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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Rettig J.H.,
Wilson H.D.,
Manhart J.R.;
"Systematics of Caryophyllales using large subunit of ribulose-1, 5-bisphosphate carboxylase/oxygenase (rbcL) gene sequence data.";
Submitted (DEC-1991) to the EMBL/GenBank/DDBJ databases.
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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: 480 AA [This is the length of the unprocessed precursor] |
Molecular weight: 53085 Da [This is the MW of the unprocessed precursor] |
CRC64: 9CC63C7F41277491 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MSPQTETKAS VGFKAGVKDY KLTYYTPEYQ PLDTDILAAF RVTPQPGVPS EEAGAAVAAE
70 80 90 100 110 120
SSTGTWTTVW TDGLTSLDRY KGRCYHIDAV PGEDNQYICY VAYPLDLFEE GSVTNMFTSI
130 140 150 160 170 180
VGNVFGFKAL RALRLEDLRI PVAYIKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
190 200 210 220 230 240
SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIYKAQA ETGEIKGHYL
250 260 270 280 290 300
NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV
310 320 330 340 350 360
IDRQKNHGMH FRVLAKALRL SGGDHIHAGT VVGKLEGERD ITLGFVDLLR DDYTEIDPER
370 380 390 400 410 420
GIYFTQFWVS TPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
430 440 450 460 470 480
RVALEACVQA RNEGRDLARE GATIIREASK WSPELAAACE VWKEIKFEFP AVDTLDKKKG
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P25826 in FASTA format |
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