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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Thiobacillus denitrificans (strain ATCC 25259)
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. Both reactions occur simultaneously and in competition at the same active site.UniRule annotation1 Publication

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

Kineticsi

The CO2/O2 specificity factor (tau) is 46.

  1. KM=43 µM for ribulose 1,5-bisphosphate1 Publication
  2. KM=138 µM for CO21 Publication
  3. KM=1637 µM for O21 Publication
  1. Vmax=1.8 µmol/min/mg enzyme with CO2 as substrate1 Publication
  2. Vmax=0.5 µmol/min/mg enzyme with O2 as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei116Substrate; in homodimeric partnerUniRule annotation1
Binding sitei166SubstrateUniRule annotation1
Active sitei168Proton acceptorUniRule annotation1
Binding sitei170SubstrateUniRule annotation1
Metal bindingi194Magnesium; via carbamate groupUniRule annotation1
Metal bindingi196MagnesiumUniRule annotation1
Metal bindingi197MagnesiumUniRule annotation1
Active sitei287Proton acceptorUniRule annotation1
Binding sitei288SubstrateUniRule annotation1
Binding sitei320SubstrateUniRule annotation1
Sitei327Transition state stabilizerUniRule annotation1
Binding sitei372SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation

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:cbbL1
Ordered Locus Names:Tbd_2624
OrganismiThiobacillus denitrificans (strain ATCC 25259)
Taxonomic identifieri292415 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeThiobacillus
Proteomesi
  • UP000008291 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000626561 – 473Ribulose bisphosphate carboxylase large chainAdd BLAST473

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei194N6-carboxylysineUniRule annotation1

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains (By similarity). In R.sphaeroides the complex is approximately 500 kDa.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi292415.Tbd_2624.

Structurei

3D structure databases

ProteinModelPortaliQ56259.
SMRiQ56259.
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.
OMAiHVHRAMH.
OrthoDBiPOG091H14UZ.

Family and domain databases

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.

Q56259-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVKTYSAGV KEYRQTYWMP EYTPLDTDIL ACFKITPQAG VDREEAAAAV
60 70 80 90 100
AAESSTGTWT TVWTDLLTDL DYYKGRAYAI EDVPGDDTCF YAFIAYPIDL
110 120 130 140 150
FEEGSVVNVF TSLVGNVFGF KAVRALRLED VRFPIAYVKT CGGPPHGIQV
160 170 180 190 200
ERDVMNKYGR PLLGCTIKPK LGLSAKNYGR AVYECLRGGL DFTKDDENVN
210 220 230 240 250
SQPFMRWRQR FDFVMEAIQK SERETGERKG HYLNVTAPTP EEMYKRAEYA
260 270 280 290 300
KEIGAPIIMH DYITGGFCAN TGLANWCRDN GMLLHIHRAM HAVLDRNPHH
310 320 330 340 350
GIHFRVLTKI LRLSGGDHLH SGTVVGKLEG DREATLGWID MMRDSFVKED
360 370 380 390 400
RSRGIFFDQD WGSMPGVFPV ASGGIHVWHM PALVTIFGDD SVLQFGGGTL
410 420 430 440 450
GHPWGNAAGA AANRVALEAC VEARNKGVAI EKEGKTVLTE AAKNSPELKI
460 470
AMETWKEIKF EFDTVDKLDV AHK
Length:473
Mass (Da):52,694
Last modified:January 1, 1998 - v2
Checksum:i470DC11519D580A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42940 Genomic DNA. Translation: AAB70697.1.
CP000116 Genomic DNA. Translation: AAZ98577.1.
RefSeqiWP_011313136.1. NC_007404.1.

Genome annotation databases

EnsemblBacteriaiAAZ98577; AAZ98577; Tbd_2624.
KEGGitbd:Tbd_2624.
PATRICi23971443. VBIThiDen82923_2608.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42940 Genomic DNA. Translation: AAB70697.1.
CP000116 Genomic DNA. Translation: AAZ98577.1.
RefSeqiWP_011313136.1. NC_007404.1.

3D structure databases

ProteinModelPortaliQ56259.
SMRiQ56259.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi292415.Tbd_2624.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAZ98577; AAZ98577; Tbd_2624.
KEGGitbd:Tbd_2624.
PATRICi23971443. VBIThiDen82923_2608.

Phylogenomic databases

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

Family and domain databases

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 nameiRBL1_THIDA
AccessioniPrimary (citable) accession number: Q56259
Secondary accession number(s): Q3SFM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 106 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. 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.