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K9SG91 (K9SG91_9CYAN) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 10. 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
Synonyms:rbcL HAMAP-Rule MF_01338
ORF Names:Pse7367_0918 EMBL AFY69218.1
OrganismPseudanabaena sp. PCC 7367 [Complete proteome] EMBL AFY69218.1
Taxonomic identifier82654 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesPseudanabaena

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 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

Sequences

Sequence LengthMass (Da)Tools
K9SG91 [UniParc].

Last modified March 6, 2013. Version 1.
Checksum: 067933F733FF88E7

FASTA47052,305
        10         20         30         40         50         60 
MATTTKGFQA GVKDYKLTYY TPDYTPKDTD ILAAFRMTPQ PGVPPEEAGA AVAAESSTGT 

        70         80         90        100        110        120 
WTTVWTDLLT DLDRYKGRCY DVESVPGEDN QYIAYVAYPL DLFEEGSVTN MLTSIVGNVF 

       130        140        150        160        170        180 
GFKALRALRL EDLRIPVAYL KTFEGPPHGI VVERDKLNKY GRPLLGCTIK PKLGLSAKNY 

       190        200        210        220        230        240 
GRACYEILRG GLDFTKDDEN INSQPFMRWR DRFLFVADAI HKAQAETGEI KGHYLNCTAA 

       250        260        270        280        290        300 
TVEEMMKRAE FAKELEMPIV MHDFLTAGFT ANTTLSKWCR NNGMLLHIHR AMHAVIDRQK 

       310        320        330        340        350        360 
NHGMHFRVLA KCLRMSGGDH IHTGTVVGKL EGDRASTLGF VDLLRENYVE QDKSRGIYFT 

       370        380        390        400        410        420 
QDWASMGGVF AVASGGIHVW HMPALVEIFG DDSVLQFGGG TLGHPWGNAP GAVANRVALE 

       430        440        450        460        470 
ACVQARNEGR NLNREGADII REAARWSPEL AVACETWKEI KFEFDTVDTL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003592 Genomic DNA. Translation: AFY69218.1.
RefSeqYP_007101646.1. NC_019701.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFY69218; AFY69218; Pse7367_0918.
GeneID14130672.
KEGGpseu:Pse7367_0918.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

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 nameK9SG91_9CYAN
AccessionPrimary (citable) accession number: K9SG91
Entry history
Integrated into UniProtKB/TrEMBL: March 6, 2013
Last sequence update: March 6, 2013
Last modified: June 11, 2014
This is version 10 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)