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Q603Q7 (RBL_METCA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
Ordered Locus Names:MCA2743
OrganismMethylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) [Complete proteome] [HAMAP]
Taxonomic identifier243233 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaMethylococcalesMethylococcaceaeMethylococcus

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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. 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

Expressed under both copper-replete and copper-limited growth conditions. 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_0000062628

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

Experimental info

Sequence conflict3721S → F in AAL40972. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q603Q7 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 5CE5048F754EA3DD

FASTA47352,857
        10         20         30         40         50         60 
MAVKTYNAGV KEYRETYWDP NYTPADTDLL AVFKITPQPG VPREEAAAAV AAESSTGTWT 

        70         80         90        100        110        120 
TVWTDLLTDL DYYKGRAYRI EDVPGQDEQF YAFIAYPIDL FEEGSVVNVF TSLVGNVFGF 

       130        140        150        160        170        180 
KAVRGLRLED VRFPLAYVMT CGGPPHGIQV ERDIMNKYGR PLLGCTIKPK LGLSAKNYGR 

       190        200        210        220        230        240 
AVYECLRGGL DFTKDDENVN SQPFMRWRQR FDFVMEAIEK AEAETGERKG HYLNVTAPTP 

       250        260        270        280        290        300 
EEMYKRAEYA KEIGAPIIMH DFITGGFCAN TGLANWCRNN GMLLHIHRAM HAVMDRNPNH 

       310        320        330        340        350        360 
GIHFRVFTKM LRLSGGDHLH TGTVVGKLEG DRQATLGWID LLRERSIKED RSRGIFFDQE 

       370        380        390        400        410        420 
WGAMPGVFAV ASGGIHVWHM PALLSIFGDD AVFQFGGGTL GHPWGNAAGA AANRVALEAC 

       430        440        450        460        470 
VEARNEGRQL EKEGKEILTE AAKSSPELKA AMETWKEIKF EFDTVDKLDV AHR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF447860 Genomic DNA. Translation: AAL40972.1.
AE017282 Genomic DNA. Translation: AAU91176.1.
RefSeqYP_115143.1. NC_002977.6.

3D structure databases

ProteinModelPortalQ603Q7.
SMRQ603Q7. Positions 16-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243233.MCA2743.

Proteomic databases

PRIDEQ603Q7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU91176; AAU91176; MCA2743.
GeneID3104087.
KEGGmca:MCA2743.
PATRIC22609356. VBIMetCap22254_2773.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAFTQDWAS.
OrthoDBEOG6ZKXMS.

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_METCA
AccessionPrimary (citable) accession number: Q603Q7
Secondary accession number(s): Q8VR29
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 66 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