Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O85040 (RBL1_HALNC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:Hneap_0922
OrganismHalothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus neapolitanus) [Complete proteome] [HAMAP]
Taxonomic identifier555778 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesHalothiobacillaceaeHalothiobacillus

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Induction

Produced when grown in air or in air supplemented with 5% CO2. 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.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000062660

Sites

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

Amino acid modifications

Modified residue1941N6-carboxylysine By similarity

Secondary structure

................................................................................. 473
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O85040 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: B84D2EDE46CAF7D8

FASTA47352,636
        10         20         30         40         50         60 
MAVKKYSAGV KEYRQTYWMP EYTPLDSDIL ACFKITPQPG VDREEAAAAV AAESSTGTWT 

        70         80         90        100        110        120 
TVWTDLLTDM DYYKGRAYRI EDVPGDDAAF YAFIAYPIDL FEEGSVVNVF TSLVGNVFGF 

       130        140        150        160        170        180 
KAVRGLRLED VRFPLAYVKT CGGPPHGIQV ERDKMNKYGR PLLGCTIKPK LGLSAKNYGR 

       190        200        210        220        230        240 
AVYECLRGGL DFTKDDENIN SQPFMRWRDR FLFVQDATET AEAQTGERKG HYLNVTAPTP 

       250        260        270        280        290        300 
EEMYKRAEFA KEIGAPIIMH DYITGGFTAN TGLAKWCQDN GVLLHIHRAM HAVIDRNPNH 

       310        320        330        340        350        360 
GIHFRVLTKI LRLSGGDHLH TGTVVGKLEG DRASTLGWID LLRESFIPED RSRGIFFDQD 

       370        380        390        400        410        420 
WGSMPGVFAV ASGGIHVWHM PALVNIFGDD SVLQFGGGTL GHPWGNAAGA AANRVALEAC 

       430        440        450        460        470 
VEARNQGRDI EKEGKEILTA AAQHSPELKI AMETWKEIKF EFDTVDKLDT QNR 

« Hide

References

« Hide 'large scale' references
[1]"Insertion mutation of the form I cbbL gene encoding ribulose bisphosphate carboxylase/oxygenase (RuBisCO) in Thiobacillus neapolitanus results in expression of form II RuBisCO, loss of carboxysomes, and an increased CO2 requirement for growth."
Baker S.H., Jin S., Aldrich H.C., Howard G.T., Shively J.M.
J. Bacteriol. 180:4133-4139(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], EXPRESSION.
[2]"Complete sequence of Halothiobacillus neapolitanus c2."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Kerfeld C., Cannon G., Heinhort S.
Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 23641 / c2.
[3]"The structure of Halothiobacillus neapolitanus Rubisco."
Kerfeld C.A., Sawaya M.R., Pashkov I., Cannon G., Williams E., Tran K., Yeates T.O.
Submitted (APR-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF038430 Genomic DNA. Translation: AAC32549.1.
CP001801 Genomic DNA. Translation: ACX95765.1.
RefSeqYP_003262812.1. NC_013422.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SVDX-ray1.80A1-473[»]
ProteinModelPortalO85040.
SMRO85040. Positions 16-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING555778.Hneap_0922.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACX95765; ACX95765; Hneap_0922.
GeneID8534063.
KEGGhna:Hneap_0922.
PATRIC32205718. VBIHalNea120669_0941.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAMETWKEV.
OrthoDBEOG6ZKXMS.

Enzyme and pathway databases

BioCycHNEA555778:GIVV-951-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...

Other

EvolutionaryTraceO85040.

Entry information

Entry nameRBL1_HALNC
AccessionPrimary (citable) accession number: O85040
Secondary accession number(s): D0KZ92
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 1, 1998
Last modified: May 14, 2014
This is version 75 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references