UniProt: A0A3D9BWU3

Database: UniProt
Entry: A0A3D9BWU3_9RHOB

LinkDB:  A0A3D9BWU3_9RHOB 
Original site:  A0A3D9BWU3_9RHOB

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (17)   

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ID   A0A3D9BWU3_9RHOB        Unreviewed;       559 AA.
AC   A0A3D9BWU3;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|RuleBase:RU362087};
DE            EC=6.6.1.1 {ECO:0000256|RuleBase:RU362087};
GN   ORFNames=DRV84_06530 {ECO:0000313|EMBL:REC57821.1};
OS   Rhodosalinus sediminis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodosalinus.
OX   NCBI_TaxID=1940533 {ECO:0000313|EMBL:REC57821.1, ECO:0000313|Proteomes:UP000257131};
RN   [1] {ECO:0000313|EMBL:REC57821.1, ECO:0000313|Proteomes:UP000257131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WDN1C137 {ECO:0000313|EMBL:REC57821.1,
RC   ECO:0000313|Proteomes:UP000257131};
RX   PubMed=29043957; DOI=10.1099/ijsem.0.002424;
RA   Guo L.Y., Ling S.K., Li C.M., Chen G.J., Du Z.J.;
RT   "Rhodosalinus sediminis gen. nov., sp. nov., isolated from marine
RT   saltern.";
RL   Int. J. Syst. Evol. Microbiol. 67:5108-5113(2017).
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:REC57821.1}.
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DR   EMBL; QOHR01000005; REC57821.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D9BWU3; -.
DR   OrthoDB; 9775079at2; -.
DR   UniPathway; UPA00669; -.
DR   Proteomes; UP000257131; 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; 3.40.50.410; 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:UP000257131}.
FT   DOMAIN          377..557
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   REGION          227..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..270
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   559 AA;  58872 MW;  E5D393D21CC046AA CRC64;
     MSEGAARWAR ALRALALFAV DPQGLRGLTV RARVGPVRQR FEALLSALDG EAHRIHPEIG
     DPELYGGLDV TATLAAGRPV MAGGLADRPS RLILPMAERA APDLAARLAQ LLDASPGHSL
     VLLDEGAEPD ERAPAALAER LALSLDLDGI GRLEAKGDLP WTAIAEARAR LPDVAIPEEV
     APALTALAAR FGIDSLRAPL LALRAARAEA ALEGRETVTE DDIRAAAELV YPDRATRTPE
     PPPEEDETPP EDTPEPEPES EQDDDGDLGD LPEEMLVEAV AALLPPDLLT RLAEGGATRA
     AKGSGAGAKR RGNRRGRPLP SRPGRPGGRE RVDLVATLRA AAPWQTIRRR QQPDAGRVLV
     HASDVRLRRY EDRSDRLVIF AVDASGSLAM TRLNEAKGAV ELLLGEAYSR RDHVALIAFR
     GTEAELLLPP TRSLVQTKRR LAALPGGGGT PLAAGLQAAG LLAHQSEGRG LSPRVALLTD
     GRANVALDGA GGRAQAMEDA ARTARALRGQ GLSALVIDTA ARRGEAGRQL AEALGAGYLA
     LPRADARRLS GAVAEALED
//

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