Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

D6CQK0 (D6CQK0_THIA3) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 26. 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:rbcL EMBL CAZ86891.1
Synonyms:cbbL HAMAP-Rule MF_01338
Ordered Locus Names:THI_0135 EMBL CAZ86891.1
OrganismThiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As) [Complete proteome] [HAMAP] EMBL CAZ86891.1
Taxonomic identifier426114 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesThiomonas

Protein attributes

Sequence length473 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 site1681Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2871Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding1941Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding1961Magnesium By similarity HAMAP-Rule MF_01338
Metal binding1971Magnesium By similarity HAMAP-Rule MF_01338
Binding site1161Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1661Substrate By similarity HAMAP-Rule MF_01338
Binding site1701Substrate By similarity HAMAP-Rule MF_01338
Binding site2881Substrate By similarity HAMAP-Rule MF_01338
Binding site3201Substrate By similarity HAMAP-Rule MF_01338
Binding site3721Substrate By similarity HAMAP-Rule MF_01338
Site3271Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue1941N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
D6CQK0 [UniParc].

Last modified July 13, 2010. Version 1.
Checksum: 46EAF8F4C060ADF4

FASTA47352,787
        10         20         30         40         50         60 
MAVKTYQAGV KEYRQTYWMP EYTPLDTDLL ACFKITPQAG VDREEAAAAV AAESSTGTWT 

        70         80         90        100        110        120 
TVWTDLLTDM DYYKGRAYRI EDVPGDDTCF YAFIAYPIDL FEEGSVVNVF TSLVGNVFGF 

       130        140        150        160        170        180 
KAIRALRLED IRFPIAYVKT CNGPPNGIQV ERDVINKYGR PLLGCTIKPK LGLSGKNYGR 

       190        200        210        220        230        240 
AVYECLRGGL DFTKDDENIN SQPFMRWKQR FDFVQEATLK AEQETGERKG HYLNVTAPTP 

       250        260        270        280        290        300 
DEMFKRAEYA KEIGAPIIMH DYITGGFCAN TGLAQWCRDN GMLLHIHRAM HAVLDRNPHH 

       310        320        330        340        350        360 
GIHFRVLTKI LRLSGGDHLH TGTVVGKLEG DRASTLGWID LLRESYVPED RSRGIFFDQD 

       370        380        390        400        410        420 
WGSMPGAFAV ASGGIHVWHM PALVTIFGDD SVLQFGGGTL GHPWGNAAGA AANRVALEAC 

       430        440        450        460        470 
VQARNEGRQV EKEGREILTA AAQHSPELKI AMETWKEIKF EFDTVDKLDV TNK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FP475956 Genomic DNA. Translation: CAZ86891.1.
RefSeqYP_003622759.1. NC_014145.1.

3D structure databases

ProteinModelPortalD6CQK0.
SMRD6CQK0. Positions 16-460.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAZ86891; CAZ86891; THI_0135.
GeneID13878401.
KEGGthi:THI_0135.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.

Enzyme and pathway databases

BioCycTARS426114-WGS:GSYJ-125-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 nameD6CQK0_THIA3
AccessionPrimary (citable) accession number: D6CQK0
Entry history
Integrated into UniProtKB/TrEMBL: July 13, 2010
Last sequence update: July 13, 2010
Last modified: July 9, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)