ID   C9RGZ0_METVM            Unreviewed;       425 AA.
AC   C9RGZ0;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000256|HAMAP-Rule:MF_01133};
DE            Short=RuBisCO {ECO:0000256|HAMAP-Rule:MF_01133};
DE            EC=4.1.1.39 {ECO:0000256|HAMAP-Rule:MF_01133};
GN   Name=rbcL {ECO:0000256|HAMAP-Rule:MF_01133};
GN   OrderedLocusNames=Metvu_0984 {ECO:0000313|EMBL:ACX72842.1};
OS   Methanocaldococcus vulcanius (strain ATCC 700851 / DSM 12094 / M7)
OS   (Methanococcus vulcanius).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=579137 {ECO:0000313|EMBL:ACX72842.1, ECO:0000313|Proteomes:UP000002063};
RN   [1] {ECO:0000313|EMBL:ACX72842.1, ECO:0000313|Proteomes:UP000002063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700851 / DSM 12094 / M7
RC   {ECO:0000313|Proteomes:UP000002063};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Lcollab F.I., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ovchinikova G., Sieprawska-Lupa M., Whitman W.B., Woyke T.;
RT   "Complete sequence of chromosome of Methanocaldococcus vulcanius M7.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the addition of molecular CO(2) and H(2)O to
CC       ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-
CC       phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation
CC       pathway, together with AMP phosphorylase and R15P isomerase.
CC       {ECO:0000256|HAMAP-Rule:MF_01133}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-
CC         bisphosphate + 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|HAMAP-
CC         Rule:MF_01133};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate +
CC         2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033,
CC         ChEBI:CHEBI:58272; Evidence={ECO:0000256|HAMAP-Rule:MF_01133};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01133};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01133};
CC   -!- SUBUNIT: Homodimer or homodecamer. In contrast to form I RuBisCO, the
CC       form III RuBisCO is composed solely of large subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_01133}.
CC   -!- MISCELLANEOUS: Because the Archaea possessing a type III RuBisCO are
CC       all anaerobic, it is most likely that only the carboxylase activity of
CC       RuBisCO, and not the competitive oxygenase activity (by which RuBP
CC       reacts with O(2) to form one molecule of 3-phosphoglycerate and one
CC       molecule of 2-phosphoglycolate), is biologically relevant in these
CC       strains. {ECO:0000256|HAMAP-Rule:MF_01133}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type III
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01133}.
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DR   EMBL; CP001787; ACX72842.1; -; Genomic_DNA.
DR   RefSeq; WP_015733062.1; NC_013407.1.
DR   AlphaFoldDB; C9RGZ0; -.
DR   STRING; 579137.Metvu_0984; -.
DR   GeneID; 8513321; -.
DR   KEGG; mvu:Metvu_0984; -.
DR   eggNOG; arCOG04443; Archaea.
DR   HOGENOM; CLU_031450_3_1_2; -.
DR   OrthoDB; 52787at2157; -.
DR   Proteomes; UP000002063; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006196; P:AMP catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   CDD; cd08213; RuBisCO_large_III; 1.
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   HAMAP; MF_01133; RuBisCO_L_type3; 1.
DR   InterPro; IPR033966; RuBisCO.
DR   InterPro; IPR017712; RuBisCO_III.
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; TIGR03326; rubisco_III; 1.
DR   PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
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.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01133};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01133, ECO:0000313|EMBL:ACX72842.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01133};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01133};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01133}.
FT   DOMAIN          2..122
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          132..424
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
FT   ACT_SITE        153
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   ACT_SITE        269
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         179
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         182
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         302
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         353..355
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         375..378
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   SITE            309
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   MOD_RES         179
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
SQ   SEQUENCE   425 AA;  47952 MW;  A2E35BB843A5A98C CRC64;
     MDYINLNYTP KESDLLSCMI IKGDDLKKLA NEIAGESSIG TWTKVQTMKS DIYEKLKPNV
     YEIKEIGNDG KYKIGLIKIA YPLYDFEINN MPGVLAGIAG NIFGMKIAKG LRILDFRFPK
     EFIDEYEGPE YGIEGVRNTL KIKERPLLGT IVKPKVGLKT EEHAKVAYEA WVGGVDLVKD
     DENLTSQDFN KFEDRVYKTL EMRDKAEEET GERKAYMPNI TAPYNEMIRR AEIAEDAESE
     YVMIDVVVSG FSAVQSFREE NFGFIIHAHR AMHAAMTRSK DFGITMLTLA KIYRLLGVDQ
     LHIGTVVGKM EGEEREVKAI RDEIVYDKVE ADNEHKFFEQ EWFGLNSVFP VSSGGVHPRL
     VPKIVEILGR DVIIQAGGGI HGHPDGTRAG AKAMRAAIEA VMEGKPLEEK AEEVIELKKA
     LEYWK
//