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Protein

Ribulose bisphosphate carboxylase large chain 2

Gene

cbbL2

Organism
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D) (Chromatium vinosum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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.

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 sitei116Substrate; in homodimeric partnerUniRule annotation1
Binding sitei166SubstrateUniRule annotation1
Active sitei168Proton acceptorUniRule annotation1
Binding sitei170SubstrateUniRule annotation1
Metal bindingi194Magnesium; via carbamate groupUniRule annotation1
Metal bindingi196MagnesiumUniRule annotation1
Metal bindingi197MagnesiumUniRule annotation1
Active sitei287Proton acceptorUniRule annotation1
Binding sitei288SubstrateUniRule annotation1
Binding sitei320SubstrateUniRule annotation1
Sitei327Transition state stabilizerUniRule annotation1
Binding sitei372SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain 2UniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunit 2UniRule annotation
Gene namesi
Name:cbbL2UniRule annotation
Synonyms:rbcLUniRule annotation
Ordered Locus Names:Alvin_2750
OrganismiAllochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D) (Chromatium vinosum)
Taxonomic identifieri572477 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeAllochromatium
Proteomesi
  • UP000001441 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000626222 – 471Ribulose bisphosphate carboxylase large chain 2Add BLAST470

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei194N6-carboxylysineUniRule annotation1
Disulfide bondi240Interchain; in linked formUniRule annotation

Post-translational modificationi

The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.UniRule annotation

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.UniRule annotation

Protein-protein interaction databases

STRINGi572477.Alvin_2750.

Structurei

3D structure databases

ProteinModelPortaliP22859.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.
HOGENOMiHOG000230831.
KOiK01601.
OMAiAVAMETW.
OrthoDBiPOG091H14UZ.

Family and domain databases

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22859-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTKTYDAGV KDYALTYWTP DYVPLDSDLL ACFKVTPQAK VSREEAAAAV
60 70 80 90 100
AAESSTGTWT TVWSDLLTDL DYYKGRAYRI EDVPGDKESF YAFIAYPLDL
110 120 130 140 150
FEEGSIVNVL TSLVGNVFGF KAVRALRLED IRFPLHYVKT CGGPPNGIQV
160 170 180 190 200
ERDRMDKYGR PFLGATVKPK LGLSAKNYGR AVYEMLRGGL DFTKDDENVN
210 220 230 240 250
SQPFMRWQNR FEFVSEAVRK AQEETGERKG HYLNVTAPTC EEMFKRAEFA
260 270 280 290 300
KECGAPIIMH DFLTGGFTAN TSLANWCRDN GMLLHIHRAM HAVIDRNPKH
310 320 330 340 350
GIHFRVLAKC LRLSGGDHLH TGTVVGKLEG DRQSTLGFVD QLRESFIPED
360 370 380 390 400
RSRGLFFDQD WGGMPGVMAV ASGGIHVWHI PALVTIFGDD SVLQFGGGTQ
410 420 430 440 450
GHPWGNAAGA AANRVATEAC VKARNEGVEI EKHAREVLSD AARHSPELAV
460 470
AMETWKEIKF EFDVVDKLDA A
Length:471
Mass (Da):52,284
Last modified:June 15, 2010 - v4
Checksum:i08A26940B6458D97
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti145P → R in BAA14229 (PubMed:1899846).Curated1
Sequence conflicti222Q → R in BAA14229 (PubMed:1899846).Curated1
Sequence conflicti297N → H in BAA14229 (PubMed:1899846).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90204 Genomic DNA. Translation: BAA14229.1.
CP001896 Genomic DNA. Translation: ADC63659.1.
PIRiJQ0586. RKKRL2.
RefSeqiWP_012971927.1. NC_013851.1.

Genome annotation databases

EnsemblBacteriaiADC63659; ADC63659; Alvin_2750.
KEGGialv:Alvin_2750.
PATRICi31925280. VBIAllVin64954_2712.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90204 Genomic DNA. Translation: BAA14229.1.
CP001896 Genomic DNA. Translation: ADC63659.1.
PIRiJQ0586. RKKRL2.
RefSeqiWP_012971927.1. NC_013851.1.

3D structure databases

ProteinModelPortaliP22859.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi572477.Alvin_2750.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADC63659; ADC63659; Alvin_2750.
KEGGialv:Alvin_2750.
PATRICi31925280. VBIAllVin64954_2712.

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.
HOGENOMiHOG000230831.
KOiK01601.
OMAiAVAMETW.
OrthoDBiPOG091H14UZ.

Family and domain databases

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 nameiRBL1B_ALLVD
AccessioniPrimary (citable) accession number: P22859
Secondary accession number(s): D3RQ48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: June 15, 2010
Last modified: November 30, 2016
This is version 108 of the entry and version 4 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

Caution

In C.vinosum two similar set of genes code for RuBisCO large and small chains: the RbcL-RbcS and the RbcA-RbcB sets. Under standard photoautotrophic culture conditions only the latter set seems active, the former probably being cryptic.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.