ID   RBL_ALHEH               Reviewed;         473 AA.
AC   Q0A4R1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain;
DE            Short=RuBisCO large subunit;
DE            EC=4.1.1.39;
GN   Name=cbbL; OrderedLocusNames=Mlg_2836;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
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., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-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.
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DR   EMBL; CP000453; ABI58176.1; -; Genomic_DNA.
DR   RefSeq; YP_743666.1; -.
DR   SMR; Q0A4R1; 6-468.
DR   GeneID; 4270880; -.
DR   GenomeReviews; CP000453_GR; Mlg_2836.
DR   KEGG; aeh:Mlg_2836; -.
DR   NMPDR; fig|187272.6.peg.2710; -.
DR   HOGENOM; Q0A4R1; -.
DR   OMA; Q0A4R1; KEDRSRG.
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.
FT   CHAIN         1    473       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000299957.
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;  52871 MW;  5CBC59C904908BEC CRC64;
     MSSKSYSAGV KDYRDTYWEP DYQVKDSDFL ACFKVVPQAG VPREEAAAAV AAESSTGTWT
     TVWTDLLTDL DYYKGRAYKI EDVPGDDEAF YAFIAYPIDL FEESSVVNVF TSLVGNVFGF
     KAVRSLRLED VRIPLAYVMT CNGPPHGIQV ERDKMDKYGR GLLGCTIKPK LGLSAKNYGR
     AVYECLRGGL DFTKDDENVN SQPFMRWRDR FLFVQEATEK AQQETGERKG HYLNVTAPSP
     EEMYERAEFA KEIGAPIIMH DFLTGGFCAN TGLARWCRKN GMLLHIHRAM HAVMDRNPRH
     GIHFRVLAKA LRLSGGDHLH TGTVVGKLEG DRAATEGWID LLRERFIPED RARGIFFDQD
     WGAMPGVFAV ASGGIHVWHM PALVSIFGDD AVFQFGGGTL GHPWGNAAGA AANRVALEAC
     VKARNEGRNL EREGKEILQA AAQHSPELKI AMETWKEIKF EFETVDKLDT THR
//