ID K8EP78_9CHLO Unreviewed; 470 AA.
AC K8EP78;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|RuleBase:RU362087};
DE EC=6.6.1.1 {ECO:0000256|RuleBase:RU362087};
GN OrderedLocusNames=Bathy15g01790 {ECO:0000313|EMBL:CCO20037.1};
OS Bathycoccus prasinos.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Bathycoccus.
OX NCBI_TaxID=41875 {ECO:0000313|EMBL:CCO20037.1, ECO:0000313|Proteomes:UP000198341};
RN [1] {ECO:0000313|EMBL:CCO20037.1, ECO:0000313|Proteomes:UP000198341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC 1105 {ECO:0000313|EMBL:CCO20037.1,
RC ECO:0000313|Proteomes:UP000198341};
RA Genoscope - CEA;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in chlorophyll biosynthesis. Catalyzes the insertion
CC of 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 -!- ACTIVITY REGULATION: Redox regulation; active in reducing conditions,
CC inactive in oxidizing conditions. {ECO:0000256|RuleBase:RU362087}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis. {ECO:0000256|ARBA:ARBA00005173,
CC ECO:0000256|RuleBase:RU362087}.
CC -!- SUBUNIT: The magnesium chelatase complex is a heterotrimer consisting
CC of subunits CHLI, CHLD and CHLH. {ECO:0000256|ARBA:ARBA00038576}.
CC -!- SUBUNIT: The magnesium chelatase complex is a heterotrimer consisting
CC of subunits CHLI, CHLD, AND CHLH. {ECO:0000256|RuleBase:RU362087}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {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; FO082264; CCO20037.1; -; Genomic_DNA.
DR RefSeq; XP_007508951.1; XM_007508889.1.
DR AlphaFoldDB; K8EP78; -.
DR STRING; 41875.K8EP78; -.
DR GeneID; 19011474; -.
DR KEGG; bpg:Bathy15g01790; -.
DR eggNOG; ENOG502QRUY; Eukaryota.
DR OrthoDB; 275672at2759; -.
DR UniPathway; UPA00668; -.
DR Proteomes; UP000198341; Chromosome_15.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015995; P:chlorophyll 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; 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-2, CHLOROPLASTIC; 1.
DR Pfam; PF17863; AAA_lid_2; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362087};
KW Chlorophyll biosynthesis {ECO:0000256|RuleBase:RU362087};
KW Chloroplast {ECO:0000256|RuleBase:RU362087};
KW Ligase {ECO:0000256|RuleBase:RU362087};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362087};
KW Photosynthesis {ECO:0000256|RuleBase:RU362087};
KW Plastid {ECO:0000256|RuleBase:RU362087};
KW Reference proteome {ECO:0000313|Proteomes:UP000198341}.
FT DOMAIN 190..260
FT /note="Magnesium chelatase ChlI-like catalytic"
FT /evidence="ECO:0000259|Pfam:PF01078"
FT DOMAIN 340..393
FT /note="ChlI/MoxR AAA lid"
FT /evidence="ECO:0000259|Pfam:PF17863"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 51605 MW; 59C1A37B3688D620 CRC64;
MARGVASTSS SASSSSCSSM RTTTGGRSNT RSIASRRWNE KERQSFVDRR RNNAATSLAA
IAEPGTEGYV ENETEITFPF VKIVDQEELK LCLIMNVIDP AIGGVLIMGD RGTAKSVAVR
SLIQLLPEID VVKGDVFNSS PTDPQLMGPD VREKFQKGEA LETAKMRVPM VEVPLGTTED
RICGTIDIEK ALSEGRKAYD PGLLAKANRG LLYIDEVNLL DDSLVDVVLD SAAGGWNTVE
REGISLSHPA KFIMIGSGNP EEGELRPQLL DRFGMKVSVA TVYDVDKRTD LVMNKIKFDE
DPKAYQAECA DETEALRARI QKARDILPSV TISRDIQLKI SSVCALVDVD GLRGDIVVTR
AAKAYVAYEG RNEVTQDDVE KVIGPCLSHR LRKNVTDTMD GGFKVKLGFN KIFKGDAMDF
TQDSKIMAEI IEEGVKEPEP EKKEEPEEPK EKPKPKAGAW DPSKMFGRGR
//