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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299)
Status
Unreviewed-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 sitei125Substrate; in homodimeric partnerUniRule annotation1
Binding sitei175SubstrateUniRule annotation1
Active sitei177Proton acceptorUniRule annotation1
Binding sitei179SubstrateUniRule annotation1
Metal bindingi203Magnesium; via carbamate groupUniRule annotation1
Metal bindingi205MagnesiumUniRule annotation1
Metal bindingi206MagnesiumUniRule annotation1
Active sitei295Proton acceptorUniRule annotation1
Binding sitei296SubstrateUniRule annotation1
Binding sitei328SubstrateUniRule annotation1
Sitei335Transition state stabilizerUniRule annotation1
Binding sitei380SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationImported, MonooxygenaseUniRule annotation, Oxidoreductase

Keywords - Biological processi

Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation, PhotosynthesisUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

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:Rvan_0010Imported
OrganismiRhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299)Imported
Taxonomic identifieri648757 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesHyphomicrobiaceaeRhodomicrobium
Proteomesi
  • UP000001399 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei203N6-carboxylysineUniRule annotation1

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi648757.Rvan_0010.

Structurei

3D structure databases

ProteinModelPortaliE3I482.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 146RuBisCO_large_NInterPro annotationAdd BLAST121
Domaini156 – 463RuBisCO_largeInterPro annotationAdd BLAST308

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.

E3I482-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDKSETVKG EDRYKAGVMS YKKMGYWEPD YQPKETDLIA LFRVTPQDGV
60 70 80 90 100
DPIEASAAVA GESSTATWTV VWTDRLTASE KYRAKCYRVD PVPNAPGSYF
110 120 130 140 150
AYIAYDLDLF EGGSISNLTA SIIGNVFGFK PLKALRLEDM RLPVAYVKTF
160 170 180 190 200
DGPPAGIIVE RERLDKFGRP LLGATVKPKL GLSGRNYGRV VYEALKGGLD
210 220 230 240 250
FTKDDENINS QPFMHWRERF LYCMEAVNKA QAETGEIKGS YLNITAGTME
260 270 280 290 300
EMYKRAEYAK ELGSCIVMID LVIGYVAIQS ISKWARDNNM LLHLHRAGHS
310 320 330 340 350
TYTRQKSHGV SFRVISKWMR LAGVDHIHAG TVVGKLEGDP LTTAGYYDIL
360 370 380 390 400
REDFVPQNLE HGVFFDQPWA SLGKVMPVAS GGIHAGQMHQ LIHYLGEDVV
410 420 430 440 450
LQFGGGTIGH PYGIQAGATA NRVALEAMIF ARNEGRDYLA EGPQILKDAA
460 470 480
KTCTPLRQAL DTWGDVTFDY TSTDTPDFVP TPTAS
Length:485
Mass (Da):53,687
Last modified:January 11, 2011 - v1
Checksum:iCACE029CBD3E6F4C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002292 Genomic DNA. Translation: ADP69301.1.
RefSeqiWP_013417708.1. NC_014664.1.

Genome annotation databases

EnsemblBacteriaiADP69301; ADP69301; Rvan_0010.
KEGGirva:Rvan_0010.
PATRICi42667006. VBIRhoVan113057_0010.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002292 Genomic DNA. Translation: ADP69301.1.
RefSeqiWP_013417708.1. NC_014664.1.

3D structure databases

ProteinModelPortaliE3I482.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi648757.Rvan_0010.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADP69301; ADP69301; Rvan_0010.
KEGGirva:Rvan_0010.
PATRICi42667006. VBIRhoVan113057_0010.

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 nameiE3I482_RHOVT
AccessioniPrimary (citable) accession number: E3I482
Entry historyi
Integrated into UniProtKB/TrEMBL: January 11, 2011
Last sequence update: January 11, 2011
Last modified: November 30, 2016
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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 proteomeImported

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.