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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Burkholderia sp. (strain CCGE1003)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei139 – 1391Substrate; in homodimeric partnerUniRule annotation
Binding sitei189 – 1891SubstrateUniRule annotation
Active sitei191 – 1911Proton acceptorUniRule annotation
Binding sitei193 – 1931SubstrateUniRule annotation
Metal bindingi217 – 2171Magnesium; via carbamate groupUniRule annotation
Metal bindingi219 – 2191MagnesiumUniRule annotation
Metal bindingi220 – 2201MagnesiumUniRule annotation
Active sitei309 – 3091Proton acceptorUniRule annotation
Binding sitei310 – 3101SubstrateUniRule annotation
Binding sitei342 – 3421SubstrateUniRule annotation
Sitei349 – 3491Transition state stabilizerUniRule annotation
Binding sitei394 – 3941SubstrateUniRule 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

LyaseUniRule annotationImported, MonooxygenaseUniRule annotation, Oxidoreductase

Keywords - Biological processi

Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciBSP640512:GBXV-5514-MONOMER.

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:BC1003_5439Imported
OrganismiBurkholderia sp. (strain CCGE1003)Imported
Taxonomic identifieri640512 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia
ProteomesiUP000001550: Chromosome 2

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei217 – 2171N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliE1TEV1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000230831.
KOiK01601.
OMAiHAAFTRN.

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.

E1TEV1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDFSQPAIE SLHKPRNAGN PRERYAAGVM KYREMGYWQP DYTPKDTDVI
60 70 80 90 100
ALFRITPQPG VEPEEAAAAV AGESSTATWT VVWTDRLTAC DMYRAKAYRV
110 120 130 140 150
DPVPASSASE PQYFAYIAYE LDLFEEGSVA NLTASIIGNV FGFKPLKALR
160 170 180 190 200
LEDMRIPVAY LKTFQGPPTG IVVERERLDK YGRPLLGATV KPKLGLSGKN
210 220 230 240 250
YGRVVYEGLR GGLDFLKDDE NINSQAFMHW RDRFLFSMEA VNRAQAETGE
260 270 280 290 300
VKGHYLNVTA GTMEDMYERA EFARELGSCI VMIDLVVGWT AIQSMGRWAR
310 320 330 340 350
KNDMILHLHR AGHSTYTRQR NHGISFRVIA KWLRMAGVDH AHAGTAVGKL
360 370 380 390 400
EGDPLTVQGF YNVCREARNE VDLSRGIFFD QPWAGLRKVM PVASGGIHAG
410 420 430 440 450
QMHQLLDLFG DDAILQFGGG TIGHPGGIQA GAVANRVALE AMVKARNEGR
460 470 480 490
DIREEGPDIL EAAARWCGPL KQALDTWRDV TFNYASTDSP DFAATPTAA
Length:499
Mass (Da):55,227
Last modified:November 30, 2010 - v1
Checksum:i4C25DD925848040E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002218 Genomic DNA. Translation: ADN61357.1.
RefSeqiWP_013342882.1. NC_014540.1.
YP_003910648.1. NC_014540.1.

Genome annotation databases

EnsemblBacteriaiADN61357; ADN61357; BC1003_5439.
GeneIDi9764153.
KEGGibgf:BC1003_5439.
PATRICi42217762. VBIBurSp98639_5838.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002218 Genomic DNA. Translation: ADN61357.1.
RefSeqiWP_013342882.1. NC_014540.1.
YP_003910648.1. NC_014540.1.

3D structure databases

ProteinModelPortaliE1TEV1.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADN61357; ADN61357; BC1003_5439.
GeneIDi9764153.
KEGGibgf:BC1003_5439.
PATRICi42217762. VBIBurSp98639_5838.

Phylogenomic databases

HOGENOMiHOG000230831.
KOiK01601.
OMAiHAAFTRN.

Enzyme and pathway databases

BioCyciBSP640512:GBXV-5514-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: CCGE1003Imported.

Entry informationi

Entry nameiE1TEV1_BURSG
AccessioniPrimary (citable) accession number: E1TEV1
Entry historyi
Integrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: November 30, 2010
Last modified: January 7, 2015
This is version 31 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 proteomeImported

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.