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E1TEV1

- E1TEV1_BURSG

UniProt

E1TEV1 - E1TEV1_BURSG

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, BC1003_5439
Organism
Burkholderia sp. (strain CCGE1003)
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
Complete GO annotation...

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-carboxylysine By similarityUniRule annotation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliE1TEV1.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.

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

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MNDFSQPAIE SLHKPRNAGN PRERYAAGVM KYREMGYWQP DYTPKDTDVI    50
ALFRITPQPG VEPEEAAAAV AGESSTATWT VVWTDRLTAC DMYRAKAYRV 100
DPVPASSASE PQYFAYIAYE LDLFEEGSVA NLTASIIGNV FGFKPLKALR 150
LEDMRIPVAY LKTFQGPPTG IVVERERLDK YGRPLLGATV KPKLGLSGKN 200
YGRVVYEGLR GGLDFLKDDE NINSQAFMHW RDRFLFSMEA VNRAQAETGE 250
VKGHYLNVTA GTMEDMYERA EFARELGSCI VMIDLVVGWT AIQSMGRWAR 300
KNDMILHLHR AGHSTYTRQR NHGISFRVIA KWLRMAGVDH AHAGTAVGKL 350
EGDPLTVQGF YNVCREARNE VDLSRGIFFD QPWAGLRKVM PVASGGIHAG 400
QMHQLLDLFG DDAILQFGGG TIGHPGGIQA GAVANRVALE AMVKARNEGR 450
DIREEGPDIL EAAARWCGPL KQALDTWRDV TFNYASTDSP DFAATPTAA 499
Length:499
Mass (Da):55,227
Last modified:November 30, 2010 - v1
Checksum:i4C25DD925848040E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CP002218 Genomic DNA. Translation: ADN61357.1 .
RefSeqi WP_013342882.1. NC_014540.1.
YP_003910648.1. NC_014540.1.

3D structure databases

ProteinModelPortali E1TEV1.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADN61357 ; ADN61357 ; BC1003_5439 .
GeneIDi 9764153.
KEGGi bgf:BC1003_5439.
PATRICi 42217762. VBIBurSp98639_5838.

Phylogenomic databases

HOGENOMi HOG000230831.
KOi K01601.
OMAi FTQDWAS.

Enzyme and pathway databases

BioCyci BSP640512:GBXV-5514-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: CCGE1003.

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: September 3, 2014
This is version 27 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