CHLD_SYNY3
ID CHLD_SYNY3 Reviewed; 676 AA.
AC P72772; Q55100;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 139.
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=slr1777;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8663186; DOI=10.1074/jbc.271.28.16662;
RA Jensen P.E., Gibson L.C.D., Henningsen K.W., Hunter C.N.;
RT "Expression of the chlI, chlD, and chlH genes from the Cyanobacterium
RT synechocystis PCC6803 in Escherichia coli and demonstration that the three
RT cognate proteins are required for magnesium-protoporphyrin chelatase
RT activity.";
RL J. Biol. Chem. 271:16662-16667(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
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).
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}.
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; X96599; CAA65418.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA16787.1; -; Genomic_DNA.
DR PIR; S74635; S74635.
DR PIR; T46870; T46870.
DR AlphaFoldDB; P72772; -.
DR SMR; P72772; -.
DR IntAct; P72772; 5.
DR STRING; 1148.1651860; -.
DR PaxDb; P72772; -.
DR EnsemblBacteria; BAA16787; BAA16787; BAA16787.
DR KEGG; syn:slr1777; -.
DR eggNOG; COG1239; Bacteria.
DR eggNOG; COG1240; Bacteria.
DR InParanoid; P72772; -.
DR OMA; YYHLPKA; -.
DR PhylomeDB; P72772; -.
DR SABIO-RK; P72772; -.
DR UniPathway; UPA00668; -.
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-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; Reference proteome.
FT CHAIN 1..676
FT /note="Magnesium-chelatase subunit ChlD"
FT /id="PRO_0000206854"
FT DOMAIN 481..672
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 328..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..349
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..377
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 302
FT /note="A -> P (in Ref. 1; CAA65418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 676 AA; 73665 MW; 923276AF9F45F92B CRC64;
MTTLTPFIPL NFPITAIVGQ EAIKLALLLG AIDPGLGGIV IAGRRGTAKS VMARAIHTLL
PPIEIIKGNR YQCDPKNPGS WDDDTLEKFA DVPLDQLETQ VIPAPFIQIP LGVTEDRLLG
SVDVEKSVKQ GEAVFQPGLL AQAHRGVLYI DELNLLDDQI ANQLLTVLTE GKNQIEREGM
SFQHPCQPLL IATYNPEEGP LRRHLLDRIA IALSADGILG LDQRVAAVDQ VLAYADSPIS
FIDQYDAELD DLKTTIILAR EWLKEVSLTP EQVSYLVEEA IRGGLQGHRG ELFAMRVAKA
IAALDGRSDV QADDLRQAVE LVIVPRSVLM DNPPPPEQAP PPPPPPQNQD EGKDEQEDQQ
DDKEDDKDNE PEAEQDPPSI PEEFIFDPEG VSLDPSVLYF AQMAQKQGKS GSRSVIFSDD
RGRYLKPILP KGKVRRIAVD ATLRAASPYQ KSRRLRHPDR QVIVEQGDIR GKKLVRKAGA
LIVFLVDASG SMALNRMQAA KGAVMQLLTE AYENRDQVSL IPFQGENAEV LLPPTRSIAM
AKKRLETLPC GGGSPLSHGL MQAVNVGMNA KRSGDIGQVV IVAITDGRGN IPLARSLGDE
IPEGEKPDIK AELLEIAAKI RGLGMQLLVI NTEKKFVSTG FGKELAQKAG GKYYQLPKAT
DQGIASMARQ AIADMQ
