CHLI_SYNY3
ID CHLI_SYNY3 Reviewed; 357 AA.
AC P51634; P73140;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Magnesium-chelatase subunit ChlI;
DE EC=6.6.1.1;
DE AltName: Full=Mg-protoporphyrin IX chelatase;
GN Name=chlI; OrderedLocusNames=slr1030;
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}.
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DR EMBL; U35144; AAC44138.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA17166.1; -; Genomic_DNA.
DR PIR; S75252; S75252.
DR PIR; T46868; T46868.
DR PDB; 6L8D; X-ray; 2.91 A; A/B/C/D/E/F=1-357.
DR PDBsum; 6L8D; -.
DR AlphaFoldDB; P51634; -.
DR SMR; P51634; -.
DR IntAct; P51634; 1.
DR STRING; 1148.1652243; -.
DR PaxDb; P51634; -.
DR EnsemblBacteria; BAA17166; BAA17166; BAA17166.
DR KEGG; syn:slr1030; -.
DR eggNOG; COG1239; Bacteria.
DR InParanoid; P51634; -.
DR OMA; RISAVCG; -.
DR PhylomeDB; P51634; -.
DR BRENDA; 6.6.1.1; 382.
DR SABIO-RK; P51634; -.
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 Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR045006; CHLI-like.
DR InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR InterPro; IPR011775; Mg_chelatase_ATPase-isu.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR32039; PTHR32039; 1.
DR Pfam; PF17863; AAA_lid_2; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02030; BchI-ChlI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chlorophyll biosynthesis; Ligase;
KW Nucleotide-binding; Photosynthesis; Reference proteome.
FT CHAIN 1..357
FT /note="Magnesium-chelatase subunit ChlI"
FT /id="PRO_0000206863"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 170
FT /note="A -> T (in Ref. 1; AAC44138)"
FT /evidence="ECO:0000305"
FT CONFLICT 302..306
FT /note="ALAAF -> PWPLL (in Ref. 1; AAC44138)"
FT /evidence="ECO:0000305"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:6L8D"
FT HELIX 25..36
FT /evidence="ECO:0007829|PDB:6L8D"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6L8D"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:6L8D"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:6L8D"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:6L8D"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:6L8D"
FT TURN 142..146
FT /evidence="ECO:0007829|PDB:6L8D"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:6L8D"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:6L8D"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:6L8D"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:6L8D"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:6L8D"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:6L8D"
FT HELIX 223..238
FT /evidence="ECO:0007829|PDB:6L8D"
FT HELIX 240..246
FT /evidence="ECO:0007829|PDB:6L8D"
FT HELIX 248..264
FT /evidence="ECO:0007829|PDB:6L8D"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:6L8D"
FT HELIX 272..284
FT /evidence="ECO:0007829|PDB:6L8D"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:6L8D"
FT HELIX 291..306
FT /evidence="ECO:0007829|PDB:6L8D"
FT HELIX 314..325
FT /evidence="ECO:0007829|PDB:6L8D"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:6L8D"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:6L8D"
SQ SEQUENCE 357 AA; 39463 MW; 80F04C2539B46A05 CRC64;
MTATLAAPSK TRRVVFPFTA IVGQDEMKLA LLLNVIDPKI GGVMIMGDRG TGKSTTIRAL
ADLLPEIEVV ANDPFNSSPS DPEMMSEEVR IRVDSQEPLS IVKKKVTMVD LPLGATEDRV
CGTIDIEKAL SEGVKAFEPG LLAKANRGIL YVDEVNLLDD HLVDVLLDSA AGGWNTVERE
GISIRHPARF VLVGSGNPEE GELRPQLLDR FGMHAEIRTV REPELRVKIV EQRTEFDQNP
HPFCDQYQTE QEALQAKIVN AQNLLPQVTI DYDYRVKVSE VCAELDVDGL RGDIVTNRAA
KALAAFEGRT EVTVDDISRV IVLCLRHRLR KDPLESIDSG SKVEKVFKRV FGVVDEA
