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Q219P7 (RBL_RHOPB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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 large chain

Short name=RuBisCO large subunit
EC=4.1.1.39
Gene names
Name:cbbL
Ordered Locus Names:RPC_1327
OrganismRhodopseudomonas palustris (strain BisB18) [Complete proteome] [HAMAP]
Taxonomic identifier316056 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

Protein attributes

Sequence length485 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 in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site By similarity. HAMAP-Rule MF_01338

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01338

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01338

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01338

Subunit structure

Heterohexadecamer of 8 large chains and 8 small chains By similarity.

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel" By similarity.

Sequence similarities

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

Sequence caution

The sequence ABD86889.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 485485Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000251457

Sites

Active site1761Proton acceptor By similarity
Active site2941Proton acceptor By similarity
Metal binding2021Magnesium; via carbamate group By similarity
Metal binding2041Magnesium By similarity
Metal binding2051Magnesium By similarity
Binding site1241Substrate; in homodimeric partner By similarity
Binding site1741Substrate By similarity
Binding site1781Substrate By similarity
Binding site2951Substrate By similarity
Binding site3271Substrate By similarity
Binding site3791Substrate By similarity
Site3341Transition state stabilizer By similarity

Amino acid modifications

Modified residue2021N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q219P7 [UniParc].

Last modified October 3, 2006. Version 2.
Checksum: B36E403B136F3FC4

FASTA48554,027
        10         20         30         40         50         60 
MNESVTIRGK DRYKSGVMEY KKMGYWEPDY EPKDTDIIAL FRVTPQDGVD PTEASAAVAG 

        70         80         90        100        110        120 
ESSTATWTVV WTDRLTAAEK YRAKCYRVDP VPNSPGQFFA YIAYDLDLFE NGSIANLSAS 

       130        140        150        160        170        180 
IIGNVFGFKP LKALRLEDMR LPVAYVKTFQ GPATGIVVER ERMDKFGRPL LGATVKPKLG 

       190        200        210        220        230        240 
LSGRNYGRVV YEALKGGLDF TKDDENINSQ PFMHWRERFL YCMEAVNKAQ AASGEIKGTY 

       250        260        270        280        290        300 
LNVTAGTMEE MYERAEFAKQ LGSVIIMIDL VIGYTAIQSM AKWARRNDMI LHLHRAGHST 

       310        320        330        340        350        360 
YTRQRNHGVS FRVIAKWMRL AGVDHIHAGT VVGKLEGDPA TTKGYYDICR EDYNPMQLEH 

       370        380        390        400        410        420 
GIFFEQNWAS LNKLMPVASG GIHAGQMHQL LDHLGEDVVL QFGGGTIGHP MGIQAGATAN 

       430        440        450        460        470        480 
RVALEAMIMA RNEGRDYLHE GEEILAKAAL TCTPLKAALE TWKNVTFNYE STDMPDYAPT 


PSVSM 

« Hide

References

[1]"Complete sequence of Rhodopseudomonas palustris BisB18."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BisB18.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000301 Genomic DNA. Translation: ABD86889.1. Different initiation.
RefSeqYP_531208.1. NC_007925.1.

3D structure databases

ProteinModelPortalQ219P7.
SMRQ219P7. Positions 22-465.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316056.RPC_1327.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD86889; ABD86889; RPC_1327.
GeneID3974066.
KEGGrpc:RPC_1327.
PATRIC23267326. VBIRhoPal29154_1368.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OrthoDBEOG6ZKXMS.
ProtClustDBPRK04208.

Enzyme and pathway databases

BioCycRPAL316056:GH3E-1342-MONOMER.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
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 nameRBL_RHOPB
AccessionPrimary (citable) accession number: Q219P7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 3, 2006
Last modified: February 19, 2014
This is version 48 of the entry and version 2 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