ID N0BMV6_9EURY Unreviewed; 414 AA.
AC N0BMV6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
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 ORFNames=Asulf_01980 {ECO:0000313|EMBL:AGK61946.1};
OS Archaeoglobus sulfaticallidus PM70-1.
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=387631 {ECO:0000313|EMBL:AGK61946.1, ECO:0000313|Proteomes:UP000013307};
RN [1] {ECO:0000313|EMBL:AGK61946.1, ECO:0000313|Proteomes:UP000013307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM70-1 {ECO:0000313|EMBL:AGK61946.1};
RX PubMed=23833130;
RA Stokke R., Hocking W.P., Steinsbu B.O., Steen I.H.;
RT "Complete Genome Sequence of the Thermophilic and Facultatively
RT Chemolithoautotrophic Sulfate Reducer Archaeoglobus sulfaticallidus Strain
RT PM70-1T.";
RL Genome Announc. 1:e00406-13(2013).
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; CP005290; AGK61946.1; -; Genomic_DNA.
DR RefSeq; WP_015591542.1; NC_021169.1.
DR AlphaFoldDB; N0BMV6; -.
DR STRING; 387631.Asulf_01980; -.
DR GeneID; 15393614; -.
DR KEGG; ast:Asulf_01980; -.
DR eggNOG; arCOG04443; Archaea.
DR HOGENOM; CLU_031450_3_1_2; -.
DR OrthoDB; 52787at2157; -.
DR Proteomes; UP000013307; 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 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};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000013307}.
FT DOMAIN 8..118
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 128..408
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT ACT_SITE 267
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 175
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 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 337..339
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 359..362
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT SITE 307
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT MOD_RES 175
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
SQ SEQUENCE 414 AA; 46072 MW; A23B25A70C95A5E1 CRC64;
MGFEWYTDFV DLSYKPEDEI VCYFKVKSDL PIEESSGRVA SESSVGTWTT LSRLPDRIKW
LMAKVFRIDG ERIAVAYKTD LFEEGNIPQF LSSVAGNIFG MRAIKGLRFE DFEVPASFAK
HFKGPNFGID GVRNIMRVHD RPLTATVPKP KVGFDADEYA EVGYRSWVGG IDILKDDENL
TSQPFIRFEK RLAKVMKARE RAENETGEKK GYLINITAEA REMERRAELV ADYGNEFVMV
DILTAGFSAV QTVRNKCEEL GLAIHAHRAM HGAFTRNEEH GISLKVLTKL ARMAGVDHMH
VGTGVGKMAG DKAEVMELRD VCRKSWHNFK PVFPVSSGGL HPGLIPDIIE LFGVDVIIQA
GGGVHGHPDG SEKGAMALRQ AISAVLEGVD LEDYAKSHSE LARALERWGR VSPK
//