ID   RBL1B_BRASO             Reviewed;         479 AA.
AC   A4YQD3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   16-JUN-2009, entry version 16.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain 2;
DE            Short=RuBisCO large subunit 2;
DE            EC=4.1.1.39;
GN   Name=cbbL2; OrderedLocusNames=BRADO2274;
OS   Bradyrhizobium sp. (strain ORS278).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=114615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S.,
RA   Rouy Z., Mangenot S., Segurens B., Dossat C., Franck W.L.,
RA   Chang W.-S., Saunders E., Bruce D., Richardson P., Normand P.,
RA   Dreyfus B., Pignol D., Stacey G., Emerich D., Vermeglio A.,
RA   Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic
RT   bradyrhizobia.";
RL   Science 316:1307-1312(2007).
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: Heterohexadecamer of 8 large chains and 8 small chains
CC       (By similarity).
CC   -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC       chain homodimer in a "head-to-tail" conformation. In form I
CC       RuBisCO this homodimer is arranged in a barrel-like tetramer with
CC       the small subunits forming a tetrameric "cap" on each end of the
CC       "barrel" (By similarity).
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily.
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DR   EMBL; CU234118; CAL76109.1; -; Genomic_DNA.
DR   RefSeq; YP_001204346.1; -.
DR   GeneID; 5115889; -.
DR   GenomeReviews; CU234118_GR; BRADO2274.
DR   KEGG; bra:BRADO2274; -.
DR   OMA; A4YQD3; YTPDYTP.
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_01338; -; 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    479       Ribulose bisphosphate carboxylase large
FT                                chain 2.
FT                                /FTId=PRO_0000299962.
FT   ACT_SITE    168    168       Proton acceptor (By similarity).
FT   ACT_SITE    287    287       Proton acceptor (By similarity).
FT   METAL       194    194       Magnesium; via carbamate group (By
FT                                similarity).
FT   METAL       196    196       Magnesium (By similarity).
FT   METAL       197    197       Magnesium (By similarity).
FT   BINDING     116    116       Substrate; in homodimeric partner (By
FT                                similarity).
FT   BINDING     166    166       Substrate (By similarity).
FT   BINDING     170    170       Substrate (By similarity).
FT   BINDING     288    288       Substrate (By similarity).
FT   BINDING     320    320       Substrate (By similarity).
FT   BINDING     372    372       Substrate (By similarity).
FT   SITE        327    327       Transition state stabilizer (By
FT                                similarity).
FT   MOD_RES     194    194       N6-carboxylysine (By similarity).
SQ   SEQUENCE   479 AA;  53334 MW;  7518D7CC0AE30D6C CRC64;
     MAEKSYQAGV KEYRKTYWTP EYVPLDTDLL AVFKIVAQAG VPREEAAAAV AAESSTGTWT
     TVWTDLLTDL DYYKGRAYRI EPVPGDDNAF YAFIAYPIDL FEEGSVVNVL TSLVGNVFGF
     KAVRSLRLED IRFPLAYVKT CGGPPNGIQL ERDRLNKYGR PLLGCTIKPK LGLSAKNYGR
     AVYECLRGGL DFTKDDENIN SQPFMRWQHR FEFVMEAVHK ATSETGERKG HYLNVTAPTP
     EEMYKRAEFA KSLGAPIIMH DFLTAGFTAN TGLANWCREN GMLLHIHRAM HAVLDRNPMH
     GIHFRVLTKC LRLSGGDHLH SGTVVGKLEG DREATIGWVD LMREPFVPEN RARGIFFDQD
     WGAMPGVMPV ASGGIHVWHM PALTAIFGDD ACFQFGGGTL GHPWGNAAGA HANRVALEAC
     VEARNQGRPV EREGREILTE AAQHSPELKI AMETWKEIKF EFDVVDKLDT GPMLRVVNA
//