[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Nargang F., McIntosh L., Somerville C.R.; "Nucleotide sequence of the ribulosebisphosphate carboxylase gene from Rhodospirillum rubrum."; Mol. Gen. Genet. 193:220-224(1984).
[2]	PROTEIN SEQUENCE OF 314-337. DOI=10.1021/bi00275a028; PubMed=6404301 [NCBI, ExPASy, EBI, Israel, Japan] Fraij B., Hartman F.C.; "Isolation and sequencing of an active-site peptide from Rhodospirillum rubrum ribulosebisphosphate carboxylase/oxygenase after affinity labeling with 2-[(bromoacetyl)amino]pentitol 1,5-bisphosphate."; Biochemistry 22:1515-1520(1983).
[3]	X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). PubMed=16453738 [NCBI, ExPASy, EBI, Israel, Japan] Schneider G., Lindqvist Y., Braenden C.-I., Lorimer G.; "Three-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9-A resolution."; EMBO J. 5:3409-3415(1986).
[4]	X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). Andersson I., Knight S., Schneider G., Lindqvist Y., Lundqvist T., Braenden C.-I., Lorimer G.H.; "Crystal structure of the active site of ribulose-bisphosphate carboxylase."; Nature 337:229-234(1989).
[5]	X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). DOI=10.1016/0022-2836(90)90088-4; PubMed=2107319 [NCBI, ExPASy, EBI, Israel, Japan] Schneider G., Lindqvist Y., Lundqvist T.; "Crystallographic refinement and structure of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum at 1.7-A resolution."; J. Mol. Biol. 211:989-1008(1990).
[6]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), COFACTOR, AND SUBUNIT. DOI=10.1021/bi00218a004; PubMed=1899197 [NCBI, ExPASy, EBI, Israel, Japan] Lundqvist T., Schneider G.; "Crystal structure of the ternary complex of ribulose-1,5-bisphosphate carboxylase, Mg(II), and activator CO2 at 2.3-A resolution."; Biochemistry 30:904-908(1991).

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. 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.
SUBUNIT: Homodimer.
MISCELLANEOUS: The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits (By similarity).
SIMILARITY: Belongs to the RuBisCO large chain family. Type II 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

X00286; CAA25080.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S07295; S07295.

3D structure databases

PDB

1RBA; X-ray; 2.60 A; A/B=1-466.	[ExPASy / RCSB / EBI]
1RUS; X-ray; 2.90 A; A/B=1-466.	[ExPASy / RCSB / EBI]
2RUS; X-ray; 2.30 A; A/B=1-466.	[ExPASy / RCSB / EBI]
5RUB; X-ray; 1.70 A; A/B=1-466.	[ExPASy / RCSB / EBI]
9RUB; X-ray; 2.60 A; A/B=1-466.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1RBA; -.
1RUS; -.
2RUS; -.
5RUB; -.
9RUB; -.

ModBase

P04718.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13280; -.

Ontologies

GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004497;	Molecular function: monooxygenase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0016984;	Molecular function: ribulose-bisphosphate carboxylase activity (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019253;	Biological process: reductive pentose-phosphate cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01339; -; 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.

Other

P04718; -.

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 466`	`466`	`Ribulose bisphosphate carboxylase.`	`PRO_0000062666`
`ACT_SITE`	`166 166`		`Proton acceptor.`
`ACT_SITE`	`287 287`		`Proton acceptor.`
`METAL`	`191 191`		`Magnesium; via carbamate group.`
`METAL`	`193 193`		`Magnesium.`
`METAL`	`194 194`		`Magnesium.`
`BINDING`	`111 111`		`Substrate; in homodimeric partner.`
`BINDING`	`168 168`		`Substrate.`
`BINDING`	`288 288`		`Substrate.`
`BINDING`	`321 321`		`Substrate.`
`BINDING`	`368 368`		`Substrate.`
`SITE`	`329 329`	`1`	`Transition state stabilizer.`
`MOD_RES`	`191 191`		`N6-carboxylysine.`
`TURN`	`4 6`	`3`
`HELIX`	`14 19`	`6`
`STRAND`	`23 32`	`10`
`STRAND`	`34 36`	`3`
`HELIX`	`38 48`	`11`
`TURN`	`49 51`	`3`
`STRAND`	`70 75`	`6`
`TURN`	`76 79`	`4`
`STRAND`	`80 86`	`7`
`HELIX`	`87 89`	`3`
`TURN`	`94 96`	`3`
`HELIX`	`101 108`	`8`
`STRAND`	`118 127`	`10`
`HELIX`	`130 133`	`4`
`HELIX`	`143 150`	`8`
`STRAND`	`154 156`	`3`
`STRAND`	`160 164`	`5`
`STRAND`	`166 169`	`4`
`HELIX`	`173 184`	`12`
`STRAND`	`188 191`	`4`
`HELIX`	`204 222`	`19`
`STRAND`	`227 231`	`5`
`HELIX`	`237 251`	`15`
`HELIX`	`252 257`	`6`
`STRAND`	`258 262`	`5`
`TURN`	`264 267`	`4`
`HELIX`	`269 278`	`10`
`STRAND`	`284 286`	`3`
`HELIX`	`291 293`	`3`
`STRAND`	`301 303`	`3`
`HELIX`	`305 315`	`11`
`STRAND`	`318 323`	`6`
`HELIX`	`337 344`	`8`
`STRAND`	`346 349`	`4`
`STRAND`	`354 356`	`3`
`STRAND`	`364 369`	`6`
`TURN`	`373 375`	`3`
`HELIX`	`376 383`	`8`
`STRAND`	`388 392`	`5`
`TURN`	`394 397`	`4`
`HELIX`	`403 419`	`17`
`HELIX`	`423 428`	`6`
`HELIX`	`431 439`	`9`
`HELIX`	`441 447`	`7`
`HELIX`	`449 451`	`3`
`HELIX`	`452 455`	`4`

Sequence information

Length: 466 AA [This is the length of the unprocessed precursor]

Molecular weight: 50504 Da [This is the MW of the unprocessed precursor]

CRC64: 37D8C0076CAF7D54 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDQSSRYVNL ALKEEDLIAG GEHVLCAYIM KPKAGYGYVA TAAHFAAESS TGTNVEVCTT 

        70         80         90        100        110        120 
DDFTRGVDAL VYEVDEAREL TKIAYPVALF HRNITDGKAM IASFLTLTMG NNQGMGDVEY 

       130        140        150        160        170        180 
AKMHDFYVPE AYRALFDGPS VNISALWKVL GRPEVDGGLV VGTIIKPKLG LRPKPFAEAC 

       190        200        210        220        230        240 
HAFWLGGDFI KNDEPQGNQP FAPLRDTIAL VADAMRRAQD ETGEAKLFSA NITADDPFEI 

       250        260        270        280        290        300 
IARGEYVLET FGENASHVAL LVDGYVAGAA AITTARRRFP DNFLHYHRAG HGAVTSPQSK 

       310        320        330        340        350        360 
RGYTAFVHCK MARLQGASGI HTGTMGFGKM EGESSDRAIA YMLTQDEAQG PFYRQSWGGM 

       370        380        390        400        410        420 
KACTPIISGG MNALRMPGFF ENLGNANVIL TAGGGAFGHI DGPVAGARSL RQAWQAWRDG 

       430        440        450        460 
VPVLDYAREH KELARAFESF PGDADQIYPG WRKALGVEDT RSALPA

P04718 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