ID   CHLI_MESVI              Reviewed;         360 AA.
AC   Q9MUT3;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Magnesium-chelatase subunit ChlI;
DE            Short=Mg-chelatase subunit I-1;
DE            EC=6.6.1.1;
DE   AltName: Full=Mg-protoporphyrin IX chelatase subunit ChlI;
GN   Name=chlI;
OS   Mesostigma viride (Green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Mesostigmatophyceae;
OC   Mesostigmatales; Mesostigmataceae; Mesostigma.
OX   NCBI_TaxID=41882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-296 / KY-14 / CCMP 2046;
RX   PubMed=10688199; DOI=10.1038/35001059;
RA   Lemieux C., Otis C., Turmel M.;
RT   "Ancestral chloroplast genome in Mesostigma viride reveals an early branch
RT   of green plant evolution.";
RL   Nature 403:649-652(2000).
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 (By similarity).
CC       {ECO:0000250}.
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 CHLI (By similarity).
CC       {ECO:0000250}.
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.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC       {ECO:0000305}.
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DR   EMBL; AF166114; AAF43818.1; -; Genomic_DNA.
DR   RefSeq; NP_038377.1; NC_002186.1.
DR   AlphaFoldDB; Q9MUT3; -.
DR   SMR; Q9MUT3; -.
DR   GeneID; 800981; -.
DR   UniPathway; UPA00668; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   ATP-binding; Chlorophyll biosynthesis; Chloroplast; Disulfide bond; Ligase;
KW   Nucleotide-binding; Photosynthesis; Plastid.
FT   CHAIN           1..360
FT                   /note="Magnesium-chelatase subunit ChlI"
FT                   /id="PRO_0000206869"
FT   BINDING         50..57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   DISULFID        285..327
FT                   /note="Inhibitory under oxidizing conditions"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   360 AA;  40384 MW;  AC08CACDF0010D9A CRC64;
     MSTIDLIKNV TKREERPVYP FTAIVGQEEM KLALILNVID PDIGGVMIMG DRGTGKSTTI
     RALVDLLPEI EVVTNDPFNS DPRDPDLMSD EVREKINNKQ EVPTIKTKIK IVDLPLGATE
     DRVCGTIDIE RALNEGVKAF EPGLLAKANR GILYVDEVNL LDDHLVDILL DSAASGWNTV
     EREGISVRHP AKFILVGSGN PEEGELRPQL LDRFGMHAEI RTVKDPDLRV KIVEERSSFD
     ENPQVFRKAY EQSQEDVKSQ IIQARKNLAN VQMDRELRIK VSQICSELDV DGLRGDLVIN
     RAAKALAAFE GRDKVLPKDI LKIITLCLRH RLRKDPLESI DSGSKVESKF YEVFGLLEEN