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F4CQ77 (F4CQ77_PSEUX) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
Short name=RuBisCO large subunit HAMAP-Rule MF_01338
EC=4.1.1.39 HAMAP-Rule MF_01338
Gene names
Name:cbbL HAMAP-Rule MF_01338
Ordered Locus Names:Psed_6249 EMBL AEA28350.1
OrganismPseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 / CB1190) [Complete proteome] [HAMAP]
Taxonomic identifier675635 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Pseudonocardia ›

Protein attributes

Sequence length476 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. 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. HAMAP-Rule MF_01338

Sequence similarities

Belongs to the RuBisCO large chain family. Type I subfamily. HAMAP-Rule MF_01338

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1681Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2861Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding1941Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding1961Magnesium By similarity HAMAP-Rule MF_01338
Metal binding1971Magnesium By similarity HAMAP-Rule MF_01338
Binding site1161Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1661Substrate By similarity HAMAP-Rule MF_01338
Binding site1701Substrate By similarity HAMAP-Rule MF_01338
Binding site2871Substrate By similarity HAMAP-Rule MF_01338
Binding site3191Substrate By similarity HAMAP-Rule MF_01338
Binding site3711Substrate By similarity HAMAP-Rule MF_01338
Site3261Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue1941N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
F4CQ77 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: 7CD92F1F43816FA0

FASTA47652,620
        10         20         30         40         50         60 
MADRWNAGVI PYAEMGYWQP DYEPKDTDIL CAFRITPQDG VPPEEAGAAV AGESSTATWT 

        70         80         90        100        110        120 
VVWTDRLTTF EHYQAKCYKV DPVPNTPGQW IAYIAYDIDL FEEASIANLT SSIIGNVFGF 

       130        140        150        160        170        180 
KPLKALRLED MRIPTHYVKT FQGPAHGIVM EREHLGKFGR PILGATTKPK LGLSARNYGR 

       190        200        210        220        230        240 
VVYEALRGGL DFTKDDENIN SQPFMRWRDR FLFCMEAVNR AQAATGEIKG HYLNVTAGTM 

       250        260        270        280        290        300 
EEMYERANFA AELGSVIVMI DLTIGYTAIQ SMAKWARDNN VILHLHRAGH GTYTRQKNHG 

       310        320        330        340        350        360 
VSFRVISKWM RLAGVDHIHA GTVVGKLEGD PMTTAGFYDT LRKDSIKADL SKGLYFDQEW 

       370        380        390        400        410        420 
ASMPGVMPVA SGGIHAGQMH QLIHYLGEDV ILQFGGGTIG HPMGIAAGAE ANRVALEAMI 

       430        440        450        460        470 
KARNEGVDYY KEGPEILKKA ASRNRALDTA LATWGDITFN YESTDTPDVV ATPTNA

« Hide

References

[1]"Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans strain CB1190."
Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T., Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A., Alvarez-Cohen L.
J. Bacteriol. 193:4549-4550(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 55486 / DSM 44775 / JCM 13855 / CB1190.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002593 Genomic DNA. Translation: AEA28350.1.
RefSeqYP_004336203.1. NC_015312.1.

3D structure databases

ProteinModelPortalF4CQ77.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEA28350; AEA28350; Psed_6249.
GeneID10368104.
KEGGpdx:Psed_6249.
PATRIC54404142. VBIPseDio141225_6325.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycPDIO675635:GHMF-6618-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. RuBisCO_large. 1 hit.
SSF54966. RuBisCO_large. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF4CQ77_PSEUX
AccessionPrimary (citable) accession number: F4CQ77
Entry history
Integrated into UniProtKB/TrEMBL: June 28, 2011
Last sequence update: June 28, 2011
Last modified: May 1, 2013
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info