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Database: UniProt
Entry: B0CC43_ACAM1
LinkDB: B0CC43_ACAM1
Original site: B0CC43_ACAM1 
ID   B0CC43_ACAM1            Unreviewed;       682 AA.
AC   B0CC43;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|RuleBase:RU362087};
DE            EC=6.6.1.1 {ECO:0000256|RuleBase:RU362087};
GN   Name=chlD {ECO:0000313|EMBL:ABW25585.1};
GN   OrderedLocusNames=AM1_0533 {ECO:0000313|EMBL:ABW25585.1};
OS   Acaryochloris marina (strain MBIC 11017).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC   Acaryochloridaceae; Acaryochloris.
OX   NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW25585.1, ECO:0000313|Proteomes:UP000000268};
RN   [1] {ECO:0000313|EMBL:ABW25585.1, ECO:0000313|Proteomes:UP000000268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBIC 11017 {ECO:0000313|Proteomes:UP000000268};
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA   Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA   Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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; CP000828; ABW25585.1; -; Genomic_DNA.
DR   RefSeq; WP_012161187.1; NC_009925.1.
DR   AlphaFoldDB; B0CC43; -.
DR   STRING; 329726.AM1_0533; -.
DR   KEGG; amr:AM1_0533; -.
DR   eggNOG; COG1239; Bacteria.
DR   eggNOG; COG1240; Bacteria.
DR   HOGENOM; CLU_016684_6_2_3; -.
DR   OrthoDB; 9775079at2; -.
DR   UniPathway; UPA00668; -.
DR   Proteomes; UP000000268; 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|ARBA:ARBA00023171,
KW   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|ARBA:ARBA00022531,
KW   ECO:0000256|RuleBase:RU362087};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000268}.
FT   DOMAIN          486..677
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   REGION          337..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..356
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..387
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   682 AA;  73808 MW;  6F4F9B8ED49FF5D1 CRC64;
     MPVAELPQKI TTFPLTAVVG QEAIKLALLL TAVDPTLGGV VIAGRRGTAK SVMARAVHAL
     LPPIEVVKGS ICQGDPEDTS AWDDDLLASL EAGAIPIVDG QPQPETEIIP TPFVQVPLGV
     TEDRLLGSVD VSQSVKLGET VFQPGLLAEA NRGVLYVDEI NLLDDQISNL LLTSLTEGRN
     QIEREGLSFQ HPCSTIFIAT YNPEEGPLRE HLLDRIAISL SADQMLGLDL RVQAVEQATA
     YANSPQAFLA QYEDETDDLK TQILLAREWL KDVQIQHSQI VYLVDEALRG GVQGHRAELF
     AVRVAKAHAA LNGRSEVTAE DLRRAVELVI VPRATVIDAP PPEQPQPPPP PPPQQDNSDQ
     SDQDEEEEDD QNEEDPPEPE EPPSIPEEFV FDPDGVVLDP QVLYFAQNAS RQGKSGSRSI
     VFSEDRGRYV KPMLPKGGVK RIAVDATLRA AAPYQKARRL RHPNRRVIVE QSDVRTKRLA
     RKAGALVVFV VDASGSMALN RMQSAKGAVM RLLTEAYQNR DQVSLIPFRG ERADVLLPPT
     RSIEAARRRL DTLPCGGGSP LAHGLTQAVR VGMNALSSGD IGQVVLVAIT DGRGNIPLTT
     SLGEPPVDGE KPDIKAELLE IAGRIRALNL KLLVIDTENK FISTGFAKEL AQNAGGNYYH
     LPKATDQAIA AVTQDAISNL TG
//
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