ID   CHLI_NEPOL              Reviewed;         355 AA.
AC   Q9TL08;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 85.
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   Nephroselmis olivacea (Green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Nephroselmidophyceae;
OC   Nephroselmidales; Nephroselmidaceae; Nephroselmis.
OX   NCBI_TaxID=31312;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-484 / S-N-5-8;
RX   PubMed=10468594; DOI=10.1073/pnas.96.18.10248;
RA   Turmel M., Otis C., Lemieux C.;
RT   "The complete chloroplast DNA sequence of the green alga Nephroselmis
RT   olivacea: insights into the architecture of ancestral chloroplast
RT   genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:10248-10253(1999).
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}.
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; AF137379; AAD54808.1; -; Genomic_DNA.
DR   RefSeq; NP_050837.1; NC_000927.1.
DR   AlphaFoldDB; Q9TL08; -.
DR   SMR; Q9TL08; -.
DR   GeneID; 801953; -.
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..355
FT                   /note="Magnesium-chelatase subunit ChlI"
FT                   /id="PRO_0000206870"
FT   BINDING         46..53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   DISULFID        281..323
FT                   /note="Inhibitory under oxidizing conditions"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   355 AA;  39224 MW;  94E872ADCDC42A74 CRC64;
     MNATITTSEQ ARPVFPFTAI VGQEEMKLAL LLNVIDPKIG GVMIMGDRGT GKSTTVRALV
     DLLPEIEVVE NDPFNSHPYD PELMSDEVRE KVHRGESIRT TTTKIPMVDL PLGATEDRVC
     GTIDIEKALT EGVKAFEPGL LAKANRGILY VDEVNLLDDH LVDVLLDSAA SGWNTVEREG
     ISICHPARFI LVGSGNPEEG ELRPQLLDRF GMHAQIGTVR EPELRVKIVE QRATFDENPK
     EFRQSYETSQ ASLTSQLTEA RARLRQVQTD YSLRVKISQV CSELNVDGLR GDIVTNRAAK
     ALAALEGRTS VSVEDIGRII TLCLRHRLRK DPLESIDSGE KVQEVFSIVF GTNPL