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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2)
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 sitei124Substrate; in homodimeric partnerUniRule annotation1
Binding sitei174SubstrateUniRule annotation1
Active sitei176Proton acceptorUniRule annotation1
Binding sitei178SubstrateUniRule annotation1
Metal bindingi202Magnesium; via carbamate groupUniRule annotation1
Metal bindingi204MagnesiumUniRule annotation1
Metal bindingi205MagnesiumUniRule annotation1
Active sitei294Proton acceptorUniRule annotation1
Binding sitei295SubstrateUniRule annotation1
Binding sitei327SubstrateUniRule annotation1
Sitei334Transition state stabilizerUniRule annotation1
Binding sitei379SubstrateUniRule 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:Msil_1195Imported
OrganismiMethylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2)Imported
Taxonomic identifieri395965 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBeijerinckiaceaeMethylocella
Proteomesi
  • UP000002257 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei202N6-carboxylysineUniRule annotation1

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi395965.Msil_1195.

Structurei

3D structure databases

ProteinModelPortaliB8EPF9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 145RuBisCO_large_NInterPro annotationAdd BLAST121
Domaini155 – 462RuBisCO_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.

B8EPF9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTASPPAQPR SRYSAGVMEY REMGYWQPDY VPGETDIIAC FRVTPQEGVD
60 70 80 90 100
PIEASAAVAG ESSTATWTVV WTDRLTASEK YRAKCYRVDP VPNAPGSWFA
110 120 130 140 150
FIAYDLDLFE PGSISNLAAS IIGNVFGFKP LRALRLEDMR FPVAYVKTFQ
160 170 180 190 200
GPATGIVVER ERLDKFGRPL LGATVKPKLG LSGRNYGRVV YEALKGGLDF
210 220 230 240 250
TKDDENINSQ PFMHWRDRFL YCMEAVNRAE AATGEIKGTY LNVTAATMED
260 270 280 290 300
MYERAEFAKE LGSVIIMIDL VIGYTAIQSM AKWARRNDMI LHLHRAGHST
310 320 330 340 350
YTRQKIHGVS FRVIAKWMRL AGVDHIHAGT VVGKLEGDPN TTRGYYDICR
360 370 380 390 400
EDYNPQQLEH GIFFDQHWAS LNKLMPVASG GIHAGQMHQL LALLGEDVVL
410 420 430 440 450
QFGGGTIGHP MGIAAGATAN RVALEAMIFA RNCGRDTLAE GQTILEDAAR
460 470 480
GCTPLRQALD VWKDVSFDYT STDSPDFIPT ATPA
Length:484
Mass (Da):53,508
Last modified:March 3, 2009 - v1
Checksum:i07A90129067ABB20
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001280 Genomic DNA. Translation: ACK50164.1.
RefSeqiWP_012590234.1. NC_011666.1.

Genome annotation databases

EnsemblBacteriaiACK50164; ACK50164; Msil_1195.
KEGGimsl:Msil_1195.
PATRICi22597875. VBIMetSil55537_1316.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001280 Genomic DNA. Translation: ACK50164.1.
RefSeqiWP_012590234.1. NC_011666.1.

3D structure databases

ProteinModelPortaliB8EPF9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi395965.Msil_1195.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACK50164; ACK50164; Msil_1195.
KEGGimsl:Msil_1195.
PATRICi22597875. VBIMetSil55537_1316.

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 nameiB8EPF9_METSB
AccessioniPrimary (citable) accession number: B8EPF9
Entry historyi
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
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.