CHLI2_ARATH
ID CHLI2_ARATH Reviewed; 418 AA.
AC Q5XF33; Q8L712; Q9FJ43;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Magnesium-chelatase subunit ChlI-2, chloroplastic;
DE Short=Mg-chelatase subunit I-2;
DE EC=6.6.1.1;
DE AltName: Full=Mg-protoporphyrin IX chelatase subunit ChlI-2;
DE Flags: Precursor;
GN Name=CHLI2; OrderedLocusNames=At5g45930; ORFNames=K15I22.13;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY.
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19363094; DOI=10.1104/pp.109.135368;
RA Huang Y.S., Li H.M.;
RT "Arabidopsis CHLI2 can substitute for CHLI1.";
RL Plant Physiol. 150:636-645(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-56, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER SER-55, 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).
CC -!- FUNCTION: Involved in chlorophyll biosynthesis. Catalyzes the insertion
CC of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
CC The reaction takes place in two steps, with an ATP-dependent activation
CC followed by an ATP-dependent chelation step. Possesses low affinity for
CC ATP and may play a limited role in chlorophyll biosynthesis, and
CC contributes to the assembly of the Mg-chelatase complex.
CC {ECO:0000269|PubMed:18846282, ECO:0000269|PubMed:19363094}.
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 CHLI2.
CC {ECO:0000269|PubMed:18846282}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.29 mM for ATP {ECO:0000269|PubMed:18846282};
CC Vmax=27.8 nmol/min/mg enzyme toward ATP
CC {ECO:0000269|PubMed:18846282};
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. {ECO:0000269|PubMed:18846282}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000305|PubMed:18846282}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:11842180}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but plants show slight decrease in chlorophyll content.
CC Chli1 and chli2 double mutants are albino.
CC {ECO:0000269|PubMed:18846282, ECO:0000269|PubMed:19363094}.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09321.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB016870; BAB09321.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95316.1; -; Genomic_DNA.
DR EMBL; AY140022; AAM98163.1; -; mRNA.
DR EMBL; BT015783; AAU90073.1; -; mRNA.
DR RefSeq; NP_199405.2; NM_123961.4.
DR AlphaFoldDB; Q5XF33; -.
DR SMR; Q5XF33; -.
DR STRING; 3702.AT5G45930.1; -.
DR iPTMnet; Q5XF33; -.
DR PaxDb; Q5XF33; -.
DR PRIDE; Q5XF33; -.
DR ProteomicsDB; 245180; -.
DR EnsemblPlants; AT5G45930.1; AT5G45930.1; AT5G45930.
DR GeneID; 834633; -.
DR Gramene; AT5G45930.1; AT5G45930.1; AT5G45930.
DR KEGG; ath:AT5G45930; -.
DR Araport; AT5G45930; -.
DR TAIR; locus:2152405; AT5G45930.
DR eggNOG; ENOG502QRUY; Eukaryota.
DR HOGENOM; CLU_016684_0_0_1; -.
DR InParanoid; Q5XF33; -.
DR OMA; VMERRFA; -.
DR OrthoDB; 918663at2759; -.
DR PhylomeDB; Q5XF33; -.
DR BioCyc; ARA:AT5G45930-MON; -.
DR UniPathway; UPA00668; -.
DR PRO; PR:Q5XF33; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q5XF33; baseline and differential.
DR Genevisible; Q5XF33; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0010007; C:magnesium chelatase complex; TAS:TAIR.
DR GO; GO:0009536; C:plastid; 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; ISS:TAIR.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IMP:TAIR.
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; Photosynthesis; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255, ECO:0007744|PubMed:22223895"
FT CHAIN 56..418
FT /note="Magnesium-chelatase subunit ChlI-2, chloroplastic"
FT /id="PRO_0000418770"
FT BINDING 113..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 56
FT /note="N-acetylvaline"
FT /evidence="ECO:0007744|PubMed:22223895"
FT DISULFID 96..187
FT /evidence="ECO:0000250"
FT DISULFID 348..390
FT /note="Inhibitory under oxidizing conditions"
FT /evidence="ECO:0000250"
FT CONFLICT 371
FT /note="A -> T (in Ref. 3; AAM98163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 46098 MW; FC3ECB5A0D406C9D CRC64;
MASLLGRSPS SILTCPRISS PSSTSSMSHL CFGPEKLSGR IQFNPKKNRS RYHVSVMNVA
TEINSVEQAK KIDSKESARP VYPFAAIVGQ DEMKLCLLLN VIDPKIGGVM IMGDRGTGKS
TTVRSLVDLL PEITVVSGDP YNSDPRDPEC MGKEVREKVQ KGEELSVIET KINMVDLPLG
ATEDRVCGTI DIEKALTEGV KAFEPGLLAK ANRGILYVDE VNLLDDHLVD VLLDSAASGW
NTVEREGISI SHPARFILIG SGNPEEGELR PQLLDRFGMH AQVGTVRDAE LRVKIVEERA
RFDSNPKEFR ETYQEEQLKL QEQITTARSN LSAVQIDQDL KVKISKVCAE LDVDGLRGDM
VINRAARALA ALQGRDQVTA EDVGIVIPNC LRHRLRKDPL ESMDSGILVT EKFYEVFT
