ID   RBL1B_NITHX             Reviewed;         488 AA.
AC   Q1QGD4;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=Nham_4049;
OS   Nitrobacter hamburgensis (strain X14 / DSM 10229).
OG   Plasmid 1.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Nitrobacter.
OX   NCBI_TaxID=323097;
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., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Ward B.,
RA   Arp D., Klotz M., Stein L., O'Mullan G., Starkenburg S., Sayavedra L.,
RA   Poret-Peterson A.T., Gentry M.E., Bruce D., Richardson P.;
RT   "Complete sequence of plasmid 1 of Nitrobacter hamburgensis X14.";
RL   Submitted (MAR-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: 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.
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; CP000320; ABE64713.1; -; Genomic_DNA.
DR   RefSeq; YP_571545.1; -.
DR   SMR; Q1QGD4; 16-482.
DR   GeneID; 4025375; -.
DR   GenomeReviews; CP000320_GR; Nham_4049.
DR   KEGG; nha:Nham_4049; -.
DR   NMPDR; fig|323097.3.peg.4094; -.
DR   HOGENOM; Q1QGD4; -.
DR   OMA; Q1QGD4; QYFAYIA.
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; Plasmid.
FT   CHAIN         1    488       Ribulose bisphosphate carboxylase large
FT                                chain 2.
FT                                /FTId=PRO_0000251447.
FT   ACT_SITE    180    180       Proton acceptor (By similarity).
FT   ACT_SITE    298    298       Proton acceptor (By similarity).
FT   METAL       206    206       Magnesium; via carbamate group (By
FT                                similarity).
FT   METAL       208    208       Magnesium (By similarity).
FT   METAL       209    209       Magnesium (By similarity).
FT   BINDING     128    128       Substrate; in homodimeric partner (By
FT                                similarity).
FT   BINDING     178    178       Substrate (By similarity).
FT   BINDING     182    182       Substrate (By similarity).
FT   BINDING     299    299       Substrate (By similarity).
FT   BINDING     331    331       Substrate (By similarity).
FT   BINDING     383    383       Substrate (By similarity).
FT   SITE        338    338       Transition state stabilizer (By
FT                                similarity).
FT   MOD_RES     206    206       N6-carboxylysine (By similarity).
SQ   SEQUENCE   488 AA;  54167 MW;  D9BE53686D953C91 CRC64;
     MNVLNEKSLT VRGKDRYKSG VMSYKKMGYW EPDYTPKDTD IICLFRVTPQ DGVDPIEAAA
     AVAGESSTAT WTVVWTDRLT AAEKYRAKCY RVDPVPGAEG QYFAYIAYDL DLFEPGSISN
     LTASVIGNVF GFKPLKALRL EDMRLPVAYV KTFKGPPTGI VVERERLDKF GRPLLGATVK
     PKLGLSGRNY GRVVYEALKG GLDFTKDDEN INSQPFMHWR ERFLYCMEAV NRAQAATGEI
     KGSYLNVTAA TMEDMYERAE FAKELGSVVV MIDLVIGYTA IQSMSNWARK NDMILHLHRA
     GHSTYTRQRN HGVSFRVISK WMRLAGVDHI HAGTVVGKLE GDPLTTRGYY DICREEHNPM
     QLEHGIFFDQ NWASLNKMMP VASGGIHAGQ MHQLIQHLGE DVVLQFGGGT IGHPMGIQAG
     ATANRVALEA MILARNEGRD YVSEGPDILA KAAASCTPLK QALEVWKDVT FNYQSTDAPD
     YVTTPAVA
//