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Q1LN92

- RBL_RALME

UniProt

Q1LN92 - RBL_RALME

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839)
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

Mg2+UniRule annotationNote: Binds 1 Mg(2+) ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161Substrate; in homodimeric partnerUniRule annotation
Binding sitei166 – 1661SubstrateUniRule annotation
Active sitei168 – 1681Proton acceptorUniRule annotation
Binding sitei170 – 1701SubstrateUniRule annotation
Metal bindingi194 – 1941Magnesium; via carbamate groupUniRule annotation
Metal bindingi196 – 1961MagnesiumUniRule annotation
Metal bindingi197 – 1971MagnesiumUniRule annotation
Active sitei287 – 2871Proton acceptorUniRule annotation
Binding sitei288 – 2881SubstrateUniRule annotation
Binding sitei320 – 3201SubstrateUniRule annotation
Sitei327 – 3271Transition state stabilizerUniRule annotation
Binding sitei372 – 3721SubstrateUniRule 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

BioCyciCMET266264:GJ5G-1564-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:Rmet_1501
OrganismiRalstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839)
Taxonomic identifieri266264 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000002429: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Ribulose bisphosphate carboxylase large chainPRO_0000251455Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941N6-carboxylysineUniRule annotation

Proteomic databases

PRIDEiQ1LN92.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi266264.Rmet_1501.

Structurei

3D structure databases

ProteinModelPortaliQ1LN92.
SMRiQ1LN92. Positions 16-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiMETWKEV.
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.

Q1LN92-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAKTYNAGV KEYRQTYWTP EYTPKDTDLL ACFKVTPQPG VAREEVAAAV
60 70 80 90 100
AAESSTGTWT TVWTDLLTDL DYYKGRAYRI EDVPGDDTCF YAFVAYPIDL
110 120 130 140 150
FEEGSIVNVL TSLVGNVFGF KALRALRLED VRFPIAYVMT CGGPPHGIQV
160 170 180 190 200
ERDIMNKYGR PLLGCTIKPK LGLSAKNYGR AVYECLRGGL DFTKDDENVN
210 220 230 240 250
SQPFMRWKQR FDFVQEATEK AQRETGERKG HYLNVTAPTP EEMYKRAEYA
260 270 280 290 300
KEIGAPIIMH DYLTGGFCAN TGLANWCRDN GMLLHIHRAM HAVLDRNPHH
310 320 330 340 350
GIHFRVLTKC LRLSGGDHLH SGTVVGKLEG DRDATLGWID IMRDDFIKED
360 370 380 390 400
RSRGIMFDQD FGSMPGVMPV ASGGIHVWHM PALVTIFGDD SVLQFGGGTL
410 420 430 440 450
GHPWGNAAGA AANRVALEAC VEARNKGVAV EKEGKSILTE AATHSPELKI
460 470
AMETWKEIKF EFDTVDKLDV AHK
Length:473
Mass (Da):52,608
Last modified:May 30, 2006 - v1
Checksum:i6CBA7F7722693534
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000352 Genomic DNA. Translation: ABF08384.1.
RefSeqiWP_011516247.1. NC_007973.1.
YP_583653.1. NC_007973.1.

Genome annotation databases

EnsemblBacteriaiABF08384; ABF08384; Rmet_1501.
GeneIDi4038304.
KEGGirme:Rmet_1501.
PATRICi20287614. VBIRalMet4734_1909.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000352 Genomic DNA. Translation: ABF08384.1 .
RefSeqi WP_011516247.1. NC_007973.1.
YP_583653.1. NC_007973.1.

3D structure databases

ProteinModelPortali Q1LN92.
SMRi Q1LN92. Positions 16-460.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 266264.Rmet_1501.

Proteomic databases

PRIDEi Q1LN92.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABF08384 ; ABF08384 ; Rmet_1501 .
GeneIDi 4038304.
KEGGi rme:Rmet_1501.
PATRICi 20287614. VBIRalMet4734_1909.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci CMET266264:GJ5G-1564-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: CH34 / ATCC 43123 / DSM 2839.

Entry informationi

Entry nameiRBL_RALME
AccessioniPrimary (citable) accession number: Q1LN92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: May 30, 2006
Last modified: November 26, 2014
This is version 59 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