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Database: UniProt
Entry: RBL2_RHOPB
LinkDB: RBL2_RHOPB
Original site: RBL2_RHOPB 
ID   RBL2_RHOPB              Reviewed;         461 AA.
AC   Q213J3;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   05-DEC-2018, entry version 77.
DE   RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000255|HAMAP-Rule:MF_01339};
DE            Short=RuBisCO {ECO:0000255|HAMAP-Rule:MF_01339};
DE            EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01339};
GN   Name=cbbM {ECO:0000255|HAMAP-Rule:MF_01339};
GN   OrderedLocusNames=RPC_2895;
OS   Rhodopseudomonas palustris (strain BisB18).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB18;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC       ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC       fixation, as well as the oxidative fragmentation of the pentose
CC       substrate. Both reactions occur simultaneously and in competition
CC       at the same active site. {ECO:0000255|HAMAP-Rule:MF_01339}.
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_01339};
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_01339};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01339};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01339};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01339}.
CC   -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC       chain homodimer in a "head-to-tail" conformation. In contrast to
CC       form I RuBisCO, the form II RuBisCO are composed solely of large
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_01339}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type II
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01339}.
DR   EMBL; CP000301; ABD88443.1; -; Genomic_DNA.
DR   RefSeq; WP_011473338.1; NC_007925.1.
DR   ProteinModelPortal; Q213J3; -.
DR   SMR; Q213J3; -.
DR   STRING; 316056.RPC_2895; -.
DR   EnsemblBacteria; ABD88443; ABD88443; RPC_2895.
DR   KEGG; rpc:RPC_2895; -.
DR   eggNOG; ENOG4105DT1; Bacteria.
DR   eggNOG; COG1850; LUCA.
DR   HOGENOM; HOG000230831; -.
DR   KO; K01601; -.
DR   OMA; TARRQYP; -.
DR   OrthoDB; POG091H14UZ; -.
DR   BioCyc; RPAL316056:G1G6B-2910-MONOMER; -.
DR   Proteomes; UP000001948; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   CDD; cd08211; RuBisCO_large_II; 1.
DR   Gene3D; 3.20.20.110; -; 1.
DR   Gene3D; 3.30.70.150; -; 1.
DR   HAMAP; MF_01339; RuBisCO_L_type2; 1.
DR   InterPro; IPR033966; RuBisCO.
DR   InterPro; IPR020878; RuBisCo_large_chain_AS.
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   InterPro; IPR020871; RuBisCO_lsuII.
DR   PANTHER; PTHR42704; PTHR42704; 1.
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   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   3: Inferred from homology;
KW   Calvin cycle; Carbon dioxide fixation; Complete proteome; Lyase;
KW   Magnesium; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Photosynthesis; Reference proteome.
FT   CHAIN         1    461       Ribulose bisphosphate carboxylase.
FT                                /FTId=PRO_0000251410.
FT   ACT_SITE    167    167       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01339}.
FT   ACT_SITE    288    288       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01339}.
FT   METAL       192    192       Magnesium; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01339}.
FT   METAL       194    194       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01339}.
FT   METAL       195    195       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01339}.
FT   BINDING     112    112       Substrate; in homodimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01339}.
FT   BINDING     169    169       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01339}.
FT   BINDING     289    289       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01339}.
FT   BINDING     322    322       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01339}.
FT   BINDING     369    369       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01339}.
FT   SITE        330    330       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01339}.
FT   MOD_RES     192    192       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01339}.
SQ   SEQUENCE   461 AA;  50554 MW;  33252C39508E66E4 CRC64;
     MDQSNRYANL NLTEKDLIAG GRHVLCAYIM KPKAGFGNFL QTAAHFAAES STGTNVEVST
     TDDFTRGVDA LVYEIDEAKQ LMKIAYPIDL FDRNIIDGRA MIASFLTLTI GNNQGMGDVE
     YAKMYDFYVP PAYLKLFDGP STTIKDLWRV LGRPVVDGGF IVGTIIKPKL GLRPQPFANA
     CYDFWLGGDF IKNDEPQGNQ VFAPFKETVR LVNDAMRRAQ DKTGQPKLFS FNITADDHHE
     MVARGEYILE TFADNADHIA FLVDGYVAGP AAVTTARRRF PKQYLHYHRA GHGAVTSPQA
     KRGYTAFVLS KMARLQGASG IHTGTMGFGK MEGEAADRAM AYMITEDSAD GPYFHQEWLG
     MNPTTPIISG GMNALRMPGF FKNLGHSNLI MTAGGGAFGH IDGGAAGAKS LRQAEQCWKE
     GADPVAFAKE HREFARAFES FPHDADALYP NWRGQLGLAA A
//
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