CHLD_TOBAC
ID CHLD_TOBAC Reviewed; 758 AA.
AC O24133;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9418040; DOI=10.1046/j.1365-313x.1997.12050981.x;
RA Papenbrock J., Graefe S., Kruse E., Haenel F., Grimm B.;
RT "Mg-chelatase of tobacco: identification of a Chl D cDNA sequence encoding
RT a third subunit, analysis of the interaction of the three subunits with the
RT yeast two-hybrid system, and reconstitution of the enzyme activity by co-
RT expression of recombinant CHL D, CHL H and CHL I.";
RL Plant J. 12:981-990(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; Y10022; CAA71128.1; -; mRNA.
DR PIR; T02925; T02925.
DR AlphaFoldDB; O24133; -.
DR SMR; O24133; -.
DR STRING; 4097.O24133; -.
DR PRIDE; O24133; -.
DR BioCyc; MetaCyc:MON-11777; -.
DR BRENDA; 6.6.1.1; 3645.
DR UniPathway; UPA00668; -.
DR Proteomes; UP000084051; Unplaced.
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; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 63..758
FT /note="Magnesium-chelatase subunit ChlD, chloroplastic"
FT /id="PRO_0000002800"
FT DOMAIN 556..752
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 395..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..419
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..441
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 83013 MW; ED531E85D5FAFEF8 CRC64;
MGFCSTSTLP QTSLSNSQSS TFFTYLKPCP ILSSTYLRPK RLKFRLRISA TATIDSPNGA
VAVVEPEKQP EKISFGRQYF PLAAVIGQDA IKTALLLGAI DREIGGIAIC GKRGTAKTLM
ARGLHAILPP IEVVVGSMAN ADPNCPDEWE DGLADRAEYG SDGNIKTQIV KSPFVQIPLG
VTEDRLIGSV DVEESVKSGT TVFQPGLLAE AHRGVLYVDE INLLDEGISN LLLNVLTEGV
NIVEREGISF RHPCKPLLIA TYNPEEGAVR EHLLDRIAIN LSADLPMSFD DRVAAVDIAT
RFQECSNEVF KMVDEETDSA KTQIILAREY LKDVTISRDQ LKYLVMEAIR GGCQGHRAEL
YAARVAKCLA AIDGREKVGV DELKKAVELV ILPRSTIVEN PPDQQNQQPP PPPPPPQNQD
SSEEQNEEEE KEEEDQEDEK DRENEQQQPQ VPDEFIFDAE GGLVDEKLLF FAQQAQRRKG
KAGRAKKVIF SEDRGRYIKP MLPKGPVKRL AVDATLRAAA PYQKLRRAKD IQKTRKVYVE
KTDMRAKRMA RKAGALVIFV VDASGSMALN RMQNAKGAAL KLLAESYTSR DQVCIIPFRG
DAAEVLLPPS RSISMARNRL ERLPCGGGSP LAHGLTTAVR VGMNAEKSGD VGRIMIVAIT
DGRANISLKR STDPEAEASD APRPSSQELK DEILEVAGKI YKTGMSLLVI DTENKFVSTG
FAKEIARVAQ GKYYYLPNAS DAVISAATKD ALSALKES
