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
//