ID   RBL1A_THICR             Reviewed;         472 AA.
AC   Q31IK0;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain 1;
DE            Short=RuBisCO large subunit 1;
DE            EC=4.1.1.39;
GN   Name=cbbL1; OrderedLocusNames=Tcr_0427;
OS   Thiomicrospira crunogena (strain XCL-2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Thiomicrospira.
OX   NCBI_TaxID=317025;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA   Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J.,
RA   Blake R.A., Boller A.J., Chain P.S.G., Clark J.A., Davis C.R.,
RA   Detter C., Do K.F., Dobrinski K.P., Faza B.I., Fitzpatrick K.A.,
RA   Freyermuth S.K., Harmer T.L., Hauser L.J., Huegler M., Kerfeld C.A.,
RA   Klotz M.G., Kong W.W., Land M., Lapidus A., Larimer F.W., Longo D.L.,
RA   Lucas S., Malfatti S.A., Massey S.E., Martin D.D., McCuddin Z.,
RA   Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H., Paulsen I.T.,
RA   Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P., Tinkham L.E.,
RA   Zeruth G.T.;
RT   "The genome of deep-sea vent chemolithoautotroph Thiomicrospira
RT   crunogena XCL-2.";
RL   PLoS Biol. 4:1-17(2006).
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; CP000109; ABB41023.1; -; Genomic_DNA.
DR   RefSeq; YP_390697.1; -.
DR   SMR; Q31IK0; 5-467.
DR   GeneID; 3761246; -.
DR   GenomeReviews; CP000109_GR; Tcr_0427.
DR   KEGG; tcx:Tcr_0427; -.
DR   NMPDR; fig|317025.3.peg.603; -.
DR   HOGENOM; Q31IK0; -.
DR   OMA; Q31IK0; KEDRSRG.
DR   BioCyc; TCRU317025:TCR_0427-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_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    472       Ribulose bisphosphate carboxylase large
FT                                chain 1.
FT                                /FTId=PRO_0000251466.
FT   ACT_SITE    167    167       Proton acceptor (By similarity).
FT   ACT_SITE    286    286       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     115    115       Substrate; in homodimeric partner (By
FT                                similarity).
FT   BINDING     165    165       Substrate (By similarity).
FT   BINDING     169    169       Substrate (By similarity).
FT   BINDING     287    287       Substrate (By similarity).
FT   BINDING     319    319       Substrate (By similarity).
FT   BINDING     371    371       Substrate (By similarity).
FT   SITE        326    326       Transition state stabilizer (By
FT                                similarity).
FT   MOD_RES     193    193       N6-carboxylysine (By similarity).
SQ   SEQUENCE   472 AA;  52568 MW;  5E70D6B51D425EC2 CRC64;
     MAKTYNAGVK EYRETYWMPE YEPKDSDFLA CFKVIPQDGV PREEIAAAVA AESSTGTWTT
     VWTDLLTDLD YYKGRAYKIE DVPGDDAAFY AFIAYPIDLF EEGSVVSVMT SLVGNVFGFK
     ALRACRLEDI RFPLAYVMTC GGPPHGIQVE RDKMDKYGRP MLGCTIKPKL GLSAKNYGRA
     VYECLRGGLD FTKDDENVTS QPFMRWRDRF LFCQDAIEKA QAETGERKGH YLNCTAGTPE
     EMYERAEFAK EIGTPIIMHD YLTGGFTANT GLANYCRKNG LLLHIHRAMH GVIDRNPHHG
     IHFRVLTKAL RLSGGDHLHS GTVVGKLEGD REATLGWIDL MRDSFIPEDR SRGIMFDQDF
     GAMPGVMPVA SGGIHVWHMP ALVSIFGDDS VLQFGGGTLG HPWGNAAGAA ANRVALEACV
     QARNEGKEVE KEGKEILTNA AKHSPELKIA METWKEIKFE FDTVDKLDVK HK
//