ID   RBL2_RHOP5              Reviewed;         460 AA.
AC   Q07N61;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Ribulose bisphosphate carboxylase;
DE            Short=RuBisCO;
DE            EC=4.1.1.39;
GN   Name=cbbM; OrderedLocusNames=RPE_2686;
OS   Rhodopseudomonas palustris (strain BisA53).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., Kim E.,
RA   Harwood C.S., Oda Y., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL   Submitted (SEP-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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
CC       1,5-bisphosphate + CO(2) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2).
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
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 (By similarity).
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type II
CC       subfamily.
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DR   EMBL; CP000463; ABJ06623.1; -; Genomic_DNA.
DR   RefSeq; YP_781603.1; -.
DR   SMR; Q07N61; 2-458.
DR   GeneID; 4360364; -.
DR   GenomeReviews; CP000463_GR; RPE_2686.
DR   KEGG; rpe:RPE_2686; -.
DR   HOGENOM; Q07N61; -.
DR   OMA; Q07N61; LRLPGFF.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   HAMAP; MF_01339; -; 1.
DR   InterPro; IPR000685; RuBisCO_lsu_C.
DR   InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR   InterPro; IPR017444; RuBisCO_lsu_N.
DR   Gene3D; G3DSA:3.20.20.110; RuBisCO_large; 1.
DR   Gene3D; G3DSA:3.30.70.150; RuBisCO_large; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 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.
FT   CHAIN         1    460       Ribulose bisphosphate carboxylase.
FT                                /FTId=PRO_1000067650.
FT   ACT_SITE    167    167       Proton acceptor (By similarity).
FT   ACT_SITE    288    288       Proton acceptor (By similarity).
FT   METAL       192    192       Magnesium; via carbamate group (By
FT                                similarity).
FT   METAL       194    194       Magnesium (By similarity).
FT   METAL       195    195       Magnesium (By similarity).
FT   BINDING     112    112       Substrate; in homodimeric partner (By
FT                                similarity).
FT   BINDING     169    169       Substrate (By similarity).
FT   BINDING     289    289       Substrate (By similarity).
FT   BINDING     322    322       Substrate (By similarity).
FT   BINDING     369    369       Substrate (By similarity).
FT   SITE        330    330       Transition state stabilizer (By
FT                                similarity).
FT   MOD_RES     192    192       N6-carboxylysine (By similarity).
SQ   SEQUENCE   460 AA;  50252 MW;  4AED8610E910F883 CRC64;
     MDQSSRYANL NLKEKDLIAG GRHVLCAYIV KPKAGFGDFL QTAAHFAAES STGTNVEVST
     TDDFTRGVDA LVYEIDESKE LMKIAYPVEL FDRNVIDGRA MIASFLTLTI GNNQGMGDVE
     YAKMYDFYVP PAYLKLFDGP STTIKDLWRV LGRPVVDGGF IVGTIIKPKL GLRPQPFANA
     CFDFWLGGDF IKNDEPQGNQ VFAPFKETVR AVNEAMRRAQ DATGQAKLFS FNITADDHYE
     MLARGEYILE TFGENADHIA FLVDGYVAGP AAVTTARRAF PKQYLHYHRA GHGAVTSPQS
     KRGYTAFVLS KMARLQGASG IHTGTMGFGK MEGEAADRAM AFMITEDSAD GPYFHQEWLG
     MNPTTPIISG GMNALRMPGF FTNLGHSNLI MTAGGGAFGH LDGGAAGAKS LRQAEQCWKL
     GADPVQFAKE HHEFARAFES FSHDADKLFP GWRGQLGLAA
//