ID   E6VJI2_RHOPX            Unreviewed;      1248 AA.
AC   E6VJI2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=magnesium chelatase {ECO:0000256|ARBA:ARBA00012825};
DE            EC=6.6.1.1 {ECO:0000256|ARBA:ARBA00012825};
GN   OrderedLocusNames=Rpdx1_3976 {ECO:0000313|EMBL:ADU45532.1};
OS   Rhodopseudomonas palustris (strain DX-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=652103 {ECO:0000313|EMBL:ADU45532.1, ECO:0000313|Proteomes:UP000001402};
RN   [1] {ECO:0000313|Proteomes:UP000001402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DX-1 {ECO:0000313|Proteomes:UP000001402};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Misra M., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Logan B., Oda Y., Harwood C.,
RA   Woyke T.;
RT   "Complete sequence of Rhodopseudomonas palustris DX-1.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Porphyrin-containing compound metabolism.
CC       {ECO:0000256|ARBA:ARBA00023444}.
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunit H family.
CC       {ECO:0000256|ARBA:ARBA00010851}.
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DR   EMBL; CP002418; ADU45532.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6VJI2; -.
DR   STRING; 652103.Rpdx1_3976; -.
DR   KEGG; rpx:Rpdx1_3976; -.
DR   eggNOG; COG1429; Bacteria.
DR   HOGENOM; CLU_002017_1_2_5; -.
DR   OrthoDB; 9757976at2; -.
DR   BioCyc; RPAL652103:RPDX1_RS19625-MONOMER; -.
DR   Proteomes; UP000001402; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   CDD; cd10150; CobN_like; 1.
DR   InterPro; IPR011771; BchH.
DR   InterPro; IPR003672; CobN/Mg_chltase.
DR   InterPro; IPR022571; Mg_chelatase_H_N.
DR   NCBIfam; TIGR02025; BchH; 1.
DR   PANTHER; PTHR44119; MAGNESIUM-CHELATASE SUBUNIT CHLH, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR44119:SF1; MAGNESIUM-CHELATASE SUBUNIT CHLH, CHLOROPLASTIC; 1.
DR   Pfam; PF02514; CobN-Mg_chel; 1.
DR   Pfam; PF11965; DUF3479; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023171};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ADU45532.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531}.
FT   DOMAIN          14..172
FT                   /note="Magnesium chelatase subunit H N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11965"
SQ   SEQUENCE   1248 AA;  135833 MW;  BFE9CAE94DF23919 CRC64;
     MPKRTSPADK TPVRVVIVTL DSHLSGAAAR ARNALRKDYP GIELTVHSAD EWGGDINALQ
     RCLADIATGD IIIATMLFMD DHVRAVMPAL QARRNDCDAL VCCMSAAEVV KLTRIGKFDM
     SAEALGMINW LKKLRGKKTE GSAGKGEMKM LRQLPKLLRF VPGTAQDMRA YFLTLQYWLA
     GCEQNIANMV RLLIDRYASG PRKGLRGVAK VEPPLDYADI GVYHPKMKGR IAETADKLPP
     GPADAKGTVG VLLLRSYLLA GNAGHYDGML ETFEAKGLRV IPVFASGLDQ RPAIEKFFIK
     NGRPVVDAVV SLTGFSLVGG PAYNDSKAAE DILTALDVPY LSAHPVEFQT LEQWAASDRG
     LMPVESTIMV AIPELDGCSN PMVYGGRSDG GDIACPGCEK FCKFDRNESG GDMYVCAERA
     EMLASRTARL IALRRSERKD RKIAAVLFNF PPNAGNTGTA AFLGVFESLF NTLKAMKAEG
     YTVEVPESVD ALREAIITGN AARFGSTANV HARVMAGDHV KAERYLREIE GQWGPAPGKQ
     QSDGSSIFIL GERFGNVFVG VQPAFGYEGD PMRLLFEKGF APTHAFSAFY RWIKQDFGAH
     AVLHFGTHGA LEFMPGKQTG LSGTCWPDRM IGDLPNMYLY ASNNPSEGAI AKRRSAATLV
     SYLTPPVAHA GLYRGLLELK SSLERWRGLT PEEETERENL ATLVQAQAAG LDLAAAEPAW
     TAEEAGTTIA KLADAVLEME YALIPHGLHV VGNVPSEEER VETLEAVADA MHGKRPDKSV
     LEALVRGGHP EHLSGNGPEA QANLDMLKEL AGIDKLLAED HELAAILRAL DGKFIRPAPG
     GDLLRTPAVL PTGRNLHGFD PFRIPSAYAL QDGAKQAQRL IDKHVAEGNP LPETVAIVLW
     GTDNLKNEGA PIGQALALMG ARPRFDGYGR LAGADLIPLE ELGRPRIDVI ITMSGIFRDL
     LPLQIKLLAE AAFMAASAEE PAEQNFIRKH SLAYQAEHKC DMETASLRVF GNADGAYGSN
     VNHLVENSRW EDEDELAETY TKRKSFAYGL KGQPVQHAEL LKSALADVDL AYQNLDSVEL
     GVTTVDHYFD TLGGISRAVR KAKGGQAAPV YIGDQTRGAG TVRTLSEQVA LETRTRMLNP
     KWYEGMLKHG YEGVRQIEEH VTNTMGWSAT TGEVAPWVYK QLTETFVLDP EMRARLAALN
     PVASAKVANR LIEAHERNYW SPDPEMLETL RKAGEELEDR LEGVGVAA
//