ID   RBL1_RHOCA              Reviewed;         473 AA.
AC   O32740;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   24-MAR-2009, entry version 51.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain;
DE            Short=RuBisCO large subunit;
DE            EC=4.1.1.39;
GN   Name=cbbL; Synonyms=cbbL1;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9467914;
RA   Paoli G.C., Soyer F., Shively J., Tabita F.R.;
RT   "Rhodobacter capsulatus genes encoding form I ribulose-1,5-
RT   bisphosphate carboxylase/oxygenase (cbbLS) and neighbouring genes were
RT   acquired by a horizontal gene transfer.";
RL   Microbiology 144:219-227(1998).
RN   [2]
RP   OPERON ORGANIZATION.
RC   STRAIN=ATCC 23782 / LMG 2373 / NCIB 11773 / SB1003 / St. Louis;
RX   MEDLINE=96118765; PubMed=8588741; DOI=10.1007/s002030050281;
RA   Paoli G.C., Morgan N.S., Tabita F.R., Shively J.M.;
RT   "Expression of the cbbLcbbS and cbbM genes and distinct organization
RT   of the cbb Calvin cycle structural genes of Rhodobacter capsulatus.";
RL   Arch. Microbiol. 164:396-405(1995).
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; L82000; AAC37141.1; -; Genomic_DNA.
DR   HSSP; O93627; 1GEH.
DR   SMR; O32740; 2-468.
DR   BRENDA; 4.1.1.39; 567.
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; Lyase; Magnesium;
KW   Metal-binding; Monooxygenase; Oxidoreductase; Photosynthesis.
FT   CHAIN         1    473       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000062645.
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   473 AA;  53037 MW;  9F2C3173618B9958 CRC64;
     MAAKTYDAGV KDYRSIYWEP QYQVKDSDIL AVFKVVPQPG VSREEAAAAV AAESSTATWT
     TVWTDLLTDL DYYKGRAYAI EDVPGSDEAF YAFIAYPMDL FEEGSVVNVF TSLVGNVFGF
     KAVRALRLED VRFPLWFVMT CPGAPHGMKV ERDLLDKYGR PLLGCTIKPK LGLAAKNYGR
     AVYECLRGGL DFTKDDENVN SQPFLRWRDR FLFCQEAIQK AEAETGERKG HYMNVTAGTM
     EEIYERAEFA KEIGTPIIMS DYLTVGWAAH TSLSRWCRKN GMLLHVHRAM HAVMDRNPNH
     GINFRVLAKI LRLMGGDHLH SGTVVGKLEG DREATIGWIN LLRDRFIKAD RSRGIFFDQD
     WGPQPGLFPV ASGGIHVWHM PALVSIFGND SVLQFGGGTL GHPWGNAAGA CANRVALEAC
     VQARNEGRHL EKEGKEILTK AAQSSPELRM AMETWKEIKF EFDTVDKLDV QHR
//