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: Homodimer (By similarity).
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

CP000250; ABD05661.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_484572.1; -.

3D structure databases

SMR

Q2J1J9; 2-456.

ModBase

Q2J1J9.

Enzyme and pathway databases

BioCyc

RPAL316058:RPB_0951-MON; -.

Ontologies

GO:0009573;	Cellular component: chloroplast ribulose bisphosphate carboxylase complex (inferred from electronic annotation from InterPro).
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.

ProtoNet

Q2J1J9.

Genome annotation databases

GeneID

3909306; -.

GenomeReviews

CP000250_GR; RPB_0951.

KEGG

rpb:RPB_0951; -.

Phylogenomic databases

HOGENOM

Q2J1J9; -.

Genome annotation databases

CMR

Q2J1J9; RPB_0951.

Other

UniRef

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

Keywords

Calvin cycle; Carbon dioxide fixation; Complete proteome; Lyase; Magnesium; Metal-binding; Monooxygenase; Oxidoreductase; Photosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 461`	`461`	`Ribulose bisphosphate carboxylase.`	`PRO_0000251409`
`ACT_SITE`	`167 167`		`Proton acceptor (By similarity).`
`ACT_SITE`	`288 288`		`Proton acceptor (By similarity).`
`METAL`	`192 192`		`Magnesium; via carbamate group (By similarity).`
`METAL`	`194 194`		`Magnesium (By similarity).`
`METAL`	`195 195`		`Magnesium (By similarity).`
`BINDING`	`112 112`		`Substrate; in homodimeric partner (By similarity).`
`BINDING`	`169 169`		`Substrate (By similarity).`
`BINDING`	`289 289`		`Substrate (By similarity).`
`BINDING`	`322 322`		`Substrate (By similarity).`
`BINDING`	`369 369`		`Substrate (By similarity).`
`SITE`	`330 330`	`1`	`Transition state stabilizer (By similarity).`
`MOD_RES`	`192 192`		`N6-carboxylysine (By similarity).`

Sequence information

Length: 461 AA [This is the length of the unprocessed precursor]

Molecular weight: 50522 Da [This is the MW of the unprocessed precursor]

CRC64: 78A84C7343DE90E9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDQSSRYANL NLKESDLIAG GRHVLCAYIM KPKDGFGNFL QTAAHFSAES STGTNVEVST 

        70         80         90        100        110        120 
TDDFTRGVDA LVYEIDEANN VMKIAYPIEL FDRNVIDGRA MIASFLTLTI GNNQGMGDVE 

       130        140        150        160        170        180 
YAKMHDFYVP PAYLRLFDGP STTIRDLWRV LGRPVVDGGF IVGTIIKPKL GLRPQPFADA 

       190        200        210        220        230        240 
CYDFWLGGDF IKNDEPQGNQ VFAPFKETVR AVNEAMRRAQ DKTGEPKLFS FNITADDHYE 

       250        260        270        280        290        300 
MVARGEYILE TFADNADHVA FLVDGYVAGP AAVTTARRAF PKQYLHYHRA GHGAVTSPQS 

       310        320        330        340        350        360 
KRGYTAFVLS KMARLQGASG IHTGTMGFGK MEGEAADRAM AYMITEDSAD GPFFHQEWLG 

       370        380        390        400        410        420 
MNPTTPIISG GMNALRMPGF FDNLGHSNLI MTAGGGAFGH IDGGAAGAKS LRQAEQCWKA 

       430        440        450        460 
GADPVEFAKD HREFARAFES FPHDADALYP NWRNSLKLAA A

Q2J1J9 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