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D5WEH0

- D5WEH0_BURSC

UniProt

D5WEH0 - D5WEH0_BURSC

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Protein

Ribulose bisphosphate carboxylase large chain

Gene
cbbL, BC1002_3207
Organism
Burkholderia sp. (strain CCGE1002)
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 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

BioCyciBSP640511:GJ7J-3277-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:BC1002_3207Imported
OrganismiBurkholderia sp. (strain CCGE1002)Imported
Taxonomic identifieri640511 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia
ProteomesiUP000002190: 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

ProteinModelPortaliD5WEH0.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000230831.
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.

D5WEH0-1 [UniParc]FASTAAdd to Basket

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MNDFSQPPIQ PEHQARDPHN PRERYAAGVM KYREMGYWQP DYEPKETDVI    50
ALFRITPQPG VEPEEAAAAV AGESSTATWT VVWTDRLTAC DMYRAKAYRV 100
EPVPASRADE PQYFAYIAYE LDLFEEGSVA NLTASIIGNV FGFKPLKALR 150
LEDMRIPVAY LKTFQGPPTG IVVERERLDK YGRPLLGATV KPKLGLSGKN 200
YGRVVYEGLR GGLDFLKDDE NINSQAFMHW RDRFLFAMEA VSRAQAETGE 250
VKGHYMNVTA GTMEDMYERA EFAKELGSCI VMIDLVIGWT AIQSMSRWAR 300
KHDMILHLHR AGHGTYTRQR NHGISFRVIA KWLRMAGVDH AHAGTAVGKL 350
EGDPLSVQGY YNVCRDAHNA VDLSRGLFFD QPWAGLRKVM PVASGGIHAG 400
QMHQLLDLFG DDAILQFGGG TIGHPAGIQA GATANRVALE AMVKARNEGR 450
DILREGPDVL EAAARWCTPL KQALDTWRDV TFNYASTDTP DFAATPTAA 499
Length:499
Mass (Da):55,451
Last modified:July 13, 2010 - v1
Checksum:iA63235F91877AC2E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002014 Genomic DNA. Translation: ADG17252.1.
RefSeqiWP_013091055.1. NC_014118.1.
YP_003606763.1. NC_014118.1.

Genome annotation databases

EnsemblBacteriaiADG17252; ADG17252; BC1002_3207.
GeneIDi9112510.
KEGGibge:BC1002_3207.
PATRICi37215466. VBIBurSp41388_3289.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002014 Genomic DNA. Translation: ADG17252.1 .
RefSeqi WP_013091055.1. NC_014118.1.
YP_003606763.1. NC_014118.1.

3D structure databases

ProteinModelPortali D5WEH0.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADG17252 ; ADG17252 ; BC1002_3207 .
GeneIDi 9112510.
KEGGi bge:BC1002_3207.
PATRICi 37215466. VBIBurSp41388_3289.

Phylogenomic databases

HOGENOMi HOG000230831.
KOi K01601.

Enzyme and pathway databases

BioCyci BSP640511:GJ7J-3277-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. "Complete sequence of chromosome 2 of Burkholderia sp. CCGE1002."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Martinez-Romero E., Hernandez M.A.R., Tiedje J.M., Woyke T.
    Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CCGE1002.

Entry informationi

Entry nameiD5WEH0_BURSC
AccessioniPrimary (citable) accession number: D5WEH0
Entry historyi
Integrated into UniProtKB/TrEMBL: July 13, 2010
Last sequence update: July 13, 2010
Last modified: September 3, 2014
This is version 25 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

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