ID   CHLI_OLILU              Reviewed;         334 AA.
AC   Q32742;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Magnesium-chelatase subunit ChlI;
DE            EC=6.6.1.1;
DE   AltName: Full=Mg-protoporphyrin IX chelatase;
GN   Name=chlI; Synonyms=ccsA;
OS   Olisthodiscus luteus (Marine phytoflagellate).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Olisthodiscophyceae;
OC   Olisthodiscaceae; Olisthodiscus.
OX   NCBI_TaxID=83000;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Valentin K.-U., Darby C., Cattolico R.A.;
RT   "bchI is encoded in a constitutively expressed dicistronic operon on the
RT   plastid DNA of Olisthodiscus luteus (Chromophyta).";
RL   Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in chlorophyll biosynthesis; introduces a magnesium
CC       ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
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   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC       {ECO:0000305}.
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DR   EMBL; Z21959; CAA79971.1; -; Genomic_DNA.
DR   PIR; S32166; S32166.
DR   AlphaFoldDB; Q32742; -.
DR   SMR; Q32742; -.
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; Ligase;
KW   Nucleotide-binding; Photosynthesis; Plastid.
FT   CHAIN           1..334
FT                   /note="Magnesium-chelatase subunit ChlI"
FT                   /id="PRO_0000206872"
FT   BINDING         43..50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   334 AA;  37209 MW;  06E39F227B3DF085 CRC64;
     MTEEKKINPP IFPFTAIVGQ EEMKLALQLN VIDPKIGGVM IMGDRGTGKS TTIRAIADLL
     PEIEVVKDNQ FNTAPSEDLN EEIVKIKTPM IDLPLGATED RVCGTIDIEK ALTDGVKAFE
     PGLLAKANRG ILYVDEVNLL DDHLVDILLD SAASGLNTVE REGISIRHAA RFVLVGSGNP
     EEGELRPQLL DRFGMHAVIK TVKDPKLRVR VVEERTLFDL NPEEWINKYR EQQEALKTRI
     IAAQNLISSV TISDDFKLKI SQVCSELDVD GLRGDIVTNR AAKAYAAFNN RTEVEIGDIE
     KVITLCLRHR LRKDPLETID SGDKVQKLFE EIFD