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- 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).
- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.
- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.
- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers (By similarity).
- SUBCELLULAR LOCATION: Plastid, chloroplast.
- PTM: The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity).
- MISCELLANEOUS: The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel" (By similarity).
- SIMILARITY: Belongs to the RuBisCO large chain family. Type I subfamily.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 465 AA [This is the length of the partial sequence of the unprocessed precursor] |
Molecular weight: 51586 Da [This is the MW of the partial sequence of the unprocessed precursor] |
CRC64: A9C68403C6C11831 [This is a checksum on the sequence] |
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10 20 30 40 50 60
VGFKAGVKDY KLTYYTPDYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE SSTGTWTTVW
70 80 90 100 110 120
TDGLTSLDRY KGRCYHIEPV AGEETQFIAY VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL
130 140 150 160 170 180
RALRLEDLRI PAAYVKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY
190 200 210 220 230 240
ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIFKAQS ETGEIKGHYL NATAGTCEEM
250 260 270 280 290 300
MKRAVFAREL GVPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV IDRQKNHGMH
310 320 330 340 350 360
FRVLAKALRM SGGDHIHAGT VVGKLEGERD ITLGFVDLLR DDYIEKDRAR GIYFTQDWVS
370 380 390 400 410 420
LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN RVALEACVQA
430 440 450 460
RNEGRDLARE GNEIIRNASK WSPELAAACE VWKEIKFEFQ AMDTL
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P28377 in FASTA format |
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