ID   RBL2_RHORT              Reviewed;         466 AA.
AC   Q2RRP5;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Ribulose bisphosphate carboxylase;
DE            Short=RuBisCO;
DE            EC=4.1.1.39;
GN   Name=cbbM; OrderedLocusNames=Rru_A2400;
OS   Rhodospirillum rubrum (strain ATCC 11170 / NCIB 8255).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G.,
RA   Reslewic S., Zhou S., Schwartz D.C.;
RT   "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC
RT   11170.";
RL   Submitted (DEC-2005) 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; CP000230; ABC23200.1; -; Genomic_DNA.
DR   RefSeq; YP_427487.1; -.
DR   SMR; Q2RRP5; 2-457.
DR   GeneID; 3835834; -.
DR   GenomeReviews; CP000230_GR; Rru_A2400.
DR   KEGG; rru:Rru_A2400; -.
DR   NMPDR; fig|1085.1.peg.49; -.
DR   HOGENOM; Q2RRP5; -.
DR   OMA; Q2RRP5; LRLPGFF.
DR   BioCyc; RRUB269796:RRU_A2400-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;
KW   Photosynthesis.
FT   CHAIN         1    466       Ribulose bisphosphate carboxylase.
FT                                /FTId=PRO_0000251412.
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   466 AA;  50482 MW;  4D9F800450AB0155 CRC64;
     MDQSSRYVNL ALKEEDLIAG GEHVLCAYIM KPKAGYGYVA TAAHFAAESS TGTNVEVCTT
     DDFTRGVDAL VYEVDEAREL TKIAYPVALF DRNITDGKAM IASFLTLTMG NNQGMGDVEY
     AKMHDFYVPE AYRALFDGPS VNISALWKVL GRPEVDGGLV VGTIIKPKLG LRPKPFAEAC
     HAFWLGGDFI KNDEPQGNQP FAPLRDTIAL VADAMRRAQD ETGEAKLFSA NITADDPFEI
     IARGEYVLET FGENASHVAL LVDGYVAGAA AITTARRRFP DNFLHYHRAG HGAVTSPQSK
     RGYTAFVHCK MARLQGASGI HTGTMGFGKM EGESSDRAIA YMLTQDEAQG PFYRQSWGGM
     KACTPIISGG MNALRMPGFF ENLGNANVIL TAGGGAFGHI DGPVAGARSL RQAWQAWRDG
     VPVLDYAREH KELARAFESF PGDADQIYPG WRKALGVEDT RSALPA
//