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A5FWR1 (RBL_ACICJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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:Acry_0824
OrganismAcidiphilium cryptum (strain JF-5) [Complete proteome] [HAMAP]
Taxonomic identifier349163 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcidiphilium

Protein attributes

Sequence length493 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 – 493493Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000355747

Sites

Active site1841Proton acceptor By similarity
Active site3021Proton acceptor By similarity
Metal binding2101Magnesium; via carbamate group By similarity
Metal binding2121Magnesium By similarity
Metal binding2131Magnesium By similarity
Binding site1321Substrate; in homodimeric partner By similarity
Binding site1821Substrate By similarity
Binding site1861Substrate By similarity
Binding site3031Substrate By similarity
Binding site3351Substrate By similarity
Binding site3871Substrate By similarity
Site3421Transition state stabilizer By similarity

Amino acid modifications

Modified residue2101N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5FWR1 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 8794E5C4AC943AD6

FASTA49354,797
        10         20         30         40         50         60 
MDTPTPNITN EALTVRGKER YRSGVLEYRK MGYWEPDYEP KITDVISLFR ITPQDGVDPV 

        70         80         90        100        110        120 
EAAAAVAGES STATWTVVWT DRLTACEKYR AKAYRVDPVP NAPGQYFAYI AYDLALFEPG 

       130        140        150        160        170        180 
SIANLTASII GNVFGFKPLK ALRLEDMRLP VAYVKTFDGP ATGIVVERER LDKFGRPLLG 

       190        200        210        220        230        240 
ATVKPKLGLS GRNYGRVVYE ALKGGLDFTK DDENINSQPF MHWRDRFLYC MEAVNKAQAA 

       250        260        270        280        290        300 
TGEVKGTYLN VTAGTMEDMY ERASFAHELG SSIIMIDLVI GYTAIQSMSK WARKHDMILH 

       310        320        330        340        350        360 
LHRAGHGTYT RHKTHGVSFR VISKWMRLAG VDHIHAGTVV GKLEGDPLTT RGFYDILRED 

       370        380        390        400        410        420 
YNETRYEHGI FFDQDWAGTR KVMPVASGGI HAGQMHQLLH HLGEDVVLQF GGGTIGHPQG 

       430        440        450        460        470        480 
IAAGAMANRV ALEAMILARN EGRDYLAEGP QILNDAARHC LPLRQALDTW GEVTFNYAST 

       490 
DTPDFVPTAM PAY 

« Hide

References

[1]"Complete sequence of chromosome of Acidiphilium cryptum JF-5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JF-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000697 Genomic DNA. Translation: ABQ30043.1.
RefSeqYP_001233962.1. NC_009484.1.

3D structure databases

ProteinModelPortalA5FWR1.
SMRA5FWR1. Positions 30-473.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349163.Acry_0824.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ30043; ABQ30043; Acry_0824.
GeneID5161365.
KEGGacr:Acry_0824.
PATRIC20646630. VBIAciCry6074_1312.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycACRY349163:GHET-836-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_ACICJ
AccessionPrimary (citable) accession number: A5FWR1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 44 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