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E3I482 (E3I482_RHOVT) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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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:cbbL HAMAP-Rule MF_01338
Ordered Locus Names:Rvan_0010 EMBL ADP69301.1
OrganismRhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299) [Complete proteome] [HAMAP] EMBL ADP69301.1
Taxonomic identifier648757 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesHyphomicrobiaceaeRhodomicrobium

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. 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 site1771Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2951Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2031Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2051Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2061Magnesium By similarity HAMAP-Rule MF_01338
Binding site1251Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1751Substrate By similarity HAMAP-Rule MF_01338
Binding site1791Substrate By similarity HAMAP-Rule MF_01338
Binding site2961Substrate By similarity HAMAP-Rule MF_01338
Binding site3281Substrate By similarity HAMAP-Rule MF_01338
Binding site3801Substrate By similarity HAMAP-Rule MF_01338
Site3351Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue2031N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
E3I482 [UniParc].

Last modified January 11, 2011. Version 1.
Checksum: CACE029CBD3E6F4C

FASTA48553,687
        10         20         30         40         50         60 
MSDKSETVKG EDRYKAGVMS YKKMGYWEPD YQPKETDLIA LFRVTPQDGV DPIEASAAVA 

        70         80         90        100        110        120 
GESSTATWTV VWTDRLTASE KYRAKCYRVD PVPNAPGSYF AYIAYDLDLF EGGSISNLTA 

       130        140        150        160        170        180 
SIIGNVFGFK PLKALRLEDM RLPVAYVKTF DGPPAGIIVE RERLDKFGRP LLGATVKPKL 

       190        200        210        220        230        240 
GLSGRNYGRV VYEALKGGLD FTKDDENINS QPFMHWRERF LYCMEAVNKA QAETGEIKGS 

       250        260        270        280        290        300 
YLNITAGTME EMYKRAEYAK ELGSCIVMID LVIGYVAIQS ISKWARDNNM LLHLHRAGHS 

       310        320        330        340        350        360 
TYTRQKSHGV SFRVISKWMR LAGVDHIHAG TVVGKLEGDP LTTAGYYDIL REDFVPQNLE 

       370        380        390        400        410        420 
HGVFFDQPWA SLGKVMPVAS GGIHAGQMHQ LIHYLGEDVV LQFGGGTIGH PYGIQAGATA 

       430        440        450        460        470        480 
NRVALEAMIF ARNEGRDYLA EGPQILKDAA KTCTPLRQAL DTWGDVTFDY TSTDTPDFVP 


TPTAS 

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References

[1]"Genome sequences of eight morphologically diverse alphaproteobacteria."
US DOE Joint Genome Institute
Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.
J. Bacteriol. 193:4567-4568(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002292 Genomic DNA. Translation: ADP69301.1.
RefSeqYP_004010400.1. NC_014664.1.

3D structure databases

ProteinModelPortalE3I482.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADP69301; ADP69301; Rvan_0010.
GeneID9930774.
KEGGrva:Rvan_0010.
PATRIC42667006. VBIRhoVan113057_0010.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.

Enzyme and pathway databases

BioCycRVAN648757:GHZT-10-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 nameE3I482_RHOVT
AccessionPrimary (citable) accession number: E3I482
Entry history
Integrated into UniProtKB/TrEMBL: January 11, 2011
Last sequence update: January 11, 2011
Last modified: February 19, 2014
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)