Skip Header

Contribute Send feedback
Read comments (?) or add your own

P04718 (RBL2_RHORU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase
Short name=RuBisCO
EC=4.1.1.39
Gene names
Name:cbbM
Synonyms:cbbL2, rbpL
OrganismRhodospirillum rubrum
Taxonomic identifier1085 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Rhodospirillaceae › Rhodospirillum

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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. HAMAP-Rule MF_01339

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01339

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01339

Cofactor

Binds 1 magnesium ion per subunit. Ref.6

Subunit structure

Homodimer. Ref.6

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. HAMAP-Rule MF_01339

Sequence similarities

Belongs to the RuBisCO large chain family. Type II subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Ribulose bisphosphate carboxylase HAMAP-Rule MF_01339
PRO_0000062666

Sites

Active site1661Proton acceptor
Active site2871Proton acceptor
Metal binding1911Magnesium; via carbamate group
Metal binding1931Magnesium
Metal binding1941Magnesium
Binding site1111Substrate; in homodimeric partner
Binding site1681Substrate
Binding site2881Substrate
Binding site3211Substrate
Binding site3681Substrate
Site3291Transition state stabilizer

Amino acid modifications

Modified residue1911N6-carboxylysine HAMAP-Rule MF_01339

Secondary structure

1 ......................................................................................... 466
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04718 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 37D8C0076CAF7D54

FASTA46650,504
        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

« Hide

References

[1]"Nucleotide sequence of the ribulosebisphosphate carboxylase gene from Rhodospirillum rubrum."
Nargang F., McIntosh L., Somerville C.R.
Mol. Gen. Genet. 193:220-224(1984)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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."
Fraij B., Hartman F.C.
Biochemistry 22:1515-1520(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 314-337.
[3]"Three-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9-A resolution."
Schneider G., Lindqvist Y., Braenden C.-I., Lorimer G.
EMBO J. 5:3409-3415(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[4]"Crystal structure of the active site of ribulose-bisphosphate carboxylase."
Andersson I., Knight S., Schneider G., Lindqvist Y., Lundqvist T., Braenden C.-I., Lorimer G.H.
Nature 337:229-234(1989)
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[5]"Crystallographic refinement and structure of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum at 1.7-A resolution."
Schneider G., Lindqvist Y., Lundqvist T.
J. Mol. Biol. 211:989-1008(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[6]"Crystal structure of the ternary complex of ribulose-1,5-bisphosphate carboxylase, Mg(II), and activator CO2 at 2.3-A resolution."
Lundqvist T., Schneider G.
Biochemistry 30:904-908(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), COFACTOR, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X00286 Genomic DNA. Translation: CAA25080.1.
PIRS07295.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RBAX-ray2.60A/B1-466[»]
1RUSX-ray2.90A/B1-466[»]
2RUSX-ray2.30A/B1-466[»]
5RUBX-ray1.70A/B1-466[»]
9RUBX-ray2.60A/B1-466[»]
ProteinModelPortalP04718.
SMRP04718. Positions 2-460.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-8090212.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13280.
SABIO-RKP04718.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01339. RuBisCO_L_type2.
InterProIPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMSSF51649. RuBisCO_large. 1 hit.
SSF54966. RuBisCO_large. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04718.

Entry information

Entry nameRBL2_RHORU
AccessionPrimary (citable) accession number: P04718
Secondary accession number(s): P19365, P72313
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: May 29, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents