Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Binding sitei123Substrate; in homodimeric partnerUniRule annotation1
Binding sitei173SubstrateUniRule annotation1
Active sitei175Proton acceptorUniRule annotation1
Binding sitei177SubstrateUniRule annotation1
Metal bindingi201Magnesium; via carbamate groupUniRule annotation1
Metal bindingi203MagnesiumUniRule annotation1
Metal bindingi204MagnesiumUniRule annotation1
Active sitei294Proton acceptorUniRule annotation1
Binding sitei295SubstrateUniRule annotation1
Binding sitei327SubstrateUniRule annotation1
Sitei334Transition state stabilizerUniRule annotation1
Binding sitei379SubstrateUniRule annotation1

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 lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeThermosynechococcus
Proteomesi
  • UP000000440 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000626491 – 475Ribulose bisphosphate carboxylase large chainAdd BLAST475

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei201N6-carboxylysineUniRule annotation1
Disulfide bondi247Interchain; 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 interactor.
STRINGi197221.tll1506.

Structurei

Secondary structure

1475
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 24Combined sources4
Beta strandi35 – 44Combined sources10
Helixi50 – 60Combined sources11
Turni61 – 63Combined sources3
Beta strandi66 – 68Combined sources3
Helixi70 – 74Combined sources5
Helixi77 – 80Combined sources4
Beta strandi83 – 89Combined sources7
Beta strandi93 – 95Combined sources3
Beta strandi97 – 103Combined sources7
Helixi105 – 107Combined sources3
Helixi113 – 121Combined sources9
Helixi124 – 126Combined sources3
Beta strandi130 – 139Combined sources10
Helixi142 – 145Combined sources4
Helixi155 – 162Combined sources8
Beta strandi169 – 173Combined sources5
Beta strandi175 – 178Combined sources4
Helixi182 – 194Combined sources13
Beta strandi198 – 201Combined sources4
Beta strandi207 – 209Combined sources3
Helixi214 – 232Combined sources19
Beta strandi237 – 241Combined sources5
Helixi247 – 259Combined sources13
Beta strandi263 – 268Combined sources6
Helixi269 – 272Combined sources4
Helixi274 – 287Combined sources14
Beta strandi290 – 294Combined sources5
Helixi298 – 302Combined sources5
Beta strandi305 – 309Combined sources5
Helixi311 – 321Combined sources11
Beta strandi324 – 327Combined sources4
Beta strandi331 – 335Combined sources5
Helixi339 – 350Combined sources12
Beta strandi352 – 354Combined sources3
Helixi358 – 360Combined sources3
Beta strandi375 – 381Combined sources7
Helixi384 – 386Combined sources3
Helixi387 – 394Combined sources8
Beta strandi396 – 401Combined sources6
Helixi404 – 407Combined sources4
Helixi413 – 431Combined sources19
Turni432 – 434Combined sources3
Turni437 – 439Combined sources3
Helixi441 – 451Combined sources11
Helixi453 – 462Combined sources10

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.
HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.
OrthoDBiPOG091H14UZ.

Family and domain databases

CDDicd08212. RuBisCO_large_I. 1 hit.
Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1. 1 hit.
InterProiIPR033966. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR020888. RuBisCO_lsuI.
[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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YBVX-ray2.30A/C/E/G/I/K/M/O1-475[»]
3ZXWX-ray2.10A/C/E/G1-475[»]
ProteinModelPortaliQ8DIS5.
SMRiQ8DIS5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8DIS5. 1 interactor.
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

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.
HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.
OrthoDBiPOG091H14UZ.

Family and domain databases

CDDicd08212. RuBisCO_large_I. 1 hit.
Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1. 1 hit.
InterProiIPR033966. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR020888. RuBisCO_lsuI.
[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...

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: November 30, 2016
This is version 91 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

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 one 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.