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P56889 (RBL1_SINMW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 82. 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:Smed_3924
Encoded onPlasmid pSMED01
OrganismSinorhizobium medicae (strain WSM419) (Ensifer medicae) [Complete proteome] [HAMAP]
Taxonomic identifier366394 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length486 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_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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000062644

Sites

Active site1781Proton acceptor By similarity
Active site2961Proton acceptor By similarity
Metal binding2041Magnesium; via carbamate group By similarity
Metal binding2061Magnesium By similarity
Metal binding2071Magnesium By similarity
Binding site1261Substrate; in homodimeric partner By similarity
Binding site1761Substrate By similarity
Binding site1801Substrate By similarity
Binding site2971Substrate By similarity
Binding site3291Substrate By similarity
Binding site3811Substrate By similarity
Site3361Transition state stabilizer By similarity

Amino acid modifications

Modified residue2041N6-carboxylysine By similarity

Experimental info

Sequence conflict61K → N in AAF25379. Ref.1
Sequence conflict351K → N in AAF25379. Ref.1
Sequence conflict521D → H in AAF25379. Ref.1
Sequence conflict561A → P in AAF25379. Ref.1
Sequence conflict761R → P in AAF25379. Ref.1
Sequence conflict1281F → L in AAF25379. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P56889 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: CF54E04F5FD76336

FASTA48653,709
        10         20         30         40         50         60 
MNADAKTEIK GRERYKAGVL KYAQMGYWNG DYEPKDTDLI ALFRITPQDG VDPIEAAAAV 

        70         80         90        100        110        120 
AGESSTATWT VVWTDRLTAC DQYRAKAYRV DPVPGTPGQY FCYVAYDLIL FEEGSIANLT 

       130        140        150        160        170        180 
ASIIGNVFSF KPLKAARLED MRLPVAYVKT FKGPPTGIVV ERERLDKFGK PLLGATTKPK 

       190        200        210        220        230        240 
LGLSGKNYGR VVYEGLKGGL DFMKDDENIN SQPFMHWRDR YLYCMEAVNH ASAVTGEVKG 

       250        260        270        280        290        300 
HYLNVTAGTM EEMYRRAEFA KELGSVIVMV DLIIGWTAIQ SMSEWCRQND MILHMHRAGH 

       310        320        330        340        350        360 
GTYTRQKNHG ISFRVIAKWL RLAGVDHLHA GTAVGKLEGD PLTVQGYYNV CREMKNAVDL 

       370        380        390        400        410        420 
PRGLFFEQDW ADLKKVLPVA SGGIHAGQMH QLLDLFGDDV VLQFGGGTIG HPMGIQAGAT 

       430        440        450        460        470        480 
ANRVALEAMV LARNEGRDIA HEGPEILRAA AKWCKPLEAA LDTWGNISFN YTPTDTSDFV 


PSVTAA 

« Hide

References

« Hide 'large scale' references
[1]"Genetic regulation of C1 metabolism in Sinorhizobium meliloti."
Fenner B.J., Tiwari R.P., Dilworth M.J.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Sinorhizobium medicae WSM419 plasmid pSMED01."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WSM419.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF211846 Genomic DNA. Translation: AAF25379.1.
CP000739 Genomic DNA. Translation: ABR62734.1.
RefSeqYP_001312667.1. NC_009620.1.

3D structure databases

ProteinModelPortalP56889.
SMRP56889. Positions 7-480.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING366394.Smed_3924.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR62734; ABR62734; Smed_3924.
GeneID5318709.
KEGGsmd:Smed_3924.
PATRIC23613394. VBISinMed134228_0370.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAHRAMHAA.
OrthoDBEOG6ZKXMS.
ProtClustDBPRK04208.

Enzyme and pathway databases

BioCycSMED366394:GJAL-3985-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 nameRBL1_SINMW
AccessionPrimary (citable) accession number: P56889
Secondary accession number(s): A6UGF4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 13, 2007
Last modified: February 19, 2014
This is version 82 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