Tag | Content |
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CPLM ID | CPLM-000134 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Ribulose bisphosphate carboxylase large chain |
Protein Synonyms/Alias | RuBisCO large subunit |
Gene Name | rbcL |
Gene Synonyms/Alias | AtCg00490 |
Created Date | July 27, 2013 |
Organism | Arabidopsis thaliana (Mouse-ear cress) |
NCBI Taxa ID | 3702 |
Lysine Modification | Position | Peptide | Type | References |
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14 | TKASVGFKAGVKEYK | acetylation | [1] | 18 | VGFKAGVKEYKLTYY | acetylation | [1] | 21 | KAGVKEYKLTYYTPE | acetylation | [1] | 146 | RIPPAYTKTFQGPPH | acetylation | [1] | 175 | PLLGCTIKPKLGLSA | acetylation | [1] | 252 | GTCEEMIKRAVFARE | acetylation | [2] | 316 | MHFRVLAKALRLSGG | acetylation | [1] | 356 | LRDDYVEKDRSRGIF | acetylation | [1] | 463 | AAACEVWKEITFNFP | acetylation | [1] |
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Reference | [1] Proteins of diverse function and subcellular location are lysine acetylated in Arabidopsis. Finkemeier I, Laxa M, Miguet L, Howden AJ, Sweetlove LJ. Plant Physiol. 2011 Apr;155(4):1779-90. [ PMID: 21311031] [2] Lysine acetylation is a widespread protein modification for diverse proteins in Arabidopsis. Wu X, Oh MH, Schwarz EM, Larue CT, Sivaguru M, Imai BS, Yau PM, Ort DR, Huber SC. Plant Physiol. 2011 Apr;155(4):1769-78. [ PMID: 21311030] |
Functional Description | 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). |
Sequence Annotation | ACT_SITE 175 175 Proton acceptor (By similarity). ACT_SITE 294 294 Proton acceptor (By similarity). METAL 201 201 Magnesium; via carbamate group (By METAL 203 203 Magnesium (By similarity). METAL 204 204 Magnesium (By similarity). BINDING 123 123 Substrate; in homodimeric partner (By BINDING 173 173 Substrate (By similarity). BINDING 177 177 Substrate (By similarity). BINDING 295 295 Substrate (By similarity). BINDING 327 327 Substrate (By similarity). BINDING 379 379 Substrate (By similarity). MOD_RES 3 3 N-acetylproline (By similarity). MOD_RES 14 14 N6,N6,N6-trimethyllysine (By similarity). MOD_RES 147 147 Phosphothreonine. MOD_RES 201 201 N6-carboxylysine (By similarity). MOD_RES 330 330 Phosphothreonine. DISULFID 247 247 Interchain; in linked form (By |
Keyword | Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast; Complete proteome; Disulfide bond; Lyase; Magnesium; Metal-binding; Methylation; Monooxygenase; Oxidoreductase; Phosphoprotein; Photorespiration; Photosynthesis; Plastid; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 479 AA |
Protein Sequence | MSPQTETKAS VGFKAGVKEY KLTYYTPEYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE 60 SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV PGEETQFIAY VAYPLDLFEE GSVTNMFTSI 120 VGNVFGFKAL AALRLEDLRI PPAYTKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL 180 SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIYKSQA ETGEIKGHYL 240 NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTSL SHYCRDNGLL LHIHRAMHAV 300 IDRQKNHGMH FRVLAKALRL SGGDHIHAGT VVGKLEGDRE STLGFVDLLR DDYVEKDRSR 360 GIFFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN 420 RVALEACVQA RNEGRDLAVE GNEIIREACK WSPELAAACE VWKEITFNFP TIDKLDGQE 479 |
Gene Ontology | GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. GO:0000287; F:magnesium ion binding; IEA:HAMAP. GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:HAMAP. GO:0009853; P:photorespiration; IEA:UniProtKB-KW. GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW. |
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