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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1139548; PubMed=17540897 [NCBI, ExPASy, EBI, Israel, Japan]
Giraud E.,
Moulin L.,
Vallenet D.,
Barbe V.,
Cytryn E.,
Avarre J.-C.,
Jaubert M.,
Simon D.,
Cartieaux F.,
Prin Y.,
Bena G.,
Hannibal L.,
Fardoux J.,
Kojadinovic M.,
Vuillet L.,
Lajus A.,
Cruveiller S.,
Rouy Z.,
Mangenot S.,
Segurens B.,
Dossat C.,
Franck W.L.,
Chang W.-S.,
Saunders E.,
Bruce D.,
Richardson P.,
Normand P.,
Dreyfus B.,
Pignol D.,
Stacey G.,
Emerich D.,
Vermeglio A.,
Medigue C.,
Sadowsky M.;
"Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
Science 316:1307-1312(2007).
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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. 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 (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: 479 AA [This is the length of the unprocessed precursor] |
Molecular weight: 53334 Da [This is the MW of the unprocessed precursor] |
CRC64: 7518D7CC0AE30D6C [This is a checksum on the sequence] |
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10 20 30 40 50 60
MAEKSYQAGV KEYRKTYWTP EYVPLDTDLL AVFKIVAQAG VPREEAAAAV AAESSTGTWT
70 80 90 100 110 120
TVWTDLLTDL DYYKGRAYRI EPVPGDDNAF YAFIAYPIDL FEEGSVVNVL TSLVGNVFGF
130 140 150 160 170 180
KAVRSLRLED IRFPLAYVKT CGGPPNGIQL ERDRLNKYGR PLLGCTIKPK LGLSAKNYGR
190 200 210 220 230 240
AVYECLRGGL DFTKDDENIN SQPFMRWQHR FEFVMEAVHK ATSETGERKG HYLNVTAPTP
250 260 270 280 290 300
EEMYKRAEFA KSLGAPIIMH DFLTAGFTAN TGLANWCREN GMLLHIHRAM HAVLDRNPMH
310 320 330 340 350 360
GIHFRVLTKC LRLSGGDHLH SGTVVGKLEG DREATIGWVD LMREPFVPEN RARGIFFDQD
370 380 390 400 410 420
WGAMPGVMPV ASGGIHVWHM PALTAIFGDD ACFQFGGGTL GHPWGNAAGA HANRVALEAC
430 440 450 460 470
VEARNQGRPV EREGREILTE AAQHSPELKI AMETWKEIKF EFDVVDKLDT GPMLRVVNA
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A4YQD3 in FASTA format |
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