ID A0A1B1Q160_9CHLB Unreviewed; 383 AA.
AC A0A1B1Q160;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|RuleBase:RU362087};
DE EC=6.6.1.1 {ECO:0000256|RuleBase:RU362087};
GN Name=bchI {ECO:0000313|EMBL:ANT64540.1};
GN ORFNames=Ptc2401_00749 {ECO:0000313|EMBL:ANT64540.1};
OS Prosthecochloris sp. CIB 2401.
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=1868325 {ECO:0000313|EMBL:ANT64540.1, ECO:0000313|Proteomes:UP000092496};
RN [1] {ECO:0000313|EMBL:ANT64540.1, ECO:0000313|Proteomes:UP000092496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB 2401 {ECO:0000313|EMBL:ANT64540.1,
RC ECO:0000313|Proteomes:UP000092496};
RA Nabhan S., Bunk B., Sproeer C., Bryant D.A., Overmann J.;
RT "Genome Sequence of Prosthecochloris phaeum CIB2401 of the phylum
RT Chlorobi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in bacteriochlorophyll biosynthesis; introduces a
CC magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
CC {ECO:0000256|RuleBase:RU362087}.
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 Evidence={ECO:0000256|ARBA:ARBA00001499,
CC ECO:0000256|RuleBase:RU362087};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC biosynthesis. {ECO:0000256|RuleBase:RU362087}.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000256|ARBA:ARBA00005799, ECO:0000256|RuleBase:RU362087}.
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DR EMBL; CP016432; ANT64540.1; -; Genomic_DNA.
DR RefSeq; WP_068866799.1; NZ_CP016432.1.
DR AlphaFoldDB; A0A1B1Q160; -.
DR STRING; 1868325.Ptc2401_00749; -.
DR KEGG; proc:Ptc2401_00749; -.
DR PATRIC; fig|1868325.3.peg.728; -.
DR InParanoid; A0A1B1Q160; -.
DR OrthoDB; 9775079at2; -.
DR UniPathway; UPA00669; -.
DR Proteomes; UP000092496; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030494; P:bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.8.80; Magnesium chelatase subunit I, C-Terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR02030; BchI-ChlI; 1.
DR PANTHER; PTHR32039; MAGNESIUM-CHELATASE SUBUNIT CHLI; 1.
DR PANTHER; PTHR32039:SF9; MAGNESIUM-CHELATASE SUBUNIT CHLI-1, CHLOROPLASTIC; 1.
DR Pfam; PF17863; AAA_lid_2; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362087};
KW Bacteriochlorophyll biosynthesis {ECO:0000256|RuleBase:RU362087};
KW Chlorophyll biosynthesis {ECO:0000256|RuleBase:RU362087};
KW Ligase {ECO:0000256|RuleBase:RU362087, ECO:0000313|EMBL:ANT64540.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362087};
KW Photosynthesis {ECO:0000256|RuleBase:RU362087};
KW Reference proteome {ECO:0000313|Proteomes:UP000092496}.
FT DOMAIN 64..267
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 383 AA; 41920 MW; D8D16A5F9C72621D CRC64;
MTQTASAAKK TASAKAKAGA AAKASAGPKK ARTKKKQGQA FPFTAIVGQE EMKLSLILNI
IDPRIGGVLV MGHRGTGKST TVRALAEVLP SIERVKDDVY NRTVSQFIEM EKTGKDGKAL
TAADMTIEDI QVPVVDLPLG ATEDRVCGTI DIEQALTSGV KAFEPGLLAQ ANRGFLYIDE
VNLLDDHLVD VLLDVAASGR NVVEREGISI RHPARFVLVG SGNPEEGELR PQLLDRFGLH
ARIITITDVE SRVDIVKRRR EYDDDPEAYV KKWDKEQKKL QARILKAKDL LPAITMSDDV
LTDIARLCMQ LGIDGHRGEL TITRTAHAFA AFNGDKEVTM EHVKEIAGLA LRHRLRKDPL
ETLDPGEKIE RELAKVLGEE VDA
//
