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I3Y991 (I3Y991_THIV6) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 11. 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
Ordered Locus Names:Thivi_1570 EMBL AFL73559.1
OrganismThiocystis violascens (strain ATCC 17096 / DSM 198 / 6111) (Chromatium violascens) [Complete proteome] [HAMAP] EMBL AFL73559.1
Taxonomic identifier765911 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeThiocystis

Protein attributes

Sequence length472 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 site1671Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2861Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding1931Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding1951Magnesium By similarity HAMAP-Rule MF_01338
Metal binding1961Magnesium By similarity HAMAP-Rule MF_01338
Binding site1151Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1651Substrate By similarity HAMAP-Rule MF_01338
Binding site1691Substrate By similarity HAMAP-Rule MF_01338
Binding site2871Substrate By similarity HAMAP-Rule MF_01338
Binding site3191Substrate By similarity HAMAP-Rule MF_01338
Binding site3711Substrate By similarity HAMAP-Rule MF_01338
Site3261Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue1931N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
I3Y991 [UniParc].

Last modified September 5, 2012. Version 1.
Checksum: 14C66F85CA42A001

FASTA47252,594
        10         20         30         40         50         60 
MAKTYSAGVK EYRETYWMPD YKPKETDLLA CFKITPQAGV PREEAAAAVA AESSTGTWTT 

        70         80         90        100        110        120 
VWTDLLTDLD HYKGRAYAIE DVPGDDTCYY AFIAYPIDLF EEGSVVNVFT SLVGNVFGFK 

       130        140        150        160        170        180 
AVRALRLEDV RFPIAYVMTC NGPPHGIQVE RDMMNKYGRP LLGCTIKPKL GLSAKNYGRA 

       190        200        210        220        230        240 
VYECLRGGLD FTKDDENVNS QPFMRWRQRF DFVIDAIDKA ERETGERKGH YLNVTAPTPE 

       250        260        270        280        290        300 
EMYKRAEHAK EIGAPIIMHD YITGGFCANT GLAQWCRDNG MLLHIHRAMH AVLDRNPHHG 

       310        320        330        340        350        360 
IHFRVLAKIL RLSGGDHLHS GTVVGKLEGD REATLGWIDI MRDSFIKEDR SRGIFFDQDW 

       370        380        390        400        410        420 
GSMPGVFPVA SGGIHVWHMP ALVTIFGDDS VLQFGGGTLG HPWGNAAGAA ANRVALEACV 

       430        440        450        460        470 
QARNEGVAIE KEGKEVLTNA AKNSPELKVA METWKEIKFE FDTVDKLDVA HK 

« Hide

References

[1]"Complete sequence of Thiocystis violascens DSM 198."
US DOE Joint Genome Institute
Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K. expand/collapse author list , Liu Z., Frigaard N.-U., Bryant D., Woyke T.
Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17096 / DSM 198 / 6111.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003154 Genomic DNA. Translation: AFL73559.1.
RefSeqYP_006413684.1. NC_018012.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFL73559; AFL73559; Thivi_1570.
GeneID13047815.
KEGGtvi:Thivi_1570.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycTVIO765911:GLMH-1563-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 nameI3Y991_THIV6
AccessionPrimary (citable) accession number: I3Y991
Entry history
Integrated into UniProtKB/TrEMBL: September 5, 2012
Last sequence update: September 5, 2012
Last modified: February 19, 2014
This is version 11 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)