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

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Cross-references

Sequence databases

EMBL

CP000230; ABC23200.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_427487.1; -.

3D structure databases

SMR

Q2RRP5; 2-457.

ModBase

Q2RRP5.

Enzyme and pathway databases

BioCyc

RRUB269796:RRU_A2400-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.

Genome annotation databases

GeneID

3835834; -.

GenomeReviews

CP000230_GR; Rru_A2400.

KEGG

rru:Rru_A2400; -.

NMPDR

fig|1085.1.peg.49; -.

Phylogenomic databases

HOGENOM

Q2RRP5; -.

Genome annotation databases

CMR

Q2RRP5; Rru_A2400.

Other

ProtoNet

Q2RRP5.

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`	`1 466`	`466`	`Ribulose bisphosphate carboxylase.`	`PRO_0000251412`
`ACT_SITE`	`166 166`		`Proton acceptor (By similarity).`
`ACT_SITE`	`287 287`		`Proton acceptor (By similarity).`
`METAL`	`191 191`		`Magnesium; via carbamate group (By similarity).`
`METAL`	`193 193`		`Magnesium (By similarity).`
`METAL`	`194 194`		`Magnesium (By similarity).`
`BINDING`	`111 111`		`Substrate; in homodimeric partner (By similarity).`
`BINDING`	`168 168`		`Substrate (By similarity).`
`BINDING`	`288 288`		`Substrate (By similarity).`
`BINDING`	`321 321`		`Substrate (By similarity).`
`BINDING`	`368 368`		`Substrate (By similarity).`
`SITE`	`329 329`	`1`	`Transition state stabilizer (By similarity).`
`MOD_RES`	`191 191`		`N6-carboxylysine (By similarity).`

Sequence information

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

Molecular weight: 50482 Da [This is the MW of the unprocessed precursor]

CRC64: 4D9F800450AB0155 [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 DRNITDGKAM 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

Q2RRP5 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