GenomeNet

Database: UniProt/SWISS-PROT
Entry: RBL_PYRFU
LinkDB: RBL_PYRFU
Original site: 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   25-OCT-2017, entry version 98.
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;
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
RT   P. 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: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
CC       1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000255|HAMAP-
CC       Rule:MF_01133}.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2). {ECO:0000255|HAMAP-
CC       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-
CC       Rule:MF_01133};
CC   -!- SUBUNIT: Homodimer or homodecamer. In contrast to form I RuBisCO,
CC       the 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
CC       are all anaerobic, it is most likely that only the carboxylase
CC       activity of RuBisCO, and not the competitive oxygenase activity
CC       (by which RuBP reacts with O(2) to form one molecule of 3-
CC       phosphoglycerate and one molecule of 2-phosphoglycolate), is
CC       biologically relevant in these strains. {ECO:0000255|HAMAP-
CC       Rule:MF_01133}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type III
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01133}.
DR   EMBL; AE009950; AAL81280.1; -; Genomic_DNA.
DR   RefSeq; WP_011012296.1; NC_003413.1.
DR   ProteinModelPortal; Q8U1P9; -.
DR   SMR; Q8U1P9; -.
DR   STRING; 186497.PF1156; -.
DR   PRIDE; Q8U1P9; -.
DR   EnsemblBacteria; AAL81280; AAL81280; PF1156.
DR   GeneID; 1469025; -.
DR   KEGG; pfu:PF1156; -.
DR   PATRIC; fig|186497.12.peg.1217; -.
DR   eggNOG; arCOG04443; Archaea.
DR   eggNOG; COG1850; LUCA.
DR   HOGENOM; HOG000230831; -.
DR   KO; K01601; -.
DR   OMA; HRAMHAA; -.
DR   OrthoDB; POG093Z02MJ; -.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
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   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; Complete proteome; Lyase; Magnesium;
KW   Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN         1    420       Ribulose bisphosphate carboxylase.
FT                                /FTId=PRO_0000062676.
FT   REGION      343    345       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   REGION      365    368       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   ACT_SITE    155    155       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   ACT_SITE    273    273       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   METAL       181    181       Magnesium; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01133}.
FT   METAL       183    183       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   METAL       184    184       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   BINDING     157    157       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   BINDING     274    274       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   BINDING     306    306       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   SITE        313    313       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01133}.
FT   MOD_RES     181    181       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                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
//
DBGET integrated database retrieval system