ID   RBL2_THIIN              Reviewed;         461 AA.
AC   O84917;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   24-MAR-2009, entry version 44.
DE   RecName: Full=Ribulose bisphosphate carboxylase;
DE            Short=RuBisCO;
DE            EC=4.1.1.39;
GN   Name=cbbM;
OS   Thiomonas intermedia (Thiobacillus intermedius).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Thiomonas.
OX   NCBI_TaxID=926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RA   Shively J.M., Soyer F.;
RT   "A form II Rubisco gene and associated genes in Thiobacillus
RT   intermedius.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   EXPRESSION IN T.INTERMEDIUS.
RX   MEDLINE=93231475; PubMed=8472910; DOI=10.1016/0378-1097(93)90324-U;
RA   Stoner M.T., Shively J.M.;
RT   "Cloning and expression of the D-ribulose-1,5-bisphosphate
RT   carboxylase/oxygenase form II gene from Thiobacillus intermedius in
RT   Escherichia coli.";
RL   FEMS Microbiol. Lett. 107:287-292(1993).
RN   [3]
RP   PROBABLE EXPRESSION.
RA   Shively J.M.;
RL   Unpublished observations (OCT-2005).
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   -!- CAUTION: No expression of this protein has been seen during
CC       autotrophic and mixotrophic growth, however the protein is
CC       probably expressed under other conditions. In a related bacteria
CC       (T.neapolitanus) expression has been seen when the form I enzyme
CC       has been knocked out.
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DR   EMBL; AF012127; AAC24964.1; -; Genomic_DNA.
DR   HSSP; P04718; 2RUS.
DR   SMR; O84917; 4-459.
DR   BRENDA; 4.1.1.39; 294944.
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; Lyase; Magnesium;
KW   Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN         1    461       Ribulose bisphosphate carboxylase.
FT                                /FTId=PRO_0000062669.
FT   ACT_SITE    168    168       Proton acceptor (By similarity).
FT   ACT_SITE    289    289       Proton acceptor (By similarity).
FT   METAL       193    193       Magnesium; via carbamate group (By
FT                                similarity).
FT   METAL       195    195       Magnesium (By similarity).
FT   METAL       196    196       Magnesium (By similarity).
FT   BINDING     113    113       Substrate; in homodimeric partner (By
FT                                similarity).
FT   BINDING     170    170       Substrate (By similarity).
FT   BINDING     290    290       Substrate (By similarity).
FT   BINDING     323    323       Substrate (By similarity).
FT   BINDING     370    370       Substrate (By similarity).
FT   SITE        331    331       Transition state stabilizer (By
FT                                similarity).
FT   MOD_RES     193    193       N6-carboxylysine (By similarity).
SQ   SEQUENCE   461 AA;  50818 MW;  D470D17F356800E2 CRC64;
     MAHDQSSRYA NLDLKESDLI AGGKHILVAY KMKPKAGYDY LATAAHFAAE SSTGTNVEVS
     TTDDFTKGVD ALVYFIDEAT EDMRIAYPIE LFDRNVIDGR FMIVSFLTLV IGNNQGMGDV
     EYGKMIDFYV PERAIQMFDG PATDISNLWR ILGRPIKDGG YIAGTIIKPK LGLRPEPFAQ
     AAYQFWLGGD FIKNDEPQGN QVFAPVKKVI PLVYDAMKRA QDETGEAKLF SMNITADDYH
     EMCARADFAL EVFGPDADKL AFLVDGYVGG PGMVTTARRQ YPNQYLHYHR AGHGAITSPS
     SKRGYTAFVL AKMSRLQGAS GIHVGTMGYG KMEGEGDDRN IAYMIERDEC QGPVYFQKWY
     GMKPTTPIIS GGMNALRLPG FFENLGHGNV INTAGGGSYG HIDSPAAGAK SLRQAYECWK
     AGADPIEYAK EHKEFARAFE SFPGDADKLF PGWRDKLGVH K
//