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Database: UniProt
Entry: D8TKE8_VOLCA
LinkDB: D8TKE8_VOLCA
Original site: D8TKE8_VOLCA 
ID   D8TKE8_VOLCA            Unreviewed;       414 AA.
AC   D8TKE8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|RuleBase:RU362087};
DE            EC=6.6.1.1 {ECO:0000256|RuleBase:RU362087};
GN   ORFNames=VOLCADRAFT_79418 {ECO:0000313|EMBL:EFJ52236.1};
OS   Volvox carteri f. nagariensis.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX   NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN   [1] {ECO:0000313|EMBL:EFJ52236.1, ECO:0000313|Proteomes:UP000001058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX   PubMed=20616280; DOI=10.1126/science.1188800;
RA   Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA   Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA   Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA   Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA   Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT   "Genomic analysis of organismal complexity in the multicellular green alga
RT   Volvox carteri.";
RL   Science 329:223-226(2010).
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   -!- FUNCTION: Protein transport. Probably involved in vesicular traffic.
CC       {ECO:0000256|ARBA:ARBA00025673}.
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|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; GL378325; EFJ52236.1; -; Genomic_DNA.
DR   RefSeq; XP_002947010.1; XM_002946964.1.
DR   AlphaFoldDB; D8TKE8; -.
DR   STRING; 3068.D8TKE8; -.
DR   GeneID; 9618047; -.
DR   KEGG; vcn:VOLCADRAFT_79418; -.
DR   eggNOG; ENOG502QRUY; Eukaryota.
DR   InParanoid; D8TKE8; -.
DR   OrthoDB; 275672at2759; -.
DR   UniPathway; UPA00668; -.
DR   Proteomes; UP000001058; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:0015995; P:chlorophyll 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   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:UP000001058}.
FT   DOMAIN          99..281
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   414 AA;  45346 MW;  5264CCA29ABFDA7A CRC64;
     MALNMRTVSS NVVAQQQHGA RTPVRVPVNA KSVVTLRVAP FQGAAVVPQR AALQVRAAAA
     TEVKPEKELG QARPIFPFTA IVGQDEMKLA LILNVIDPKI GGVMIMGDRG TGKSTTIRAL
     ADLLPEMKVV ASDPFNSDPS DPELMSEEVR NRVKAGEQMS VASKKIPMVD LPLGATEDRV
     CGTIDIEKAL TEGVKAFEPG LLAKANRGIL YVDEVNLLDD HLVDVLLDSA ASGWNTVERE
     GISISHPARF ILVGSGNPEE GELRPQLLDR FGMHAQIGTV KDPRLRVQIV SQRGTFDENP
     ASFRKDYEAS QNALTNRIVE ASKLLKQVEV SYEYRVKISQ ICSDLNVDGI RGDIVTNRAA
     KALAAFEGRT EVTPEDIYRV IPLCLRHRLR KDPLAEIDDG DRVREVFKKV FGME
//
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