ID K9XY08_STAC7 Unreviewed; 1255 AA.
AC K9XY08;
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=Sta7437_3486 {ECO:0000313|EMBL:AFZ36986.1};
OS Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Dermocarpellaceae;
OC Stanieria.
OX NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ36986.1, ECO:0000313|Proteomes:UP000010473};
RN [1] {ECO:0000313|Proteomes:UP000010473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29371 / PCC 7437 {ECO:0000313|Proteomes:UP000010473};
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; CP003653; AFZ36986.1; -; Genomic_DNA.
DR RefSeq; WP_015194648.1; NC_019748.1.
DR AlphaFoldDB; K9XY08; -.
DR STRING; 111780.Sta7437_3486; -.
DR KEGG; scs:Sta7437_3486; -.
DR PATRIC; fig|111780.3.peg.3613; -.
DR eggNOG; COG1429; Bacteria.
DR HOGENOM; CLU_002017_1_2_3; -.
DR OrthoDB; 9757976at2; -.
DR Proteomes; UP000010473; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AFZ36986.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW Reference proteome {ECO:0000313|Proteomes:UP000010473}.
FT DOMAIN 3..159
FT /note="Magnesium chelatase subunit H N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11965"
FT COILED 811..845
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1255 AA; 140764 MW; E43188E9725BA5CE CRC64;
MKRIVLIAGF ESFNATLYRQ AAQISTSRCN ELEIEVFSDR DITSSSDKIE NALQDADVFF
ASLIFDYDQV MWLRQRVEHI AIRLVFESAL ELMSLTRLGK FVIGDKPKGM PKPVQFILSK
FSNSREEDKL AGYLSFLKTG PKLLKYIPAK KVQDLRNWLI IYGYWNAGGT ENVAAMFWTI
AEKYLGLKVG EIPSVIETPN MGLLHPDYPG YFTSPKDYLD WYQNHVGANH RSSLPTIGIL
LYRKHVITKQ PYIPQLISYF EAEGLIPLPI FINGVEGHVA VRDWLTTNYE QLQREKDNKE
ILSLSENAVK VDAIISTIGF PLVGGPAGSM EAGRQVEVAK RILSAKNIPY IVAAPLLIQD
IHSWTRQGIG GLQSVVLYSL PELDGAIDTV PLGGLVGEDI YLIPERVKRL TGRIKNWIKL
KQTQPKDRKI AIILYDFPPG YGATGTAALL NVPKSLLNFL IALKEQGYNV GELPQDGEEI
INQVKQADTT DLHLSLENFT GNGIKTDGKG QVAINVRTLE KWLGYLLTTR VEKQWKSLTD
TGIKTYGDDF HLGGIQLGNI WIGVQPPLGL SGDPMRLMFE KDLTPHPQYA AFYKWLQNDF
QANAVVHFGM HGTVEWLPGS PLGNTGYSWS DILLGNLPNL YIYAANNPSE SLLAKRRGYG
VLISHNVPPY GRAGLYKELI SLRDLITEYR ENTEKNYLLK DIICQKIIDT GLDADCKFTE
GEKLGIAFNV ENAKLFSKKV INEYFVKIYE YLQVVEQRLF SSGLHVLGNA PNDEKLKSYL
EAYFGDDLSV ELIELIIAHK DAEAQRIVET QHIASNQLEE AQKIRDLLEQ NRDELTNLLR
GLNGEYIPPA PGGDLLRDGS GVLPTGRNIH ALDPYRMPSP AAYERGKEIA KKIIAQHLEE
KGNYPETVAV MLWGLDAIKT KGESLGILLE LVGAEPVKEG TGRIVRYELK SLAEIGHPRI
DVLANLSGIF RDTFVNIIEL LDDLLQRAAE ADESPEDNFI RKHYLALKSQ GIENASARLF
SNPTGDFGSL VNDQVVDGNW ESGEELANTW KNRNVFSYGR KDKGQARPEI LNQLLQTSER
IVQEIDSVEY GLTDIQEYYG NTGGLKLAAE KQSGKQVEAS FVESFSKDTN PRKLKDLLRL
EYRTKLLNPK WAEAMSNQGS GGAYEISQRM TALVGWGGTA NFRDDWVYDQ AADTYALDAE
MAAKLREANP EAFRNIVGRM IEAHGRGFWD ADEEKLQKLR ELYNLTEDEL EGVTV
//
