ID   P73020_SYNY3            Unreviewed;      1331 AA.
AC   P73020;
DT   01-FEB-1997, integrated into UniProtKB/TrEMBL.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=magnesium chelatase {ECO:0000256|ARBA:ARBA00012825};
DE            EC=6.6.1.1 {ECO:0000256|ARBA:ARBA00012825};
GN   Name=chlH {ECO:0000313|EMBL:BAA17040.1};
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708 {ECO:0000313|EMBL:BAA17040.1, ECO:0000313|Proteomes:UP000001425};
RN   [1] {ECO:0000313|EMBL:BAA17040.1, ECO:0000313|Proteomes:UP000001425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa {ECO:0000313|Proteomes:UP000001425};
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2] {ECO:0007829|PDB:4ZHJ}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
RX   PubMed=27250678; DOI=10.1038/nplants.2015.125;
RA   Chen X., Pu H., Fang Y., Wang X., Zhao S., Lin Y., Zhang M., Dai H.,
RA   Gong W., Liu L.;
RT   "Crystal structure of the catalytic subunit of magnesium chelatase.";
RL   Nat. Plants 1:15125-15125(2015).
RN   [3] {ECO:0007829|PDB:6YSG, ECO:0007829|PDB:6YT0}
RP   X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS).
RX   PubMed=33257858; DOI=10.1038/s41477-020-00806-9;
RA   Adams N.B.P., Bisson C., Brindley A.A., Farmer D.A., Davison P.A.,
RA   Reid J.D., Hunter C.N.;
RT   "The active site of magnesium chelatase.";
RL   J. Am. Chem. Soc. 6:1491-1502(2020).
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   -!- INTERACTION:
CC       P73020; Q55525: rpoD; NbExp=4; IntAct=EBI-1611912, EBI-1613647;
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunit H family.
CC       {ECO:0000256|ARBA:ARBA00010851}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000022; BAA17040.1; -; Genomic_DNA.
DR   PIR; S75000; S75000.
DR   PDB; 4ZHJ; X-ray; 2.50 A; A/B=1-1331.
DR   PDB; 6YSG; X-ray; 2.54 A; A/B=1-1331.
DR   PDB; 6YT0; X-ray; 2.85 A; A/B=1-1331.
DR   PDB; 6YTJ; X-ray; 2.79 A; AAA/BBB=1-1331.
DR   PDB; 6YTN; X-ray; 2.70 A; AAA/BBB=1-1331.
DR   PDBsum; 4ZHJ; -.
DR   SMR; P73020; -.
DR   DIP; DIP-48797N; -.
DR   IntAct; P73020; 5.
DR   STRING; 1148.gene:10497901; -.
DR   PaxDb; 1148-1652115; -.
DR   EnsemblBacteria; BAA17040; BAA17040; BAA17040.
DR   KEGG; syn:slr1055; -.
DR   eggNOG; COG1429; Bacteria.
DR   InParanoid; P73020; -.
DR   PhylomeDB; P73020; -.
DR   SABIO-RK; P73020; -.
DR   Proteomes; UP000001425; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4ZHJ, ECO:0007829|PDB:6YSG};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023171};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001425}.
FT   DOMAIN          24..187
FT                   /note="Magnesium chelatase subunit H N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11965"
SQ   SEQUENCE   1331 AA;  148555 MW;  DD58A4693295F1E5 CRC64;
     MFTNVKSTIR RVDPEALNGR QLLKVVYVVL ESQYQSALSA AVRNINRTNS SLAIQLTGYL
     IEELRDPENY ANFKHDVSEA NLFIASLIFI EDLADKVVEA VTPYRDNLDA AIVFPSMPQV
     MRLNKMGSFS MAQLGQSKSA IAQFMKKRKE NSSGAGFQDA MLKLLRTLPT VLKYLPVEKA
     QDARNFMLSF QYWLGGSQEN LENFLLMLTD KYVYPDLGLD KLVNYQEPVV YPDMGIWHPL
     SMQMFENVKD YLEWYNQRPD ISEDLKDPLA PCIGLIMQRT HLVTGDDAHY VGMVQELEAM
     GARVICVFSG GLDFSKPVNE YFWDKSVNGV EPLPIVDAVV SLTGFALVGG PARQDHPRAI
     ESLKKLNRPY MCALPLVFQT TEEWEASDLG LHPIQVALQI AIPELDGAIE PIILSGRDGS
     TGRAIALQDR LEAIAQRAMK WANLRKKPKL DKKVAITVFS FPPDKGNVGT AAYLDVFGSI
     YEVMKGLQGN GYDVQDLPGS AKELMEAVIH DAQAQYNSPE LNIAHRMSVE QYERLTPYSV
     RLEENWGKPP GHLNSDGQNL LIYGKEFGNV FIGVQPTFGY EGDPMRLLFS RSASPHHGFA
     AYYTYLNHIW KADAVLHFGT HGSLEFMPGK QMGMSGECYP DNLIGTIPNL YYYAANNPSE
     ATIAKRRGYA STISYLTPPA ENAGLYKGLQ ELNELIGSYQ TLKDSGRGIQ IVNTIMDQAR
     ICNLDQDVNL PDINAEEMDQ GQRDTIVGSV YRKLMEIESR LLPCGLHVIG QPPSAEEAIA
     TLVNIASLDR EDEGIWALPT LIAESIGRNM EEIYRNSDKG ILADVELLQD ITLATRAAVA
     ALVQEQINAD GRVSFVSKLN FFKIGKKAPW VKSLCDSGYP NVNEEKLKPL FEYLEFCLEQ
     VCADNEFGGL LQALEGEYVL PGPGGDPIRN PNVLPTGKNI HALDPQSIPT LAAVQSAKVV
     VDRLLERQRA ENGGNYPETI ASVLWGTDNI KTYGESLAQI MWMVGAKPVP DALGRVNKIE
     LVPLEELGRP RIDVVVNCSG VFRDLFINQM NLLDQAVKLA AEADEPLEMN FVRKHALEQA
     EEMGIGVREA ATRIFSNASG SYSSNVNLAV ENSSWEDESE LQEMYLKRKS FAFNSDNPGM
     MDQNRDMFER ALKTADATFQ NLDSSEISLT DVSHYFDSDP TKLISTLRDD GKAPAAYIAD
     TTTANAQVRT LSETVRLDAR TKLLNPKWYE GMLSHGYEGV RELSKRLVNT MGWSATAGAV
     DNWVYEDANS TFIKDEEMCK RLMDLNPNSF RRMVSTLLEV NGRGYWETSD ENLERLQELY
     QEVEDRIEGV E
//