ID   BCHI_CHLTE              Reviewed;         392 AA.
AC   Q93SW1;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Magnesium-chelatase 38 kDa subunit;
DE            EC=6.6.1.1;
DE   AltName: Full=Mg-protoporphyrin IX chelatase;
GN   Name=bchI; Synonyms=chlI; OrderedLocusNames=CT1297;
OS   Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS   (Chlorobium tepidum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10976061; DOI=10.1126/science.289.5485.1724;
RA   Xiong J., Fischer W.M., Inoue K., Nakahara M., Bauer C.E.;
RT   "Molecular evidence for the early evolution of photosynthesis.";
RL   Science 289:1724-1730(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA   DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA   Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA   Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA   Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA   White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA   Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT   anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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; AY005135; AAG12405.1; -; Genomic_DNA.
DR   EMBL; AE006470; AAM72527.1; -; Genomic_DNA.
DR   RefSeq; NP_662185.1; NC_002932.3.
DR   RefSeq; WP_010932966.1; NC_002932.3.
DR   AlphaFoldDB; Q93SW1; -.
DR   SMR; Q93SW1; -.
DR   STRING; 194439.CT1297; -.
DR   EnsemblBacteria; AAM72527; AAM72527; CT1297.
DR   KEGG; cte:CT1297; -.
DR   PATRIC; fig|194439.7.peg.1182; -.
DR   eggNOG; COG1239; Bacteria.
DR   HOGENOM; CLU_016684_0_2_10; -.
DR   OMA; RISAVCG; -.
DR   OrthoDB; 895310at2; -.
DR   UniPathway; UPA00669; -.
DR   Proteomes; UP000001007; 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   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; Reference proteome.
FT   CHAIN           1..392
FT                   /note="Magnesium-chelatase 38 kDa subunit"
FT                   /id="PRO_0000206857"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         80..87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   392 AA;  42800 MW;  44EE22F1DD79B0BD CRC64;
     MTQTANAAKK TTSTKASAAK EAKVKVTAEE KAVTEVKKPA AKKKSALAFP FTAIVGQEEM
     KLSLILNIID PRIGGVLVMG HRGTGKSTTV RALAEVLPLI PRVKGDIYNR TVEQYIEMEA
     AGKGAPAIKP EDVETELIPV PVVDLPLGAT EDRVCGTIDI EKALTSGVKA FEPGLLAQSN
     RGFLYIDEVN LLDDHLVDVL LDVAASGKNV VEREGISIRH PARFVLVGSG NPEEGELRPQ
     LLDRFGLHAR ITTINDVAKR VQIVKLRREF DEDPEAFMKK VSREQQKLRK KIVAAQQLLP
     QVTMDDAVLT DIAKLCMNLG IDGHRGELTI TRTAHAYAAW EGDKKVTMKH VREIAGLCLR
     HRLRKDPLET VDAGEKIDRE LAKVLGEAEA AA