ID   BCHD_CHLP8              Reviewed;         619 AA.
AC   O50313; B3QMJ2;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Magnesium-chelatase 67 kDa subunit;
DE            Short=Mg-chelatase subunit D;
DE            EC=6.6.1.1;
DE   AltName: Full=Mg-protoporphyrin IX chelatase;
GN   Name=bchD; OrderedLocusNames=Cpar_0726;
OS   Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme
OS   subsp. thiosulfatophilum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=517417;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Petersen B.L., Moeller M.G., Stummann B.M., Henningsen K.W.;
RT   "Clustering of genes with function in the biosynthesis of
RT   bacteriochlorophyll and heme in the green sulfur bacterium Chlorobium
RT   vibrioforme.";
RL   Hereditas 125:93-96(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 263 / NCIMB 8327;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobaculum parvum NCIB 8327.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in bacteriochlorophyll biosynthesis; introduces a
CC       magnesium 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; bacteriochlorophyll
CC       biosynthesis.
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC       {ECO:0000305}.
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DR   EMBL; Z83933; CAB06300.1; -; Genomic_DNA.
DR   EMBL; CP001099; ACF11145.1; -; Genomic_DNA.
DR   PIR; T17193; T17193.
DR   RefSeq; WP_012501978.1; NC_011027.1.
DR   AlphaFoldDB; O50313; -.
DR   SMR; O50313; -.
DR   STRING; 517417.Cpar_0726; -.
DR   EnsemblBacteria; ACF11145; ACF11145; Cpar_0726.
DR   KEGG; cpc:Cpar_0726; -.
DR   eggNOG; COG1239; Bacteria.
DR   eggNOG; COG1240; Bacteria.
DR   HOGENOM; CLU_016684_6_2_10; -.
DR   OMA; DTQMNYL; -.
DR   OrthoDB; 1068772at2; -.
DR   UniPathway; UPA00669; -.
DR   Proteomes; UP000008811; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030494; P:bacteriochlorophyll 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   3: Inferred from homology;
KW   ATP-binding; Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis;
KW   Ligase; Nucleotide-binding; Photosynthesis.
FT   CHAIN           1..619
FT                   /note="Magnesium-chelatase 67 kDa subunit"
FT                   /id="PRO_0000206850"
FT   DOMAIN          431..619
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   REGION          273..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..321
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   619 AA;  66807 MW;  1F9D3712D79426AC CRC64;
     MIAFTDIVGM DLAKQALMLL AVDPSLGGVV IPSTVGSGKS TLARAFADIL PEGTPFVELP
     LNVTEDRLIG GVDLEATLAS GQRVVQHGVL SKAHKGVLYV DSLSLLDSSA VSHIMDAMSR
     GAVIVEREGL SEVHPADFML VGTYDPSDGE VRMGLLDRIG IIVPFTPVND YRARKQIVSL
     VMGTRNEEDT QDELRMLRGI IGAAREQLHH VSITNEQIKG LIQTAISLGV EGNRVDIFAI
     RAALANAALG QRTEVDDEDL KLAVKLVLVP RATRMPEREP SEEEMQQEEP PPPEEQPEQE
     GEDENAPPDE TDSDADEEQE ETPDMIEELM MDAIETDLPE NILNISLASK KKAKSGSRGE
     ALNNKRGRFV RSQPGEIKSG KVALIPTLIS AAPWQAARKA EKAKKGIKTG ALVISTDDVK
     IKRFRDKSGT LFIFMVDASG SMALNRMRQA KGAVASLLQN AYVHRDQVSL ISFRGKQAQV
     LLPPSQSVDR AKRELDVLPT GGGTPLASAL LTGWETAKQA RTKGITQIMF VMITDGRGNI
     PLAAAVDPAA AKAPKEELEK EVEALALSIQ SDGIASIVVD TQMNYLSRGE APKLAQKLGG
     RYFYLPNAKA EQIVEAALS