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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL1

Organism
Rhodospirillum centenum (strain ATCC 51521 / SW)
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 sitei127Substrate; in homodimeric partnerUniRule annotation1
Binding sitei177SubstrateUniRule annotation1
Active sitei179Proton acceptorUniRule annotation1
Binding sitei181SubstrateUniRule annotation1
Metal bindingi205Magnesium; via carbamate groupUniRule annotation1
Metal bindingi207MagnesiumUniRule annotation1
Metal bindingi208MagnesiumUniRule annotation1
Active sitei297Proton acceptorUniRule annotation1
Binding sitei298SubstrateUniRule annotation1
Binding sitei330SubstrateUniRule annotation1
Sitei337Transition state stabilizerUniRule annotation1
Binding sitei382SubstrateUniRule 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:cbbL1Imported
Synonyms:cbbLUniRule annotation
Ordered Locus Names:RC1_4061Imported
OrganismiRhodospirillum centenum (strain ATCC 51521 / SW)Imported
Taxonomic identifieri414684 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum
Proteomesi
  • UP000001591 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei205N6-carboxylysineUniRule annotation1

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi414684.RC1_4061.

Structurei

3D structure databases

ProteinModelPortaliB6IYM6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 148RuBisCO_large_NInterPro annotationAdd BLAST121
Domaini158 – 465RuBisCO_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.
OMAiEAQYFAY.
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.

B6IYM6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTRVSGDQL DAKARYKPGV LKYRQMGYWV PDYEPKDTDV LAVFRITPQD
60 70 80 90 100
GVDAEEAAAA VAGESSTATW TVVWTDRLTN CDHYRAKAYR VDPVPGSPGQ
110 120 130 140 150
YFAYIAYDLD LFEEGSIANL TASIIGNVFG FKPLKALRLE DMRIPVAYLK
160 170 180 190 200
TFQGPATGIV VERERLNVYG RPLLGATMKP KLGLSGRNYG RVVYEALKGG
210 220 230 240 250
LDFTKDDENI NSQPFMHWRD RFLYCMEGVN RAMAETGEVK GTYLNVTAAT
260 270 280 290 300
MEDMYERAEF AKELGSVIIM IDLVIGYTAI QSMAKWARKN DMILHLHRAG
310 320 330 340 350
HSTYTRQKSH GVSFRVIAKW MRMAGVDHIH AGTVVGKLEG DPNVIRGVYD
360 370 380 390 400
TCRETHVPQN LQHGIFFDQP WASLKKLMPV ASGGIHAGQM HQLLTYLGED
410 420 430 440 450
VVLQFGGGTI GHPEGIQAGA TANRVALEAM VKARNEGRDI WNEGPQILQD
460 470 480
AARWCGPLRA ALETWKDVTF DYASTDSVDF VPTPTPA
Length:487
Mass (Da):54,092
Last modified:December 16, 2008 - v1
Checksum:i5CA7C2B73054AE37
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000613 Genomic DNA. Translation: ACJ01400.1.
RefSeqiWP_012569173.1. NC_011420.2.

Genome annotation databases

EnsemblBacteriaiACJ01400; ACJ01400; RC1_4061.
KEGGirce:RC1_4061.
PATRICi23323296. VBIRhoCen1465_3954.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000613 Genomic DNA. Translation: ACJ01400.1.
RefSeqiWP_012569173.1. NC_011420.2.

3D structure databases

ProteinModelPortaliB6IYM6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi414684.RC1_4061.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACJ01400; ACJ01400; RC1_4061.
KEGGirce:RC1_4061.
PATRICi23323296. VBIRhoCen1465_3954.

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.
HOGENOMiHOG000230831.
KOiK01601.
OMAiEAQYFAY.
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 nameiB6IYM6_RHOCS
AccessioniPrimary (citable) accession number: B6IYM6
Entry historyi
Integrated into UniProtKB/TrEMBL: December 16, 2008
Last sequence update: December 16, 2008
Last modified: November 30, 2016
This is version 58 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.