ID   BCHD_CHLTE              Reviewed;         620 AA.
AC   Q93SW0;
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 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=CT1296;
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; AAG12406.1; -; Genomic_DNA.
DR   EMBL; AE006470; AAM72526.1; -; Genomic_DNA.
DR   RefSeq; NP_662184.1; NC_002932.3.
DR   RefSeq; WP_010932965.1; NC_002932.3.
DR   AlphaFoldDB; Q93SW0; -.
DR   SMR; Q93SW0; -.
DR   STRING; 194439.CT1296; -.
DR   EnsemblBacteria; AAM72526; AAM72526; CT1296.
DR   KEGG; cte:CT1296; -.
DR   PATRIC; fig|194439.7.peg.1181; -.
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; 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   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; Reference proteome.
FT   CHAIN           1..620
FT                   /note="Magnesium-chelatase 67 kDa subunit"
FT                   /id="PRO_0000206849"
FT   DOMAIN          432..620
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   REGION          272..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..322
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   620 AA;  67016 MW;  05BE07DD3D96F917 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
     RAAIANAALN QRTEVDDEDL KLAMKLVLVP RATRMPEREP NPEEMAQDEP PPQEEQPQDE
     AEDQNAPPDE ADSDADEEQE ETPDMIEELM MDAVETELPD NILNISLASK KKAKSGSRGE
     ALNNKRGRFV RSQPGEIKSG KVALIPTLIS AAPWQASRKA EQAKKGIKST AALIIGKDDI
     KIKRFRDKSG TLFIFMVDAS GSMALNRMRQ AKGAVASLLQ NAYVHRDQVS LISFRGKQAQ
     VLLPPSQSVD RAKRELDVLP TGGGTPLASA LLTGWETAKQ ARAKGITQIM FVMITDGRGN
     IPLGAAYDPN ATKASKEELE KEVEALALSI QADGIASIVV DTQMNYLSRG EAPKLAQKLG
     GRYFYLPNAK AEQIVEAALS