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Reviewed, UniProtKB/Swiss-Prot B0CCC1 (RBL_ACAM1)

Last modified November 3, 2009. Version 12. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
Synonyms: rbcL
Ordered Locus Names: AM1_1785
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Acaryochloris

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Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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 in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site By similarity.

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP MF_01338

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP MF_01338

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Subunit structure

Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity.

Post-translational modification

The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover 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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 476476Ribulose bisphosphate carboxylase large chain HAMAP MF_01338
PRO_1000142747

Sites

Active site1761Proton acceptor By similarity
Active site2951Proton acceptor By similarity
Metal binding2021Magnesium; via carbamate group By similarity
Metal binding2041Magnesium By similarity
Metal binding2051Magnesium By similarity
Binding site1241Substrate; in homodimeric partner By similarity
Binding site1741Substrate By similarity
Binding site1781Substrate By similarity
Binding site2961Substrate By similarity
Binding site3281Substrate By similarity
Binding site3801Substrate By similarity
Site3351Transition state stabilizer By similarity

Amino acid modifications

Modified residue2021N6-carboxylysine By similarity
Disulfide bond248Interchain; in linked form By similarity

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Sequences

Sequence LengthMass (Da)Tools
B0CCC1-1 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 4991C37529C5BBC1

FASTA47652,981
        10         20         30         40         50         60 
MSYSQTRTQS KAGYDAGVKD YKLTYYTPDY TPKDTDILAA FRMTPQPGVP PEEAGAAVAA 

        70         80         90        100        110        120 
ESSTGTWTTV WTDLLTDLDR YKGRCYDIEA VANEDNQYIA YIAYPLDLFE EGSVVNLLTS 

       130        140        150        160        170        180 
LVGNVFGFKA LRALRLEDIR IPVAYMKTFQ GPPHGITVER DKINKYGRPL LGCTIKPKLG 

       190        200        210        220        230        240 
LSAKNYGRAV YECLRGGLDF TKDDENINSQ PFMRWRDRFL FVAEAIHKAQ AETGEIKGHY 

       250        260        270        280        290        300 
LNVTAATCEE MLKRAEFAKE LEMPIIMHDF ITGGFTANTT LSHWCRDNGV LLHIHRAMHA 

       310        320        330        340        350        360 
VIDRQKNHGM HFRVLSKCLR MSGGDHIHTG TVVGKLEGEK GITMGFVDLL RENYVEKDLS 

       370        380        390        400        410        420 
RGIYFTQDWA SMGGVMAVAS GGIHVWHMPA LVEIFGDDSV LQFGGGTLGH PWGCAPGATA 

       430        440        450        460        470 
NRVALEACVQ ARNEGRDMAR EGGDILREAA KWSPELAVAL EVWKEIKFEF EAMDTV

« Hide

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References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000828 Genomic DNA. Translation: ABW26806.1.
RefSeqYP_001516120.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5680601.
GenomeReviewsGene locus AM1_1785 in contig CP000828_GR.
KEGGamr:AM1_1785.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAYTPDYTP.

Family and domain databases

HAMAPMF_01338.
[Tree]
InterProIPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
Gene3DG3DSA:3.20.20.110. RuBisCO_large. 1 hit.
G3DSA:3.30.70.150. RuBisCO_large. 1 hit.
PfamPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameRBL_ACAM1
AccessionPrimary (citable) accession number: B0CCC1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 26, 2008
Last modified: November 3, 2009
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents