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D5AUD5 (RBL2_RHOCB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase

Short name=RuBisCO
EC=4.1.1.39
Gene names
Name:cbbM
Ordered Locus Names:RCAP_rcc01829
OrganismRhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) [Complete proteome] [HAMAP]
Taxonomic identifier272942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

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 By similarity. 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 By similarity. HAMAP-Rule MF_01339

Subunit structure

Homodimer By similarity. HAMAP-Rule 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.

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-Rule MF_01339
PRO_0000410720

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
D5AUD5 [UniParc].

Last modified June 15, 2010. Version 1.
Checksum: A03E0FF321EF3B6C

FASTA45850,205
        10         20         30         40         50         60 
MDQSNRYARL DLKEADLIAG GRHVLCAYVM KPKAGYGYLE TAAHFAAESS TGTNVEVSTT 

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

       130        140        150        160        170        180 
AKMHEFYVPP 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 AITTARRQFP RQFLHYHRAG HGAVTSPQSM 

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

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

       430        440        450 
VDLVTYAKSH RELARAFESF PNDADKLYPG WRVALGVN 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the photosynthetic purple nonsulfur bacterium Rhodobacter capsulatus SB 1003."
Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., Haselkorn R.
J. Bacteriol. 192:3545-3546(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
[2]"Expression of the cbbLcbbS and cbbM genes and distinct organization of the cbb Calvin cycle structural genes of Rhodobacter capsulatus."
Paoli G.C., Morgan N.S., Tabita F.R., Shively J.M.
Arch. Microbiol. 164:396-405(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: OPERON ORGANIZATION, EXPRESSION IN R.SPHAEROIDES.
Strain: ATCC BAA-309 / NBRC 16581 / SB1003.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001312 Genomic DNA. Translation: ADE85574.1.
RefSeqYP_003577981.1. NC_014034.1.

3D structure databases

ProteinModelPortalD5AUD5.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADE85574; ADE85574; RCAP_rcc01829.
GeneID9004652.
KEGGrcp:RCAP_rcc01829.
PATRIC35503806. VBIRhoCap134200_1861.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.
OMAAKEHREF.

Enzyme and pathway databases

BioCycRCAP272942:GJIY-1854-MONOMER.

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. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRBL2_RHOCB
AccessionPrimary (citable) accession number: D5AUD5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 15, 2010
Last modified: June 11, 2014
This is version 25 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