ID   RBL2_RHOFD              Reviewed;         459 AA.
AC   Q21YM9;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Ribulose bisphosphate carboxylase;
DE            Short=RuBisCO;
DE            EC=4.1.1.39;
GN   Name=cbbM; OrderedLocusNames=Rfer_1391;
OS   Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
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., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM
RT   15236.";
RL   Submitted (FEB-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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000267; ABD69124.1; -; Genomic_DNA.
DR   RefSeq; YP_522655.1; -.
DR   GeneID; 3960215; -.
DR   GenomeReviews; CP000267_GR; Rfer_1391.
DR   KEGG; rfr:Rfer_1391; -.
DR   NMPDR; fig|338969.3.peg.3068; -.
DR   HOGENOM; Q21YM9; -.
DR   OMA; Q21YM9; LRLPGFF.
DR   BioCyc; RFER338969:RFER_1391-MON; -.
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.
FT   CHAIN         1    459       Ribulose bisphosphate carboxylase.
FT                                /FTId=PRO_0000251408.
FT   ACT_SITE    166    166       Proton acceptor (By similarity).
FT   ACT_SITE    287    287       Proton acceptor (By similarity).
FT   METAL       191    191       Magnesium; via carbamate group (By
FT                                similarity).
FT   METAL       193    193       Magnesium (By similarity).
FT   METAL       194    194       Magnesium (By similarity).
FT   BINDING     111    111       Substrate; in homodimeric partner (By
FT                                similarity).
FT   BINDING     168    168       Substrate (By similarity).
FT   BINDING     288    288       Substrate (By similarity).
FT   BINDING     321    321       Substrate (By similarity).
FT   BINDING     368    368       Substrate (By similarity).
FT   SITE        329    329       Transition state stabilizer (By
FT                                similarity).
FT   MOD_RES     191    191       N6-carboxylysine (By similarity).
SQ   SEQUENCE   459 AA;  50391 MW;  089F31E7B2FF938D CRC64;
     MDQSKRYADL SLQEAALIAG GQHILCAYKM APKDGLNYLE AAAHFAAESS TGTNVEVCTT
     DDFTRDVDAL VYYVNEATED MRIAYPLALF DRNITDGRFM LVSFLTLAVG NNQGMGDIKH
     AKMIDFYVPE RVIQMFDGPA KDISDLWRIL GRPVKDGGFI VGTIIKPKLG LRPEPFAQAA
     YQFWLGGDFI KNDEPQGNQV FSPIKKTLPL VYDALKRAQD ETGQAKLFSM NITADDHFEM
     CARADFALET FGADADKLAF LVDGFVGGPG MVTTARRQYP NQYLHYHRGG HGMVTSPSSK
     RGYTALVLAK MSRLQGASGI HVGTMGHGKM EGAGDDRVMA YMIERDECQG PVYFQKWYGI
     KPTTPIVSGG MNALRLPGFF DNLGHGNIIN TAGGGSYGHL DSPAAGAVSL RQAYECWKAG
     ADPIEWAKEH REFARAFESF PQDADRLFAG WRDKLGVGA
//