ID A0A166DW84_9EURY Unreviewed; 445 AA.
AC A0A166DW84;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Magnesium-chelatase 38 kDa subunit {ECO:0000313|EMBL:KZX16018.1};
DE EC=6.6.1.1 {ECO:0000313|EMBL:KZX16018.1};
GN Name=bchI_1 {ECO:0000313|EMBL:KZX16018.1};
GN ORFNames=MBCUT_11540 {ECO:0000313|EMBL:KZX16018.1};
OS Methanobrevibacter cuticularis.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=47311 {ECO:0000313|EMBL:KZX16018.1, ECO:0000313|Proteomes:UP000077275};
RN [1] {ECO:0000313|EMBL:KZX16018.1, ECO:0000313|Proteomes:UP000077275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11139 {ECO:0000313|EMBL:KZX16018.1,
RC ECO:0000313|Proteomes:UP000077275};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanobrevibacter cuticularis DSM 11139.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000256|ARBA:ARBA00005799}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZX16018.1}.
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DR EMBL; LWMW01000102; KZX16018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166DW84; -.
DR STRING; 47311.MBCUT_11540; -.
DR PATRIC; fig|47311.3.peg.1267; -.
DR Proteomes; UP000077275; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-EC.
DR CDD; cd00009; AAA; 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 InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR045006; CHLI-like.
DR InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR32039; MAGNESIUM-CHELATASE SUBUNIT CHLI; 1.
DR PANTHER; PTHR32039:SF9; MAGNESIUM-CHELATASE SUBUNIT CHLI-1, CHLOROPLASTIC; 1.
DR Pfam; PF17863; AAA_lid_2; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils}; Ligase {ECO:0000313|EMBL:KZX16018.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000077275}.
FT DOMAIN 33..215
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 238..265
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 329..387
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 445 AA; 50477 MW; 0B716D554EACD6F4 CRC64;
MVKIMKRTVF PFTAIVGQEK IKKALILNAI NPSIGGVLIK GDRGTGKTTA VRALADLLPE
IEIVENSPFN ADENSYKEFE LYKANDKKLT DEIKLVKTPM NVVELPLGAT EDRVVGSLDI
EKALHMGIKA LEPGLLAQAN NNILYIDEIN LLDDNLVDIL LDAAAYGVNI IEREGISISH
PSKFILIGTM NPEEGELRGQ LSDRIGLEIE VEGILDVEDR ILIMQRREEF EKDPIAFNKK
FEKEVKKLQN RIIKARNILE NIEINTVFLE IIARITLELG AEGHRSDIAI LKTAKTIASF
NEHMEVQNND LEEAVFLVLG DDNLLFQRIQ KIKREIEKRE EDLKKSKLES IEESLQESLQ
DKLGEINQKL DINLNNEKEE IQDEDKSNDE HLDLSDSISK KTSFVDDSDF KAKDDLESKI
NEGKQLENFN EIETEERKFD IKKSS
//
