ID   BCHI_ACIRU              Reviewed;         345 AA.
AC   Q9WXA9;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Magnesium-chelatase 38 kDa subunit;
DE            EC=6.6.1.1;
DE   AltName: Full=Mg-protoporphyrin IX chelatase;
GN   Name=bchI;
OS   Acidiphilium rubrum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=526;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35905 / OP;
RX   PubMed=10559247; DOI=10.1074/jbc.274.47.33594;
RA   Masuda T., Inoue K., Masuda M., Nagayama M., Tamaki A., Ohta H.,
RA   Shimada H., Takamiya K.;
RT   "Magnesium insertion by magnesium chelatase in the biosynthesis of zinc
RT   bacteriochlorophyll a in an aerobic acidophilic bacterium Acidiphilium
RT   rubrum.";
RL   J. Biol. Chem. 274:33594-33600(1999).
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   -!- MISCELLANEOUS: Substitution of the magnesium ion by a zinc ion in this
CC       bacteria has been shown to occur after this step of bacteriochlorophyll
CC       biosynthesis.
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC       {ECO:0000305}.
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DR   EMBL; AB017350; BAA76531.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9WXA9; -.
DR   SMR; Q9WXA9; -.
DR   STRING; 526.SAMN05421828_10289; -.
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   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR045006; CHLI-like.
DR   InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR   InterPro; IPR011775; Mg_chelatase_ATPase-isu.
DR   InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR32039; PTHR32039; 1.
DR   Pfam; PF17863; AAA_lid_2; 1.
DR   Pfam; PF01078; Mg_chelatase; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02030; BchI-ChlI; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis;
KW   Ligase; Nucleotide-binding; Photosynthesis.
FT   CHAIN           1..345
FT                   /note="Magnesium-chelatase 38 kDa subunit"
FT                   /id="PRO_0000206856"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   345 AA;  37402 MW;  5E0CCC5A3869840E CRC64;
     MALYPFTAIV GQTEMIRAML IATVEPTLGG VLAFGDRGTG KSTAVRALAA LLPTMRAVAG
     CRYHCDPAAR SALCPECRNR RAAGRLASER VRIPVVDLPL GATEDRVVGA LDLERALADG
     VKAFEPGLLA RAHRGFLYID EINLLEDHLV DLLLDVAASG ENVVEREGLS LRHPARFVLI
     GSGNPEEGEL RPQLLDRFGL CVEVKTPTDL DQRIEVVRRR DAFEHDQAGF TRRFAADEAA
     LRRQLVTAMK LLPLVSVPEA ILRLAAKLCI ELGTDGLRGE LTLLRAARAE AALEGDTVVT
     ESHLRAVAPA ALRHRLRRDP LDESLAGARV ERAMAALFSQ AAIAR