ID   CHLI_CHLVU              Reviewed;         354 AA.
AC   P56304;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 84.
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   Chlorella vulgaris (Green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX   NCBI_TaxID=3077;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAM C-27 / Tamiya;
RX   PubMed=9159184; DOI=10.1073/pnas.94.11.5967;
RA   Wakasugi T., Nagai T., Kapoor M., Sugita M., Ito M., Ito S., Tsudzuki J.,
RA   Nakashima K., Tsudzuki T., Suzuki Y., Hamada A., Ohta T., Inamura A.,
RA   Yoshinaga K., Sugiura M.;
RT   "Complete nucleotide sequence of the chloroplast genome from the green alga
RT   Chlorella vulgaris: the existence of genes possibly involved in chloroplast
RT   division.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:5967-5972(1997).
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; AB001684; BAA57990.1; -; Genomic_DNA.
DR   PIR; T07342; T07342.
DR   RefSeq; NP_045914.1; NC_001865.1.
DR   AlphaFoldDB; P56304; -.
DR   SMR; P56304; -.
DR   GeneID; 809149; -.
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..354
FT                   /note="Magnesium-chelatase subunit ChlI"
FT                   /id="PRO_0000206864"
FT   BINDING         47..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   DISULFID        282..324
FT                   /note="Inhibitory under oxidizing conditions"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  39425 MW;  4E66026EED242FB4 CRC64;
     MNTVVENSLE QARPVFPFTA IVGQEEMKLA LILNVIDPKI GGVMIMGDRG TGKSTTVRAL
     VDLLPEIQVV ADDPFNSDPK DPELMSQEVR GRLQRKETVP ITTKKISMVD LPLGATEDRV
     CGTIDIEKAL TEGVKAFEPG LLAKANRGIL YVDEVNLLDD HLVDVLLDSA ASGWNTVERE
     GISISHPARF ILVGSGNPEE GELRPQLLDR FGMHAQIGTV KEPNLRVQIV EQRANFDAAP
     LEFRETYQDS QAQLGNQILE ARNLLPQIQL EYDYRVKISQ ICSELDVDGL RGDLVTNRAS
     KAIASFEGRT EVTPEDIFRV IPLCLRHRLR KDPLESIDSG DKVRDIFKRV FGYE