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F7US61 (F7US61_SYNYG) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 18. 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:rbcL HAMAP-Rule MF_01338
Synonyms:cbbL HAMAP-Rule MF_01338
Ordered Locus Names:SYNGTS_2225 EMBL BAK50973.1
OrganismSynechocystis sp. (strain PCC 6803 / GT-S) [Complete proteome] [HAMAP]
Taxonomic identifier1111707 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis ›

Protein attributes

Sequence length470 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; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity. HAMAP-Rule MF_01338

Post-translational modification

The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover 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 site1701Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2891Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding1961Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding1981Magnesium By similarity HAMAP-Rule MF_01338
Metal binding1991Magnesium By similarity HAMAP-Rule MF_01338
Binding site1181Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1681Substrate By similarity HAMAP-Rule MF_01338
Binding site1721Substrate By similarity HAMAP-Rule MF_01338
Binding site2901Substrate By similarity HAMAP-Rule MF_01338
Binding site3221Substrate By similarity HAMAP-Rule MF_01338
Binding site3741Substrate By similarity HAMAP-Rule MF_01338
Site3291Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue1961N6-carboxylysine By similarity HAMAP-Rule MF_01338
Disulfide bond242Interchain; in linked form By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
F7US61 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: 45B9322482745B2B

FASTA47052,491
        10         20         30         40         50         60 
MVQAKAGFKA GVQDYRLTYY TPDYTPKDTD LLACFRMTPQ PGVPAEEAAA AVAAESSTGT 

        70         80         90        100        110        120 
WTTVWTDNLT DLDRYKGRCY DLEAVPNEDN QYFAFIAYPL DLFEEGSVTN VLTSLVGNVF 

       130        140        150        160        170        180 
GFKALRALRL EDIRFPVALI KTFQGPPHGI TVERDKLNKY GRPLLGCTIK PKLGLSAKNY 

       190        200        210        220        230        240 
GRAVYECLRG GLDFTKDDEN INSQPFMRWR DRFLFVQEAI EKAQAETNEM KGHYLNVTAG 

       250        260        270        280        290        300 
TCEEMMKRAE FAKEIGTPII MHDFFTGGFT ANTTLARWCR DNGILLHIHR AMHAVVDRQK 

       310        320        330        340        350        360 
NHGIHFRVLA KCLRLSGGDH LHSGTVVGKL EGERGITMGF VDLMREDYVE EDRSRGIFFT 

       370        380        390        400        410        420 
QDYASMPGTM PVASGGIHVW HMPALVEIFG DDSCLQFGGG TLGHPWGNAP GATANRVALE 

       430        440        450        460        470 
ACVQARNEGR NLAREGNDVI REACRWSPEL AAACELWKEI KFEFEAMDTL

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References

[1]"Genomic structure of the cyanobacterium Synechocystis sp. PCC 6803 strain GT-S."
Tajima N., Sato S., Maruyama F., Kaneko T., Sasaki N.V., Kurokawa K., Ohta H., Kanesaki Y., Yoshikawa H., Tabata S., Ikeuchi M., Sato N.
DNA Res. 18:393-399(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / GT-S.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP012205 Genomic DNA. Translation: BAK50973.1.
RefSeqNP_442120.1. NC_000911.1.
YP_005652178.1. NC_017277.1.
YP_007451997.1. NC_020286.1.

3D structure databases

ProteinModelPortalF7US61.
SMRF7US61. Positions 6-464.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAK50973; BAK50973; SYNGTS_2225.
GeneID12253395.
14617671.
952593.
KEGGsyn:slr0009.
syy:SYNGTS_2225.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycSSP1148:GJOT-2263-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 nameF7US61_SYNYG
AccessionPrimary (citable) accession number: F7US61
Entry history
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: May 29, 2013
This is version 18 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