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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Oligotropha carboxidovorans (strain OM4)
Status
Unreviewed-Annotation score: 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 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei125 – 1251Substrate; in homodimeric partnerUniRule annotation
Binding sitei175 – 1751SubstrateUniRule annotation
Active sitei177 – 1771Proton acceptorUniRule annotation
Binding sitei179 – 1791SubstrateUniRule annotation
Metal bindingi203 – 2031Magnesium; via carbamate groupUniRule annotation
Metal bindingi205 – 2051MagnesiumUniRule annotation
Metal bindingi206 – 2061MagnesiumUniRule annotation
Active sitei295 – 2951Proton acceptorUniRule annotation
Binding sitei296 – 2961SubstrateUniRule annotation
Binding sitei328 – 3281SubstrateUniRule annotation
Sitei335 – 3351Transition state stabilizerUniRule annotation
Binding sitei380 – 3801SubstrateUniRule 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

BioCyciOCAR1031710:GLI1-3562-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 annotationImported
Ordered Locus Names:OCA4_pHCG3B00470Imported
Encoded oniPlasmid pHCG3BImported
OrganismiOligotropha carboxidovorans (strain OM4)Imported
Taxonomic identifieri1031710 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeOligotropha
ProteomesiUP000000487: Plasmid pHCG3B

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliF8BQM8.
SMRiF8BQM8. Positions 13-479.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

KOiK01601.
OMAiHAAFTRN.

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.

F8BQM8-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MNDQSMTIRG KDRYKSGVMA YKKMGYWEPD YVPKDTDVIA LFRVTPQDGV
60 70 80 90 100
DPIEAAAAVA GESSTATWTV VWTDRLTAAE KYRAKCYRVD PVPNSPGQYF
110 120 130 140 150
AYIAYDLDLF EPGSISNLTA SIIGNVFGFK PLKGLRLEDM RLPVAYVKTF
160 170 180 190 200
QGPATGIVVE RERLDKFGRP LLGATVKPKL GLSGRNYGRV VYEALKGGLD
210 220 230 240 250
FTKDDENINS QPFMHWRERF LYCMEAVNRA QAASGEVKGT YLNVTAATME
260 270 280 290 300
DMYERAEFAK ELGSCIVMID LVIGYTAIQS MAKWARKNDM ILHLHRAGHS
310 320 330 340 350
TYTRQKNHGV SFRVIAKWMR LAGVDHIHAG TVVGKLEGDP NTTRGYYDIC
360 370 380 390 400
REEFNPTKLE HGIFFDQNWA SLNKMMPVAS GGIHAGQMHQ LLDLLGEDVV
410 420 430 440 450
LQFGGGTIGH PMGIQAGAIA NRVALEAMIL ARNEGRDYVA EGPEILAKAA
460 470 480
ATCTPLKSAL EVWKDVTFNY ESTDAPDFVP TAIAAV
Length:486
Mass (Da):53,763
Last modified:September 21, 2011 - v1
Checksum:iB200320194573F67
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002822 Genomic DNA. Translation: AEI04493.1.
RefSeqiWP_013913745.1. NC_017536.1.
YP_005945987.1. NC_017536.1.

Genome annotation databases

EnsemblBacteriaiAEI04493; AEI04493; OCA4_pHCG3B00470.
GeneIDi12536746.
KEGGioco:OCA4_pHCG3B00470.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002822 Genomic DNA. Translation: AEI04493.1.
RefSeqiWP_013913745.1. NC_017536.1.
YP_005945987.1. NC_017536.1.

3D structure databases

ProteinModelPortaliF8BQM8.
SMRiF8BQM8. Positions 13-479.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAEI04493; AEI04493; OCA4_pHCG3B00470.
GeneIDi12536746.
KEGGioco:OCA4_pHCG3B00470.

Phylogenomic databases

KOiK01601.
OMAiHAAFTRN.

Enzyme and pathway databases

BioCyciOCAR1031710:GLI1-3562-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequences of the chemolithoautotrophic Oligotropha carboxidovorans strains OM4 and OM5."
    Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G., Meyer O.
    J. Bacteriol. 193:5043-5043(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiF8BQM8_OLICM
AccessioniPrimary (citable) accession number: F8BQM8
Entry historyi
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: January 7, 2015
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".UniRule annotation

Keywords - Technical termi

Complete proteomeImported, PlasmidImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.