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I0HVA8 (I0HVA8_RUBGI) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 13. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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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 BAL96945.1
Ordered Locus Names:RGE_36060 EMBL BAL96945.1
OrganismRubrivivax gelatinosus (strain NBRC 100245 / IL144) [Complete proteome] [HAMAP] EMBL BAL96945.1
Taxonomic identifier983917 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesRubrivivax

Protein attributes

Sequence length493 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 site1841Proton acceptor By similarity HAMAP-Rule MF_01338
Active site3021Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2101Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2121Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2131Magnesium By similarity HAMAP-Rule MF_01338
Binding site1321Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1821Substrate By similarity HAMAP-Rule MF_01338
Binding site1861Substrate By similarity HAMAP-Rule MF_01338
Binding site3031Substrate By similarity HAMAP-Rule MF_01338
Binding site3351Substrate By similarity HAMAP-Rule MF_01338
Binding site3871Substrate By similarity HAMAP-Rule MF_01338
Site3421Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue2101N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
I0HVA8 [UniParc].

Last modified June 13, 2012. Version 1.
Checksum: 780F4633E7415C06

FASTA49354,372
        10         20         30         40         50         60 
MNKPHEPGAT GDQILDKKQR YSAGVLKYRQ MGYWDSDYVP KATDVVCLFR ITPQEGVDPI 

        70         80         90        100        110        120 
EAAAAVAGES STATWTVVWT DRLTACDSYR AKAYKVEPVP GRPGEYFAWV AYDLILFEEG 

       130        140        150        160        170        180 
SIANMTASLI GNVFSFKPLK AARLEDIQIP VAYVKTFKGP PTGLIVERER LDKFGRPLLG 

       190        200        210        220        230        240 
ATTKPKLGLS GRNYGRVIYE GLKGGLDFMK DDENINSQPF MHWRDRFLYV MDGVNKASAA 

       250        260        270        280        290        300 
TGEVKGSYLN VTGATMEDIY ERAEFAKELG SVVIMVDLII GWSAIQSIAN WARKNDMIVH 

       310        320        330        340        350        360 
MHRAGHGTYT RQKNHGVSFR VMAKWLRLAG VDHLHTGTAV GKLEGDPLTV QGYYNVCRDA 

       370        380        390        400        410        420 
YTKQDLPRGL FFDQDWADLR KVMPVASGGI HAGQMHQLID LFGDDVILQF GGGTIGHPAG 

       430        440        450        460        470        480 
IQAGAVANRV ALEAMVKARN EGRDIKNEGP EILQKAAQFC TPLKQALDTW KDVSFNYAST 

       490 
DQSDYAVTPA TSA 

« Hide

References

[1]"Complete genome sequence of phototrophic betaproteobacterium Rubrivivax gelatinosus IL144."
Nagashima S., Sekine M., Takami A., Shimizu T., Nakamura S., Aono E., Sakamoto K., Nakazawa H., Yamazaki S., Fujita N., Shimada K., Hanada S., Nagashima K.
Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NBRC 100245 / IL144.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP012320 Genomic DNA. Translation: BAL96945.1.
RefSeqYP_005438444.1. NC_017075.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAL96945; BAL96945; RGE_36060.
GeneID12027736.
KEGGrge:RGE_36060.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycRGEL983917:GLJR-3646-MONOMER.

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 nameI0HVA8_RUBGI
AccessionPrimary (citable) accession number: I0HVA8
Entry history
Integrated into UniProtKB/TrEMBL: June 13, 2012
Last sequence update: June 13, 2012
Last modified: February 19, 2014
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)