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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Mesorhizobium ciceri biovar biserrulae (strain HAMBI 2942 / LMG 23838 / WSM1271)
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 sitei136Substrate; in homodimeric partnerUniRule annotation1
Binding sitei186SubstrateUniRule annotation1
Active sitei188Proton acceptorUniRule annotation1
Binding sitei190SubstrateUniRule annotation1
Metal bindingi214Magnesium; via carbamate groupUniRule annotation1
Metal bindingi216MagnesiumUniRule annotation1
Metal bindingi217MagnesiumUniRule annotation1
Active sitei306Proton acceptorUniRule annotation1
Binding sitei307SubstrateUniRule annotation1
Binding sitei339SubstrateUniRule annotation1
Sitei346Transition state stabilizerUniRule annotation1
Binding sitei391SubstrateUniRule 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

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:Mesci_4283Imported
OrganismiMesorhizobium ciceri biovar biserrulae (strain HAMBI 2942 / LMG 23838 / WSM1271)Imported
Taxonomic identifieri765698 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium
Proteomesi
  • UP000007471 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei214N6-carboxylysineUniRule annotation1

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi765698.Mesci_4283.

Structurei

3D structure databases

ProteinModelPortaliE8TEA0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 157RuBisCO_large_NInterPro annotationAdd BLAST127
Domaini167 – 474RuBisCO_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.

E8TEA0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKIDILPAG TLKEGKERYK SGVIPYKKMG YWEPDYRPKE TDLIAMFRIT
60 70 80 90 100
PQPGVDHEEA AAAIAGESST ATWTVVWTDR LTACELYRAK AFRSEPVPNT
110 120 130 140 150
GPGTKTEQQY FAYIAYDLDL FEPGSIANLT ASIIGNVFGF KAVKALRLED
160 170 180 190 200
MRIPVAYLKT FQGPATGIVV ERERLDKFGR PLLGATTKPK LGLSGRNYGR
210 220 230 240 250
VVYEALKGGL DFVKDDENIN SQPFMHWRDR FLYCMEAVNK ASAATGEVKG
260 270 280 290 300
HYLNVTAGTM EEMYERAEFA KQLGSCIVMI DLVIGYTAIQ SMAKWARRND
310 320 330 340 350
MILHLHRAGN STYSRQKNHG MNFRVICKWM RMAGVDHIHA GTVVGKLEGD
360 370 380 390 400
PLMIKGFYDT LREERTPQNL ETGLFFDQEW ASLNKVMPVA SGGIHAGQMH
410 420 430 440 450
QLIHYLGEDV ILQFGGGTIG HPDGIQAGAT ANRVALEAMI LARNEGRDYL
460 470 480 490
REGTKILEQA ARWCTPLKAA LETWKDVTFN YESTDTADFV PTATPSF
Length:497
Mass (Da):55,476
Last modified:April 5, 2011 - v1
Checksum:i95D543D064004907
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002447 Genomic DNA. Translation: ADV13393.1.
RefSeqiWP_013532056.1. NC_014923.1.
YP_004143443.1. NC_014923.1.

Genome annotation databases

EnsemblBacteriaiADV13393; ADV13393; Mesci_4283.
GeneIDi10119774.
KEGGimci:Mesci_4283.
PATRICi45258702. VBIMesCic160642_4780.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002447 Genomic DNA. Translation: ADV13393.1.
RefSeqiWP_013532056.1. NC_014923.1.
YP_004143443.1. NC_014923.1.

3D structure databases

ProteinModelPortaliE8TEA0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi765698.Mesci_4283.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADV13393; ADV13393; Mesci_4283.
GeneIDi10119774.
KEGGimci:Mesci_4283.
PATRICi45258702. VBIMesCic160642_4780.

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 nameiE8TEA0_MESCW
AccessioniPrimary (citable) accession number: E8TEA0
Entry historyi
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: November 30, 2016
This is version 46 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.