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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

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

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 sitei139Substrate; in homodimeric partnerUniRule annotation1
Binding sitei189SubstrateUniRule annotation1
Active sitei191Proton acceptorUniRule annotation1
Binding sitei193SubstrateUniRule annotation1
Metal bindingi217Magnesium; via carbamate groupUniRule annotation1
Metal bindingi219MagnesiumUniRule annotation1
Metal bindingi220MagnesiumUniRule annotation1
Active sitei309Proton acceptorUniRule annotation1
Binding sitei310SubstrateUniRule annotation1
Binding sitei342SubstrateUniRule annotation1
Sitei349Transition state stabilizerUniRule annotation1
Binding sitei394SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyaseUniRule annotationImported, MonooxygenaseUniRule annotation, Oxidoreductase
Biological processCalvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation
LigandMagnesiumUniRule 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:BC1003_5439Imported
OrganismiBurkholderia sp. (strain CCGE1003)Imported
Taxonomic identifieri640512 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia
Proteomesi
  • UP000001550 Componenti: Chromosome 2

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei217N6-carboxylysineUniRule annotation1

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi640512.BC1003_5439.

Structurei

3D structure databases

ProteinModelPortaliE1TEV1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini37 – 160RuBisCO_large_NInterPro annotationAdd BLAST124
Domaini170 – 477RuBisCO_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.
OMAiHRAMHAA.
OrthoDBiPOG091H14UZ.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1. 1 hit.
InterProiView protein in InterPro
IPR033966. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR036376. RuBisCO_lsu_C_sf.
IPR017443. RuBisCO_lsu_fd_N.
IPR036422. RuBisCO_lsu_N_sf.
IPR020888. RuBisCO_lsuI.
PfamiView protein in Pfam
PF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
SFLDiSFLDS00014. RuBisCO. 1 hit.
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEiView protein in PROSITE
PS00157. RUBISCO_LARGE. 1 hit.

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.

Genome annotation databases

EnsemblBacteriaiADN61357; ADN61357; BC1003_5439.
KEGGibgf:BC1003_5439.

Similar proteinsi

Entry informationi

Entry nameiE1TEV1_BURSG
AccessioniPrimary (citable) accession number: E1TEV1
Entry historyiIntegrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: November 30, 2010
Last modified: October 25, 2017
This is version 51 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteomeImported