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Database: UniProt/SWISS-PROT
Entry: RBL_PYRAB
LinkDB: RBL_PYRAB
Original site: RBL_PYRAB 
ID   RBL_PYRAB               Reviewed;         424 AA.
AC   Q9UZD7; G8ZKK4;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   05-DEC-2018, entry version 112.
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};
GN   OrderedLocusNames=PYRAB12110; ORFNames=PAB1580;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C.,
RA   Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic
RT   archaeon Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5
RT   and Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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 3-phospho-D-glycerate + 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 = 2-phosphoglycolate +
CC         3-phospho-D-glycerate + 2 H(+); Xref=Rhea:RHEA:36631,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58033, ChEBI:CHEBI:58272;
CC         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-
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; AJ248286; CAB50122.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70647.1; -; Genomic_DNA.
DR   PIR; E75102; E75102.
DR   ProteinModelPortal; Q9UZD7; -.
DR   SMR; Q9UZD7; -.
DR   STRING; 272844.PAB1580; -.
DR   EnsemblBacteria; CAB50122; CAB50122; PAB1580.
DR   KEGG; pab:PAB1580; -.
DR   PATRIC; fig|272844.11.peg.1291; -.
DR   eggNOG; arCOG04443; Archaea.
DR   eggNOG; COG1850; LUCA.
DR   HOGENOM; HOG000230831; -.
DR   KO; K01601; -.
DR   OMA; FTQDWAS; -.
DR   OrthoDB; POG093Z02MJ; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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; Complete proteome; Lyase; Magnesium;
KW   Metal-binding; Oxidoreductase.
FT   CHAIN         1    424       Ribulose bisphosphate carboxylase.
FT                                /FTId=PRO_0000062675.
FT   REGION      347    349       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   REGION      369    372       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   ACT_SITE    159    159       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   ACT_SITE    277    277       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   METAL       185    185       Magnesium; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01133}.
FT   METAL       187    187       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   METAL       188    188       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   BINDING     161    161       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   BINDING     278    278       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   BINDING     310    310       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   SITE        317    317       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01133}.
FT   MOD_RES     185    185       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
SQ   SEQUENCE   424 AA;  47606 MW;  CFBC3EEDB1D16A1F CRC64;
     MVSSMKVEWY LDFVDLNYEP GRDELIVEYY FEPNGVSPEE AAGRIASESS IGTWTTLWKL
     PEMAKRSMAK VFYLEKHGEG YIAKIAYPLT LFEEGSLVQL FSAIAGNVFG MKALKNLRLL
     DFHPPYEYLR HFKGPQFGVK GIREFMGIKD RPLTATVPKP KMGWSVEEYA EIAYELWSGG
     IDLLKDDENF TSFPFNRFEE RVKKLYRVRD RVEAETGETK EYLINITGPV NVMEKRAELV
     ANEGGQYVMI DIVVAGWSAL QYMREVTEDL GLAIHAHRAM HAAFTRNPKH GITMFALAKA
     ARMIGVDQIH TGTAVGKMAG DYEEIKKIND FLLSKWEHIR PVFPVASGGL HPGLMPELIR
     LFGKDLVIQA GGGVMGHPDG PRAGAKALRD AIDAAIEGLD LEEKAKSSPE LKKALDKWGY
     LKPK
//
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