ID F2KRW1_ARCVS Unreviewed; 415 AA.
AC F2KRW1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 62.
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=Arcve_0786 {ECO:0000313|EMBL:AEA46802.1};
OS Archaeoglobus veneficus (strain DSM 11195 / SNP6).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=693661 {ECO:0000313|EMBL:AEA46802.1, ECO:0000313|Proteomes:UP000008136};
RN [1] {ECO:0000313|EMBL:AEA46802.1, ECO:0000313|Proteomes:UP000008136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SNP6;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Lu M.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Archaeoglobus veneficus SNP6.";
RL Submitted (MAR-2011) 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;
CC Evidence={ECO:0000256|HAMAP-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; CP002588; AEA46802.1; -; Genomic_DNA.
DR RefSeq; WP_013683474.1; NC_015320.1.
DR AlphaFoldDB; F2KRW1; -.
DR STRING; 693661.Arcve_0786; -.
DR GeneID; 10393889; -.
DR KEGG; ave:Arcve_0786; -.
DR eggNOG; arCOG04443; Archaea.
DR HOGENOM; CLU_031450_3_1_2; -.
DR OMA; IHGHPDG; -.
DR OrthoDB; 52787at2157; -.
DR Proteomes; UP000008136; 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; 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; 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.
DR PROSITE; PS00157; RUBISCO_LARGE; 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:AEA46802.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01133};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01133}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01133};
KW Reference proteome {ECO:0000313|Proteomes:UP000008136}.
FT DOMAIN 8..120
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 130..409
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT ACT_SITE 151
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 153
FT /ligand="substrate"
FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_01133"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 180
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 338..340
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 360..363
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 177
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
SQ SEQUENCE 415 AA; 45962 MW; 74680EC3F2F95AF2 CRC64;
MSFEWYTEFV DLSYEPEENE IICVFRVEPD GISMEEAAGR VASESSVGTW TTLAKLPERI
KRLMAKVFEI DGNVVKIAYP LDLFEEGSIP QLLSSVAGNV FGMKALKNLR LEDIEFPAEY
CKHFSGPLLG IEGVRKLFGV YDRPLTATVP KPKVGFDADE YADIAYQGWS GGIDFIKDDE
NLTSQPFVRF EKRLEKVMKA REKAEKETGE KKVYLANVTA VGKEMLRRAK LVADYGNEYV
MVDILTAGFS AVQMLREECE DLGLGIHAHR AMHAAFTRNP KHGISLDVLV KISRLAGVDN
FHVGTGVGKM EGSKDMVKRL ADICRREWYV KPVFPVSSGG LHPGLVPDIV QLFGKDVIIQ
AGGGVHGHPD GTHAGAKALR QAIDAVIKGI SLDEHAKKHA ELARALEKWG YTRPK
//