位置:首页 > 蛋白库 > RBL_PYRFU
RBL_PYRFU
ID   RBL_PYRFU               Reviewed;         420 AA.
AC   Q8U1P9;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=PF1156;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009950; AAL81280.1; -; Genomic_DNA.
DR   RefSeq; WP_011012296.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U1P9; -.
DR   SMR; Q8U1P9; -.
DR   STRING; 186497.PF1156; -.
DR   EnsemblBacteria; AAL81280; AAL81280; PF1156.
DR   GeneID; 41712965; -.
DR   KEGG; pfu:PF1156; -.
DR   PATRIC; fig|186497.12.peg.1217; -.
DR   eggNOG; arCOG04443; Archaea.
DR   HOGENOM; CLU_031450_3_1_2; -.
DR   OMA; IHGHPDG; -.
DR   OrthoDB; 9533at2157; -.
DR   PhylomeDB; Q8U1P9; -.
DR   Proteomes; UP000001013; 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   3: Inferred from homology;
KW   Carbon dioxide fixation; Lyase; Magnesium; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..420
FT                   /note="Ribulose bisphosphate carboxylase"
FT                   /id="PRO_0000062676"
FT   ACT_SITE        155
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT   ACT_SITE        273
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT   BINDING         181
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         183
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT   BINDING         184
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT   BINDING         274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT   BINDING         306
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT   BINDING         343..345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT   BINDING         365..368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT   SITE            313
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT   MOD_RES         181
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
SQ   SEQUENCE   420 AA;  47348 MW;  0271D055DCFF3DC4 CRC64;
     MKVEWYLDFV DLDYTPGRDE LIVEYYFEPN GVSPEEAAGR IASESSIGTW TTLWKMPEMA
     KRSMAKVFYL EKSGEGYIAK IAYPLTLFEE GSIVQLLSAI AGNIFGMKAL KNLRLLDFHP
     PYEYLRHFKG PQYGVKGIRE FMGVKERPLT ATVPKPKMGW SVDEYAEIAY ELWSGGIDLL
     KDDENFTSFP FNRFEERVKK LYRIRDIVEA ETEERKEYLI NITGSVDVME KRAELVANEG
     GQYVMIDIIV TGWSALQYMR EVTEDLGLAI HAHRAMHAAF TRNPKHGITM YAIAKLARMI
     GVDQIHTGTA VGKMAGDYEE VKRINDFLLS KWEHIREVFP VASGGLHPGL MPELIRLFGK
     DLVIQAGGGV MGHPDGPRAG AKALRDAIDA ALEGVDLEEK AKSSPELKKA LDKWGYLKPK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024