LUT5_ARATH
ID LUT5_ARATH Reviewed; 595 AA.
AC Q93VK5; Q9C6S0;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein LUTEIN DEFICIENT 5, chloroplastic;
DE EC=1.14.-.-;
DE AltName: Full=Cytochrome P450 97A3;
DE Flags: Precursor;
GN Name=CYP97A3; Synonyms=LUT5; OrderedLocusNames=At1g31800; ORFNames=F5M6.19;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-283.
RX PubMed=16492736; DOI=10.1073/pnas.0511207103;
RA Kim J., DellaPenna D.;
RT "Defining the primary route for lutein synthesis in plants: the role of
RT Arabidopsis carotenoid beta-ring hydroxylase CYP97A3.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3474-3479(2006).
RN [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 78-595 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 beta-ring hydroxylation of alpha- and
CC beta-carotene. Has also a low activity toward the epsilon-rings of
CC alpha-carotene. The beta-ring of alpha-carotene is the preferred
CC substrate in planta. {ECO:0000269|PubMed:16492736,
CC ECO:0000269|PubMed:16890225, ECO:0000269|PubMed:19147649}.
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: Accumulation of alpha-carotene and alpha-
CC cryptoxanthin. Triple mutant cyp97a3, bch1 and bch2 has a highly
CC retarded growth. {ECO:0000269|PubMed:16492736,
CC ECO:0000269|PubMed:16890225}.
CC -!- MISCELLANEOUS: Alpha-carotene is incorporated into photosystems in lut5
CC mutants.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50718.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC079041; AAG50718.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE31394.1; -; Genomic_DNA.
DR EMBL; AY056446; AAL08302.1; -; mRNA.
DR EMBL; AY058173; AAL25587.1; -; mRNA.
DR EMBL; AY142017; AAM98281.1; -; mRNA.
DR PIR; F86441; F86441.
DR RefSeq; NP_564384.1; NM_102914.3.
DR PDB; 6J94; X-ray; 2.40 A; A/B=78-595.
DR PDB; 6J95; X-ray; 2.00 A; A=78-595.
DR PDB; 6L8I; X-ray; 1.70 A; A=78-595.
DR PDB; 6L8J; X-ray; 2.40 A; A=78-595.
DR PDBsum; 6J94; -.
DR PDBsum; 6J95; -.
DR PDBsum; 6L8I; -.
DR PDBsum; 6L8J; -.
DR AlphaFoldDB; Q93VK5; -.
DR SMR; Q93VK5; -.
DR STRING; 3702.AT1G31800.1; -.
DR iPTMnet; Q93VK5; -.
DR PaxDb; Q93VK5; -.
DR PRIDE; Q93VK5; -.
DR ProteomicsDB; 238683; -.
DR EnsemblPlants; AT1G31800.1; AT1G31800.1; AT1G31800.
DR GeneID; 840067; -.
DR Gramene; AT1G31800.1; AT1G31800.1; AT1G31800.
DR KEGG; ath:AT1G31800; -.
DR Araport; AT1G31800; -.
DR TAIR; locus:2034476; AT1G31800.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_5_5_1; -.
DR InParanoid; Q93VK5; -.
DR OMA; TENFAYL; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; Q93VK5; -.
DR BRENDA; 1.14.14.158; 399.
DR PRO; PR:Q93VK5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93VK5; baseline and differential.
DR Genevisible; Q93VK5; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0010291; F:carotene beta-ring hydroxylase activity; IMP:TAIR.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IMP:TAIR.
DR GO; GO:0016123; P:xanthophyll biosynthetic process; IGI: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..28
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 29..595
FT /note="Protein LUTEIN DEFICIENT 5, chloroplastic"
FT /id="PRO_0000412811"
FT BINDING 516
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 MUTAGEN 283
FT /note="E->K: In lut5-2; decreased activity."
FT /evidence="ECO:0000269|PubMed:16492736"
FT HELIX 129..139
FT /evidence="ECO:0007829|PDB:6L8I"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:6L8I"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:6L8I"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:6L8I"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:6L8I"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:6L8I"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:6L8I"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:6L8I"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:6L8I"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:6L8I"
FT HELIX 210..237
FT /evidence="ECO:0007829|PDB:6L8I"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:6L8J"
FT HELIX 243..260
FT /evidence="ECO:0007829|PDB:6L8I"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:6L8I"
FT HELIX 272..286
FT /evidence="ECO:0007829|PDB:6L8I"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:6J94"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:6J94"
FT HELIX 306..334
FT /evidence="ECO:0007829|PDB:6L8I"
FT HELIX 351..357
FT /evidence="ECO:0007829|PDB:6L8I"
FT HELIX 364..395
FT /evidence="ECO:0007829|PDB:6L8I"
FT HELIX 397..410
FT /evidence="ECO:0007829|PDB:6L8I"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:6L8I"
FT HELIX 418..423
FT /evidence="ECO:0007829|PDB:6L8I"
FT HELIX 425..437
FT /evidence="ECO:0007829|PDB:6L8I"
FT STRAND 440..450
FT /evidence="ECO:0007829|PDB:6L8I"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:6L8I"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:6L8I"
FT STRAND 464..468
FT /evidence="ECO:0007829|PDB:6L8I"
FT HELIX 469..474
FT /evidence="ECO:0007829|PDB:6L8I"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:6L8I"
FT TURN 480..483
FT /evidence="ECO:0007829|PDB:6L8I"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:6L8I"
FT TURN 499..504
FT /evidence="ECO:0007829|PDB:6L8I"
FT HELIX 512..514
FT /evidence="ECO:0007829|PDB:6L8I"
FT HELIX 519..536
FT /evidence="ECO:0007829|PDB:6L8I"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:6L8I"
FT STRAND 553..555
FT /evidence="ECO:0007829|PDB:6L8I"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:6L8I"
FT STRAND 563..570
FT /evidence="ECO:0007829|PDB:6L8I"
SQ SEQUENCE 595 AA; 66846 MW; A548A33A48323B7D CRC64;
MAMAFPLSYT PTITVKPVTY SRRSNFVVFS SSSNGRDPLE ENSVPNGVKS LEKLQEEKRR
AELSARIASG AFTVRKSSFP STVKNGLSKI GIPSNVLDFM FDWTGSDQDY PKVPEAKGSI
QAVRNEAFFI PLYELFLTYG GIFRLTFGPK SFLIVSDPSI AKHILKDNAK AYSKGILAEI
LDFVMGKGLI PADGEIWRRR RRAIVPALHQ KYVAAMISLF GEASDRLCQK LDAAALKGEE
VEMESLFSRL TLDIIGKAVF NYDFDSLTND TGVIEAVYTV LREAEDRSVS PIPVWDIPIW
KDISPRQRKV ATSLKLINDT LDDLIATCKR MVEEEELQFH EEYMNERDPS ILHFLLASGD
DVSSKQLRDD LMTMLIAGHE TSAAVLTWTF YLLTTEPSVV AKLQEEVDSV IGDRFPTIQD
MKKLKYTTRV MNESLRLYPQ PPVLIRRSID NDILGEYPIK RGEDIFISVW NLHRSPLHWD
DAEKFNPERW PLDGPNPNET NQNFSYLPFG GGPRKCIGDM FASFENVVAI AMLIRRFNFQ
IAPGAPPVKM TTGATIHTTE GLKLTVTKRT KPLDIPSVPI LPMDTSRDEV SSALS
