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F6DAZ0 (F6DAZ0_THICA) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 21. 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
Ordered Locus Names:Thicy_1565 EMBL AEG32323.1
OrganismThioalkalimicrobium cyclicum (strain DSM 14477 / JCM 11371 / ALM1) [Complete proteome] [HAMAP] EMBL AEG32323.1
Taxonomic identifier717773 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesPiscirickettsiaceaeThioalkalimicrobium

Protein attributes

Sequence length470 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity. HAMAP-Rule MF_01338

Post-translational modification

The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover 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
Disulfide bond240Interchain; in linked form By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
F6DAZ0 [UniParc].

Last modified July 27, 2011. Version 1.
Checksum: 9CE28847060ECC49

FASTA47051,764
        10         20         30         40         50         60 
MANQTFNAGV QDYKLTYWTP DYTPLDTDLL ACFKVIPQAG VPREEAAAAV AAESSTGTWT 

        70         80         90        100        110        120 
TVWTDLLTDM EFYKGRCYRI EDVPGNKDAF YAFIAYPLDL FEEGSVVNVL TSLVGNVFGF 

       130        140        150        160        170        180 
KAVRSLRLED IRFPVAFIKT CGGPPSGIQV ERDKLNKYGR PMLGCTIKPK LGLSAKNYGR 

       190        200        210        220        230        240 
AVYECLRGGL DLTKDDENIN SQPFQRWRDR FSFVADAINK AEAETGEVKG HYLNVTAATC 

       250        260        270        280        290        300 
EDMMERAEYA KELGVRIVMH DFLTGGFTAN TSLANWCRKN GMLLHIHRAM HAVIDRNPNH 

       310        320        330        340        350        360 
GIHFRVLAKC LRLSGGDHLH TGTVVGKLEG DRASTLGFVD QLREAFVPED RSRGVFFDQD 

       370        380        390        400        410        420 
WGSMPGVMAV ASGGIHVWHM PALVTIFGDD SVLQFGGGTQ GHPGGNAAGA AANRVALEAC 

       430        440        450        460        470 
VKARNEGRDL EREGGDILRD AARHSPELAV ALETWKEIKF EFDTVDKLDA 

« Hide

References

[1]"Complete sequence of Thioalkalimicrobium cyclicum ALM1."
US DOE Joint Genome Institute
Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Mikhailova N., Davenport K., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Kappler U., Woyke T.
Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14477 / JCM 11371 / ALM1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002776 Genomic DNA. Translation: AEG32323.1.
RefSeqYP_004537802.1. NC_015581.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEG32323; AEG32323; Thicy_1565.
GeneID10720405.
KEGGtcy:Thicy_1565.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.
OMAVIVTFRV.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020888. 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.
ProtoNetSearch...

Entry information

Entry nameF6DAZ0_THICA
AccessionPrimary (citable) accession number: F6DAZ0
Entry history
Integrated into UniProtKB/TrEMBL: July 27, 2011
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)