ID   CHLD_PEA                Reviewed;         754 AA.
AC   O22437;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Magnesium-chelatase subunit ChlD, chloroplastic;
DE            Short=Mg-chelatase subunit D;
DE            EC=6.6.1.1;
DE   AltName: Full=Mg-protoporphyrin IX chelatase subunit ChlD;
DE   Flags: Precursor;
GN   Name=CHLD;
OS   Pisum sativum (Garden pea).
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; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Spring; TISSUE=Leaf;
RA   Luo M., Weinstein J.D.;
RT   "Cloning and sequencing of a cDNA encoding the putative Mg-chelatase
RT   subunit D from pea (Pisum sativum L. cv. Spring).";
RL   (er) Plant Gene Register PGR97-139(1997).
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   -!- 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; AF014399; AAB72194.1; -; mRNA.
DR   PIR; T06249; T06249.
DR   AlphaFoldDB; O22437; -.
DR   SMR; O22437; -.
DR   EnsemblPlants; Psat0s3604g0040.1; Psat0s3604g0040.1.cds; Psat0s3604g0040.
DR   Gramene; Psat0s3604g0040.1; Psat0s3604g0040.1.cds; Psat0s3604g0040.
DR   BRENDA; 6.6.1.1; 4872.
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   CDD; cd01451; vWA_Magnesium_chelatase; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041702; BchD/ChlD_VWA.
DR   InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR   InterPro; IPR011776; Mg_chelatase_ATPase-dsu.
DR   InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   Pfam; PF17863; AAA_lid_2; 1.
DR   Pfam; PF01078; Mg_chelatase; 1.
DR   Pfam; PF13519; VWA_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   TIGRFAMs; TIGR02031; BchD-ChlD; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chlorophyll biosynthesis; Chloroplast; Ligase;
KW   Nucleotide-binding; Photosynthesis; Plastid; Transit peptide.
FT   TRANSIT         1..51
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           52..754
FT                   /note="Magnesium-chelatase subunit ChlD, chloroplastic"
FT                   /id="PRO_0000002799"
FT   DOMAIN          551..751
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   REGION          395..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..415
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..443
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   754 AA;  82865 MW;  1D56BA3139080A90 CRC64;
     MGFSLTHTPH TTASPNLQLR FHSLLPPSFT SQPFLSLHST FPPKRTVPKL RAQSENGAVL
     QASEEKLDAS NYGRQYFPLA AVIGQDAIKT ALLLGATDPR IGGIAISGRR GTAKTIMARG
     MHAILPPIEV VQGSIANADP SCPEEWEDGL YKRVEYDSDG NVKTHIIKSP FVQIPLGVTE
     DRLIGSVDVE ESVKTGTTVF QPGLLAEAHR GVLYVDEINL LDEGISNLLL NVLTEGVNIV
     EREGISFRHP CRPLLIATYN PDEGSVREHL LDRIAINLSA DLPMSFENRV EAVGIATEFQ
     DNCGQVFKMV DEDTDNAKTQ IILAREYLKD VTISKEQLKY LVIEALRGGV QGHRAELYAA
     RVAKCLAALE GREKVYVDDL KKAVELVILP RSIITDTPPE QQNQPPPPPP PPQNQESNEE
     QNEEEEQEEE EEDDNDEENE QQQDQLPEEF IFDAEGGLVD EKLLFFAQQA QRRRGKAGRA
     KNVIFSEDRG RYIKPMLPKG PVKRLAVDAT LRAAAPYQKL RREKDTENRR KVYVEKTDMR
     AKRMARKAGA LVIFVVDASG SMALNRMQNA KGAALKLLAE SYTSRDQVSI IPFRGDSAEV
     LLPPSRSIAM ARKRLERLPC GGGSPLAHGL TTAVRVGLNA EKSGDVGRIM IVAITDGRAN
     ISLKRSNDPE AAAASDAPKP TSQELKDEII EVAAKIYKTG MSLLVIDTEN KFVSTGFAKE
     IARVAQGKYY YLPNASDAVV SLATREALAA LKSS