ID K9SST6_9SYNE Unreviewed; 659 AA.
AC K9SST6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|RuleBase:RU362087};
DE EC=6.6.1.1 {ECO:0000256|RuleBase:RU362087};
GN ORFNames=Syn7502_00688 {ECO:0000313|EMBL:AFY72834.1};
OS Synechococcus sp. PCC 7502.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1173263 {ECO:0000313|EMBL:AFY72834.1, ECO:0000313|Proteomes:UP000010385};
RN [1] {ECO:0000313|EMBL:AFY72834.1, ECO:0000313|Proteomes:UP000010385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7502 {ECO:0000313|EMBL:AFY72834.1,
RC ECO:0000313|Proteomes:UP000010385};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Synechococcus sp. PCC 7502.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in chlorophyll biosynthesis. Catalyzes the insertion
CC of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
CC {ECO:0000256|RuleBase:RU362087}.
CC -!- FUNCTION: Involved in chlorophyll biosynthesis; introduces a magnesium
CC ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
CC {ECO:0000256|ARBA:ARBA00003398}.
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; chlorophyll
CC biosynthesis. {ECO:0000256|RuleBase:RU362087}.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000256|ARBA:ARBA00005799, ECO:0000256|RuleBase:RU362087}.
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DR EMBL; CP003594; AFY72834.1; -; Genomic_DNA.
DR RefSeq; WP_015167493.1; NC_019702.1.
DR AlphaFoldDB; K9SST6; -.
DR STRING; 1173263.Syn7502_00688; -.
DR KEGG; synp:Syn7502_00688; -.
DR PATRIC; fig|1173263.3.peg.707; -.
DR eggNOG; COG1239; Bacteria.
DR eggNOG; COG1240; Bacteria.
DR HOGENOM; CLU_016684_6_2_3; -.
DR OrthoDB; 9775079at2; -.
DR UniPathway; UPA00668; -.
DR Proteomes; UP000010385; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015995; P:chlorophyll 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041702; BchD/ChlD_VWA.
DR InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR InterPro; IPR011776; Mg_chelatase_ATPase-dsu.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
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; PF01078; Mg_chelatase; 1.
DR Pfam; PF13519; VWA_2; 1.
DR SMART; SM00382; AAA; 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|ARBA:ARBA00022840, 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|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362087};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531,
KW ECO:0000256|RuleBase:RU362087};
KW Reference proteome {ECO:0000313|Proteomes:UP000010385}.
FT DOMAIN 463..654
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 316..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..338
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..359
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 659 AA; 71322 MW; AD990E26F9F07187 CRC64;
MGQNLTFPIS AVVGQEAIKT ALLLASIDPM LGGVAIAGRR GTAKSVLARG VHALLPPIEI
VANSISNCDP TKPETWDSAT NPDIVETKVI PAPFIQIPLG ITEDRLIGSV DVAKSVQQGK
TIFQPGLLAE ANRGVLYVDE INLLDPQISN LLLATLSNGV NQIEREGISF QHPCEPILIA
TYNPEEGALG KHLLDRIAIH LSADEVLGID DRVEAVDMAI SYANSPASFL AQYQGNLDNL
RTQIILAREW LKDVQISSAQ INYLVQEAIR GGVQGHRAEL FALRVAKALA ALDSRVNVNA
DDLRTAVELV IVSRSTIKPE QQQPQPPNAP PPPPQNSNQD QENPEEPEDE EEPEETQEPP
SIPEEFLFDP EGVILDPEVM YFAQTFTKQG NSGSRSLIYS QDRGRYIKPV LPQGKGDRIA
VDATLRACAP YQKARRLRNP HRKVIVENPD IRAKKLARKA GALVIFLVDA SGSMSLNRMQ
SAKGAVLRLL TEAYQNRDQV SLIPFRGEQA EVLLPPTRSI EAAKIRLDVL PCGGGSPLAH
GLTQAVRVGI NAKASGDIGQ VMIVAVTDGR GNISLGRSLG ETIDPENKPN IKEELLEIAK
KVRALGIALL VIDTENKFVS TGFAKELAAA AAGKYYHLPK ASDQAIANVT RNAINDMRN
//
