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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / STM815) (Burkholderia phymatum)
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 sitei141Substrate; in homodimeric partnerUniRule annotation1
Binding sitei191SubstrateUniRule annotation1
Active sitei193Proton acceptorUniRule annotation1
Binding sitei195SubstrateUniRule annotation1
Metal bindingi219Magnesium; via carbamate groupUniRule annotation1
Metal bindingi221MagnesiumUniRule annotation1
Metal bindingi222MagnesiumUniRule annotation1
Active sitei311Proton acceptorUniRule annotation1
Binding sitei312SubstrateUniRule annotation1
Binding sitei344SubstrateUniRule annotation1
Sitei351Transition state stabilizerUniRule annotation1
Binding sitei396SubstrateUniRule 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
Ordered Locus Names:Bphy_6497
Encoded oniPlasmid pBPHY010 Publication
OrganismiParaburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / STM815) (Burkholderia phymatum)
Taxonomic identifieri391038 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeParaburkholderia
Proteomesi
  • UP000001192 Componenti: Plasmid pBPHY01

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003557481 – 501Ribulose bisphosphate carboxylase large chainAdd BLAST501

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei219N6-carboxylysineUniRule annotation1

Proteomic databases

PRIDEiB2JX50.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliB2JX50.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

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.

B2JX50-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDFSKEAVK PADSATAAAK AEKRSRYAAG VMKYREMGYW QPDYTPKDTD
60 70 80 90 100
VIALFRITPQ PGVEPEEAAA AVAGESSTAT WTVVWTDRLT ACDMYRAKAF
110 120 130 140 150
RVEPVPNPAE GEPQYFAFIA YELDLFEEGS VANLTASIIG NVFGFKPLKA
160 170 180 190 200
LRLEDMRIPV AYLKTFQGPP TGIVVERERL DKYGRPLLGA TVKPKLGLSG
210 220 230 240 250
KNYGRVVYEG LKGGLDFLKD DENINSQPFM HWRDRYLFAM EAVHRAQAET
260 270 280 290 300
GEVKGHYLNV TAGTMEDMYE RAEFAKELGS CIVMIDLVIG WTAITSMGRW
310 320 330 340 350
ARKNDMILHL HRAGHGTYTR QRNHGISFRV IAKWLRMAGV DHAHAGTAVG
360 370 380 390 400
KLDGDPLSVQ GYYNVLRESH NSVDLTRGIF FDQHWAGLRK VMPVASGGIH
410 420 430 440 450
AGQMHQLLDL FGDDAILQFG GGTIGHPSGI QAGATANRVA LETMVKARNE
460 470 480 490 500
GRDIANEGSD LLEAAARHCT PLKQALDTWG DVTFNYTPTD SPDFAVTPSV

A
Length:501
Mass (Da):55,176
Last modified:June 10, 2008 - v1
Checksum:iE8238E2EFE685A2D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001045 Genomic DNA. Translation: ACC75527.1.
RefSeqiWP_012405686.1. NC_010625.1.

Genome annotation databases

EnsemblBacteriaiACC75527; ACC75527; Bphy_6497.
GeneIDi27746061.
KEGGibph:Bphy_6497.
PATRICi19199896. VBIBurPhy25146_6827.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001045 Genomic DNA. Translation: ACC75527.1.
RefSeqiWP_012405686.1. NC_010625.1.

3D structure databases

ProteinModelPortaliB2JX50.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiB2JX50.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACC75527; ACC75527; Bphy_6497.
GeneIDi27746061.
KEGGibph:Bphy_6497.
PATRICi19199896. VBIBurPhy25146_6827.

Phylogenomic databases

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_PARP8
AccessioniPrimary (citable) accession number: B2JX50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: June 10, 2008
Last modified: November 30, 2016
This is version 55 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, Plasmid, 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.