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E8TEA0 (E8TEA0_MESCW) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 23. 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:cbbL HAMAP-Rule MF_01338
Ordered Locus Names:Mesci_4283 EMBL ADV13393.1
OrganismMesorhizobium ciceri bv. biserrulae (strain HAMBI 2942 / LMG 23838 / WSM1271) [Complete proteome] [HAMAP] EMBL ADV13393.1
Taxonomic identifier765698 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length497 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 site1881Proton acceptor By similarity HAMAP-Rule MF_01338
Active site3061Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2141Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2161Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2171Magnesium By similarity HAMAP-Rule MF_01338
Binding site1361Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1861Substrate By similarity HAMAP-Rule MF_01338
Binding site1901Substrate By similarity HAMAP-Rule MF_01338
Binding site3071Substrate By similarity HAMAP-Rule MF_01338
Binding site3391Substrate By similarity HAMAP-Rule MF_01338
Binding site3911Substrate By similarity HAMAP-Rule MF_01338
Site3461Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue2141N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
E8TEA0 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: 95D543D064004907

FASTA49755,476
        10         20         30         40         50         60 
MNKIDILPAG TLKEGKERYK SGVIPYKKMG YWEPDYRPKE TDLIAMFRIT PQPGVDHEEA 

        70         80         90        100        110        120 
AAAIAGESST ATWTVVWTDR LTACELYRAK AFRSEPVPNT GPGTKTEQQY FAYIAYDLDL 

       130        140        150        160        170        180 
FEPGSIANLT ASIIGNVFGF KAVKALRLED MRIPVAYLKT FQGPATGIVV ERERLDKFGR 

       190        200        210        220        230        240 
PLLGATTKPK LGLSGRNYGR VVYEALKGGL DFVKDDENIN SQPFMHWRDR FLYCMEAVNK 

       250        260        270        280        290        300 
ASAATGEVKG HYLNVTAGTM EEMYERAEFA KQLGSCIVMI DLVIGYTAIQ SMAKWARRND 

       310        320        330        340        350        360 
MILHLHRAGN STYSRQKNHG MNFRVICKWM RMAGVDHIHA GTVVGKLEGD PLMIKGFYDT 

       370        380        390        400        410        420 
LREERTPQNL ETGLFFDQEW ASLNKVMPVA SGGIHAGQMH QLIHYLGEDV ILQFGGGTIG 

       430        440        450        460        470        480 
HPDGIQAGAT ANRVALEAMI LARNEGRDYL REGTKILEQA ARWCTPLKAA LETWKDVTFN 

       490 
YESTDTADFV PTATPSF 

« Hide

References

[1]"Complete sequence of chromosome of Mesorhizobium ciceri bv. biserrulae WSM1271."
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Nandasena K., Reeve W.G., Howieson J.G., O'Hara G., Tiwari R.P., Woyke T.
Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HAMBI 2942 / LMG 23838 / WSM1271.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002447 Genomic DNA. Translation: ADV13393.1.
RefSeqYP_004143443.1. NC_014923.1.

3D structure databases

ProteinModelPortalE8TEA0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADV13393; ADV13393; Mesci_4283.
GeneID10119774.
KEGGmci:Mesci_4283.
PATRIC45258702. VBIMesCic160642_4780.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.
OMAHRAMHAA.

Enzyme and pathway databases

BioCycMCIC765698:GHQ5-4336-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 nameE8TEA0_MESCW
AccessionPrimary (citable) accession number: E8TEA0
Entry history
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: February 19, 2014
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)