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

K9XMW7 (K9XMW7_STAC7) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 8. 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
Synonyms:rbcL HAMAP-Rule MF_01338
Ordered Locus Names:Sta7437_0333 EMBL AFZ33945.1
OrganismStanieria cyanosphaera (strain ATCC 29371 / PCC 7437) [Complete proteome] [HAMAP] EMBL AFZ33945.1
Taxonomic identifier111780 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaPleurocapsalesStanieria

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 in the photorespiration process. 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 site1721Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2911Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding1981Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2001Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2011Magnesium By similarity HAMAP-Rule MF_01338
Binding site1201Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1701Substrate By similarity HAMAP-Rule MF_01338
Binding site1741Substrate By similarity HAMAP-Rule MF_01338
Binding site2921Substrate By similarity HAMAP-Rule MF_01338
Binding site3241Substrate By similarity HAMAP-Rule MF_01338
Binding site3761Substrate By similarity HAMAP-Rule MF_01338
Site3311Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue1981N6-carboxylysine By similarity HAMAP-Rule MF_01338
Disulfide bond244Interchain; in linked form By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
K9XMW7 [UniParc].

Last modified March 6, 2013. Version 1.
Checksum: 586DDCB635D31207

FASTA47252,535
        10         20         30         40         50         60 
MVQTKSSSGF KAGVQDYRLT YYTPDYTPKD TDLLACFRMT PQPGVPPEEA GAAVAAESST 

        70         80         90        100        110        120 
GTWTTVWTDG LTDLDRYKGR CYDLEPVPGE DNQYFAFIAY PLDLFEEGSV TNVLTSLVGN 

       130        140        150        160        170        180 
VFGFKALRAL RLEDIRFPVA LIKTFQGPPH GITVERDKLN KYGRPLLGCT IKPKLGLSAK 

       190        200        210        220        230        240 
NYGRAVYECL RGGLDFTKDD ENINSQPFMR WRDRFLFVQE AIEKSQAETN EIKGHYLNVT 

       250        260        270        280        290        300 
AGTCEEMMKR AEFAKEIGTP IIMHDFLTGG FTANTTLAKY CRDNGLLLHI HRAMHAVIDR 

       310        320        330        340        350        360 
QKNHGIHFRV LAKCLRLSGG DHLHSGTVVG KLEGERGITM GFVDLMREDY VEEDRSRGIF 

       370        380        390        400        410        420 
FTQDYASMPG TMPVASGGIH VWHMPALVEI FGDDSCLQFG GGTLGHPWGN APGATANRVA 

       430        440        450        460        470 
LEACVQARNE GRSLAREGND VIREACRWSP ELAAACELWK EIKFEFEAMD TL 

« Hide

References

[1]"Improving the coverage of the cyanobacterial phylum using diversity-driven genome sequencing."
Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A., Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K., Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S. expand/collapse author list , Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.
Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29371 / PCC 7437.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003653 Genomic DNA. Translation: AFZ33945.1.
RefSeqYP_007130911.1. NC_019748.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFZ33945; AFZ33945; Sta7437_0333.
GeneID14161629.
KEGGscs:Sta7437_0333.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

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 nameK9XMW7_STAC7
AccessionPrimary (citable) accession number: K9XMW7
Entry history
Integrated into UniProtKB/TrEMBL: March 6, 2013
Last sequence update: March 6, 2013
Last modified: February 19, 2014
This is version 8 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)