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H6SPP4 (H6SPP4_RHOPH) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 13. 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 CCG07164.1
Synonyms:cbbL HAMAP-Rule MF_01338
ORF Names:RSPPHO_00538 EMBL CCG07164.1
OrganismRhodospirillum photometricum DSM 122 EMBL CCG07164.1
Taxonomic identifier1150469 [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
H6SPP4 [UniParc].

Last modified April 18, 2012. Version 1.
Checksum: 9DBA64443B15D972

FASTA47252,779
        10         20         30         40         50         60 
MGKTYQAGVK EYRETYWDPN YTPKDSDILA CFKVVPQPGV PREEAAAAVC AESSTATWTT 

        70         80         90        100        110        120 
VWTDLLTDLD YYKGRAYAIE DVPGHDEAFY AFIAYPMGLF EEGSIVNVFT SLVGNVFGFK 

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

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

       250        260        270        280        290        300 
DIYQRAAFAK EIGTPIIMSD YLTIGWAAHA SLSRWCRNNG MLLHVHRAMH AVIDRNPMHG 

       310        320        330        340        350        360 
INFRVLAKLL RLLGGDHLHS GTVVGKLEGD RDATLGWIDL MRERHVKEDR SRGIFFDQDW 

       370        380        390        400        410        420 
GHMPSVMPVA SGGIHVWHMP ALLAIFGDDA VFQFGGGTLG HPWGNAAGAA ANRVALEACV 

       430        440        450        460        470 
QARNEGRSLE SEGKAILTAA ARHSPELKMA METWKEVKFE FETVDTLDVS HK 

« Hide

References

[1]"Shotgun genome sequence of Phaeospirillum photometricum DSM 122."
Duquesne K., Sturgis J.
Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: DSM 122 EMBL CCG07164.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
HE663493 Genomic DNA. Translation: CCG07164.1.
RefSeqYP_005416134.1. NC_017059.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCG07164; CCG07164; RSPPHO_00538.
GeneID12211237.
KEGGrpm:RSPPHO_00538.

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycRPHO1150469:GLJ6-619-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 nameH6SPP4_RHOPH
AccessionPrimary (citable) accession number: H6SPP4
Entry history
Integrated into UniProtKB/TrEMBL: April 18, 2012
Last sequence update: April 18, 2012
Last modified: June 11, 2014
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)