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B2JX50

- RBL_BURP8

UniProt

B2JX50 - RBL_BURP8

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, Bphy_6497
Organism
Burkholderia phymatum (strain DSM 17167 / STM815)
Status
Reviewed - 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 By similarity.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

Binds 1 magnesium ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei141 – 1411Substrate; in homodimeric partner By similarity
Binding sitei191 – 1911Substrate By similarity
Active sitei193 – 1931Proton acceptor By similarity
Binding sitei195 – 1951Substrate By similarity
Metal bindingi219 – 2191Magnesium; via carbamate group By similarity
Metal bindingi221 – 2211Magnesium By similarity
Metal bindingi222 – 2221Magnesium By similarity
Active sitei311 – 3111Proton acceptor By similarity
Binding sitei312 – 3121Substrate By similarity
Binding sitei344 – 3441Substrate By similarity
Sitei351 – 3511Transition state stabilizer By similarity
Binding sitei396 – 3961Substrate By similarity

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

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciBPHY391038:GI4Z-6575-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain (EC:4.1.1.39)
Short name:
RuBisCO large subunit
Gene namesi
Name:cbbL
Ordered Locus Names:Bphy_6497
Encoded oniPlasmid pBPHY010 Publication
OrganismiBurkholderia phymatum (strain DSM 17167 / STM815)
Taxonomic identifieri391038 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia
ProteomesiUP000001192: Plasmid pBPHY01

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 501501Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_0000355748Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei219 – 2191N6-carboxylysine By similarity

Proteomic databases

PRIDEiB2JX50.

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains By similarity.

Protein-protein interaction databases

STRINGi391038.Bphy_6497.

Structurei

3D structure databases

ProteinModelPortaliB2JX50.
SMRiB2JX50. Positions 22-495.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiCTPLKQA.
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.

B2JX50-1 [UniParc]FASTAAdd to Basket

« Hide

MNDFSKEAVK PADSATAAAK AEKRSRYAAG VMKYREMGYW QPDYTPKDTD    50
VIALFRITPQ PGVEPEEAAA AVAGESSTAT WTVVWTDRLT ACDMYRAKAF 100
RVEPVPNPAE GEPQYFAFIA YELDLFEEGS VANLTASIIG NVFGFKPLKA 150
LRLEDMRIPV AYLKTFQGPP TGIVVERERL DKYGRPLLGA TVKPKLGLSG 200
KNYGRVVYEG LKGGLDFLKD DENINSQPFM HWRDRYLFAM EAVHRAQAET 250
GEVKGHYLNV TAGTMEDMYE RAEFAKELGS CIVMIDLVIG WTAITSMGRW 300
ARKNDMILHL HRAGHGTYTR QRNHGISFRV IAKWLRMAGV DHAHAGTAVG 350
KLDGDPLSVQ GYYNVLRESH NSVDLTRGIF FDQHWAGLRK VMPVASGGIH 400
AGQMHQLLDL FGDDAILQFG GGTIGHPSGI QAGATANRVA LETMVKARNE 450
GRDIANEGSD LLEAAARHCT PLKQALDTWG DVTFNYTPTD SPDFAVTPSV 500
A 501
Length:501
Mass (Da):55,176
Last modified:June 10, 2008 - v1
Checksum:iE8238E2EFE685A2D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001045 Genomic DNA. Translation: ACC75527.1.
RefSeqiYP_001862573.1. NC_010625.1.

Genome annotation databases

EnsemblBacteriaiACC75527; ACC75527; Bphy_6497.
GeneIDi6248036.
KEGGibph:Bphy_6497.
PATRICi19199896. VBIBurPhy25146_6827.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001045 Genomic DNA. Translation: ACC75527.1 .
RefSeqi YP_001862573.1. NC_010625.1.

3D structure databases

ProteinModelPortali B2JX50.
SMRi B2JX50. Positions 22-495.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 391038.Bphy_6497.

Proteomic databases

PRIDEi B2JX50.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACC75527 ; ACC75527 ; Bphy_6497 .
GeneIDi 6248036.
KEGGi bph:Bphy_6497.
PATRICi 19199896. VBIBurPhy25146_6827.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OMAi CTPLKQA.
OrthoDBi EOG6ZKXMS.

Enzyme and pathway databases

BioCyci BPHY391038:GI4Z-6575-MONOMER.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01338. RuBisCO_L_type1.
InterProi IPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view ]
Pfami PF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view ]
SUPFAMi SSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 17167 / STM815.

Entry informationi

Entry nameiRBL_BURP8
AccessioniPrimary (citable) accession number: B2JX50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: June 10, 2008
Last modified: May 14, 2014
This is version 37 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" By similarity.

Keywords - Technical termi

Complete proteome, Plasmid

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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