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Database: UniProt
Entry: P00877
LinkDB: P00877
Original site: P00877 
ID   RBL_CHLRE               Reviewed;         475 AA.
AC   P00877; B7U1I9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-OCT-2017, entry version 136.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain;
DE            Short=RuBisCO large subunit;
DE            EC=4.1.1.39;
DE   Flags: Precursor;
GN   Name=rbcL;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae;
OC   Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CARBAMYLATION AT LYS-201.
RX   PubMed=6302265; DOI=10.1016/0022-2836(82)90547-2;
RA   Dron M., Rahire M., Rochaix J.-D.;
RT   "Sequence of the chloroplast DNA region of Chlamydomonas reinhardii
RT   containing the gene of the large subunit of ribulose bisphosphate
RT   carboxylase and parts of its flanking genes.";
RL   J. Mol. Biol. 162:775-793(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-503;
RX   PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA   Smith D.R., Lee R.W.;
RT   "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT   addressing the mutational-hazard hypothesis.";
RL   BMC Evol. Biol. 9:120-120(2009).
RN   [3]
RP   PROTEIN SEQUENCE OF 3-14, AND ACETYLATION AT PRO-3.
RX   PubMed=16668742; DOI=10.1104/pp.98.3.1170;
RA   Houtz R.L., Poneleit L., Jones S.B., Royer M., Stults J.T.;
RT   "Posttranslational modifications in the amino-terminal region of the
RT   large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from
RT   several plant species.";
RL   Plant Physiol. 98:1170-1174(1992).
RN   [4]
RP   IDENTIFICATION, AND COMPLETE PLASTID GENOME.
RX   PubMed=12417694; DOI=10.1105/tpc.006155;
RA   Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W.,
RA   Harris E.H., Stern D.B.;
RT   "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in
RT   a sea of repeats.";
RL   Plant Cell 14:2659-2679(2002).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF HOLOENZYME IN COMPLEX WITH
RP   TRANSITION-STATE ANALOG 2-CABP AND MAGNESIUM, SUBUNIT, HYDROXYLATION
RP   AT PRO-104 AND PRO-151, CARBAMYLATION AT LYS-201, AND METHYLATION AT
RP   CYS-256 AND CYS-369.
RC   STRAIN=2137;
RX   PubMed=11641402; DOI=10.1074/jbc.M107765200;
RA   Taylor T.C., Backlund A., Bjorhall K., Spreitzer R.J., Andersson I.;
RT   "First crystal structure of Rubisco from a green alga, Chlamydomonas
RT   reinhardtii.";
RL   J. Biol. Chem. 276:48159-48164(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.8
RP   ANGSTROMS) OF ACTIVATED HOLOENZYME IN COMPLEX WITH TRANSITION-STATE
RP   ANALOG 2-CABP AND MAGNESIUM, FUNCTION, SUBUNIT, DISULFIDE BONDS,
RP   CARBOXYLATION AT LYS-201, HYDROXYLATION AT PRO-104 AND PRO-151, AND
RP   METHYLATION AT CYS-256 AND CYS-369.
RC   STRAIN=137c / CC-125;
RX   PubMed=11866526; DOI=10.1006/jmbi.2001.5381;
RA   Mizohata E., Matsumura H., Okano Y., Kumei M., Takuma H., Onodera J.,
RA   Kato K., Shibata N., Inoue T., Yokota A., Kai Y.;
RT   "Crystal structure of activated ribulose-1,5-bisphosphate
RT   carboxylase/oxygenase from green alga Chlamydomonas reinhardtii
RT   complexed with 2-carboxyarabinitol-1,5-bisphosphate.";
RL   J. Mol. Biol. 316:679-691(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:0000269|PubMed:11866526}.
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:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:11641402,
CC         ECO:0000269|PubMed:11866526};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:11641402,
CC       ECO:0000269|PubMed:11866526};
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:0000269|PubMed:11641402,
CC       ECO:0000269|PubMed:11866526}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- PTM: The disulfide bond which can form between Cys-247 in the
CC       large chain dimeric partners within the hexadecamer appears to be
CC       associated with oxidative stress and protein turnover (By
CC       similarity). The disulfide bond reported in 1IR2 may be the result
CC       of oxidation during crystallization.
CC       {ECO:0000250|UniProtKB:P11383, ECO:0000305}.
CC   -!- PTM: The electron density found in the position of Thr-471
CC       (PubMed:11866526 only) suggests it is either O-methylthreonine, or
CC       Ile, which may be produced by RNA editing.
CC       {ECO:0000305|PubMed:11866526}.
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:0000269|PubMed:11641402}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000305}.
DR   EMBL; J01399; AAA84449.1; -; Genomic_DNA.
DR   EMBL; FJ423446; ACJ50136.1; -; Genomic_DNA.
DR   EMBL; BK000554; DAA00950.1; -; Genomic_DNA.
DR   PIR; A01097; RKKML.
DR   RefSeq; NP_958405.1; NC_005353.1.
DR   PDB; 1GK8; X-ray; 1.40 A; A/C/E/G=1-475.
DR   PDB; 1IR2; X-ray; 1.84 A; A/B/C/D/E/F/G/H/S/T/U/V/W/X/Y/Z=1-475.
DR   PDB; 1UW9; X-ray; 2.05 A; A/B/E/H/K/O/R/V=1-475.
DR   PDB; 1UWA; X-ray; 2.30 A; A/B/E/H/K/O/R/V=1-475.
DR   PDB; 1UZD; X-ray; 2.40 A; A/B/E/H/K/O/R/V=1-475.
DR   PDB; 1UZH; X-ray; 2.20 A; A/B/E/H/K/O/R/V=1-475.
DR   PDB; 2V63; X-ray; 1.80 A; A/B/C/D/E/F/G/H=1-475.
DR   PDB; 2V67; X-ray; 2.00 A; A/B/C/D/E/F/G/H=1-475.
DR   PDB; 2V68; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-475.
DR   PDB; 2V69; X-ray; 2.80 A; A/B/C/D/E/F/G/H=1-475.
DR   PDB; 2V6A; X-ray; 1.50 A; A/B/C/D/E/F/G/H=1-475.
DR   PDB; 2VDH; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-475.
DR   PDB; 2VDI; X-ray; 2.65 A; A/B/C/D/E/F/G/H=1-475.
DR   PDB; 5BS2; X-ray; 1.97 A; A/B=462-473, R=462-467.
DR   PDBsum; 1GK8; -.
DR   PDBsum; 1IR2; -.
DR   PDBsum; 1UW9; -.
DR   PDBsum; 1UWA; -.
DR   PDBsum; 1UZD; -.
DR   PDBsum; 1UZH; -.
DR   PDBsum; 2V63; -.
DR   PDBsum; 2V67; -.
DR   PDBsum; 2V68; -.
DR   PDBsum; 2V69; -.
DR   PDBsum; 2V6A; -.
DR   PDBsum; 2VDH; -.
DR   PDBsum; 2VDI; -.
DR   PDBsum; 5BS2; -.
DR   ProteinModelPortal; P00877; -.
DR   SMR; P00877; -.
DR   STRING; 3055.DAA00950; -.
DR   iPTMnet; P00877; -.
DR   PaxDb; P00877; -.
DR   PRIDE; P00877; -.
DR   EnsemblPlants; DAA00950; DAA00950; DAA00950.
DR   GeneID; 2717040; -.
DR   Gramene; DAA00950; DAA00950; DAA00950.
DR   KEGG; cre:ChreCp049; -.
DR   eggNOG; ENOG410IIVP; Eukaryota.
DR   eggNOG; COG1850; LUCA.
DR   InParanoid; P00877; -.
DR   KO; K01601; -.
DR   BioCyc; CHLAMY:CHRECP049-MONOMER; -.
DR   EvolutionaryTrace; P00877; -.
DR   Proteomes; UP000006906; Chloroplast.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; Acetylation; Calvin cycle; Carbon dioxide fixation;
KW   Chloroplast; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Hydroxylation; Lyase; Magnesium; Metal-binding;
KW   Methylation; Monooxygenase; Oxidoreductase; Photorespiration;
KW   Photosynthesis; Plastid; Reference proteome.
FT   PROPEP        1      2       {ECO:0000269|PubMed:16668742}.
FT                                /FTId=PRO_0000031175.
FT   CHAIN         3    475       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000031176.
FT   ACT_SITE    175    175       Proton acceptor.
FT   ACT_SITE    294    294       Proton acceptor.
FT   METAL       201    201       Magnesium; via carbamate group.
FT                                {ECO:0000269|PubMed:11641402,
FT                                ECO:0000269|PubMed:11866526}.
FT   METAL       203    203       Magnesium. {ECO:0000269|PubMed:11641402,
FT                                ECO:0000269|PubMed:11866526}.
FT   METAL       204    204       Magnesium. {ECO:0000269|PubMed:11641402,
FT                                ECO:0000269|PubMed:11866526}.
FT   BINDING     123    123       Substrate; in homodimeric partner.
FT   BINDING     173    173       Substrate.
FT   BINDING     177    177       Substrate.
FT   BINDING     295    295       Substrate.
FT   BINDING     327    327       Substrate.
FT   BINDING     379    379       Substrate.
FT   SITE        334    334       Transition state stabilizer.
FT   MOD_RES       3      3       N-acetylproline.
FT                                {ECO:0000269|PubMed:16668742}.
FT   MOD_RES     104    104       4-hydroxyproline.
FT                                {ECO:0000269|PubMed:11641402,
FT                                ECO:0000269|PubMed:11866526}.
FT   MOD_RES     151    151       4-hydroxyproline.
FT                                {ECO:0000269|PubMed:11641402,
FT                                ECO:0000269|PubMed:11866526}.
FT   MOD_RES     201    201       N6-carboxylysine.
FT                                {ECO:0000269|PubMed:11641402,
FT                                ECO:0000269|PubMed:11866526,
FT                                ECO:0000269|PubMed:6302265}.
FT   MOD_RES     256    256       S-methylcysteine.
FT                                {ECO:0000269|PubMed:11641402,
FT                                ECO:0000269|PubMed:11866526}.
FT   MOD_RES     369    369       S-methylcysteine.
FT                                {ECO:0000269|PubMed:11641402,
FT                                ECO:0000269|PubMed:11866526}.
FT   DISULFID    247    247       Interchain; in linked form.
FT                                {ECO:0000269|PubMed:11641402,
FT                                ECO:0000269|PubMed:11866526}.
FT   VARIANT      46     46       L -> P (in strain: 137c and CC-503).
FT   HELIX        21     24       {ECO:0000244|PDB:1GK8}.
FT   STRAND       36     44       {ECO:0000244|PDB:1GK8}.
FT   HELIX        50     60       {ECO:0000244|PDB:1GK8}.
FT   TURN         61     63       {ECO:0000244|PDB:1GK8}.
FT   STRAND       66     68       {ECO:0000244|PDB:2V68}.
FT   HELIX        70     74       {ECO:0000244|PDB:1GK8}.
FT   HELIX        77     80       {ECO:0000244|PDB:1GK8}.
FT   STRAND       83     89       {ECO:0000244|PDB:1GK8}.
FT   STRAND       93     95       {ECO:0000244|PDB:2V6A}.
FT   STRAND       97    103       {ECO:0000244|PDB:1GK8}.
FT   HELIX       105    107       {ECO:0000244|PDB:1GK8}.
FT   HELIX       113    121       {ECO:0000244|PDB:1GK8}.
FT   HELIX       124    126       {ECO:0000244|PDB:1GK8}.
FT   STRAND      130    139       {ECO:0000244|PDB:1GK8}.
FT   HELIX       142    145       {ECO:0000244|PDB:1GK8}.
FT   HELIX       155    162       {ECO:0000244|PDB:1GK8}.
FT   STRAND      169    171       {ECO:0000244|PDB:1GK8}.
FT   STRAND      175    178       {ECO:0000244|PDB:1GK8}.
FT   HELIX       182    194       {ECO:0000244|PDB:1GK8}.
FT   STRAND      198    201       {ECO:0000244|PDB:1GK8}.
FT   STRAND      207    209       {ECO:0000244|PDB:1GK8}.
FT   HELIX       214    232       {ECO:0000244|PDB:1GK8}.
FT   STRAND      237    241       {ECO:0000244|PDB:1GK8}.
FT   HELIX       247    260       {ECO:0000244|PDB:1GK8}.
FT   STRAND      263    268       {ECO:0000244|PDB:1GK8}.
FT   HELIX       269    272       {ECO:0000244|PDB:1GK8}.
FT   HELIX       274    287       {ECO:0000244|PDB:1GK8}.
FT   STRAND      290    294       {ECO:0000244|PDB:1GK8}.
FT   HELIX       298    302       {ECO:0000244|PDB:1GK8}.
FT   STRAND      305    309       {ECO:0000244|PDB:1GK8}.
FT   HELIX       311    321       {ECO:0000244|PDB:1GK8}.
FT   STRAND      324    327       {ECO:0000244|PDB:1GK8}.
FT   STRAND      331    335       {ECO:0000244|PDB:1GK8}.
FT   HELIX       339    350       {ECO:0000244|PDB:1GK8}.
FT   STRAND      352    354       {ECO:0000244|PDB:1GK8}.
FT   HELIX       358    360       {ECO:0000244|PDB:1GK8}.
FT   STRAND      375    381       {ECO:0000244|PDB:1GK8}.
FT   HELIX       384    386       {ECO:0000244|PDB:1GK8}.
FT   HELIX       387    394       {ECO:0000244|PDB:1GK8}.
FT   STRAND      396    401       {ECO:0000244|PDB:1GK8}.
FT   HELIX       404    407       {ECO:0000244|PDB:1GK8}.
FT   HELIX       413    432       {ECO:0000244|PDB:1GK8}.
FT   HELIX       437    451       {ECO:0000244|PDB:1GK8}.
FT   HELIX       453    462       {ECO:0000244|PDB:1GK8}.
SQ   SEQUENCE   475 AA;  52543 MW;  5A9BFD394CF7D4D4 CRC64;
     MVPQTETKAG AGFKAGVKDY RLTYYTPDYV VRDTDILAAF RMTPQLGVPP EECGAAVAAE
     SSTGTWTTVW TDGLTSLDRY KGRCYDIEPV PGEDNQYIAY VAYPIDLFEE GSVTNMFTSI
     VGNVFGFKAL RALRLEDLRI PPAYVKTFVG PPHGIQVERD KLNKYGRGLL GCTIKPKLGL
     SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF VAEAIYKAQA ETGEVKGHYL
     NATAGTCEEM MKRAVCAKEL GVPIIMHDYL TGGFTANTSL AIYCRDNGLL LHIHRAMHAV
     IDRQRNHGIH FRVLAKALRM SGGDHLHSGT VVGKLEGERE VTLGFVDLMR DDYVEKDRSR
     GIYFTQDWCS MPGVMPVASG GIHVWHMPAL VEIFGDDACL QFGGGTLGHP WGNAPGAAAN
     RVALEACTQA RNEGRDLARE GGDVIRSACK WSPELAAACE VWKEIKFEFD TIDKL
//
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