RBL_ARCFU
ID RBL_ARCFU Reviewed; 441 AA.
AC O28635;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
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=AF_1638;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=12730164; DOI=10.1128/jb.185.10.3049-3059.2003;
RA Finn M.W., Tabita F.R.;
RT "Synthesis of catalytically active form III ribulose 1,5-bisphosphate
RT carboxylase/oxygenase in archaea.";
RL J. Bacteriol. 185:3049-3059(2003).
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, ECO:0000269|PubMed:12730164};
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 ECO:0000269|PubMed:12730164};
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 -!- ACTIVITY REGULATION: Reversibly inhibited by O(2).
CC {ECO:0000269|PubMed:12730164}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Active over a broad temperature range. {ECO:0000269|PubMed:12730164};
CC -!- SUBUNIT: Homodimer. In contrast to form I RuBisCO, the form III RuBisCO
CC is composed solely of large subunits. {ECO:0000269|PubMed:12730164}.
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; AE000782; AAB89603.1; -; Genomic_DNA.
DR PIR; E69454; E69454.
DR RefSeq; WP_010879134.1; NC_000917.1.
DR AlphaFoldDB; O28635; -.
DR SMR; O28635; -.
DR STRING; 224325.AF_1638; -.
DR EnsemblBacteria; AAB89603; AAB89603; AF_1638.
DR GeneID; 24795382; -.
DR KEGG; afu:AF_1638; -.
DR eggNOG; arCOG04443; Archaea.
DR HOGENOM; CLU_031450_3_1_2; -.
DR OMA; IHGHPDG; -.
DR OrthoDB; 9533at2157; -.
DR PhylomeDB; O28635; -.
DR BRENDA; 4.1.1.39; 414.
DR Proteomes; UP000002199; 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; -; 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; 2.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 1.
DR TIGRFAMs; TIGR03326; rubisco_III; 1.
PE 1: Evidence at protein level;
KW Carbon dioxide fixation; Lyase; Magnesium; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..441
FT /note="Ribulose bisphosphate carboxylase"
FT /id="PRO_0000062671"
FT ACT_SITE 160
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT ACT_SITE 278
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 186
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 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 364..366
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 386..389
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT SITE 319
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT MOD_RES 186
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
SQ SEQUENCE 441 AA; 48557 MW; F191B4A83F36F3FD CRC64;
MAEFEIYREY VDKSYEPQKD DIVAVFRITP AEGFTIEDAA GAVAAESSTG TWTSLHPWYD
EERVKGLSAK AYDFVDLGDG SSIVRIAYPS ELFEPHNMPG LLASIAGNVF GMKRVKGLRL
EDLQLPKSFL KDFKGPSKGK EGVKKIFGVA DRPIVGTVPK PKVGYSAEEV EKLAYELLSG
GMDYIKDDEN LTSPAYCRFE ERAERIMKVI EKVEAETGEK KSWFANITAD VREMERRLKL
VAELGNPHVM VDVVITGWGA LEYIRDLAED YDLAIHGHRA MHAAFTRNAK HGISMFVLAK
LYRIIGIDQL HIGTAGAGKL EGQKWDTVQN ARIFSEVEYT PDEGDAFHLS QNFHHIKPAM
PVSSGGLHPG NLEPVIDALG KEIVIQVGGG VLGHPMGAKA GAKAVRQALD AIISAIPLEE
HAKQHPELQA ALEKWGRVTP I
