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Database: UniProt/SWISS-PROT
Entry: RBL_THEEB
LinkDB: RBL_THEEB
Original site: RBL_THEEB 
ID   RBL_THEEB               Reviewed;         475 AA.
AC   Q8DIS5;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   28-FEB-2018, entry version 98.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000255|HAMAP-Rule:MF_01338};
DE            Short=RuBisCO large subunit {ECO:0000255|HAMAP-Rule:MF_01338};
DE            EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338};
GN   Name=cbbL {ECO:0000255|HAMAP-Rule:MF_01338};
GN   Synonyms=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
GN   OrderedLocusNames=tll1506;
OS   Thermosynechococcus elongatus (strain BP-1).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N.,
RA   Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
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 in the photorespiration process. Both reactions occur
CC       simultaneously and in competition at the same active site.
CC       {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
CC       1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000255|HAMAP-
CC       Rule:MF_01338}.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2). {ECO:0000255|HAMAP-
CC       Rule:MF_01338}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01338};
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains;
CC       disulfide-linked. The disulfide link is formed within the large
CC       subunit homodimers. {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- INTERACTION:
CC       Q8DI26:tlr1766; NbExp=2; IntAct=EBI-9639313, EBI-9639332;
CC   -!- PTM: The disulfide bond which can form in the large chain dimeric
CC       partners within the hexadecamer appears to be associated with
CC       oxidative stress and protein turnover. {ECO:0000255|HAMAP-
CC       Rule:MF_01338}.
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". {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
DR   EMBL; BA000039; BAC09058.1; -; Genomic_DNA.
DR   RefSeq; NP_682296.1; NC_004113.1.
DR   RefSeq; WP_011057346.1; NC_004113.1.
DR   PDB; 2YBV; X-ray; 2.30 A; A/C/E/G/I/K/M/O=1-475.
DR   PDB; 3ZXW; X-ray; 2.10 A; A/C/E/G=1-475.
DR   PDB; 6EKC; X-ray; 2.63 A; A1/A2/A3/A4/A5/A6/A7/A8/C1/C2/C3/C4/C5/C6/C7/C8/E1/E2/E3/E4/E5/E6/E7/E8/G1/G2/G3/G4/G5/G6=1-475.
DR   PDBsum; 2YBV; -.
DR   PDBsum; 3ZXW; -.
DR   PDBsum; 6EKC; -.
DR   ProteinModelPortal; Q8DIS5; -.
DR   SMR; Q8DIS5; -.
DR   IntAct; Q8DIS5; 1.
DR   MINT; Q8DIS5; -.
DR   STRING; 197221.tll1506; -.
DR   PRIDE; Q8DIS5; -.
DR   EnsemblBacteria; BAC09058; BAC09058; BAC09058.
DR   GeneID; 1011208; -.
DR   KEGG; tel:tll1506; -.
DR   PATRIC; fig|197221.4.peg.1580; -.
DR   eggNOG; ENOG4105DT1; Bacteria.
DR   eggNOG; COG1850; LUCA.
DR   HOGENOM; HOG000230831; -.
DR   KO; K01601; -.
DR   OMA; HRAMHAA; -.
DR   OrthoDB; POG091H14UZ; -.
DR   BioCyc; TELO197221:G1G3I-1532-MONOMER; -.
DR   Proteomes; UP000000440; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   CDD; cd08212; RuBisCO_large_I; 1.
DR   Gene3D; 3.20.20.110; -; 1.
DR   Gene3D; 3.30.70.150; -; 1.
DR   HAMAP; MF_01338; RuBisCO_L_type1; 1.
DR   InterPro; IPR033966; RuBisCO.
DR   InterPro; IPR020878; RuBisCo_large_chain_AS.
DR   InterPro; IPR000685; RuBisCO_lsu_C.
DR   InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR   InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR   InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR   InterPro; IPR020888; RuBisCO_lsuI.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SUPFAM; SSF51649; SSF51649; 1.
DR   SUPFAM; SSF54966; SSF54966; 1.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calvin cycle; Carbon dioxide fixation;
KW   Complete proteome; Disulfide bond; Lyase; Magnesium; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis;
KW   Reference proteome.
FT   CHAIN         1    475       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000062649.
FT   ACT_SITE    175    175       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   ACT_SITE    294    294       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   METAL       201    201       Magnesium; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   METAL       203    203       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   METAL       204    204       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     123    123       Substrate; in homodimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   BINDING     173    173       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     177    177       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     295    295       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     327    327       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     379    379       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   SITE        334    334       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   MOD_RES     201    201       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   DISULFID    247    247       Interchain; in linked form.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   HELIX        21     24       {ECO:0000244|PDB:3ZXW}.
FT   STRAND       35     44       {ECO:0000244|PDB:3ZXW}.
FT   HELIX        50     60       {ECO:0000244|PDB:3ZXW}.
FT   TURN         61     63       {ECO:0000244|PDB:3ZXW}.
FT   STRAND       66     68       {ECO:0000244|PDB:3ZXW}.
FT   HELIX        70     74       {ECO:0000244|PDB:3ZXW}.
FT   HELIX        77     80       {ECO:0000244|PDB:3ZXW}.
FT   STRAND       83     89       {ECO:0000244|PDB:3ZXW}.
FT   STRAND       93     95       {ECO:0000244|PDB:3ZXW}.
FT   STRAND       97    103       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       105    107       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       113    121       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       124    126       {ECO:0000244|PDB:3ZXW}.
FT   STRAND      130    139       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       142    145       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       155    162       {ECO:0000244|PDB:3ZXW}.
FT   STRAND      169    173       {ECO:0000244|PDB:3ZXW}.
FT   STRAND      175    178       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       182    194       {ECO:0000244|PDB:3ZXW}.
FT   STRAND      198    201       {ECO:0000244|PDB:3ZXW}.
FT   STRAND      207    209       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       214    232       {ECO:0000244|PDB:3ZXW}.
FT   STRAND      237    241       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       247    259       {ECO:0000244|PDB:3ZXW}.
FT   STRAND      263    268       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       269    272       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       274    287       {ECO:0000244|PDB:3ZXW}.
FT   STRAND      290    294       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       298    302       {ECO:0000244|PDB:3ZXW}.
FT   STRAND      305    309       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       311    321       {ECO:0000244|PDB:3ZXW}.
FT   STRAND      324    327       {ECO:0000244|PDB:3ZXW}.
FT   STRAND      331    335       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       339    350       {ECO:0000244|PDB:3ZXW}.
FT   STRAND      352    354       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       358    360       {ECO:0000244|PDB:3ZXW}.
FT   STRAND      375    381       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       384    386       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       387    394       {ECO:0000244|PDB:3ZXW}.
FT   STRAND      396    401       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       404    407       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       413    431       {ECO:0000244|PDB:3ZXW}.
FT   TURN        432    434       {ECO:0000244|PDB:3ZXW}.
FT   TURN        437    439       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       441    451       {ECO:0000244|PDB:3ZXW}.
FT   HELIX       453    462       {ECO:0000244|PDB:3ZXW}.
SQ   SEQUENCE   475 AA;  53025 MW;  B4A97CD4D6A3EB91 CRC64;
     MAYTQSKSQK VGYQAGVKDY RLTYYTPDYT PKDTDILAAF RVTPQPGVPF EEAAAAVAAE
     SSTGTWTTVW TDLLTDLDRY KGCCYDIEPL PGEDNQFIAY IAYPLDLFEE GSVTNMLTSI
     VGNVFGFKAL KALRLEDLRI PVAYLKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
     SAKNYGRAVY ECLRGGLDFT KDDENINSQP FQRWRDRFLF VADAIHKAQA ETGEIKGHYL
     NVTAPTCEEM LKRAEFAKEL EMPIIMHDFL TAGFTANTTL SKWCRDNGML LHIHRAMHAV
     MDRQKNHGIH FRVLAKCLRM SGGDHIHTGT VVGKLEGDKA VTLGFVDLLR ENYIEQDRSR
     GIYFTQDWAS MPGVMAVASG GIHVWHMPAL VDIFGDDAVL QFGGGTLGHP WGNAPGATAN
     RVALEACIQA RNEGRDLMRE GGDIIREAAR WSPELAAACE LWKEIKFEFE AQDTI
//
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