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Q13QV1

- RBL_BURXL

UniProt

Q13QV1 - RBL_BURXL

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Burkholderia xenovorans (strain LB400)
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.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.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

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciBXEN266265:GJII-5191-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:Bxeno_B0570
ORF Names:Bxe_B2453
OrganismiBurkholderia xenovorans (strain LB400)
Taxonomic identifieri266265 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia
ProteomesiUP000001817: Chromosome 2

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499Ribulose bisphosphate carboxylase large chainPRO_0000251445Add
BLAST

Amino acid modifications

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

Proteomic databases

PRIDEiQ13QV1.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi266265.Bxe_B2453.

Structurei

3D structure databases

ProteinModelPortaliQ13QV1.
SMRiQ13QV1. Positions 34-480.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

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.

Q13QV1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNDFSQPVID SIHKPRDAAN PRERYAAGVM KYREMGYWQP DYAPKDTDVI
60 70 80 90 100
ALFRITPQPG VDPEEAAAAV AGESSTATWT VVWTDRLTAC DIYRAKAYRV
110 120 130 140 150
DPVPASNAAE PQYFAYIAYE LDLFEEGSVA NLTASIIGNV FGFKPLKALR
160 170 180 190 200
LEDMRIPVAY LKTFQGPPTG IVVERERLDK YGRPLLGATV KPKLGLSGKN
210 220 230 240 250
YGRVVYEGLR GGLDFLKDDE NINSQAFMHW RDRFLFAMEA VNRAQAETGE
260 270 280 290 300
VKGHYLNVTA GTMEDMYERA EFAKELGSCI VMIDLVIGWT AIQSMARWAR
310 320 330 340 350
RNDMILHLHR AGHSTYTRQR NHGISFRVIA KWLRMAGVDH AHAGTAVGKL
360 370 380 390 400
EGDPLSVQGY YNVCRESHNE VDLSRGIFFD QPWAGLRKVM PVASGGIHAG
410 420 430 440 450
QMHQLLDLFG DDAILQFGGG TIGHPAGIQA GAVANRVALE AMVKARNEGR
460 470 480 490
DIVHEGPDIL EAAARWCTPL KQALDTWRDV TFNYASTDTP DFAATPTAA
Length:499
Mass (Da):55,239
Last modified:August 22, 2006 - v1
Checksum:i5F82AF41666CDB74
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000271 Genomic DNA. Translation: ABE33538.1.
RefSeqiYP_552888.1. NC_007952.1.

Genome annotation databases

EnsemblBacteriaiABE33538; ABE33538; Bxe_B2453.
GeneIDi4007051.
KEGGibxe:Bxe_B2453.
PATRICi19335974. VBIBurXen52548_5256.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000271 Genomic DNA. Translation: ABE33538.1 .
RefSeqi YP_552888.1. NC_007952.1.

3D structure databases

ProteinModelPortali Q13QV1.
SMRi Q13QV1. Positions 34-480.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 266265.Bxe_B2453.

Proteomic databases

PRIDEi Q13QV1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABE33538 ; ABE33538 ; Bxe_B2453 .
GeneIDi 4007051.
KEGGi bxe:Bxe_B2453.
PATRICi 19335974. VBIBurXen52548_5256.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci BXEN266265:GJII-5191-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: LB400.

Entry informationi

Entry nameiRBL_BURXL
AccessioniPrimary (citable) accession number: Q13QV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: August 22, 2006
Last modified: October 29, 2014
This is version 56 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".UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3