RBL_METBF
ID RBL_METBF Reviewed; 428 AA.
AC Q46E16;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000255|HAMAP-Rule:MF_01133};
DE Short=RuBisCO {ECO:0000255|HAMAP-Rule:MF_01133};
DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01133};
GN Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01133}; OrderedLocusNames=Mbar_A0902;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01133};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01133};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01133}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type III
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01133}.
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DR EMBL; CP000099; AAZ69876.1; -; Genomic_DNA.
DR RefSeq; WP_011305925.1; NC_007355.1.
DR AlphaFoldDB; Q46E16; -.
DR SMR; Q46E16; -.
DR STRING; 269797.Mbar_A0902; -.
DR EnsemblBacteria; AAZ69876; AAZ69876; Mbar_A0902.
DR GeneID; 3625947; -.
DR KEGG; mba:Mbar_A0902; -.
DR eggNOG; arCOG04443; Archaea.
DR HOGENOM; CLU_031450_3_1_2; -.
DR OMA; IHGHPDG; -.
DR OrthoDB; 9533at2157; -.
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; -; 1.
DR Gene3D; 3.30.70.150; -; 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 PANTHER; PTHR42704; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 1.
DR TIGRFAMs; TIGR03326; rubisco_III; 1.
PE 3: Inferred from homology;
KW Carbon dioxide fixation; Lyase; Magnesium; Metal-binding; Oxidoreductase.
FT CHAIN 1..428
FT /note="Ribulose bisphosphate carboxylase"
FT /id="PRO_1000065430"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT ACT_SITE 270
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 354..356
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 376..379
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT SITE 310
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT MOD_RES 177
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
SQ SEQUENCE 428 AA; 47061 MW; 74DCE0F7F03502E3 CRC64;
MQRDYIDAGY SPKDTDLICE FHIEPSAGVN FEEAATHMAG ESSIDSWTEI ATLSPELAAR
LKPHVFYMDE DAQTVRVAYS EELFELGSVP QVLSAVAGNI LSMKIVDNLR LQDIAFPKSM
LREFKGPGFG LSGIRELTGV QDRPLIGTIV KPKVGLTSEK HAEVAYNSFA GGCDLVKDDE
NLTDQKFNKF EKRAELTLKL AEKAESETGE RKMYLCNITA PTCKEMIRRM NILKDLGASY
AMIDIVPAGW TALQTLREEA DDAGLALHAH RCMHSAYTRN PRHGISMLVV AKLCRLIGLD
QLHIGTVVGK MHGEKHEVLS LRDECVLDNV PADESQHVLA QDWGGLKPMF PVASGGLAPT
MIPDLYTIFG RDVIMQFGGG IHAHPMGTKA GAAACRQALE ASLEGVSLQE YAKNHRELEA
AINKWLKK
