GenomeNet

Database: UniProt
Entry: K8EP78_9CHLO
LinkDB: K8EP78_9CHLO
Original site: K8EP78_9CHLO 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system