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H0Q551 (H0Q551_9RHOO) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338

Short name=RuBisCO large subunit HAMAP-Rule MF_01338
EC=4.1.1.39 HAMAP-Rule MF_01338
Gene names
Name:cbbL HAMAP-Rule MF_01338 EMBL BAL27114.1
Synonyms:rbcL EMBL BAL27114.1
ORF Names:AZKH_p0231 EMBL BAL27114.1
Encoded onPlasmid pAZKH Ref.1 EMBL BAL27114.1
OrganismAzoarcus sp. KH32C [Complete proteome] EMBL BAL27114.1
Taxonomic identifier748247 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAzoarcus

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_01338

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01338

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01338

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01338

Subunit structure

Heterohexadecamer of 8 large chains and 8 small chains By similarity. HAMAP-Rule MF_01338

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. HAMAP-Rule MF_01338

Sequence similarities

Belongs to the RuBisCO large chain family. Type I subfamily. HAMAP-Rule MF_01338

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1801Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2981Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2061Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2081Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2091Magnesium By similarity HAMAP-Rule MF_01338
Binding site1281Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1781Substrate By similarity HAMAP-Rule MF_01338
Binding site1821Substrate By similarity HAMAP-Rule MF_01338
Binding site2991Substrate By similarity HAMAP-Rule MF_01338
Binding site3311Substrate By similarity HAMAP-Rule MF_01338
Binding site3831Substrate By similarity HAMAP-Rule MF_01338
Site3381Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue2061N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
H0Q551 [UniParc].

Last modified February 22, 2012. Version 1.
Checksum: A955779E87AD0C45

FASTA48853,586
        10         20         30         40         50         60 
MGALETAEAI IDPKQRYRAG VLKYAQMGYW DGDYEPKETD VLALFRITPQ EGVDPIEAAA 

        70         80         90        100        110        120 
AVAGESSTAT WTVVWTDRLT ACDRYRAKAY RVDPVPGQPG QYFCYVAYEL DLFEEGSIAN 

       130        140        150        160        170        180 
LTASIIGNVF SFKPIKAARL EDMRLPVAYV KTFRGPPTGI VVERERLNCF GRPLLGATTK 

       190        200        210        220        230        240 
PKLGLSGKNY GRVVYEALLG GLDFTKDDEN INSQPFMHWR DRFLYVMEGV NRASAATGEV 

       250        260        270        280        290        300 
KGHYLNVTAG TMEEMYARAE FAKSLGSTIV MVDLIIGWTA IQSMSNWCRA NDMILHMHRA 

       310        320        330        340        350        360 
GHGTYTRQKN HGISFRVIAK WLRLAGVDHL HAGTAVGKLE GDPMTVQGYY NVCREMKNAV 

       370        380        390        400        410        420 
DLPRGIFFEQ DWASLRRVMP VASGGIHAGQ MHQLLDLFGD DVVLQFGGGT IGHPMGIQAG 

       430        440        450        460        470        480 
ATANRVALEA MVLARNEGRD IASEGSDILK AAARDCAPLR AALDTWGEVS FNYTSTDTSD 


FVPTASVA 

« Hide

References

[1]"Complete genome sequence of Azoarcus sp. KH32C."
Nishizawa T., Tago T., Oshima K., Hattori M., Ishii S., Otsuka S., Senoo K.
Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: KH32C EMBL BAL27114.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP012305 Genomic DNA. Translation: BAL27114.1.
RefSeqYP_007598171.1. NC_020548.1.

3D structure databases

ProteinModelPortalH0Q551.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAL27114; BAL27114; AZKH_p0231.
GeneID14823035.
KEGGaza:AZKH_p0231.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameH0Q551_9RHOO
AccessionPrimary (citable) accession number: H0Q551
Entry history
Integrated into UniProtKB/TrEMBL: February 22, 2012
Last sequence update: February 22, 2012
Last modified: July 9, 2014
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)