ID F9U6N2_9GAMM Unreviewed; 341 AA.
AC F9U6N2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|RuleBase:RU362087};
DE EC=6.6.1.1 {ECO:0000256|RuleBase:RU362087};
GN ORFNames=ThimaDRAFT_0584 {ECO:0000313|EMBL:EGV19908.1};
OS Thiocapsa marina 5811.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocapsa.
OX NCBI_TaxID=768671 {ECO:0000313|EMBL:EGV19908.1, ECO:0000313|Proteomes:UP000005459};
RN [1] {ECO:0000313|EMBL:EGV19908.1, ECO:0000313|Proteomes:UP000005459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5811 {ECO:0000313|EMBL:EGV19908.1,
RC ECO:0000313|Proteomes:UP000005459};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L.,
RA Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V., Frigaard N.-U.,
RA Bryant D., Woyke T.J.;
RT "The draft genome of Thiocapsa marina 5811.";
RL Submitted (JUN-2011) 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; AFWV01000002; EGV19908.1; -; Genomic_DNA.
DR RefSeq; WP_007191461.1; NZ_AFWV01000002.1.
DR AlphaFoldDB; F9U6N2; -.
DR STRING; 768671.ThimaDRAFT_0584; -.
DR PATRIC; fig|768671.3.peg.637; -.
DR eggNOG; COG1239; Bacteria.
DR OrthoDB; 9775079at2; -.
DR UniPathway; UPA00669; -.
DR Proteomes; UP000005459; Unassembled WGS sequence.
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; 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:EGV19908.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362087};
KW Photosynthesis {ECO:0000256|RuleBase:RU362087};
KW Reference proteome {ECO:0000313|Proteomes:UP000005459}.
FT DOMAIN 28..209
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 341 AA; 37302 MW; AFB9AF9BB7D626DE CRC64;
MPIPFPFSAV VAQEEMKRSL LIAAIDPSIG GVLVFGDRGT GKSTAIRGLA ALLPKMRAVD
CVYNCDPEAG EDALCAECRT KRAKGPLKSR MVPVPVVDLP LGATEDRVIG ALDLERALTK
GEKAFEPGLL ARAHRGFLYI DEVNLLEDHL VDSLLDVAAS GENLVEREGL SIRHPARFVL
VGSGNPEEGE LRPQLQDRFG LSVEVRTPQD LPTRMKVVRL RDEFERDPPA FVQKWKRQDG
KVRSQIQKAR DFLPTVEVPD ATLEQAGRLC IKLGTDGLRG ELTLIRAARA FAALKGDAEV
LDAHLVQVAA SALRHRLRRD PLDESGSTSR VERAVGELFG E
//
