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E0U7P5 (E0U7P5_CYAP2) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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
Synonyms:rbcL HAMAP-Rule MF_01338
Ordered Locus Names:Cyan7822_2899 EMBL ADN14857.1
OrganismCyanothece sp. (strain PCC 7822) [Complete proteome] [HAMAP] EMBL ADN14857.1
Taxonomic identifier497965 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanothece

Protein attributes

Sequence length472 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 in the photorespiration process. 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 site1721Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2911Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding1981Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2001Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2011Magnesium By similarity HAMAP-Rule MF_01338
Binding site1201Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1701Substrate By similarity HAMAP-Rule MF_01338
Binding site1741Substrate By similarity HAMAP-Rule MF_01338
Binding site2921Substrate By similarity HAMAP-Rule MF_01338
Binding site3241Substrate By similarity HAMAP-Rule MF_01338
Binding site3761Substrate By similarity HAMAP-Rule MF_01338
Site3311Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue1981N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
E0U7P5 [UniParc].

Last modified November 2, 2010. Version 1.
Checksum: CE42E983A700A93A

FASTA47252,657
        10         20         30         40         50         60 
MVQSKAKGGF QAGVKDYRLT YYTPDYTPKD TDLLACFRVT PQPGVPPEEA GAAVAAESST 

        70         80         90        100        110        120 
GTWTTVWTDG LTDLDRYKGR CYDIEPVPNE DNQYFCFVAY PLDLFEEGSV TNILTSIVGN 

       130        140        150        160        170        180 
VFGFKALRAL RLEDIRFPVA LLKTFQGPPH GITVERDKLN KYGRPLLGCT IKPKLGLSAK 

       190        200        210        220        230        240 
NYGRAVYECL RGGLDFTKDD ENINSQPFMR WRDRFLFVQE AIEKAQAETN EIKGHYLNVT 

       250        260        270        280        290        300 
AGTLEEMMKR AEFAKEIKTP IIMHDYLTGG FTANTTLAKF CRDNGLLLHI HRAMHAVIDR 

       310        320        330        340        350        360 
QKNHGIHFRV LAKCLRMSGG DHLHSGTVVG KLEGERGITM GFVDLMREDY VEEDRARGIF 

       370        380        390        400        410        420 
FTQDWASMPG VMPVASGGIH VWHMPALVEI FGDDSCLQFG GGTLGHPWGN APGATANRVA 

       430        440        450        460        470 
LEACIQARNE GRSLAREGNE VIREAARWSP ELAAACELWK EIKFEFEAMD TL 

« Hide

References

[1]"Novel metabolic attributes of the genus Cyanothece, comprising a group of unicellular nitrogen-fixing Cyanobacteria."
Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., Sherman L.A., Pakrasi H.B.
MBio 2:E214-E214(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7822.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002198 Genomic DNA. Translation: ADN14857.1.
RefSeqYP_003888132.1. NC_014501.1.

3D structure databases

ProteinModelPortalE0U7P5.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADN14857; ADN14857; Cyan7822_2899.
GeneID9739388.
KEGGcyj:Cyan7822_2899.
PATRIC42286569. VBICyaSp18455_3032.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.
OMAHRAMHAA.

Enzyme and pathway databases

BioCycCSP497965:GJAC-2935-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...

Entry information

Entry nameE0U7P5_CYAP2
AccessionPrimary (citable) accession number: E0U7P5
Entry history
Integrated into UniProtKB/TrEMBL: November 2, 2010
Last sequence update: November 2, 2010
Last modified: February 19, 2014
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)