CC {ECO:0000269|PubMed:12782726, ECO:0000269|PubMed:14709673,
CC ECO:0000269|PubMed:16890225, ECO:0000269|PubMed:18466360}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM13903.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB64216.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY424805; AAR83120.1; -; mRNA.
DR EMBL; AL132958; CAB64216.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79040.1; -; Genomic_DNA.
DR EMBL; AY091083; AAM13903.1; ALT_INIT; mRNA.
DR EMBL; AK220829; BAD94136.1; -; mRNA.
DR PIR; T46159; T46159.
DR RefSeq; NP_190881.2; NM_115173.3.
DR PDB; 6L8H; X-ray; 2.00 A; A/B/C/D=70-539.
DR PDBsum; 6L8H; -.
DR AlphaFoldDB; Q6TBX7; -.
DR SMR; Q6TBX7; -.
DR BioGRID; 9796; 11.
DR IntAct; Q6TBX7; 11.
DR STRING; 3702.AT3G53130.1; -.
DR iPTMnet; Q6TBX7; -.
DR PaxDb; Q6TBX7; -.
DR PRIDE; Q6TBX7; -.
DR ProteomicsDB; 238579; -.
DR EnsemblPlants; AT3G53130.1; AT3G53130.1; AT3G53130.
DR GeneID; 824479; -.
DR Gramene; AT3G53130.1; AT3G53130.1; AT3G53130.
DR KEGG; ath:AT3G53130; -.
DR Araport; AT3G53130; -.
DR TAIR; locus:2102023; AT3G53130.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_5_5_1; -.
DR InParanoid; Q6TBX7; -.
DR OMA; WPHPETF; -.
DR OrthoDB; 1247045at2759; -.
DR BioCyc; ARA:AT3G53130-MON; -.
DR BioCyc; MetaCyc:AT3G53130-MON; -.
DR BRENDA; 1.14.14.158; 399.
DR PRO; PR:Q6TBX7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q6TBX7; baseline and differential.
DR Genevisible; Q6TBX7; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0009974; F:zeinoxanthin epsilon hydroxylase activity; IMP:TAIR.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IMP:TAIR.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carotenoid biosynthesis; Chloroplast; Heme; Iron;
KW Metal-binding; Monooxygenase; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..539
FT /note="Carotene epsilon-monooxygenase, chloroplastic"
FT /id="PRO_0000412810"
FT BINDING 487
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:32513704"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:6L8H"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:6L8H"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:6L8H"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 144..148
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:6L8H"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 189..206
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 212..229
FT /evidence="ECO:0007829|PDB:6L8H"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 241..258
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 267..272
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 274..304
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 321..328
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 334..364
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 367..381
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 388..393
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 395..407
FT /evidence="ECO:0007829|PDB:6L8H"
FT STRAND 410..420
FT /evidence="ECO:0007829|PDB:6L8H"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:6L8H"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:6L8H"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:6L8H"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 440..445
FT /evidence="ECO:0007829|PDB:6L8H"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:6L8H"
FT TURN 451..454
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:6L8H"
FT TURN 470..475
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:6L8H"
FT HELIX 490..507
FT /evidence="ECO:0007829|PDB:6L8H"
FT STRAND 508..512
FT /evidence="ECO:0007829|PDB:6L8H"
FT STRAND 520..530
FT /evidence="ECO:0007829|PDB:6L8H"
FT STRAND 533..538
FT /evidence="ECO:0007829|PDB:6L8H"
SQ SEQUENCE 539 AA; 60555 MW; 4C25C728B676AEEB CRC64;
MESSLFSPSS SSYSSLFTAK PTRLLSPKPK FTFSIRSSIE KPKPKLETNS SKSQSWVSPD
WLTTLTRTLS SGKNDESGIP IANAKLDDVA DLLGGALFLP LYKWMNEYGP IYRLAAGPRN
FVIVSDPAIA KHVLRNYPKY AKGLVAEVSE FLFGSGFAIA EGPLWTARRR AVVPSLHRRY
LSVIVERVFC KCAERLVEKL QPYAEDGSAV NMEAKFSQMT LDVIGLSLFN YNFDSLTTDS
PVIEAVYTAL KEAELRSTDL LPYWKIDALC KIVPRQVKAE KAVTLIRETV EDLIAKCKEI
VEREGERIND EEYVNDADPS ILRFLLASRE EVSSVQLRDD LLSMLVAGHE TTGSVLTWTL
YLLSKNSSAL RKAQEEVDRV LEGRNPAFED IKELKYITRC INESMRLYPH PPVLIRRAQV
PDILPGNYKV NTGQDIMISV YNIHRSSEVW EKAEEFLPER FDIDGAIPNE TNTDFKFIPF
SGGPRKCVGD QFALMEAIVA LAVFLQRLNV ELVPDQTISM TTGATIHTTN GLYMKVSQR
