ID   BCHH_CHLP8              Reviewed;        1272 AA.
AC   O50314; B3QMJ4;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Magnesium-chelatase subunit H;
DE            EC=6.6.1.1;
DE   AltName: Full=Mg-protoporphyrin IX chelatase subunit H;
GN   Name=bchH; OrderedLocusNames=Cpar_0728;
OS   Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme
OS   subsp. thiosulfatophilum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=517417;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Petersen B.L., Moeller M.G., Stummann B.M., Henningsen K.W.;
RT   "Clustering of genes with function in the biosynthesis of
RT   bacteriochlorophyll and heme in the green sulfur bacterium Chlorobium
RT   vibrioforme.";
RL   Hereditas 125:93-96(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 263 / NCIMB 8327;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobaculum parvum NCIB 8327.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in bacteriochlorophyll pigment biosynthesis;
CC       introduces a magnesium ion into protoporphyrin IX to yield Mg-
CC       protoroporphyrin 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 (light-independent).
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunit H family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB06301.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Z83933; CAB06301.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001099; ACF11147.1; -; Genomic_DNA.
DR   PIR; T17194; T17194.
DR   RefSeq; WP_012501980.1; NC_011027.1.
DR   AlphaFoldDB; O50314; -.
DR   SMR; O50314; -.
DR   STRING; 517417.Cpar_0728; -.
DR   PRIDE; O50314; -.
DR   EnsemblBacteria; ACF11147; ACF11147; Cpar_0728.
DR   KEGG; cpc:Cpar_0728; -.
DR   eggNOG; COG1429; Bacteria.
DR   HOGENOM; CLU_002017_1_2_10; -.
DR   OMA; YGTYVDD; -.
DR   OrthoDB; 8025at2; -.
DR   UniPathway; UPA00671; -.
DR   Proteomes; UP000008811; 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:0036070; P:light-independent bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   CDD; cd10150; CobN_like; 1.
DR   InterPro; IPR011771; BchH.
DR   InterPro; IPR003672; CobN/Mg_chltase.
DR   InterPro; IPR022571; Mg_chelatase_H_N.
DR   PANTHER; PTHR44119; PTHR44119; 1.
DR   Pfam; PF02514; CobN-Mg_chel; 1.
DR   Pfam; PF11965; DUF3479; 1.
DR   TIGRFAMs; TIGR02025; BchH; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis;
KW   Ligase; Nucleotide-binding; Photosynthesis.
FT   CHAIN           1..1272
FT                   /note="Magnesium-chelatase subunit H"
FT                   /id="PRO_0000219884"
FT   CONFLICT        183
FT                   /note="L -> W (in Ref. 1; CAB06301)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1272 AA;  143947 MW;  7A4872634633A227 CRC64;
     MAQRRKITAI VGLEQYNAGL WRKIKSMLDK DAELVQLSDV DLEKQNPEAA TAIREADCVF
     MSMINFKEQI DWFKEQLDQA INEKTIFIFE SMPEAMALTK VGSYQVTEGK SGMPDMVKKI
     AKMLVKGRDE DALYGYMKLM KIMRTILPLV PNKAKDFKNW LMVYSYWLQP TPENIVNMFR
     LILREYFDSN VKVEPIVDVP NMGLYHPDAK EYFKDVKSFK SWSKKRGVNF DKSQKMALLF
     FRKHLLQEKT YIDNTIRTLE KHGVNVFPAF VMGVEGHVLV RDWLMKEKID LLVNMMGFGL
     VGGPAGSTKP GTAADARHEI LTGLDVPYMV AQPLLVQDFE SWHELGVSPM QVTFTYSIPE
     MDGATAPVIL GALQDGKVET VQERLDRLAI LSKKWMRLRA TSNRDKRVAL VVYDYPPGLG
     KKATAALLDV PTTLLRILER LKKEGYNVGT LPESPTKLFE MLDRATDYQI MQNKPEAIKV
     SREKYNELAT YHERERIEER WQAFPGEIAP VGSEEVFLGG LRLGNIYIGV QPRLGVQGDP
     MRLIFDKANT PHHQYISFYR WISREFDAHA LVHVGMHGSV EWMPGLQTGL TGECWPDALL
     GEVPHFYIYP VNNPSESTIA KRRGLATMVS HVVPPLARAG LYKELPALKD LLADYRERNQ
     AQGEDVEQVQ EAIMTKAELL NLTDDCPRRP DEPFSDFVSR LYIYIVELEN RLISNSLHVF
     GEAGPLESQI ITITETIKNR GENGRSLPYI FIDTSGRNGH YGSYEEISSL SRKGDEAAIQ
     LREWAENACR EFVKQTMFDR KNPMQVFESV TGGGRMPEED KPFIQRIIQE GAMMIQALSD
     NSSEMNSLVK VLDGGYIPSG PGGDLVRDGM NVLPSGRNIH SIDPWRIPSE TAFKRGTLIA
     DGLISKHVAE NDGQYPETIA EVIWGLDTIK TKGEAVAVVI RLMGAEPAYD AFGKISHYNL
     TPLDKLGRPR VDVLMQLSPI FRDAFGILMD QLDRLVKDAA KADEPHEMNF IKKHVDEALA
     EGMDFEAATS RQFTQAPGAY GTYVDDMIED SAWENEGDLD DLFIRRNSSA YGGGRKGEKQ
     SEILQKLLGS VDRVVHQVDS TEFGISDIDH YFSSSGSLQL AARRRNTKTS DIKLNYVESF
     TSDIKLDEAD KSLRVEYRSK LLNPKWFEGM LKHGHSGAGE ISNRVTYMLG WDAVTKSVDD
     WVYKKTAETY ALDPEMRERL ATLNPQAIKN IVGRMLEAHG RGMWKADQSM IEELQEIYAD
     LEDRLEGMAD DD