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S6AP25 (S6AP25_9PROT) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 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 HAMAP-Rule MF_01339

Short name=RuBisCO HAMAP-Rule MF_01339
EC=4.1.1.39 HAMAP-Rule MF_01339
Gene names
Name:cbbM HAMAP-Rule MF_01339 EMBL BAN36649.1
ORF Names:SCD_n02850 EMBL BAN36649.1
OrganismSulfuricella denitrificans skB26 [Complete proteome] EMBL BAN36649.1
Taxonomic identifier1163617 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeSulfuricella

Protein attributes

Sequence length459 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_01339

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01339

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01339

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01339

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01339

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits By similarity. HAMAP-Rule MF_01339

Sequence similarities

Belongs to the RuBisCO large chain family. Type II subfamily. HAMAP-Rule MF_01339

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1661Proton acceptor By similarity HAMAP-Rule MF_01339
Active site2871Proton acceptor By similarity HAMAP-Rule MF_01339
Metal binding1911Magnesium; via carbamate group By similarity HAMAP-Rule MF_01339
Metal binding1931Magnesium By similarity HAMAP-Rule MF_01339
Metal binding1941Magnesium By similarity HAMAP-Rule MF_01339
Binding site1111Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01339
Binding site1681Substrate By similarity HAMAP-Rule MF_01339
Binding site2881Substrate By similarity HAMAP-Rule MF_01339
Binding site3211Substrate By similarity HAMAP-Rule MF_01339
Binding site3681Substrate By similarity HAMAP-Rule MF_01339
Site3291Transition state stabilizer By similarity HAMAP-Rule MF_01339

Amino acid modifications

Modified residue1911N6-carboxylysine By similarity HAMAP-Rule MF_01339

Sequences

Sequence LengthMass (Da)Tools
S6AP25 [UniParc].

Last modified October 16, 2013. Version 1.
Checksum: 4A820FEB687B8F86

FASTA45950,557
        10         20         30         40         50         60 
MDQSNRYADL SLKEEDLIKG DNHILVAYHM QPATGYGYLE VAAHIAAESS TGTNVEVSTT 

        70         80         90        100        110        120 
DDFTKGVDAL VYFIDEAKGI MKVAYPNDLF DRNVTDGRAM LVSFLTLAIG NNQGMGDVKH 

       130        140        150        160        170        180 
LQMQDFYVPW SMLRLYDGPA KDITDLWDIL GRPRINGGYI AGTIIKPKLG LRPEPFAKAA 

       190        200        210        220        230        240 
YQFWLGGDFI KNDEPQGNQV FCPTKKVIPL VYDSMKRAMD ETGQAKLFSA NITADDHYEM 

       250        260        270        280        290        300 
LARADYILET FGPDANKVAF LVDGYVGGPG MITTARRQYP GQYLHYHRAG HGAITSPSAV 

       310        320        330        340        350        360 
RGYTAFVLSK MSRLQGASGI HVGTMGYGKM EGGKDDRNIA YMIERDSADG PYYHQEWHGM 

       370        380        390        400        410        420 
KPTTPIISGG MNALRLPGFF ENLGHGNVIN TSGGGSYGHI DSPAAGAISL RQSYECWKAG 

       430        440        450 
ADPIEFAKEH KEFARAFESF PGDADKIFPG WREKLGVHK 

« Hide

References

[1]"Draft genome sequence of a psychrotolerant sulfur-oxidizing bacterium, Sulfuricella denitrificans skB26, and proteomic insights into cold adaptation."
Watanabe T., Kojima H., Fukui M.
Appl. Environ. Microbiol. 78:6545-6549(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SkB26 EMBL BAN36649.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP013066 Genomic DNA. Translation: BAN36649.1.
RefSeqYP_008547681.1. NC_022357.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAN36649; BAN36649; SCD_n02850.
GeneID16926628.
KEGGsdr:SCD_n02850.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01339. RuBisCO_L_type2.
InterProIPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
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 nameS6AP25_9PROT
AccessionPrimary (citable) accession number: S6AP25
Entry history
Integrated into UniProtKB/TrEMBL: October 16, 2013
Last sequence update: October 16, 2013
Last modified: June 11, 2014
This is version 8 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)