ID A0A2S6NJ22_RHOGL Unreviewed; 604 AA.
AC A0A2S6NJ22;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|RuleBase:RU362087};
DE EC=6.6.1.1 {ECO:0000256|RuleBase:RU362087};
GN ORFNames=CCS01_09835 {ECO:0000313|EMBL:PPQ34709.1};
OS Rhodopila globiformis (Rhodopseudomonas globiformis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Rhodopila.
OX NCBI_TaxID=1071 {ECO:0000313|EMBL:PPQ34709.1, ECO:0000313|Proteomes:UP000239724};
RN [1] {ECO:0000313|EMBL:PPQ34709.1, ECO:0000313|Proteomes:UP000239724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 161 {ECO:0000313|EMBL:PPQ34709.1,
RC ECO:0000313|Proteomes:UP000239724};
RX PubMed=29423563;
RA Imhoff J.F., Rahn T., Kunzel S., Neulinger S.C.;
RT "New insights into the metabolic potential of the phototrophic purple
RT bacterium Rhodopila globiformis DSM 161(T) from its draft genome sequence
RT and evidence for a vanadium-dependent nitrogenase.";
RL Arch. Microbiol. 0:0-0(2018).
CC -!- FUNCTION: Involved in bacteriochlorophyll biosynthesis; introduces a
CC 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 -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC biosynthesis. {ECO:0000256|RuleBase:RU362087}.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000256|RuleBase:RU362087}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PPQ34709.1}.
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DR EMBL; NHRY01000092; PPQ34709.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6NJ22; -.
DR OrthoDB; 9775079at2; -.
DR UniPathway; UPA00669; -.
DR Proteomes; UP000239724; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030494; P:bacteriochlorophyll 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; IPR041702; BchD/ChlD_VWA.
DR InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR InterPro; IPR011776; Mg_chelatase_ATPase-dsu.
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; PF13519; VWA_2; 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|RuleBase:RU362087};
KW Bacteriochlorophyll biosynthesis {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|RuleBase:RU362087};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531,
KW ECO:0000256|RuleBase:RU362087};
KW Reference proteome {ECO:0000313|Proteomes:UP000239724}.
FT DOMAIN 422..602
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 273..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 64161 MW; 22410127873E5D30 CRC64;
MSGAAASGAA NWAAALQSLS LFAADPIGLG GISLRAGAGP VRDRWLKILY DSLPPEMPLR
RVPLNAGDDR LLGGLDLAAT LQAGRLIEQK GLLSEANGGV IVLAMAERIE LGAAARLRSV
FDEGVVTLQR DGLSRVLPAR FAMVALDEGA DVDERPPASL LDRMAFLVDL TNVSLRDIDF
DDWTGTESLK ARRDAVAEER APPVVIHAGN QAETDKAVET LCNVAAALGV DSIRAPLYAL
RAARVAAAQD GRTEVDQDDL SLAVALVYGP RATRLPQQQQ PEEAPPEPEP PPEDQQEPPP
PDDDDDKDKI PDLPLEDIVL EAALATLPPD LLSQLASMSG RGQVRMPGRV GQAKMSLKRG
RPIGTRQGEP KGGARLHLLE TLKAAAPWQT LRRHAREHKS ERFEVRRDDF RIIRFRQRIG
TTTVFAVDAS GSAAMNRLGE AKGAVELLLA DCYVRRDQVA LIAFRGLGAQ LLLPPTSSLV
RAKRSLAGLP GGGPTPLAAG IEAATALAES IRRGGRTPVI TLLTDARANI GRDGLGGRPK
AEAEALESAR ALRALGIATL LVDTSPRPNP FARTLAAEMN ARYVPLPYAN ANALTNAVRS
AAGV
//
