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Q8DIS5

- RBL_THEEB

UniProt

Q8DIS5 - RBL_THEEB

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, rbcL, tll1506
Organism
Thermosynechococcus elongatus (strain BP-1)
Status
Reviewed - 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 By similarity.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

Binds 1 magnesium ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei123 – 1231Substrate; in homodimeric partner By similarity
Binding sitei173 – 1731Substrate By similarity
Active sitei175 – 1751Proton acceptor By similarity
Binding sitei177 – 1771Substrate By similarity
Metal bindingi201 – 2011Magnesium; via carbamate group By similarity
Metal bindingi203 – 2031Magnesium By similarity
Metal bindingi204 – 2041Magnesium By similarity
Active sitei294 – 2941Proton acceptor By similarity
Binding sitei295 – 2951Substrate By similarity
Binding sitei327 – 3271Substrate By similarity
Sitei334 – 3341Transition state stabilizer By similarity
Binding sitei379 – 3791Substrate By similarity

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. monooxygenase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. photorespiration Source: UniProtKB-KW
  2. reductive pentose-phosphate cycle Source: UniProtKB-KW
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 chain (EC:4.1.1.39)
Short name:
RuBisCO large subunit
Gene namesi
Name:cbbL
Synonyms:rbcL
Ordered Locus Names:tll1506
OrganismiThermosynechococcus elongatus (strain BP-1)
Taxonomic identifieri197221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
ProteomesiUP000000440: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 475475Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_0000062649Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei201 – 2011N6-carboxylysine By similarity
Disulfide bondi247 – 247Interchain; in linked form By similarity

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 By similarity.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 By similarity.

Protein-protein interaction databases

STRINGi197221.tll1506.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.
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

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MAYTQSKSQK VGYQAGVKDY RLTYYTPDYT PKDTDILAAF RVTPQPGVPF    50
EEAAAAVAAE SSTGTWTTVW TDLLTDLDRY KGCCYDIEPL PGEDNQFIAY 100
IAYPLDLFEE GSVTNMLTSI VGNVFGFKAL KALRLEDLRI PVAYLKTFQG 150
PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT 200
KDDENINSQP FQRWRDRFLF VADAIHKAQA ETGEIKGHYL NVTAPTCEEM 250
LKRAEFAKEL EMPIIMHDFL TAGFTANTTL SKWCRDNGML LHIHRAMHAV 300
MDRQKNHGIH FRVLAKCLRM SGGDHIHTGT VVGKLEGDKA VTLGFVDLLR 350
ENYIEQDRSR GIYFTQDWAS MPGVMAVASG GIHVWHMPAL VDIFGDDAVL 400
QFGGGTLGHP WGNAPGATAN RVALEACIQA RNEGRDLMRE GGDIIREAAR 450
WSPELAAACE LWKEIKFEFE AQDTI 475
Length:475
Mass (Da):53,025
Last modified:March 1, 2003 - v1
Checksum:iB4A97CD4D6A3EB91
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
BA000039 Genomic DNA. Translation: BAC09058.1 .
RefSeqi NP_682296.1. NC_004113.1.
WP_011057346.1. NC_004113.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YBV X-ray 2.30 A/C/E/G/I/K/M/O 1-475 [» ]
3ZXW X-ray 2.10 A/C/E/G 1-475 [» ]
ProteinModelPortali Q8DIS5.
SMRi Q8DIS5. Positions 12-475.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 197221.tll1506.

Proteomic databases

PRIDEi Q8DIS5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC09058 ; BAC09058 ; BAC09058 .
GeneIDi 1011208.
KEGGi tel:tll1506.
PATRICi 23928370. VBITheElo119873_1580.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OMAi FTQDWAS.
OrthoDBi EOG6ZKXMS.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01338. RuBisCO_L_type1.
InterProi IPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view ]
Pfami PF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view ]
SUPFAMi SSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 74 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" By similarity.

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

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