| Tag | Content |
|---|
| CPLM ID | CPLM-001818 |
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 | rbcA |
Created Date | July 27, 2013 |
Organism | Nicotiana tabacum (Common tobacco) |
NCBI Taxa ID | 4097 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 14 | TKASVGFKAGVKEYK | methylation | [1, 2] |
|
Reference | [1] Rubisco small and large subunit N-methyltransferases. Bi- and mono-functional methyltransferases that methylate the small and large subunits of Rubisco. Ying Z, Mulligan RM, Janney N, Houtz RL. J Biol Chem. 1999 Dec 17;274(51):36750-6. [ PMID: 10593982] [2] Update on activities at the Universal Protein Resource (UniProt) in 2013. e="String">UniProt Consortium. Nucleic Acids Res. 2013 Jan;41(Database issue):D43-7. [ PMID: 23161681] |
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. |
Sequence Annotation | ACT_SITE 175 175 Proton acceptor.
ACT_SITE 294 294 Proton acceptor.
METAL 201 201 Magnesium; via carbamate group.
METAL 203 203 Magnesium.
METAL 204 204 Magnesium.
BINDING 123 123 Substrate; in homodimeric partner.
BINDING 173 173 Substrate.
BINDING 177 177 Substrate.
BINDING 295 295 Substrate.
BINDING 327 327 Substrate.
BINDING 379 379 Substrate.
MOD_RES 3 3 N-acetylproline.
MOD_RES 14 14 N6,N6,N6-trimethyllysine.
MOD_RES 201 201 N6-carboxylysine.
DISULFID 247 247 Interchain; in linked form. |
Keyword | 3D-structure; Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast; Direct protein sequencing; Disulfide bond; Lyase; Magnesium; Metal-binding; Methylation; Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis; Plastid. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 477 AA |
Protein Sequence | MSPQTETKAS VGFKAGVKEY KLTYYTPEYQ TKDTDILAAF RVTPQPGVPP EEAGAAVAAE 60
SSTGTWTTVW TDGLTSLDRY KGRCYRIERV VGEKDQYIAY VAYPLDLFEE GSVTNMFTSI 120
VGNVFGFKAL RALRLEDLRI PPAYVKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL 180
SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEALYKAQA ETGEIKGHYL 240
NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV 300
IDRQKNHGIH FRVLAKALRM SGGDHIHSGT VVGKLEGERD ITLGFVDLLR DDFVEQDRSR 360
GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN 420
RVALEACVKA RNEGRDLAQE GNEIIREACK WSPELAAACE VWKEIVFNFA AVDVLDK 477 |
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. |
Interpro | |
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