ID   CHLI_CHLRE              Reviewed;         417 AA.
AC   Q94FT3;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Magnesium-chelatase subunit ChlI, chloroplastic;
DE            Short=Mg-chelatase subunit I-1;
DE            EC=6.6.1.1;
DE   AltName: Full=Mg-protoporphyrin IX chelatase subunit ChlI;
DE   Flags: Precursor;
GN   Name=CHLI;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CC-124;
RA   Lake V., Willows R.D.;
RT   "Magnesium chelatase genes in Chlamydomonas reinhardtii are co-ordinately
RT   regulated.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
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; AF343974; AAK69657.1; -; mRNA.
DR   AlphaFoldDB; Q94FT3; -.
DR   SMR; Q94FT3; -.
DR   STRING; 3055.EDP04965; -.
DR   ProMEX; Q94FT3; -.
DR   eggNOG; ENOG502QRUY; Eukaryota.
DR   BRENDA; 6.6.1.1; 1318.
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   2: Evidence at transcript level;
KW   ATP-binding; Chlorophyll biosynthesis; Chloroplast; Disulfide bond; Ligase;
KW   Nucleotide-binding; Photosynthesis; Plastid; Transit peptide.
FT   TRANSIT         1..54
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           55..417
FT                   /note="Magnesium-chelatase subunit ChlI, chloroplastic"
FT                   /id="PRO_0000002802"
FT   BINDING         110..117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   DISULFID        345..387
FT                   /note="Inhibitory under oxidizing conditions"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   417 AA;  45393 MW;  AD9C1D9EE8C60DD0 CRC64;
     MALNMRVSSS KVAAKQQGRI SAVPVVSSKV ASSARVAPFQ GAPVAAQRAA LLVRAAAATE
     VKAAEGRTGK ELGQARPIFP FTAIVGQDEM KLALILNVID PKIGGVMIMG DRGTGKSTTI
     RALADLLPEM QVVANDPFNS DPTDPELMSE EVRNRVKAGE QLPVSSKKIP MVDLPLGATE
     DRVCGTIDIE KALTEGVKAF EPGLLAKANR GILYVDEVNL LDDHLVDVLL DSAASGWNTV
     EREGISISHP ARFILVGSGN PEEGELRPQL LDRFGMHAQI GTVKDPRLRV QIVSQRSTFD
     ENPAAFRKDY EAGQMALTQR IVDARKLLKQ GEVNYDFRVK ISQICSDLNV DGIRGDIVTN
     RAAKALAAFE GRTEVTPEDI YRVIPLCLRH RLRKDPLAEI DDGDRVREIF KQVFGME