ID   RBL2_DECAR              Reviewed;         459 AA.
AC   Q479W5;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Ribulose bisphosphate carboxylase;
DE            Short=RuBisCO;
DE            EC=4.1.1.39;
GN   Name=cbbM; OrderedLocusNames=Daro_3637;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Dechloromonas.
OX   NCBI_TaxID=159087;
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., Di Bartolo G., Trong S., Kellar K.,
RA   Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.;
RT   "Complete sequence of Dechloromonas aromatica RCB.";
RL   Submitted (AUG-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; CP000089; AAZ48366.1; -; Genomic_DNA.
DR   RefSeq; YP_286836.1; -.
DR   SMR; Q479W5; 2-455.
DR   GeneID; 3568282; -.
DR   GenomeReviews; CP000089_GR; Daro_3637.
DR   KEGG; dar:Daro_3637; -.
DR   NMPDR; fig|159087.4.peg.3087; -.
DR   HOGENOM; Q479W5; -.
DR   OMA; Q479W5; LRLPGFF.
DR   BioCyc; DARO159087:DARO_3637-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_0000251406.
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;  50788 MW;  813D3C3753EE1C0F CRC64;
     MDQSNRYADL SLTEAELIAG GQHILCAYKM KPKAGHRYLE AAAHFAAESS TGTNVEVCTT
     DEFTKGVDAL VYHIDEASED MRIAYPLDLF DRNMTDGRMM MASFLTLTIG NNQGMGDIEH
     AKMVDFYVPR RGIELFDGPS KDISDLWRML GRPVKDGGYI AGTIIKPKLG LRPEPFARAA
     YEFWLGGDFI KNDEPQGNQV FAPLKKVIPL VYDSMKRAMD ETGEAKLFSM NITADDHFEM
     CARADFALEA FGPDADKLAF LVDGYVGGPG MITTARRQYP NQYLHYHRAG HGAVTSPSSK
     RGYTAYVLAK MSRLQGASGI HVGTMGYGKM EGDKDDRACA YIIERDSYTG PVYHQEWYGM
     KPTTPIISGG MNALRLPGFF ENLGHGNVIN TAGGGAYGHI DSPAAGARSL RQAYDCWKAG
     ADPVEWARDH YEFARAFESF PQDADQLYPG WRHKLRPAA
//