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Protein

Ribulose bisphosphate carboxylase large chain 2

Gene

cbbL2

Organism
Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182)
Status
Reviewed-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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161Substrate; in homodimeric partnerUniRule annotation
Binding sitei166 – 1661SubstrateUniRule annotation
Active sitei168 – 1681Proton acceptorUniRule annotation
Binding sitei170 – 1701SubstrateUniRule annotation
Metal bindingi194 – 1941Magnesium; via carbamate groupUniRule annotation
Metal bindingi196 – 1961MagnesiumUniRule annotation
Metal bindingi197 – 1971MagnesiumUniRule annotation
Active sitei287 – 2871Proton acceptorUniRule annotation
Binding sitei288 – 2881SubstrateUniRule annotation
Binding sitei320 – 3201SubstrateUniRule annotation
Sitei327 – 3271Transition state stabilizerUniRule annotation
Binding sitei372 – 3721SubstrateUniRule annotation

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. monooxygenase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciBSP288000:GJBR-2514-MONOMER.

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
Ordered Locus Names:BBta_2641
OrganismiBradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182)
Taxonomic identifieri288000 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
ProteomesiUP000000246: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 479479Ribulose bisphosphate carboxylase large chain 2PRO_0000299959Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi288000.BBta_2641.

Structurei

3D structure databases

ProteinModelPortaliA5EF40.
SMRiA5EF40. Positions 16-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiMSIFKGV.
OrthoDBiEOG6ZKXMS.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1.
InterProiIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[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.

A5EF40-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEKSYQAGV KEYRKTYWTP DYVPLDTDLL AVFKIVAQAG VPREEAAAAV
60 70 80 90 100
AAESSTGTWT TVWTDLLTDL DYYKGRAYRI EPVPGDDNAF YAFIAYPIDL
110 120 130 140 150
FEEGSVVNVL TSLVGNVFGF KAVRSLRLED IRFPLAYVKT CGGPPNGIQL
160 170 180 190 200
ERDRLNKYGR PLLGCTIKPK LGLSAKNYGR AVYECLRGGL DFTKDDENIN
210 220 230 240 250
SQPFMRWQHR FEFVMEAVHK ATSETGERKG HYLNVTAPTP EEMYKRAEFA
260 270 280 290 300
KSLGAPIIMH DFLTAGFTAN TGLANWCREN GMLLHIHRAM HAVLDRNPMH
310 320 330 340 350
GIHFRVLTKC LRLSGGDHLH SGTVVGKLEG DREATIGWVD LMREPFVPEN
360 370 380 390 400
RARGIFFDQD WGAMPGVMPV ASGGIHVWHM PALTAIFGDD ACFQFGGGTL
410 420 430 440 450
GHPWGNAAGA HANRVALEAC VEARNQGRPV EREGREILTE AAQHSPELKI
460 470
AMETWKEIKF EFDVVDKLDT GPMLRVVNA
Length:479
Mass (Da):53,320
Last modified:June 12, 2007 - v1
Checksum:i6F76C64885B6CDA7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000494 Genomic DNA. Translation: ABQ34784.1.
RefSeqiWP_012042812.1. NC_009485.1.
YP_001238690.1. NC_009485.1.

Genome annotation databases

EnsemblBacteriaiABQ34784; ABQ34784; BBta_2641.
GeneIDi5153528.
KEGGibbt:BBta_2641.
PATRICi21206117. VBIBraSp29847_2741.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000494 Genomic DNA. Translation: ABQ34784.1.
RefSeqiWP_012042812.1. NC_009485.1.
YP_001238690.1. NC_009485.1.

3D structure databases

ProteinModelPortaliA5EF40.
SMRiA5EF40. Positions 16-460.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi288000.BBta_2641.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABQ34784; ABQ34784; BBta_2641.
GeneIDi5153528.
KEGGibbt:BBta_2641.
PATRICi21206117. VBIBraSp29847_2741.

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiMSIFKGV.
OrthoDBiEOG6ZKXMS.

Enzyme and pathway databases

BioCyciBSP288000:GJBR-2514-MONOMER.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1.
InterProiIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BTAi1 / ATCC BAA-1182.

Entry informationi

Entry nameiRBL1B_BRASB
AccessioniPrimary (citable) accession number: A5EF40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 12, 2007
Last modified: January 7, 2015
This is version 47 of the entry and version 1 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

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.