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Database: UniProt
Entry: Q46H86_PROMT
LinkDB: Q46H86_PROMT
Original site: Q46H86_PROMT 
ID   Q46H86_PROMT            Unreviewed;       717 AA.
AC   Q46H86;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   24-JAN-2024, entry version 110.
DE   RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|RuleBase:RU362087};
DE            EC=6.6.1.1 {ECO:0000256|RuleBase:RU362087};
GN   OrderedLocusNames=PMN2A_1654 {ECO:0000313|EMBL:AAZ59142.1};
OS   Prochlorococcus marinus (strain NATL2A).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=59920 {ECO:0000313|EMBL:AAZ59142.1, ECO:0000313|Proteomes:UP000002535};
RN   [1] {ECO:0000313|EMBL:AAZ59142.1, ECO:0000313|Proteomes:UP000002535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL2A {ECO:0000313|EMBL:AAZ59142.1,
RC   ECO:0000313|Proteomes:UP000002535};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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: Involved in chlorophyll biosynthesis; introduces a magnesium
CC       ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
CC       {ECO:0000256|ARBA:ARBA00003398}.
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; chlorophyll
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; CP000095; AAZ59142.1; -; Genomic_DNA.
DR   RefSeq; WP_011294287.1; NC_007335.2.
DR   AlphaFoldDB; Q46H86; -.
DR   STRING; 59920.PMN2A_1654; -.
DR   KEGG; pmn:PMN2A_1654; -.
DR   HOGENOM; CLU_016684_6_2_3; -.
DR   OMA; YYHLPKA; -.
DR   OrthoDB; 9775079at2; -.
DR   PhylomeDB; Q46H86; -.
DR   UniPathway; UPA00668; -.
DR   Proteomes; UP000002535; 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:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR   CDD; cd01451; vWA_Magnesium_chelatase; 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   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041702; BchD/ChlD_VWA.
DR   InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR   InterPro; IPR011776; Mg_chelatase_ATPase-dsu.
DR   InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   NCBIfam; TIGR02031; BchD-ChlD; 1.
DR   PANTHER; PTHR43473; MAGNESIUM-CHELATASE SUBUNIT CHLD, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43473:SF2; MAGNESIUM-CHELATASE SUBUNIT CHLD, CHLOROPLASTIC; 1.
DR   Pfam; PF17863; AAA_lid_2; 1.
DR   Pfam; PF01078; Mg_chelatase; 1.
DR   Pfam; PF13519; VWA_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50234; VWFA; 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   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU362087};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362087};
KW   Photosynthesis {ECO:0000256|RuleBase:RU362087};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002535}.
FT   DOMAIN          521..713
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   REGION          371..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..420
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   717 AA;  76902 MW;  1FB038E1B3A5833F CRC64;
     MVSSGLNNNN MSSTSKDIAV KDRANLAFPL AAITGHGTLK LALMLAAVDP GLGGVIIAGG
     RGTGKSVLAR GLHALLPPIE IIDLDELANT EDGDDSFIYP AGRNLDPSFS GEWDDLTKKL
     FTKKIGSYEN TDDLENIPTK VVSAPFIQVP LGVTEDRLVG AVDVAASLSS GTPVFQPGLL
     AEAHRGVLYI DELNLLDDGI VNLLLASVGA GENRVEREGL SLSHPCRPLL IATYNPEEGG
     LRDHLLDRFA IVLSADQLIT NEQRVEITQS AISHGQSSEA FSKKWSEDTE SLSTQLLLAR
     QWLPDVQISE DQIEYLVVEA IRGGVEGHRS ELYSVRVAKA HAALCGRDSV DAEDLKAAVR
     LVIAPRAMQM PSEEEMEPPA PEDQQPPPPP PEDSDDNNDQ EEDQEEDQEE EQDEESSPPI
     PEEFMLDPEA CAVDPDLLLF SSTKSKSGNS GSRSAVLSDN RGRYVKPIIP RGPVRRIAVD
     ATLRAAAPYQ KARREREPNR KVIVEEGDLR AKLLQRKAGA LVIFLVDASG SMALNRMQSA
     KGAVIRLLTE AYENRDEVSL IPFRGDQAEV LLPPTRSITA AKRRLEAMPC GGGSPLAHGL
     TQAARVGANA LATGDLGQVV VVAITDGRGN VPLSTSLGQP ILEGETPPDL KQEVLDVASR
     YRALGIKLLV IDTERKFIAS GMGKDLADAS GGKYVQLPKA SDKAIASIAM DAINSVT
//
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