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L0H228 (L0H228_9GAMM) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 8. 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
ORF Names:Thimo_2947 EMBL AGA91639.1
OrganismThioflavicoccus mobilis 8321 EMBL AGA91639.1
Taxonomic identifier765912 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeThioflavicoccus

Protein attributes

Sequence length471 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 site1681Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2871Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding1941Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding1961Magnesium By similarity HAMAP-Rule MF_01338
Metal binding1971Magnesium By similarity HAMAP-Rule MF_01338
Binding site1161Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1661Substrate By similarity HAMAP-Rule MF_01338
Binding site1701Substrate By similarity HAMAP-Rule MF_01338
Binding site2881Substrate By similarity HAMAP-Rule MF_01338
Binding site3201Substrate By similarity HAMAP-Rule MF_01338
Binding site3721Substrate By similarity HAMAP-Rule MF_01338
Site3271Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue1941N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
L0H228 [UniParc].

Last modified March 6, 2013. Version 1.
Checksum: 88447B6AE24F2CFC

FASTA47152,517
        10         20         30         40         50         60 
MAAKTYDAGV KEYRDMYWTP EYVPLDTDLL ACFKCTGQPG VPREEVAAAV AAESSTGTWS 

        70         80         90        100        110        120 
TVWSELLTDL EYYKGRAYRI EDVPGDKESF YAFVAYPIDL FEEGSVVNVL TSLVGNVFGF 

       130        140        150        160        170        180 
KALRHLRLED IRFPIAYIKT CNGPPAGIQV ERDRLNKYAR PLLGCTIKPK LGLSAKNYGR 

       190        200        210        220        230        240 
AVYECLRGGL DLTKDDENVN SQPFMRWRDR FEFVGEAIQK SQQETGERKG HYLNVTAPDP 

       250        260        270        280        290        300 
EQMYERAEFA KEVGCPIIMH DFLTGGFTAN TGLAKWCRKN GMLLHIHRAM HAVIDRHPKH 

       310        320        330        340        350        360 
GIHFRVLAKC LRLSGGDHLH TGTVVGKLEG DRASTLGYVD QLRESFVPED RSRGVFFDQD 

       370        380        390        400        410        420 
WGSMPGVFAV ASGGIHVWHM PALVTIFGDD SVLQFGGGTQ GHPWGNAAGA AANRVALEAC 

       430        440        450        460        470 
IKARNQGRGL EKESRDILTE AARHSPELAM AMETWKEIKF EFETVDKLDV A 

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References

[1]"Complete sequence of chromosome of Thioflavicoccus mobilis 8321."
US DOE Joint Genome Institute
Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K. expand/collapse author list , Liu Z., Imhoff J., Thiel V., Frigaard N.-U., Bryant D., Woyke T.
Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 8321 EMBL AGA91639.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003051 Genomic DNA. Translation: AGA91639.1.
RefSeqYP_007245269.1. NC_019940.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAGA91639; AGA91639; Thimo_2947.
GeneID14305208.
KEGGtmb:Thimo_2947.

Phylogenomic databases

KOK01601.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020888. 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.
ProtoNetSearch...

Entry information

Entry nameL0H228_9GAMM
AccessionPrimary (citable) accession number: L0H228
Entry history
Integrated into UniProtKB/TrEMBL: March 6, 2013
Last sequence update: March 6, 2013
Last modified: February 19, 2014
This is version 8 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)