CHLD_SYNE7
ID CHLD_SYNE7 Reviewed; 677 AA.
AC O07345; Q31KW5;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Magnesium-chelatase subunit ChlD;
DE Short=Mg-chelatase subunit D;
DE EC=6.6.1.1;
DE AltName: Full=Mg-protoporphyrin IX chelatase;
GN Name=chlD; OrderedLocusNames=Synpcc7942_2274;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Masuda T., Nakayama M., Ohta H., Takayama K.;
RT "Cloning and sequencing of a chlD gene encoding a subunit of magnesium-
RT chelatase from the cyanobacterium Synechococcus sp. PCC 7942.";
RL (er) Plant Gene Register PGR97-091(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in chlorophyll biosynthesis; introduces a magnesium
CC ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
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 -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000305}.
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DR EMBL; AB003135; BAA20346.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB58304.1; -; Genomic_DNA.
DR RefSeq; WP_011244135.1; NC_007604.1.
DR AlphaFoldDB; O07345; -.
DR SMR; O07345; -.
DR STRING; 1140.Synpcc7942_2274; -.
DR PRIDE; O07345; -.
DR EnsemblBacteria; ABB58304; ABB58304; Synpcc7942_2274.
DR KEGG; syf:Synpcc7942_2274; -.
DR eggNOG; COG1239; Bacteria.
DR eggNOG; COG1240; Bacteria.
DR HOGENOM; CLU_016684_6_2_3; -.
DR OMA; YYHLPKA; -.
DR OrthoDB; 1068772at2; -.
DR BioCyc; SYNEL:SYNPCC7942_2274-MON; -.
DR UniPathway; UPA00668; -.
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-UniPathway.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR CDD; cd01451; vWA_Magnesium_chelatase; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.410; -; 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 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; SSF52540; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR TIGRFAMs; TIGR02031; BchD-ChlD; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chlorophyll biosynthesis; Ligase; Nucleotide-binding;
KW Photosynthesis.
FT CHAIN 1..677
FT /note="Magnesium-chelatase subunit ChlD"
FT /id="PRO_0000206855"
FT DOMAIN 481..676
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 325..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..347
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..371
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 207..208
FT /note="IA -> MP (in Ref. 1; BAA20346)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="E -> K (in Ref. 1; BAA20346)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="S -> L (in Ref. 1; BAA20346)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 677 AA; 73299 MW; 9CD691159022EF13 CRC64;
MIAAAPSPTA FPLPAVVGQG PIKLALILAA VDPGLGGVAI AGRRGTAKSV MARALHALLP
PIEILENSFN ADPNRAGDWD ALTQQRQANG EELPTRVIPA PFCQVPLGIT EDRLLGSVDV
AQSIKRGETV FQPGLLAEAH RGVLYVDEIN LLDDQIANLL LTAISEGRNR IEREGISIEH
ACRPLLIATY NPEEGPLRLH LLDRIAIALS ADAILEIEER VQAVDQALRY ANDPAKVLEA
YAEETESLRT QILLAREWLP DVTITPEQIG YLVREAIRGQ VQGHRAELFA VRVARAAAAL
EGRTEVNADD LRLAVQLVIV PRATVLDSPP PPEEPPAAPP PPPPSQEQQG EDEQNEQEPD
EPDEPENDSD DQQPDTPPPI PEEFVFDAEG VVLDPSVLVF AQQFSRQGKS GSRSLIFSED
RGRYIKPMLP RGPVRRIAVD ATLRASAPYQ KARRQRQPDR KVIVEDADIR SKQLVRKAGA
LVIFLVDASG SMALNRMQSA KGAVIRLLTE AYENRDQVAL IPFRGEQAEV LLPPTRSITA
ARKRLEKMPC GGGSPLAHGL TQAVRVGTNA AQSGDIGQVV IVAITDGRGN IPLARSLGQP
MEEGEKPDLK EELLDIAKRI RGLSMQLLVI DTERKFVGAG FGKELANAAG GQYYHLPKVS
DQAIAAMAQS ALRATLN
