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Reviewed, UniProtKB/Swiss-Prot P24672 (RBL_ALVHS)

Last modified May 5, 2009. Version 55. 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
OrganismAlvinoconcha hessleri symbiotic bacterium
Taxonomic identifier2326 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › sulfur-oxidizing symbionts

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Protein attributes

Sequence length471 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. Both reactions occur simultaneously and in competition at the same active site. HAMAP MF_01338

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 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 – 471471Ribulose bisphosphate carboxylase large chain HAMAP MF_01338
PRO_0000062618

Sites

Active site1671Proton acceptor By similarity
Active site2861Proton acceptor By similarity
Metal binding1931Magnesium; via carbamate group By similarity
Metal binding1951Magnesium By similarity
Metal binding1961Magnesium By similarity
Binding site1151Substrate; in homodimeric partner By similarity
Binding site1651Substrate By similarity
Binding site1691Substrate By similarity
Binding site2871Substrate By similarity
Binding site3191Substrate By similarity
Binding site3711Substrate By similarity
Site3261Transition state stabilizer By similarity

Amino acid modifications

Modified residue1931N6-carboxylysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
P24672-1 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: 990F5E9B5E55C504

FASTA47152,770
        10         20         30         40         50         60 
MAKKYDAGVK DYRETYWMPD YTPKETDLLA CFKIIPQPGV PREEARAAVA AESSTGTWTT 

        70         80         90        100        110        120 
VWTDLLTDLD HYKGRAYAIE DVPGDEEAFY AFIAYPIDLF EEGSVVNVFT SLVGNVFGFK 

       130        140        150        160        170        180 
AIRALRLEDV RFPIAYVMTC NGPPHGIQVE RDIMNKYGRP LLGCTIKPKL GLSAKNYGRA 

       190        200        210        220        230        240 
VYECLRGGLD FTKDDENVNS QPFMRWRHGF DFVMEAIEKA ERETGERKGH YLNVTAPTPD 

       250        260        270        280        290        300 
EMFKRAEYAK EIGAPIIMHD YITGGFTANT GLAQWCRDNG VLLHIHRAMH AVLDRNPHHG 

       310        320        330        340        350        360 
IHFRVLTKIL RLSGGDHLHT GTVVGKLEGD REATLGWIDL LRESYIKEDR SRGIFFDQDW 

       370        380        390        400        410        420 
GSMPGVFAAC SGGIHVWHMP ALVTIFGEHA VLQFGGGTLG HPWGNAGAAA NRVALEACVE 

       430        440        450        460        470 
ARNEGHELEK EGKDILIQAA KHSPELKTAM ETWKEIKFEF DTVDKLDVAH K

« Hide

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References

[1]"Nucleotide sequence and expression of a deep-sea ribulose-1,5-bisphosphate carboxylase gene cloned from a chemoautotrophic bacterial endosymbiont."
Stein J.L., Haygood M., Felbeck H.
Proc. Natl. Acad. Sci. U.S.A. 87:8850-8854(1990) [PubMed: 2247456] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

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Cross-references

Sequence databases

M34536 Genomic DNA. Translation: AAA27387.1.
PIRA38262.

3D structure databases

HSSPHSSP built from PDB template 1GEH based on UniProtKB O93627.
SMRP24672. Positions 5-466.
ModBaseSearch...

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_ALVHS
AccessionPrimary (citable) accession number: P24672
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: May 5, 2009
This is version 55 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