ID A0A3S8UAS4_9RHOB Unreviewed; 340 AA.
AC A0A3S8UAS4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:AZL60704.1};
GN ORFNames=EI545_18895 {ECO:0000313|EMBL:AZL60704.1};
OS Tabrizicola piscis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tabrizicola.
OX NCBI_TaxID=2494374 {ECO:0000313|EMBL:AZL60704.1, ECO:0000313|Proteomes:UP000282002};
RN [1] {ECO:0000313|EMBL:AZL60704.1, ECO:0000313|Proteomes:UP000282002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K13M18 {ECO:0000313|EMBL:AZL60704.1,
RC ECO:0000313|Proteomes:UP000282002};
RA Bae J.-W.;
RT "Complete genome sequencing of Tabrizicola sp. K13M18.";
RL Submitted (DEC-2018) 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; CP034328; AZL60704.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S8UAS4; -.
DR KEGG; taw:EI545_18895; -.
DR OrthoDB; 9775079at2; -.
DR UniPathway; UPA00669; -.
DR Proteomes; UP000282002; 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 CDD; cd00009; AAA; 1.
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; 2.
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:AZL60704.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362087};
KW Photosynthesis {ECO:0000256|RuleBase:RU362087};
KW Reference proteome {ECO:0000313|Proteomes:UP000282002}.
FT DOMAIN 34..209
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 340 AA; 37116 MW; 464A23427A72DF6D CRC64;
MTKTHTPRQP FPFSAIVGQE DMKSAMTLTA IDPGIGGVLV FGDRGTGKST AVRALAALLP
PIEAVEGCPI NAPRRDLCPP WAQGVTDRMV TKPTPVVDLP LGVTEDRVVG ALDIERALTR
GEKAFEPGLL ARANRGYLYI DEVNLLEDHI VDLLLDVAQS GENVVEREGL SIRHPARFVL
VGSGNPEEGE LRPQLLDRFG LSVEVTSPRD IETRVEVIRR RDAYENQYDK FMKTWRVMDA
GLRNQILAAR EALPKLKTPG VVLHDCAALC LALGSDGLRG ELTLLRAARA LAAFEGDTAV
RRTHLRRVAP MALSHRLRRD PLDEAGSAAR VGRTLAEVLP
//
