[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=6307620 [NCBI, ExPASy, EBI, Israel, Japan] Reichelt B.Y., Delaney S.F.; "The nucleotide sequence for the large subunit of ribulose 1,5-bisphosphate carboxylase from a unicellular cyanobacterium, Synechococcus PCC6301."; DNA 2:121-129(1983).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=16593333 [NCBI, ExPASy, EBI, Israel, Japan] Shinozaki K., Yamada C., Takahata N., Sugiura M.; "Molecular cloning and sequence analysis of the cyanobacterial gene for the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase."; Proc. Natl. Acad. Sci. U.S.A. 80:4050-4054(1983).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Shinozaki K., Sugiura M.; "Genes for the large and small subunits of ribulose-1,5-bisphosphate carboxylase/oxygenase constitute a single operon in a cyanobacterium Anacystis nidulans 6301."; Mol. Gen. Genet. 200:27-32(1985).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1007/s11120-006-9122-4; PubMed=17211581 [NCBI, ExPASy, EBI, Israel, Japan] Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M., Kanehisa M., Omata T., Sugiura M., Sugita M.; "Complete nucleotide sequence of the freshwater unicellular cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene content and organization."; Photosyn. Res. 93:55-67(2007).
[5]	PROTEIN SEQUENCE OF 333-342. DOI=10.1006/abbi.1994.1301; PubMed=8031129 [NCBI, ExPASy, EBI, Israel, Japan] Read B.A., Tabita F.R.; "High substrate specificity factor ribulose bisphosphate carboxylase/oxygenase from eukaryotic marine algae and properties of recombinant cyanobacterial RubiSCO containing 'algal' residue modifications."; Arch. Biochem. Biophys. 312:210-218(1994).
[6]	KINETIC CHARACTERIZATION. DOI=10.1006/abbi.1998.0979; PubMed=9882445 [NCBI, ExPASy, EBI, Israel, Japan] Horken K.M., Tabita F.R.; "Closely related form I ribulose bisphosphate carboxylase/oxygenase molecules that possess different CO2/O2 substrate specificities."; Arch. Biochem. Biophys. 361:183-194(1999).
[7]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). PubMed=8245022 [NCBI, ExPASy, EBI, Israel, Japan] Newman J., Gutteridge S.; "The X-ray structure of Synechococcus ribulose-bisphosphate carboxylase/oxygenase-activated quaternary complex at 2.2-A resolution."; J. Biol. Chem. 268:25876-25886(1993).
[8]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). DOI=10.1016/S0969-2126(00)00050-2; PubMed=7922027 [NCBI, ExPASy, EBI, Israel, Japan] Newman J., Gutteridge S.; "Structure of an effector-induced inactivated state of ribulose 1,5-bisphosphate carboxylase/oxygenase: the binary complex between enzyme and xylulose 1,5-bisphosphate."; Structure 2:495-502(1994).

Comments

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.
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.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=39 µM for ribulose 1,5-bisphosphate;
K_M=173 µM for CO₂;
V_max=2.5 µmol/min/mg enzyme with CO₂ as substrate;
Note=The CO(2)/O(2) specificity factor (tau) is 39;
SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.
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). Note this disulfide bond has not been seen in these crystal structures.
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".
SIMILARITY: Belongs to the RuBisCO large chain family. Type I subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

K00486; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
X03220; CAA26972.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP008231; BAD78320.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A90941; RKYCL.

RefSeq

YP_170840.1; -.

3D structure databases

PDB

1RBL; X-ray; 2.20 A; A/B/C/D/E/F/G/H=6-472.	[ExPASy / RCSB / EBI]
1RSC; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-472.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1RBL; -.
1RSC; -.

ModBase

P00880.

Protein-protein interaction databases

DIP

DIP:6210N; -.

Enzyme and pathway databases

BioCyc

SELO269084:SYC0130_C-MON; -.

Ontologies

GO:0016984;	Molecular function: ribulose-bisphosphate carboxylase activity (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01338; -; 1.
PBIL [Tree]

InterPro

IPR000685; RuBisCO_lsu_C.
IPR017443; RuBisCO_lsu_fd_N.
IPR017444; RuBisCO_lsu_N.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.110; RuBisCO_large; 1.
G3DSA:3.30.70.150; RuBisCO_large; 1.

Pfam

PF00016; RuBisCO_large; 1.
PF02788; RuBisCO_large_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00157; RUBISCO_LARGE; 1.

BLOCKS

P00880.

Genome annotation databases

GeneID

3200134; -.

GenomeReviews

AP008231_GR; syc0130_c.

KEGG

syc:syc0130_c; -.

Phylogenomic databases

HOGENOM

P00880; -.

Other

LinkHub

P00880; -.

Genome annotation databases

CMR

P00880; syc0130_c.

Other

ProtoNet

P00880.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Calvin cycle; Carbon dioxide fixation; Complete proteome; Direct protein sequencing; Lyase; Magnesium; Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 472`	`472`	`Ribulose bisphosphate carboxylase large chain.`	`PRO_0000062651`
`ACT_SITE`	`172 172`		`Proton acceptor.`
`ACT_SITE`	`291 291`		`Proton acceptor.`
`METAL`	`198 198`		`Magnesium; via carbamate group.`
`METAL`	`200 200`		`Magnesium.`
`METAL`	`201 201`		`Magnesium.`
`BINDING`	`120 120`		`Substrate; in homodimeric partner.`
`BINDING`	`170 170`		`Substrate.`
`BINDING`	`174 174`		`Substrate.`
`BINDING`	`292 292`		`Substrate.`
`BINDING`	`324 324`		`Substrate.`
`BINDING`	`376 376`		`Substrate.`
`SITE`	`331 331`	`1`	`Transition state stabilizer.`
`MOD_RES`	`198 198`		`N6-carboxylysine.`
`CONFLICT`	`38 39`		`RF -> PV (in Ref. 1).`
`CONFLICT`	`353 353`		`A -> R (in Ref. 1).`
`HELIX`	`18 21`	`4`
`STRAND`	`32 41`	`10`
`HELIX`	`47 57`	`11`
`TURN`	`58 60`	`3`
`STRAND`	`63 65`	`3`
`HELIX`	`67 71`	`5`
`HELIX`	`74 77`	`4`
`STRAND`	`80 86`	`7`
`STRAND`	`94 100`	`7`
`HELIX`	`102 104`	`3`
`HELIX`	`110 118`	`9`
`HELIX`	`121 123`	`3`
`STRAND`	`127 136`	`10`
`HELIX`	`139 142`	`4`
`HELIX`	`152 159`	`8`
`STRAND`	`166 168`	`3`
`STRAND`	`172 175`	`4`
`HELIX`	`179 191`	`13`
`STRAND`	`195 198`	`4`
`STRAND`	`204 206`	`3`
`HELIX`	`211 229`	`19`
`STRAND`	`234 238`	`5`
`HELIX`	`244 256`	`13`
`STRAND`	`260 265`	`6`
`HELIX`	`266 269`	`4`
`HELIX`	`271 284`	`14`
`STRAND`	`287 291`	`5`
`HELIX`	`295 299`	`5`
`STRAND`	`302 306`	`5`
`HELIX`	`308 318`	`11`
`STRAND`	`321 324`	`4`
`STRAND`	`328 332`	`5`
`HELIX`	`336 347`	`12`
`STRAND`	`349 351`	`3`
`HELIX`	`355 357`	`3`
`STRAND`	`372 378`	`7`
`HELIX`	`381 383`	`3`
`HELIX`	`384 391`	`8`
`STRAND`	`396 398`	`3`
`HELIX`	`401 404`	`4`
`HELIX`	`410 430`	`21`
`HELIX`	`434 448`	`15`
`HELIX`	`450 459`	`10`

Sequence information

Length: 472 AA [This is the length of the unprocessed precursor]

Molecular weight: 52448 Da [This is the MW of the unprocessed precursor]

CRC64: CDD8519AA9D493C9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPKTQSAAGY KAGVKDYKLT YYTPDYTPKD TDLLAAFRFS PQPGVPADEA GAAIAAESST 

        70         80         90        100        110        120 
GTWTTVWTDL LTDMDRYKGK CYHIEPVQGE ENSYFAFIAY PLDLFEEGSV TNILTSIVGN 

       130        140        150        160        170        180 
VFGFKAIRSL RLEDIRFPVA LVKTFQGPPH GIQVERDLLN KYGRPMLGCT IKPKLGLSAK 

       190        200        210        220        230        240 
NYGRAVYECL RGGLDFTKDD ENINSQPFQR WRDRFLFVAD AIHKSQAETG EIKGHYLNVT 

       250        260        270        280        290        300 
APTCEEMMKR AEFAKELGMP IIMHDFLTAG FTANTTLAKW CRDNGVLLHI HRAMHAVIDR 

       310        320        330        340        350        360 
QRNHGIHFRV LAKCLRLSGG DHLHSGTVVG KLEGDKASTL GFVDLMREDH IEADRSRGVF 

       370        380        390        400        410        420 
FTQDWASMPG VLPVASGGIH VWHMPALVEI FGDDSVLQFG GGTLGHPWGN APGATANRVA 

       430        440        450        460        470 
LEACVQARNE GRDLYREGGD ILREAGKWSP ELAAALDLWK EIKFEFETMD KL

P00880 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools