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D7A343 (D7A343_STAND) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 27. 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:Snov_0428 EMBL ADH87761.1
OrganismStarkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB 9113) [Complete proteome] [HAMAP] EMBL ADH87761.1
Taxonomic identifier639283 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesXanthobacteraceaeStarkeya

Protein attributes

Sequence length489 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 site1801Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2981Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2061Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2081Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2091Magnesium By similarity HAMAP-Rule MF_01338
Binding site1281Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1781Substrate By similarity HAMAP-Rule MF_01338
Binding site1821Substrate By similarity HAMAP-Rule MF_01338
Binding site2991Substrate By similarity HAMAP-Rule MF_01338
Binding site3311Substrate By similarity HAMAP-Rule MF_01338
Binding site3831Substrate By similarity HAMAP-Rule MF_01338
Site3381Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue2061N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
D7A343 [UniParc].

Last modified August 10, 2010. Version 1.
Checksum: F62FCB0F0878F040

FASTA48954,138
        10         20         30         40         50         60 
MNAIDKTASA DKPRSRYSAG VMEYRKMGYW QPDYEPKDTD VIALFRVTPQ DGVDPIEASA 

        70         80         90        100        110        120 
AVAGESSTAT WTVVWTDRLT ACDKYRAKCY RVDPVPNSPG SWFAYIAYDL DLFEPGSISN 

       130        140        150        160        170        180 
LSASIIGNVF GFKPLKALRL EDMRLPVAYV KTFDGPATGI VVERERLDKF GRPLLGATVK 

       190        200        210        220        230        240 
PKLGLSGRNY GRVVYEALKG GLDFTKDDEN INSQPFMHWR ERFLYCMEAV NKAQASTGEI 

       250        260        270        280        290        300 
KGTYLNVTAG TMEDMYERAD FAKSLGSNIV MIDLVIGYTA IQSMAKWARR NDMILHLHRA 

       310        320        330        340        350        360 
GHSTYTRQKS HGVSFRVIAK WMRLAGVDHI HAGTVVGKLE GDPHTTKGYY DICRDDFVPQ 

       370        380        390        400        410        420 
NLAHGVFFDQ DWASTRKLMP VASGGIHAGQ MHQLIDLLGE DVVLQFGGGT IGHPMGIQAG 

       430        440        450        460        470        480 
ATANRVALEC MILARNEGRD ILAEGPDILN EAARHCMPLK QALETWKDVT FNYSSTDTPD 


FVPQATAAE 

« Hide

References

[1]"Complete sequence of Starkeya novella DSM 506."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U., Woyke T.
Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB 9113.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002026 Genomic DNA. Translation: ADH87761.1.
RefSeqYP_003692380.1. NC_014217.1.

3D structure databases

ProteinModelPortalD7A343.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADH87761; ADH87761; Snov_0428.
GeneID9331485.
KEGGsno:Snov_0428.
PATRIC38253389. VBIStaNov45716_0429.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.
OMAFTQDWAS.

Enzyme and pathway databases

BioCycSNOV639283:GCS4-435-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 nameD7A343_STAND
AccessionPrimary (citable) accession number: D7A343
Entry history
Integrated into UniProtKB/TrEMBL: August 10, 2010
Last sequence update: August 10, 2010
Last modified: June 11, 2014
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)