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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: 443 AA [This is the length of the partial sequence of the unprocessed precursor] |
Molecular weight: 48936 Da [This is the MW of the partial sequence of the unprocessed precursor] |
CRC64: 052EB0E18B60DE82 [This is a checksum on the sequence] |
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10 20 30 40 50 60
KASVGFKAGV KDYRLTYYTP EYQTKDTDIL AAFRVTPQPG VPPEEAGAAV AAESSTGTWT
70 80 90 100 110 120
TVWTDGLTSL DRYKGRCYDI EPVAGEESQF IAYVAYPLDL FEEGSVTNLF TSIVGNVFGF
130 140 150 160 170 180
KALRALRLED LRIPPAYSKT FQGPPHGIQV ERDKLNKYGR PLLGCTIKPK LGLSAKNYGR
190 200 210 220 230 240
AVYECLRGGL DFTKDDENVN SQPFMRWRDR FVFCAEAINK AQAETGEIKG HYLNATAGTC
250 260 270 280 290 300
EEMMKRAIFA RELGVPIVMH DYLTGGFTAN TSLAHYCRDN GLLLHIHRAM HAVIDRQRNH
310 320 330 340 350 360
GMHFRVLAKA LRMSGGDHVH AGTVVGKLEG ERDVTLGFVD LLRDDFIEKD RSRGIYFTQD
370 380 390 400 410 420
WVSMPGVLPV ASGGIHVWHM PALTEIFGDD SVLQFGGGTL GHPWGNAPGA VTNRVAVEAC
430 440
VQARNEGRDL AREGNEVIRE ACK
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O78259 in FASTA format |
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