| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Ribulose bisphosphate carboxylase large chain |
Protein Synonyms/Alias | RuBisCO large subunit |
Gene Name | cbbL |
Gene Synonyms/Alias | rbcL; OrderedLocusNames=SYNPCC7002_A1798 |
Created Date | 3-June-2014 |
Organism | Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) |
NCBI Taxa ID | 32049 |
Phosphorylation | Position | Peptide | Code | Type | References | | 18 | GVQDYRLTYYTPDYT | T | HTP | [1] | | 25 | TYYTPDYTPKDTDLL | T | HTP | [1] | | 15 | FNAGVQDYRLTYYTP | Y | HTP | [1] | | 447 | LREAGKWSPELAAAL | S | HTP | [1] | | 323 | SGGDHLHSGTVVGKL | S | HTP | [1] | | 21 | DYRLTYYTPDYTPKD | T | HTP | [1] | |
Reference | [1]Global phosphoproteomic analysis reveals diverse functions of serine/threonine/tyrosine phosphorylation in the model cyanobacterium Synechococcus sp. strain PCC 7002. Yang MK,Qiao ZX,Zhang WY,Xiong Q,Zhang J,Li T,Ge F,Zhao JD J. Proteome Res. 2013, Apr, 5;12(4):1909-23. [ PMID:23461524] |
Functional Description From UniProt | FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (By similarity) |
| MOD_RES 196 196 N6-carboxylysine (By similarity)
DISULFID 242 242 Interchain; in linked form (By similarity) |
| 3D-structure; Calvincycle; Carbondioxidefixation; Completeproteome; Disulfidebond; Lyase; Magnesium; Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis |
Protein Sequence | MQTKSAGFNA GVQDYRLTYY TPDYTPKDTD LLACFRMTPQ PGVPPEECAA AVAAESSTGT 60
WTTVWTDGLT DLDRYKGRCY NVEPVPGEDN QYFCFVAYPL DLFEEGSVTN VLTSLVGNVF 120
GFKALRALRL EDIRFPVALI KTYQGPPHGI TVERDLLNKY GRPLLGCTIK PKLGLSAKNY 180
GRAVYECLRG GLDFTKDDEN INSQPFMRWR DRFLFVQEAI EKSQAETNEV KGHYLNVTAG 240
TCEEMLKRAE FAKEIGTPII MHDFLTGGFT ANTTLAKWCR DNGVLLHIHR AMHAVIDRQK 300
NHGIHFRVLA KCLRLSGGDH LHSGTVVGKL EGDRAATLGF VDLMREDYVE EDRSRGVFFT 360
QDYASLPGTM PVASGGIHVW HMPALVEIFG DDSCLQFGGG TLGHPWGNAP GATANRVALE 420
ACVQARNEGR SLAREGNDVL REAGKWSPEL AAALDLWKEI KFEFDTVDTL 470 |
| GO:0000287 F:magnesium ion binding IEA:UniProtKB-HAMAP GO:0004497 F:monooxygenase activity IEA:UniProtKB-KW GO:0016984 F:ribulose-bisphosphate carboxylase activity IEA:UniProtKB-HAMAP GO:0009853 P:photorespiration IEA:UniProtKB-KW GO:0019253 P:reductive pentose-phosphate cycle IEA:UniProtKB-KW |
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