ID   CHLI_BIGNA              Reviewed;         365 AA.
AC   Q06J65;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Magnesium-chelatase subunit ChlI;
DE            EC=6.6.1.1;
DE   AltName: Full=Mg-protoporphyrin IX chelatase;
GN   Name=chlI;
OS   Bigelowiella natans (Pedinomonas minutissima) (Chlorarachnion sp. (strain
OS   CCMP621)).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Rhizaria; Cercozoa; Chlorarachniophyceae; Bigelowiella.
OX   NCBI_TaxID=227086;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16990439; DOI=10.1093/molbev/msl129;
RA   Rogers M.B., Gilson P.R., Su V., McFadden G.I., Keeling P.J.;
RT   "The complete chloroplast genome of the chlorarachniophyte Bigelowiella
RT   natans: evidence for independent origins of chlorarachniophyte and euglenid
RT   secondary endosymbionts.";
RL   Mol. Biol. Evol. 24:54-62(2007).
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; DQ851108; ABG91394.1; -; Genomic_DNA.
DR   RefSeq; YP_778562.1; NC_008408.1.
DR   AlphaFoldDB; Q06J65; -.
DR   SMR; Q06J65; -.
DR   GeneID; 4352979; -.
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; 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   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..365
FT                   /note="Magnesium-chelatase subunit ChlI"
FT                   /id="PRO_0000310406"
FT   BINDING         54..61
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   365 AA;  40729 MW;  785A24B9F7C136C1 CRC64;
     MKKYNKSFLI DVNCETLKVR QAFPFTALIG QTNMKLALIL NVIDPKIGGV MSMGDRGTGK
     STIVRSLVDL LPNIQVVSED PFNSDPIDYD LMSQEVKEAK KSGEKIYTTS IKTPMVDLPL
     GATEDRVCGT IDIEKALIDG TKAFEPGLLA KANRGILYVD EVNLLDDHLV DILLDSAAGG
     WNTVEREGIS IVHPARFILI GSGNPEEGEL RPQLLDRFGM HVRIKTIKDP LSRVKIVERR
     SNFDKSAESF LKNYEYLQDF LKNRIVNAQG SLKDIKIDYQ YKVNIAELCS NLNIDGLRGD
     IVTNRAVKAF VALNSRKTVL DKDVFTIMSL CLTHRLKKNP LESIDSSQNI VTIFKDIFGY
     SDLTA