CHLI1_ARATH
ID CHLI1_ARATH Reviewed; 424 AA.
AC P16127; Q0WUK7;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Magnesium-chelatase subunit ChlI-1, chloroplastic;
DE Short=Mg-chelatase subunit I-1;
DE EC=6.6.1.1;
DE AltName: Full=Mg-protoporphyrin IX chelatase subunit ChlI-1;
DE AltName: Full=Protein CHLORINA 42;
DE Flags: Precursor;
GN Name=CHLI1; Synonyms=CH42, CS; OrderedLocusNames=At4g18480;
GN ORFNames=F28J12.140;
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], AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=2158442; DOI=10.1002/j.1460-2075.1990.tb08248.x;
RA Koncz C., Mayerhofer R., Koncz-Kalman Z., Nawrath C., Reiss B., Redei G.P.,
RA Schell J.;
RT "Isolation of a gene encoding a novel chloroplast protein by T-DNA tagging
RT in Arabidopsis thaliana.";
RL EMBO J. 9:1337-1346(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Dijon; TISSUE=Callus;
RA Putnoky P., Koncz C.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11842180; DOI=10.1104/pp.010625;
RA Rissler H.M., Collakova E., DellaPenna D., Whelan J., Pogson B.J.;
RT "Chlorophyll biosynthesis. Expression of a second chl I gene of magnesium
RT chelatase in Arabidopsis supports only limited chlorophyll synthesis.";
RL Plant Physiol. 128:770-779(2002).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-240.
RC STRAIN=cv. Dijon;
RX PubMed=15815918; DOI=10.1007/s00438-005-1129-6;
RA Soldatova O., Apchelimov A., Radukina N., Ezhova T., Shestakov S.,
RA Ziemann V., Hedtke B., Grimm B.;
RT "An Arabidopsis mutant that is resistant to the protoporphyrinogen oxidase
RT inhibitor acifluorfen shows regulatory changes in tetrapyrrole
RT biosynthesis.";
RL Mol. Genet. Genomics 273:311-318(2005).
RN [9]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, DISULFIDE
RP BOND, AND MUTAGENESIS OF CYS-102; CYS-193; CYS-354 AND CYS-396.
RX PubMed=17472958; DOI=10.1074/jbc.m703324200;
RA Ikegami A., Yoshimura N., Motohashi K., Takahashi S., Romano P.G.,
RA Hisabori T., Takamiya K., Masuda T.;
RT "The CHLI1 subunit of Arabidopsis thaliana magnesium chelatase is a target
RT protein of the chloroplast thioredoxin.";
RL J. Biol. Chem. 282:19282-19291(2007).
RN [10]
RP FUNCTION.
RX PubMed=18846282; DOI=10.1039/b802604c;
RA Kobayashi K., Mochizuki N., Yoshimura N., Motohashi K., Hisabori T.,
RA Masuda T.;
RT "Functional analysis of Arabidopsis thaliana isoforms of the Mg-chelatase
RT CHLI subunit.";
RL Photochem. Photobiol. Sci. 7:1188-1195(2008).
RN [11]
RP INDUCTION BY LIGHT.
RX PubMed=18846290; DOI=10.1039/b802596g;
RA Stephenson P.G., Terry M.J.;
RT "Light signalling pathways regulating the Mg-chelatase branchpoint of
RT chlorophyll synthesis during de-etiolation in Arabidopsis thaliana.";
RL Photochem. Photobiol. Sci. 7:1243-1252(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, AND IDENTIFICATION BY
RP 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-61, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER SER-60, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP INTERACTION WITH CHLH AND CHLD, AND FUNCTION.
RX PubMed=23011401; DOI=10.1007/s11103-012-9965-3;
RA Du S.Y., Zhang X.F., Lu Z., Xin Q., Wu Z., Jiang T., Lu Y., Wang X.F.,
RA Zhang D.P.;
RT "Roles of the different components of magnesium chelatase in abscisic acid
RT signal transduction.";
RL Plant Mol. Biol. 80:519-537(2012).
CC -!- FUNCTION: Involved in chlorophyll biosynthesis. Catalyzes the insertion
CC of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
CC The magnesium-chelatase is a complex of three subunits, CHLI, CHLD and
CC CHLH. The reaction takes place in two steps, with an ATP-dependent
CC activation followed by an ATP-dependent chelation step. Possesses high
CC affinity for ATP and may play a major role in chlorophyll biosynthesis.
CC Does not bind abscisic acid (ABA), but is a positive regulator of ABA
CC signaling. {ECO:0000269|PubMed:11842180, ECO:0000269|PubMed:15815918,
CC ECO:0000269|PubMed:17472958, ECO:0000269|PubMed:18846282,
CC ECO:0000269|PubMed:23011401}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Mg(2+) + protoporphyrin IX = ADP + 3 H(+) + Mg-
CC protoporphyrin IX + phosphate; Xref=Rhea:RHEA:13961,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18420,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57306,
CC ChEBI:CHEBI:60492, ChEBI:CHEBI:456216; EC=6.6.1.1;
CC -!- ACTIVITY REGULATION: Redox regulation; active in reducing conditions,
CC inactive in oxidizing conditions. Thioredoxins f and m mediate the
CC reversible reductive activation of oxidized CHLI1.
CC {ECO:0000269|PubMed:17472958}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=460 uM for ATP {ECO:0000269|PubMed:17472958};
CC Vmax=55 nmol/min/mg enzyme toward ATP {ECO:0000269|PubMed:17472958};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis.
CC -!- SUBUNIT: The magnesium chelatase complex is a heterotrimer consisting
CC of subunits CHLI, CHLD, AND CHLH. Interacts with CHLH and CHLD.
CC {ECO:0000269|PubMed:23011401}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- INDUCTION: Not regulated by light. {ECO:0000269|PubMed:18846290}.
CC -!- DISRUPTION PHENOTYPE: Homozygous mutants are chlorotic lethal when
CC grown on soil, but can grow on sucrose-containing medium.
CC {ECO:0000269|PubMed:11842180, ECO:0000269|PubMed:15815918,
CC ECO:0000269|PubMed:2158442}.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X51799; CAB38561.1; -; Genomic_DNA.
DR EMBL; X91411; CAA62754.1; -; Genomic_DNA.
DR EMBL; AL021710; CAA16728.1; -; Genomic_DNA.
DR EMBL; AL161548; CAB78850.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84051.1; -; Genomic_DNA.
DR EMBL; AY093192; AAM13191.1; -; mRNA.
DR EMBL; BT010129; AAQ22598.1; -; mRNA.
DR EMBL; AK227146; BAE99191.1; -; mRNA.
DR PIR; S12785; S12785.
DR RefSeq; NP_193583.1; NM_117962.3.
DR AlphaFoldDB; P16127; -.
DR SMR; P16127; -.
DR BioGRID; 12873; 1.
DR IntAct; P16127; 1.
DR STRING; 3702.AT4G18480.1; -.
DR iPTMnet; P16127; -.
DR MetOSite; P16127; -.
DR SWISS-2DPAGE; P16127; -.
DR PaxDb; P16127; -.
DR PRIDE; P16127; -.
DR ProteomicsDB; 245179; -.
DR EnsemblPlants; AT4G18480.1; AT4G18480.1; AT4G18480.
DR GeneID; 827580; -.
DR Gramene; AT4G18480.1; AT4G18480.1; AT4G18480.
DR KEGG; ath:AT4G18480; -.
DR Araport; AT4G18480; -.
DR TAIR; locus:2005500; AT4G18480.
DR eggNOG; ENOG502QRUY; Eukaryota.
DR HOGENOM; CLU_016684_0_0_1; -.
DR InParanoid; P16127; -.
DR OMA; PICFKPG; -.
DR OrthoDB; 918663at2759; -.
DR PhylomeDB; P16127; -.
DR BioCyc; ARA:AT4G18480-MON; -.
DR BioCyc; MetaCyc:MON1F-75; -.
DR SABIO-RK; P16127; -.
DR UniPathway; UPA00668; -.
DR PRO; PR:P16127; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P16127; baseline and differential.
DR Genevisible; P16127; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0010007; C:magnesium chelatase complex; TAS:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:TAIR.
DR GO; GO:0016851; F:magnesium chelatase activity; NAS:TAIR.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IBA:GO_Central.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR045006; CHLI-like.
DR InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR InterPro; IPR011775; Mg_chelatase_ATPase-isu.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR32039; PTHR32039; 1.
DR Pfam; PF17863; AAA_lid_2; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02030; BchI-ChlI; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chlorophyll biosynthesis; Chloroplast;
KW Disulfide bond; Ligase; Nucleotide-binding; Phosphoprotein; Photosynthesis;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..60
FT /note="Chloroplast"
FT /evidence="ECO:0000255, ECO:0007744|PubMed:22223895"
FT CHAIN 61..424
FT /note="Magnesium-chelatase subunit ChlI-1, chloroplastic"
FT /id="PRO_0000002801"
FT BINDING 119..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 61
FT /note="N-acetylvaline"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT DISULFID 102..193
FT /evidence="ECO:0000305|PubMed:17472958"
FT DISULFID 354..396
FT /note="Inhibitory under oxidizing conditions"
FT /evidence="ECO:0000305|PubMed:17472958"
FT MUTAGEN 102
FT /note="C->S: Reduces ATPase activity 2-fold."
FT /evidence="ECO:0000269|PubMed:17472958"
FT MUTAGEN 193
FT /note="C->S: Reduces ATPase activity 2-fold."
FT /evidence="ECO:0000269|PubMed:17472958"
FT MUTAGEN 240
FT /note="D->N: In aci5-3; white and inviable plants.
FT Resistance to the herbicide acifluorfen when grown on
FT sucrose-containing medium."
FT /evidence="ECO:0000269|PubMed:15815918"
FT MUTAGEN 354
FT /note="C->S: Reduces ATPase activity 5-fold."
FT /evidence="ECO:0000269|PubMed:17472958"
FT MUTAGEN 396
FT /note="C->S: Reduces ATPase activity 5-fold."
FT /evidence="ECO:0000269|PubMed:17472958"
SQ SEQUENCE 424 AA; 46270 MW; 30075DBBC31330DE CRC64;
MASLLGTSSS AIWASPSLSS PSSKPSSSPI CFRPGKLFGS KLNAGIQIRP KKNRSRYHVS
VMNVATEINS TEQVVGKFDS KKSARPVYPF AAIVGQDEMK LCLLLNVIDP KIGGVMIMGD
RGTGKSTTVR SLVDLLPEIN VVAGDPYNSD PIDPEFMGVE VRERVEKGEQ VPVIATKINM
VDLPLGATED RVCGTIDIEK ALTEGVKAFE PGLLAKANRG ILYVDEVNLL DDHLVDVLLD
SAASGWNTVE REGISISHPA RFILIGSGNP EEGELRPQLL DRFGMHAQVG TVRDADLRVK
IVEERARFDS NPKDFRDTYK TEQDKLQDQI STARANLSSV QIDRELKVKI SRVCSELNVD
GLRGDIVTNR AAKALAALKG KDRVTPDDVA TVIPNCLRHR LRKDPLESID SGVLVSEKFA
EIFS
