ID   CHLI_GUITH              Reviewed;         353 AA.
AC   Q39516;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Magnesium-chelatase subunit ChlI;
DE            EC=6.6.1.1;
DE   AltName: Full=Mg-protoporphyrin IX chelatase;
GN   Name=chlI;
OS   Guillardia theta (Cryptophyte) (Cryptomonas phi).
OG   Plastid; Chloroplast.
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX   NCBI_TaxID=55529;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Douglas S.E., Reith M.;
RT   "A bchI homolog, encoding a subunit of Mg chelatase, is located on the
RT   plastid genomes of red and cryptomonad algae.";
RL   J. Mar. Biotechnol. 1:135-141(1993).
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; AF041468; AAC35636.1; -; Genomic_DNA.
DR   PIR; S37138; S37138.
DR   RefSeq; NP_050702.1; NC_000926.1.
DR   AlphaFoldDB; Q39516; -.
DR   SMR; Q39516; -.
DR   PRIDE; Q39516; -.
DR   GeneID; 856998; -.
DR   HOGENOM; CLU_016684_0_2_1; -.
DR   OMA; RISAVCG; -.
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..353
FT                   /note="Magnesium-chelatase subunit ChlI"
FT                   /id="PRO_0000206868"
FT   BINDING         45..52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   353 AA;  39411 MW;  31F27C4618C944A9 CRC64;
     MTINITKTKE RPVFPFTAIV GQEEMKLALT LNVIDPKIGG VIIMGDRGTG KSTTIRAITD
     ILPEIPIVEN DPFNSHPQDF DLMSDEVRSR IEKGESIPSV MKKVSMIDLP LGATEDRVCG
     TIDIEKALTE GVKAFEPGLL AKANRGILYV DEVNLLDDHL VDILLDSAAS GWNTVEREGI
     SIRHPARFVL VGSGNPEEGE LRPQLLDRFG MHSEIRTVRD PELRVKIVEQ RSEFDKNPSA
     CLETYKNQQT EFKQRIIQAQ KVLPTVELDY DLRIRISKIC GELDVDGLRG DIVTNRAAKA
     HAAFNGKQTV TVDDIKAVIT MCLRHRLRKD PLETIDSGSK VQKVFEDIFA DLM