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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Thermosynechococcus elongatus (strain BP-1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.UniRule annotation
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei123 – 1231Substrate; in homodimeric partnerUniRule annotation
Binding sitei173 – 1731SubstrateUniRule annotation
Active sitei175 – 1751Proton acceptorUniRule annotation
Binding sitei177 – 1771SubstrateUniRule annotation
Metal bindingi201 – 2011Magnesium; via carbamate groupUniRule annotation
Metal bindingi203 – 2031MagnesiumUniRule annotation
Metal bindingi204 – 2041MagnesiumUniRule annotation
Active sitei294 – 2941Proton acceptorUniRule annotation
Binding sitei295 – 2951SubstrateUniRule annotation
Binding sitei327 – 3271SubstrateUniRule annotation
Sitei334 – 3341Transition state stabilizerUniRule annotation
Binding sitei379 – 3791SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chainUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunitUniRule annotation
Gene namesi
Name:cbbLUniRule annotation
Synonyms:rbcLUniRule annotation
Ordered Locus Names:tll1506
OrganismiThermosynechococcus elongatus (strain BP-1)
Taxonomic identifieri197221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
ProteomesiUP000000440 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 475475Ribulose bisphosphate carboxylase large chainPRO_0000062649Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei201 – 2011N6-carboxylysineUniRule annotation
Disulfide bondi247 – 247Interchain; in linked formUniRule annotation

Post-translational modificationi

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.UniRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ8DIS5.

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
tlr1766Q8DI262EBI-9639313,EBI-9639332

Protein-protein interaction databases

IntActiQ8DIS5. 1 interaction.
STRINGi197221.tll1506.

Structurei

Secondary structure

1
475
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 244Combined sources
Beta strandi35 – 4410Combined sources
Helixi50 – 6011Combined sources
Turni61 – 633Combined sources
Beta strandi66 – 683Combined sources
Helixi70 – 745Combined sources
Helixi77 – 804Combined sources
Beta strandi83 – 897Combined sources
Beta strandi93 – 953Combined sources
Beta strandi97 – 1037Combined sources
Helixi105 – 1073Combined sources
Helixi113 – 1219Combined sources
Helixi124 – 1263Combined sources
Beta strandi130 – 13910Combined sources
Helixi142 – 1454Combined sources
Helixi155 – 1628Combined sources
Beta strandi169 – 1735Combined sources
Beta strandi175 – 1784Combined sources
Helixi182 – 19413Combined sources
Beta strandi198 – 2014Combined sources
Beta strandi207 – 2093Combined sources
Helixi214 – 23219Combined sources
Beta strandi237 – 2415Combined sources
Helixi247 – 25913Combined sources
Beta strandi263 – 2686Combined sources
Helixi269 – 2724Combined sources
Helixi274 – 28714Combined sources
Beta strandi290 – 2945Combined sources
Helixi298 – 3025Combined sources
Beta strandi305 – 3095Combined sources
Helixi311 – 32111Combined sources
Beta strandi324 – 3274Combined sources
Beta strandi331 – 3355Combined sources
Helixi339 – 35012Combined sources
Beta strandi352 – 3543Combined sources
Helixi358 – 3603Combined sources
Beta strandi375 – 3817Combined sources
Helixi384 – 3863Combined sources
Helixi387 – 3948Combined sources
Beta strandi396 – 4016Combined sources
Helixi404 – 4074Combined sources
Helixi413 – 43119Combined sources
Turni432 – 4343Combined sources
Turni437 – 4393Combined sources
Helixi441 – 45111Combined sources
Helixi453 – 46210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YBVX-ray2.30A/C/E/G/I/K/M/O1-475[»]
3ZXWX-ray2.10A/C/E/G1-475[»]
ProteinModelPortaliQ8DIS5.
SMRiQ8DIS5. Positions 12-475.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO large chain family. Type I subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiHAAFTRN.
OrthoDBiEOG6ZKXMS.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1.
InterProiIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8DIS5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYTQSKSQK VGYQAGVKDY RLTYYTPDYT PKDTDILAAF RVTPQPGVPF
60 70 80 90 100
EEAAAAVAAE SSTGTWTTVW TDLLTDLDRY KGCCYDIEPL PGEDNQFIAY
110 120 130 140 150
IAYPLDLFEE GSVTNMLTSI VGNVFGFKAL KALRLEDLRI PVAYLKTFQG
160 170 180 190 200
PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT
210 220 230 240 250
KDDENINSQP FQRWRDRFLF VADAIHKAQA ETGEIKGHYL NVTAPTCEEM
260 270 280 290 300
LKRAEFAKEL EMPIIMHDFL TAGFTANTTL SKWCRDNGML LHIHRAMHAV
310 320 330 340 350
MDRQKNHGIH FRVLAKCLRM SGGDHIHTGT VVGKLEGDKA VTLGFVDLLR
360 370 380 390 400
ENYIEQDRSR GIYFTQDWAS MPGVMAVASG GIHVWHMPAL VDIFGDDAVL
410 420 430 440 450
QFGGGTLGHP WGNAPGATAN RVALEACIQA RNEGRDLMRE GGDIIREAAR
460 470
WSPELAAACE LWKEIKFEFE AQDTI
Length:475
Mass (Da):53,025
Last modified:March 1, 2003 - v1
Checksum:iB4A97CD4D6A3EB91
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC09058.1.
RefSeqiNP_682296.1. NC_004113.1.
WP_011057346.1. NC_004113.1.

Genome annotation databases

EnsemblBacteriaiBAC09058; BAC09058; BAC09058.
GeneIDi1011208.
KEGGitel:tll1506.
PATRICi23928370. VBITheElo119873_1580.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC09058.1.
RefSeqiNP_682296.1. NC_004113.1.
WP_011057346.1. NC_004113.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YBVX-ray2.30A/C/E/G/I/K/M/O1-475[»]
3ZXWX-ray2.10A/C/E/G1-475[»]
ProteinModelPortaliQ8DIS5.
SMRiQ8DIS5. Positions 12-475.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8DIS5. 1 interaction.
STRINGi197221.tll1506.

Proteomic databases

PRIDEiQ8DIS5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC09058; BAC09058; BAC09058.
GeneIDi1011208.
KEGGitel:tll1506.
PATRICi23928370. VBITheElo119873_1580.

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiHAAFTRN.
OrthoDBiEOG6ZKXMS.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1.
InterProiIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BP-1.

Entry informationi

Entry nameiRBL_THEEB
AccessioniPrimary (citable) accession number: Q8DIS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: March 1, 2003
Last modified: May 27, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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".UniRule annotation

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.