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F1KLD0 (F1KLD0_FRAVE) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 19. 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
ORF Names:FvH4_C0049 EMBL ADY15359.1
Encoded onPlastid; Chloroplast EMBL ADY15359.1
OrganismFragaria vesca subsp. vesca EMBL ADY15359.1
Taxonomic identifier101020 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeRosoideaePotentilleaeFragariinaeFragaria

Protein attributes

Sequence length475 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

Subcellular location

Plastidchloroplast By similarity RuleBase RU000303 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

Molecule processing

Propeptide1 – 22 By similarity HAMAP-Rule MF_01338

Sites

Active site1751Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2941Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2011Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2031Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2041Magnesium By similarity HAMAP-Rule MF_01338
Binding site1231Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1731Substrate By similarity HAMAP-Rule MF_01338
Binding site1771Substrate By similarity HAMAP-Rule MF_01338
Binding site2951Substrate By similarity HAMAP-Rule MF_01338
Binding site3271Substrate By similarity HAMAP-Rule MF_01338
Binding site3791Substrate By similarity HAMAP-Rule MF_01338
Site3341Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue31N-acetylproline By similarity HAMAP-Rule MF_01338
Modified residue141N6,N6,N6-trimethyllysine By similarity HAMAP-Rule MF_01338
Modified residue2011N6-carboxylysine By similarity HAMAP-Rule MF_01338
Disulfide bond247Interchain; in linked form By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
F1KLD0 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: 7AD3188E4B7CC028

FASTA47552,707
        10         20         30         40         50         60 
MSPQTETKAS VGFKAGVKDY KLTYYTPDYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE 

        70         80         90        100        110        120 
SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV PGEESQFIAY VAYPLDLFEE GSVTNMFTSI 

       130        140        150        160        170        180 
VGNVFGFKAL RALRLEDLRI PTAYVKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL 

       190        200        210        220        230        240 
SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIYKAQA ETGEIKGHYL 

       250        260        270        280        290        300 
NATAGTCEDM MKRAVFAREL GVPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV 

       310        320        330        340        350        360 
IDRQKNHGMH FRVLAKALRM SGGDHIHAGT VVGKLEGERE ITLGFVDLLR DDFIEKDRSR 

       370        380        390        400        410        420 
GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN 

       430        440        450        460        470 
RVALEACVQA RNEGRDLARE GNDIIREACK WSPELAAACE VWKEIKFEFE AMDTL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
JF345175 Genomic DNA. Translation: ADY15359.1.
RefSeqYP_004286110.1. NC_015206.1.

3D structure databases

ProteinModelPortalF1KLD0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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 nameF1KLD0_FRAVE
AccessionPrimary (citable) accession number: F1KLD0
Entry history
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: February 19, 2014
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)