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D5CQ59 (D5CQ59_SIDLE) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 23. 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:Slit_0985 EMBL ADE11223.1
OrganismSideroxydans lithotrophicus (strain ES-1) [Complete proteome] [HAMAP] EMBL ADE11223.1
Taxonomic identifier580332 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaGallionellalesGallionellaceaeSideroxydans

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
D5CQ59 [UniParc].

Last modified June 15, 2010. Version 1.
Checksum: 313B299AE15AF9C3

FASTA47352,606
        10         20         30         40         50         60 
MAVKTYNAGV KEYRQTYWTP EYTPLDTDIL ACFKITPQPG VDREEVAAAV AAESSTGTWT 

        70         80         90        100        110        120 
TVWTDLLTDL DYYKGRAYRI EDVPGDDTCF YAFVAYPIDL FEEGSVVNVL TSLVGNVFGF 

       130        140        150        160        170        180 
KALRALRLED VRFPIAYVKT CGGPPQGIQV ERDKMNKYGR PLLGCTIKPK LGLSAKNYGR 

       190        200        210        220        230        240 
AVYECLRGGL DFTKDDENVN SQPFMRWRDR FEFVHEATLK AERETGERKG HYLNVTAPTP 

       250        260        270        280        290        300 
EEMYKRAEFA KEIGAPIIMH DYLTGGLTAN TGLANWCRNN GMLLHIHRAM HAVLDRNPHH 

       310        320        330        340        350        360 
GIHFRVLTKV LRLSGGDHLH SGTVVGKLEG DREATLGWID TMRDEFIKED RSRGLFFDQD 

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

       430        440        450        460        470 
VAARNQGVAV EKEGKSILTE AAKSSPELKI AMETWKEIKF EFDTVDKLDV AHK 

« Hide

References

[1]"Complete sequence of Sideroxydans lithotrophicus ES-1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Emerson D., Woyke T.
Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ES-1 EMBL ADE11223.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001965 Genomic DNA. Translation: ADE11223.1.
RefSeqYP_003523610.1. NC_013959.1.

3D structure databases

ProteinModelPortalD5CQ59.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADE11223; ADE11223; Slit_0985.
GeneID8891657.
KEGGslt:Slit_0985.
PATRIC35400070. VBISidLit69165_0978.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.

Enzyme and pathway databases

BioCycSLIT580332:GH9F-1002-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 nameD5CQ59_SIDLE
AccessionPrimary (citable) accession number: D5CQ59
Entry history
Integrated into UniProtKB/TrEMBL: June 15, 2010
Last sequence update: June 15, 2010
Last modified: June 11, 2014
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)