CHLI_SOYBN
ID CHLI_SOYBN Reviewed; 421 AA.
AC P93162;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 116.
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 Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Resnik;
RX PubMed=7575622; DOI=10.1006/bbrc.1995.2481;
RA Nakayama M., Masuda T., Sato N., Yamagata H., Bowler C., Ohta H., Shioi Y.,
RA Takamiya K.;
RT "Cloning, subcellular localization and expression of CHL1, a subunit of
RT magnesium-chelatase in soybean.";
RL Biochem. Biophys. Res. Commun. 215:422-428(1995).
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; D45857; BAA08291.1; -; mRNA.
DR PIR; JC4312; JC4312.
DR RefSeq; XP_003543008.1; XM_003542960.3.
DR AlphaFoldDB; P93162; -.
DR SMR; P93162; -.
DR STRING; 3847.GLYMA13G30560.1; -.
DR PRIDE; P93162; -.
DR ProMEX; P93162; -.
DR EnsemblPlants; KRH21317; KRH21317; GLYMA_13G232500.
DR Gramene; KRH21317; KRH21317; GLYMA_13G232500.
DR eggNOG; ENOG502QRUY; Eukaryota.
DR HOGENOM; CLU_016684_0_0_1; -.
DR InParanoid; P93162; -.
DR OMA; RDPEFMG; -.
DR OrthoDB; 918663at2759; -.
DR UniPathway; UPA00668; -.
DR Proteomes; UP000008827; Chromosome 13.
DR Genevisible; P93162; GM.
DR GO; GO:0009570; C:chloroplast stroma; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..61
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 62..421
FT /note="Magnesium-chelatase subunit ChlI, chloroplastic"
FT /id="PRO_0000002803"
FT BINDING 116..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT DISULFID 99..190
FT /evidence="ECO:0000250"
FT DISULFID 351..393
FT /note="Inhibitory under oxidizing conditions"
FT /evidence="ECO:0000250"
SQ SEQUENCE 421 AA; 45871 MW; FAB92C5D19B6CD8D CRC64;
MASALGTSSI AVLPSRYFSS SSSKPSIHTL SLTSGQNYGR KFYGGIGIHG IKGRAQLSVT
NVATEVNSVE QAQSIASKES QRPVYPFSAI VGQDEMKLCL LLNVIDPKIG GVMIMGDRGT
GKSTTVRSLV DLLPEIKVVA GDPYNSDPQD PEFMGVEVRE RVLQGEELSV VLTKINMVDL
PLGATEDRVC GTIDIEKALT EGVKAFEPGL LAKANRGILY VDEVNLLDDH LVDVLLDSAA
SGWNTVEREG ISISHPARFI LIGSGNPEEG ELRPQLLDRF GMHAQVGTVR DAELRVKIVE
ERGRFDKNPK EFRDSYKAEQ EKLQQQITSA RSVLSSVQID QDLKVKISKV CAELNVDGLR
GDIVTNRAAK ALAALKGRDN VSAEDIATVI PNCLRHRLRK DPLESIDSGL LVTEKFYEVF
S
