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Database: UniProt/TrEMBL
Entry: K9QR35_NOSS7
LinkDB: K9QR35_NOSS7
Original site: K9QR35_NOSS7 
ID   K9QR35_NOSS7            Unreviewed;      1239 AA.
AC   K9QR35;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=magnesium chelatase {ECO:0000256|ARBA:ARBA00012825};
DE            EC=6.6.1.1 {ECO:0000256|ARBA:ARBA00012825};
GN   OrderedLocusNames=Nos7524_1986 {ECO:0000313|EMBL:AFY47843.1};
OS   Nostoc sp. (strain ATCC 29411 / PCC 7524).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=28072 {ECO:0000313|EMBL:AFY47843.1, ECO:0000313|Proteomes:UP000010378};
RN   [1] {ECO:0000313|Proteomes:UP000010378}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29411 / PCC 7524 {ECO:0000313|Proteomes:UP000010378};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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; CP003552; AFY47843.1; -; Genomic_DNA.
DR   RefSeq; WP_015138291.1; NC_019684.1.
DR   AlphaFoldDB; K9QR35; -.
DR   STRING; 28072.Nos7524_1986; -.
DR   KEGG; nop:Nos7524_1986; -.
DR   PATRIC; fig|28072.8.peg.2161; -.
DR   eggNOG; COG1429; Bacteria.
DR   HOGENOM; CLU_002017_1_2_3; -.
DR   OrthoDB; 9757976at2; -.
DR   Proteomes; UP000010378; 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; 2.
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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010378}.
FT   DOMAIN          3..159
FT                   /note="Magnesium chelatase subunit H N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11965"
SQ   SEQUENCE   1239 AA;  138465 MW;  DD07AA40F189FA1A CRC64;
     MKRIVLIAGF ESFNADLYRK AAIVAKSRCP DLDIRVFSDR DITSIRPEVE AALQGADVFF
     GSLIFDYDQV LWLRDRISQI PIRLVFESAL ELMSLTQIGA FAIGDKPKGM PKPVKFILDK
     FSNGREEDKL AGYISFLKIG PKLLKFVPVQ KVQDLRNWLI IYGYWNAGGT ENVAALFWTL
     AEKYLDLKVG EIPPPIETPN IGLLHPDYQG FFTSPKAYLE WYQKRSSPCS LPPAPCPLPP
     TPCPLPPAPC PPITAILLYR KHVITKQPYI PQLIRRFEEA GLIPLPIFIN GVEGHVAVRD
     WITTDYELQQ RQQGKIETPS LSQEAVKVDA IVSTIGFPLV GGPAGSMEAG RQVEVAKRIL
     TAKNVPYIVA APLLIQDIHS WTRQGVGGLQ SVVLYALPEL DGAIDTVPLG GLVGEDIYLV
     PERVQRLIGR VKNWVKLRQT PPAERKIAII LYGFPPGYGA VGTAALLNVP RSLIKLLHAL
     KDQGYNVGDI PEDGEELIRQ VREIDEEMER WEINKPFPSS ATTVNARKLE KWLGYLRTSR
     IEKQWKSLTG SGIKTYGDEL HVGGVQLGNV WIGIQPPLGI QGDPMRLMFE RDLTPHPQYA
     AFYKWLQNEL QADAVIHFGM HGTVEWLPGS PLGNTGYSWS DILLGDLPNL YIYAANNPSE
     SILAKRRGYG VLISHNVPPY GRAGLYKELV ALRDLISEYR EDPKKNYVLK EGICKKIVDT
     GLDVDCPFED AKKLGIPFTP ENIKMFSAHA FDDYLVKLYE YLQVLETRLF SSGLHILGEP
     PNEEELASYL EAYFGQEQPK NPEEAQQIKD LLMQTTDEIT NLLRGLNGEF IPPAPGGDLL
     RDGAGVLPTG RNIHALDPYR MPSPAAYERG REIGQKIISQ HLQEHGKYPE TVAVLLWGLD
     AIKTKGESLG ILLELVGAEP VKEGTGRIVR YELKSLSEVG HPRIDVLGNL SGIFRDSFVN
     IIELLDDLFQ RAAEADEPED QNFIKKHALA LKAQGVENTS ARLFSNPAGD FGSLVNDRVV
     DGNWESGDEL GKTWQSRNVF SYGRQDKGQA RPEVLNQLLQ TSDRIVQEID SVEYGLTDIQ
     EYYANTGGLK KAAEQRSGKK VTASFVESFS KDTTPRNLDD LLRMEYRTKL LNPKWAEAMA
     NQGSGGAFEI SQRMTALIGW GGTADFKDDW VYDQAADTYA LDPEMAEKLR QANPEAFRNI
     VSRMLEAHGR GFWQADTDKL DKLRQLYELT DEQLEGVTV
//
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