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P50922 (RBL2_RHOCA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase
Short name=RuBisCO
EC=4.1.1.39
Gene names
Name:cbbM
Synonyms:cbbL2, rbpL
OrganismRhodobacter capsulatus (Rhodopseudomonas capsulata)
Taxonomic identifier1061 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 MF_01339

Catalytic activity

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

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

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01339

Subunit structure

Homodimer By similarity. HAMAP MF_01339

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 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 – 458458Ribulose bisphosphate carboxylase HAMAP MF_01339
PRO_0000062664

Sites

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

Amino acid modifications

Modified residue1911N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P50922 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 2C63CDD57C653FAA

FASTA45850,092
        10         20         30         40         50         60 
MDQSNRYARL DLKEADLIAG GRHVLCAYIM KPKAGYGYLE TAAHFAAESS TGTNVEVSTT 

        70         80         90        100        110        120 
DDFTRGVDAL VYEIDPEKEI MKIAYPVELF DRNIIDGGAM LCSFLTLTIG NNQGMGDVEY 

       130        140        150        160        170        180 
AKMHDFYVPP CYLRLFDGPS MNIADMWRVL GRPVVDGGMV VGTIIKPKLG LRPKPFADAC 

       190        200        210        220        230        240 
YEFWLGGDFI KNDEPQGNQT FAPLKETIRL VADAMKRAQD ETGEAKLFSA NITADDHYEM 

       250        260        270        280        290        300 
VARGEYILET FGENADHVAF LVDGYVTGPA AITTARRSFP RQFLHYHRAG HGAVTSPQSM 

       310        320        330        340        350        360 
RGYTAFVLSK MSRLQGASGI HTGTMGYGKM EGDASDKIMA YMLNDEAAQG PFYHQDWLGM 

       370        380        390        400        410        420 
KATTPIISGG MNALRLPGFF DNLGHSNVIQ TSGGGAFGHL DGATAGAKSL RQSCDAWKAG 

       430        440        450 
VDLVTYAKSH RELARAFESF PNDADKLYPG WRVALGVN

« Hide

References

[1]"Sequence and expression of the form II ribulose-bisphosphate carboxylase/oxygenase (RuBisCO) gene from Rhodobacter capsulatus."
Larimer F.W., Lu T.-Y.S., Buley D.M.
FASEB J. 9:A1275-A1275(1997)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 11166 / DSM 1710 / JCM 21090 / LMG 2962 / NBRC 16435 / NCIMB 8254.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U23145 Genomic DNA. Translation: AAB82048.1.
PIRT10506.

3D structure databases

ProteinModelPortalP50922.
SMRP50922. Positions 2-457.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_01339. RuBisCO_L_type2.
[Tree]
InterProIPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
Gene3DG3DSA:3.20.20.110. RuBisCO_large. 1 hit.
G3DSA:3.30.70.150. RuBisCO_large. 1 hit.
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...

Entry information

Entry nameRBL2_RHOCA
AccessionPrimary (citable) accession number: P50922
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 28, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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