ID   F4BTL5_METSG            Unreviewed;       475 AA.
AC   F4BTL5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   02-SEP-2026, entry version 67.
DE   RecName: Full=Ribulose-bisphosphate carboxylase {ECO:0000256|PROSITE-ProRule:PRU10114};
DE            EC=4.1.1.39 {ECO:0000256|PROSITE-ProRule:PRU10114};
GN   Name=cbbM {ECO:0000313|EMBL:AEB69400.1};
GN   OrderedLocusNames=MCON_3086 {ECO:0000313|EMBL:AEB69400.1};
OS   Methanothrix soehngenii (strain ATCC 5969 / DSM 3671 / JCM 10134 / NBRC
OS   103675 / OCM 69 / GP-6) (Methanosaeta concilii).
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Methanomicrobia; Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=990316 {ECO:0000313|EMBL:AEB69400.1, ECO:0000313|Proteomes:UP000007807};
RN   [1] {ECO:0000313|EMBL:AEB69400.1, ECO:0000313|Proteomes:UP000007807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 5969 / DSM 3671 / JCM 10134 / NBRC 103675 / OCM 69 / GP-6
RC   {ECO:0000313|Proteomes:UP000007807};
RX   PubMed=21571998; DOI=10.1128/JB.05031-11;
RA   Barber R.D., Zhang L., Harnack M., Olson M.V., Kaul R., Ingram-Smith C.,
RA   Smith K.S.;
RT   "Complete genome sequence of Methanosaeta concilii, a specialist in
RT   aceticlastic methanogenesis.";
RL   J. Bacteriol. 193:3668-3669(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = D-ribulose 1,5-
CC         bisphosphate + CO2 + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU10114};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; CP002565; AEB69400.1; -; Genomic_DNA.
DR   RefSeq; WP_013720421.1; NC_015416.1.
DR   AlphaFoldDB; F4BTL5; -.
DR   SMR; F4BTL5; -.
DR   FunCoup; F4BTL5; 60.
DR   STRING; 990316.MCON_3086; -.
DR   GeneID; 10462358; -.
DR   KEGG; mcj:MCON_3086; -.
DR   HOGENOM; CLU_031450_3_1_2; -.
DR   InParanoid; F4BTL5; -.
DR   Proteomes; UP000007807; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:InterPro.
DR   GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR   Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 1.
DR   InterPro; IPR033966; RuBisCO.
DR   InterPro; IPR020878; RuBisCo_large_chain_AS.
DR   InterPro; IPR000685; RuBisCO_lsu_C.
DR   InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR   InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR   InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR   NCBIfam; NF010002; PRK13475.1; 1.
DR   PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42704:SF17; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR   Pfam; PF00016; RuBisCO_large; 2.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SFLD; SFLDG00301; RuBisCO-like_proteins; 1.
DR   SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR   SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007807}.
FT   DOMAIN          28..134
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          146..362
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
FT   DOMAIN          369..469
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
FT   BINDING         193
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10114"
FT   MOD_RES         191
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10114"
SQ   SEQUENCE   475 AA;  53078 MW;  CD45A1C8883A93F1 CRC64;
     MIQEELSKTL NPKQVQYMRM DLPDPRNGEY LLAVFHLIPS GELNIMQAAA EVAAESSTGT
     NFAVKTETPF SRVMNALVYK VDIEKNLVWI AYPWRLFDRN GNVQNIMTYI AGNALGMKEI
     KALKLLDIWF PPSMLEQYDG PSYTLDDMRT YLNVHDRPIL GTIIKPKMGL TSSEYAEVCY
     DFWVGGGDFV KNDEPQADQD FCPYDKMVKY VKMAMDKAVK ETGKKKVHSF NVSSADFDTM
     IERCEMIREA GFEPGSYAFL IDGITAGWMA VQTLRRRYPD VFLHFHRAGH GGFTRPENPI
     GFSVLVLSKF ARLAGASGIH TGTAGVGKMA GSPEEDVTAA RNILKVEGKG HFFTQNWGRI
     PPQDDDAIKM VEMDDAHHVV LEDDSWRGLK KCCPIISGGL NPTLLEPFID VMGGIDFITT
     MGAGCHAHPR GTRAGAMALV QACEAYKNKI DIADYAKDHR ELAEAIEFFS KKKKK
//