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A7IGM0 (RBL_XANP2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain

Short name=RuBisCO large subunit
EC=4.1.1.39
Gene names
Name:cbbL
Ordered Locus Names:Xaut_1918
OrganismXanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) [Complete proteome] [HAMAP]
Taxonomic identifier78245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesXanthobacteraceaeXanthobacter

Protein attributes

Sequence length488 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.

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.

Sequence similarities

Belongs to the RuBisCO large chain family. Type I subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 488488Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_1000142753

Sites

Active site1801Proton acceptor By similarity
Active site2981Proton acceptor By similarity
Metal binding2061Magnesium; via carbamate group By similarity
Metal binding2081Magnesium By similarity
Metal binding2091Magnesium By similarity
Binding site1281Substrate; in homodimeric partner By similarity
Binding site1781Substrate By similarity
Binding site1821Substrate By similarity
Binding site2991Substrate By similarity
Binding site3311Substrate By similarity
Binding site3831Substrate By similarity
Site3381Transition state stabilizer By similarity

Amino acid modifications

Modified residue2061N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7IGM0 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 58FCD8DDBCBE6386

FASTA48853,824
        10         20         30         40         50         60 
MGADAAIGQI KDAKKRYAAG VLKYAQMGYW DGDYQPKDTD VLALFRITPQ DGVDAVEAAA 

        70         80         90        100        110        120 
AVAGESSTAT WTVVWTDRLT AADMYRAKAY KVEPVPGQPG QYFCWVAYDL DLFEEGSIAN 

       130        140        150        160        170        180 
LTASIIGNVF SFKPLKACRL EDMRLPVAYV KTFRGPPTGI VVERERLDKF GRPLLGATTK 

       190        200        210        220        230        240 
PKLGLSGKNY GRVVYEGLKG GLDFVKDDEN INSQPFMHWR DRFLYCMEAV NKAQAETGEV 

       250        260        270        280        290        300 
KGHYLNITAG TMEEMYRRAE FAKELGSVVV MVDLIVGWTA IQSISNWCRE NDVLLHMHRA 

       310        320        330        340        350        360 
GHGTYTRQKG HGISFRVIAK WLRLAGVDHL HTGTAVGKLE GDPMTVQGYY NVCRETVTKT 

       370        380        390        400        410        420 
DYTRGIFFDQ DWAGLRKVMP VASGGIHAGQ MHQLIDLFGE DVVLQFGGGT IGHPDGIQAG 

       430        440        450        460        470        480 
AIANRVALET MILARNEGRD IKNEGPEILI EAAKWCRPLR AALDTWGEVT FNYASTDTSD 


FVPTASVA 

« Hide

References

[1]"Complete sequence of chromosome of Xanthobacter autotrophicus Py2."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Brainard J., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1158 / Py2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000781 Genomic DNA. Translation: ABS67163.1.
RefSeqYP_001416820.1. NC_009720.1.

3D structure databases

ProteinModelPortalA7IGM0.
SMRA7IGM0. Positions 26-469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING78245.Xaut_1918.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS67163; ABS67163; Xaut_1918.
GeneID5424516.
KEGGxau:Xaut_1918.
PATRIC24045907. VBIXanAut29526_2243.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAHRAMHAA.
OrthoDBEOG6ZKXMS.
ProtClustDBPRK04208.

Enzyme and pathway databases

BioCycXAUT78245:GHS6-1940-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 nameRBL_XANP2
AccessionPrimary (citable) accession number: A7IGM0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 11, 2007
Last modified: February 19, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families