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B6IQF2 (B6IQF2_RHOCS) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 38. Feed History...

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

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338

Short name=RuBisCO large subunit HAMAP-Rule MF_01338
EC=4.1.1.39 HAMAP-Rule MF_01338
Gene names
Name:cbbL2 EMBL ACI97688.1
Synonyms:cbbL HAMAP-Rule MF_01338
Ordered Locus Names:RC1_0239 EMBL ACI97688.1
OrganismRhodospirillum centenum (strain ATCC 51521 / SW) [Complete proteome] [HAMAP] EMBL ACI97688.1
Taxonomic identifier414684 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum

Protein attributes

Sequence length472 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. HAMAP-Rule MF_01338

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. HAMAP-Rule MF_01338

Sequence similarities

Belongs to the RuBisCO large chain family. Type I subfamily. HAMAP-Rule MF_01338

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1671Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2861Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding1931Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding1951Magnesium By similarity HAMAP-Rule MF_01338
Metal binding1961Magnesium By similarity HAMAP-Rule MF_01338
Binding site1151Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1651Substrate By similarity HAMAP-Rule MF_01338
Binding site1691Substrate By similarity HAMAP-Rule MF_01338
Binding site2871Substrate By similarity HAMAP-Rule MF_01338
Binding site3191Substrate By similarity HAMAP-Rule MF_01338
Binding site3711Substrate By similarity HAMAP-Rule MF_01338
Site3261Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue1931N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
B6IQF2 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 87C10C0D404C1BC8

FASTA47253,152
        10         20         30         40         50         60 
MGKTYQAGVK EYRETYWDPN YTPKDSDILA CFKVVPQPGV PREEAAAAVC AESSTATWTT 

        70         80         90        100        110        120 
VWTDLLTDLD YYKGRAYAIE DVPGDDEAFY AFVAYPMGLF EEGSIVNVFT SLVGNVFGFK 

       130        140        150        160        170        180 
AVRSLRLEDV RFPLWFVTTC DGPPHGIQVE RDKLDKYGRP LLGCTIKPKL GLSAKNYGRA 

       190        200        210        220        230        240 
VYECLRGGLD FTKDDENVNS QPFMRWRDRF LFCQEAIEKA EAETGERKGH YLNVTAPNME 

       250        260        270        280        290        300 
EIYRRAEYAK EIGSPIIMSD YLTIGWAAHS SLSRWCRNNG MLLHVHRAMH GVIDRNPRHG 

       310        320        330        340        350        360 
INFRVLAKLL RLLGGDHLHS GTVVGKLEGD REATLGWVDL MRERHVKEDR SRGLFFDQEW 

       370        380        390        400        410        420 
GHMAPVMPVA SGGIHVWHMP ALLSIFGDDA VFQFGGGTLG HPWGNAAGAC ANRVALEACV 

       430        440        450        460        470 
EARNQGRDVE REGKDILTAA ARHSPELKMA METWKEVRFE FDVVDKLDVV HR 

« Hide

References

[1]"Genome sequence of Rhodospirillum centenum."
Touchman J.W., Bauer C., Blankenship R.E.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51521 / SW.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000613 Genomic DNA. Translation: ACI97688.1.
RefSeqYP_002296501.1. NC_011420.2.

3D structure databases

ProteinModelPortalB6IQF2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING414684.RC1_0239.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI97688; ACI97688; RC1_0239.
GeneID7005016.
KEGGrce:RC1_0239.
PATRIC23315704. VBIRhoCen1465_0219.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMADTDILAC.
OrthoDBEOG6ZKXMS.
ProtClustDBPRK04208.

Enzyme and pathway databases

BioCycRCEN414684:GHCM-229-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 nameB6IQF2_RHOCS
AccessionPrimary (citable) accession number: B6IQF2
Entry history
Integrated into UniProtKB/TrEMBL: December 16, 2008
Last sequence update: December 16, 2008
Last modified: April 16, 2014
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)