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K0DP73

- K0DP73_9BURK

UniProt

K0DP73 - K0DP73_9BURK

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Protein

Ribulose bisphosphate carboxylase large chain

Gene
cbbL, BUPH_00547
Organism
Burkholderia phenoliruptrix BR3459a
Status
Unreviewed - 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 sitei139 – 1391Substrate; in homodimeric partner By similarityUniRule annotation
Binding sitei189 – 1891Substrate By similarityUniRule annotation
Active sitei191 – 1911Proton acceptor By similarityUniRule annotation
Binding sitei193 – 1931Substrate By similarityUniRule annotation
Metal bindingi217 – 2171Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi219 – 2191Magnesium By similarityUniRule annotation
Metal bindingi220 – 2201Magnesium By similarityUniRule annotation
Active sitei309 – 3091Proton acceptor By similarityUniRule annotation
Binding sitei310 – 3101Substrate By similarityUniRule annotation
Binding sitei342 – 3421Substrate By similarityUniRule annotation
Sitei349 – 3491Transition state stabilizer By similarityUniRule annotation
Binding sitei394 – 3941Substrate By similarityUniRule 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 annotation, MonooxygenaseUniRule annotation, Oxidoreductase

Keywords - Biological processi

Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation

Keywords - Ligandi

MagnesiumUniRule 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
ORF Names:BUPH_00547Imported
OrganismiBurkholderia phenoliruptrix BR3459aImported
Taxonomic identifieri1229205 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia
ProteomesiUP000010105: Chromosome 2

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei217 – 2171N6-carboxylysine By similarityUniRule annotation

Interactioni

Subunit structurei

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

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK01601.

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.

K0DP73-1 [UniParc]FASTAAdd to Basket

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MNDFSQPAIE SLHKPRNAGD PRERYAAGVM KYREMGYWQP DYTPKDTDVI    50
ALFRITPQPG VEPEEAAAAV AGESSTATWT VVWTDRLTAC DMYRAKAYRV 100
DPVPASNAGE PQYFAYIAYE LDLFEEGSVA NLTASIIGNV FGFKPLKALR 150
LEDMRIPVAY LKTFQGPPTG IVVERERLDK YGRPLLGATV KPKLGLSGKN 200
YGRVVYEGLR GGLDFLKDDE NINSQAFMHW RDRFLFSMEA VNRAQAETGE 250
VKGHYLNVTA GTMEDMYERA EFAKELGSCI VMIDLVIGWT AIQSMGRWAR 300
RNDMILHLHR AGHSTYTRQR NHGISFRVIA KWLRMAGVDH AHAGTAVGKL 350
EGDPLTVQGF YNVCREARNE VDLSRGLFFD QPWAGLRKVM PVASGGIHAG 400
QMHQLLELFG DDAILQFGGG TIGHPGGIQA GAVANRVALE AMVKARNEGR 450
DIRHEGSDIL EAAARWCGPL KQALDTWRDV TFNYASTDSP DFAATPTAA 499
Length:499
Mass (Da):55,251
Last modified:November 28, 2012 - v1
Checksum:i6991FFC279364257
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003864 Genomic DNA. Translation: AFT88011.1.
RefSeqiYP_006792994.1. NC_018672.1.

Genome annotation databases

EnsemblBacteriaiAFT88011; AFT88011; BUPH_00547.
GeneIDi13735304.
KEGGibpx:BUPH_00547.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003864 Genomic DNA. Translation: AFT88011.1 .
RefSeqi YP_006792994.1. NC_018672.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AFT88011 ; AFT88011 ; BUPH_00547 .
GeneIDi 13735304.
KEGGi bpx:BUPH_00547.

Phylogenomic databases

KOi K01601.

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: BR3459aImported.

Entry informationi

Entry nameiK0DP73_9BURK
AccessioniPrimary (citable) accession number: K0DP73
Entry historyi
Integrated into UniProtKB/TrEMBL: November 28, 2012
Last sequence update: November 28, 2012
Last modified: September 3, 2014
This is version 10 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" By similarity.UniRule annotation

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

Similar proteinsi