ID   BCHD_HELMO              Reviewed;         666 AA.
AC   Q9ZGE6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 80.
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;
OS   Heliobacterium mobile (Heliobacillus mobilis).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Heliobacteriaceae;
OC   Heliobacterium.
OX   NCBI_TaxID=28064;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9843979; DOI=10.1073/pnas.95.25.14851;
RA   Xiong J., Inoue K., Bauer C.E.;
RT   "Tracking molecular evolution of photosynthesis by characterization of a
RT   major photosynthesis gene cluster from Heliobacillus mobilis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:14851-14856(1998).
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; AF080002; AAC84032.1; -; Genomic_DNA.
DR   PIR; T31461; T31461.
DR   AlphaFoldDB; Q9ZGE6; -.
DR   SMR; Q9ZGE6; -.
DR   UniPathway; UPA00669; -.
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; 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; 2.
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   3: Inferred from homology;
KW   ATP-binding; Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis;
KW   Ligase; Nucleotide-binding; Photosynthesis.
FT   CHAIN           1..666
FT                   /note="Magnesium-chelatase 67 kDa subunit"
FT                   /id="PRO_0000206851"
FT   DOMAIN          475..661
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   REGION          327..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..348
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..367
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         37..44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   666 AA;  72579 MW;  5CB072BD72072BE5 CRC64;
     MKVNTLPLAA ITGQEAVKLA LTLAAVDPGL KGVAIAGRRG TGKTVLARGL RHLLPPIDQL
     EGCPCHCNPA EPHSWCNRCR ERFTEESGLS DSEVPVVQRN APFSEVPLGA TEDRLLGAID
     VEQSLAGGVR AWQPGLLGEA NRGVLYIDQL NLLDDGLVNS LFDAMSGTCR LEREGISVQY
     PSNFVLIGTY DPDEGGLRGH LADRIAMHVS SGVIVDLEQR LEIMRRQELF SEAPEDFFDL
     YNDEQEQTLR RIEKARTVLP QVTISEAQTL YLIGQSLKRG VPGHRADLFS VRLAKAHAAW
     QGRTAVEPID LAVAVEFVIK PRQTVDLPDE EEQMQPPPPP PPPPPPPEPD KPDDPETPPD
     EAPKDEQTLQ LPEEFFFDAE EVPMEDELLS LQNKVQRQAR GGAHGKQKSL ERGRYARALL
     PPPGKNSRVA VDATLRAAAP YQRQRRESGQ YGDRQVIVTN SDIRAKQFVR KSGALIIFVV
     DASGSMAFNR MSSAKGAVSV LLNEAYVNRD KVALIIFRGQ QAETLVPPTR SVELAKKRFD
     QVPVGGGSPL AGAIAQAIEV GVNSIGSDVG QVIITLITDG RGNVPMDPQA GPKNREQLNE
     EILALSRLVP ENGFSMLVID TANKFTSTGF AKKIADAAFA QYYYLPKMTA ASLAETVKSG
     VHALRK