ID   BCHD_RHOCB              Reviewed;         561 AA.
AC   P26175; D5ANT7;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Magnesium-chelatase 60 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=RCAP_rcc00676;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RA   Burke D.H., Alberti M., Armstrong G.A., Hearst J.E.;
RL   Submitted (NOV-1991) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
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   -!- INTERACTION:
CC       P26175; P26239: bchI; NbExp=5; IntAct=EBI-8453255, EBI-8453273;
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC       {ECO:0000305}.
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DR   EMBL; Z11165; CAA77537.1; -; Genomic_DNA.
DR   EMBL; CP001312; ADE84441.1; -; Genomic_DNA.
DR   PIR; S17821; S17821.
DR   RefSeq; WP_013066420.1; NC_014034.1.
DR   PDB; 2X31; EM; 7.50 A; A/B/C/D/E/F=373-561.
DR   PDBsum; 2X31; -.
DR   AlphaFoldDB; P26175; -.
DR   SMR; P26175; -.
DR   DIP; DIP-58975N; -.
DR   IntAct; P26175; 4.
DR   MINT; P26175; -.
DR   STRING; 272942.RCAP_rcc00676; -.
DR   PRIDE; P26175; -.
DR   EnsemblBacteria; ADE84441; ADE84441; RCAP_rcc00676.
DR   GeneID; 31489622; -.
DR   KEGG; rcp:RCAP_rcc00676; -.
DR   eggNOG; COG1240; Bacteria.
DR   HOGENOM; CLU_016684_6_2_5; -.
DR   OMA; DTQMNYL; -.
DR   OrthoDB; 1068772at2; -.
DR   UniPathway; UPA00669; -.
DR   Proteomes; UP000002361; 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; 3.40.50.410; -; 1.
DR   InterPro; IPR041702; BchD/ChlD_VWA.
DR   InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR   InterPro; IPR011776; Mg_chelatase_ATPase-dsu.
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; PF13519; VWA_2; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Bacteriochlorophyll biosynthesis;
KW   Chlorophyll biosynthesis; Ligase; Nucleotide-binding; Photosynthesis;
KW   Reference proteome.
FT   CHAIN           1..561
FT                   /note="Magnesium-chelatase 60 kDa subunit"
FT                   /id="PRO_0000206852"
FT   DOMAIN          379..559
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   REGION          234..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..252
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   561 AA;  59741 MW;  A54EBCE1C68FCD2D CRC64;
     MDHERLKSAL AVLTVDPAAV GGLWLRSRAG PIRLAFTDTL AKLPFPMALR RLPPNVDDGA
     LYGGLDVAET LHSGKPVLKG GLLDRPSVFI LPMAERCTAK LGARLAQALD LRQHALIALD
     EAAEPDEALP HAVADRLGLF VDLSEVRSID GPGLLPETAQ IERARELLPQ VQMPAERVSE
     IVEGCRQLGI SSLRAPMLAL TAARILTALS GRTRVEAEDV LHAAELTLAH RALPLQEAPP
     PPPPPPEPPE PNEGENQQDE QDQIDPLDGI PPEIVVEAVR AMLPDNILQT LNMGSRLRAA
     SGGQGAGQEQ IGNRRGRPLP SRKGKLEDDA KIDLVATLRS AAPWQGLRRR QAPAGTERVL
     LVESSDIHIK RRKEMSDRVL IFAVDASGSA AVARLSEAKG AVELLLGRAY AARDHVSLIT
     FRGTAAQVLL QPSRSLTQTK RQLQGLPGGG GTPLASGMEM AMVTAKQARS RGMTPTIALL
     TDGRGNIALD GTANRELAGE QATKVARAIR ASGMPAVIID TAMRPNPALV DLARTMDAHY
     IALPRATAHK MADVLGAALE A