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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CIP 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424))
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 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 sitei126Substrate; in homodimeric partnerUniRule annotation1
Binding sitei176SubstrateUniRule annotation1
Active sitei178Proton acceptorUniRule annotation1
Binding sitei180SubstrateUniRule annotation1
Metal bindingi204Magnesium; via carbamate groupUniRule annotation1
Metal bindingi206MagnesiumUniRule annotation1
Metal bindingi207MagnesiumUniRule annotation1
Active sitei296Proton acceptorUniRule annotation1
Binding sitei297SubstrateUniRule annotation1
Binding sitei329SubstrateUniRule annotation1
Sitei336Transition state stabilizerUniRule annotation1
Binding sitei381SubstrateUniRule 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

Enzyme and pathway databases

BioCyciCTAI164546:GJNE-4893-MONOMER.

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
Ordered Locus Names:RALTA_B1702
OrganismiCupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CIP 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424))
Taxonomic identifieri977880 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
Proteomesi
  • UP000001692 Componenti: Chromosome 2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001427481 – 486Ribulose bisphosphate carboxylase large chainAdd BLAST486

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei204N6-carboxylysineUniRule annotation1

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains.UniRule annotation

Protein-protein interaction databases

STRINGi977880.RALTA_B1702.

Structurei

3D structure databases

ProteinModelPortaliB3RBL8.
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.

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.

B3RBL8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAPEPVQGK PRKRYDAGVM KYKEMGYWDA DYEPKDTDLL ALFRITPQDG
60 70 80 90 100
VDPVEAAAAV AGESSTATWT VVWTDRLTAC DMYRAKAYRV DPVPNNPEQF
110 120 130 140 150
FCYVAYDLSL FEEGSIANLT ASIIGNVFSF KPIKAARLED MRFPVAYVKT
160 170 180 190 200
FAGPSTGIIV ERERLDKFGR PLLGATTKPK LGLSGRNYGR VVYEGLKGGL
210 220 230 240 250
DFMKDDENIN SQPFMHWRDR FLFVMDAVNK ASAATGEVKG SYLNVTAGTM
260 270 280 290 300
EEMYRRAEFA KSLGSVIIMV DLIVGWTCIQ SMSNWCRQND MILHLHRAGH
310 320 330 340 350
GTYTRQKNHG VSFRVIAKWL RLAGVDHMHT GTAVGKLEGD PLTVQGYYNV
360 370 380 390 400
CRDAYTRTDL TRGLFFDQDW ASLRKVMPVA SGGIHAGQMH QLISLFGDDV
410 420 430 440 450
VLQFGGGTIG HPQGIQAGAT ANRVALEAMV LARNEGRDIL NEGPEILRDA
460 470 480
ARWCGPLRAA LDTWGDITFN YTPTDTSDFV PTASVA
Length:486
Mass (Da):53,830
Last modified:September 2, 2008 - v1
Checksum:i3CD2D42BD416E19A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU633750 Genomic DNA. Translation: CAQ72293.1.
RefSeqiWP_012356508.1. NC_010530.1.

Genome annotation databases

EnsemblBacteriaiCAQ72293; CAQ72293; RALTA_B1702.
KEGGicti:RALTA_B1702.
PATRICi21537087. VBICupTai42494_5151.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU633750 Genomic DNA. Translation: CAQ72293.1.
RefSeqiWP_012356508.1. NC_010530.1.

3D structure databases

ProteinModelPortaliB3RBL8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi977880.RALTA_B1702.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAQ72293; CAQ72293; RALTA_B1702.
KEGGicti:RALTA_B1702.
PATRICi21537087. VBICupTai42494_5151.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciCTAI164546:GJNE-4893-MONOMER.

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_CUPTR
AccessioniPrimary (citable) accession number: B3RBL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: November 30, 2016
This is version 54 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

Complete 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.