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Protein

Ribulose bisphosphate carboxylase small chain

Gene
N/A
Organism
Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

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.UniRule annotationSAAS annotation

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.UniRule annotationSAAS annotation
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.UniRule annotationSAAS annotation

GO - Molecular functioni

  1. monooxygenase activity Source: UniProtKB-KW
  2. ribulose-bisphosphate carboxylase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbon fixation Source: UniProtKB-KW
  2. photorespiration Source: UniProtKB-KW
  3. photosynthesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationSAAS annotation, MonooxygenaseUniRule annotationSAAS annotation, Oxidoreductase

Keywords - Biological processi

Carbon dioxide fixationUniRule annotationSAAS annotation, PhotorespirationUniRule annotation, PhotosynthesisUniRule annotationSAAS annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase small chainUniRule annotation (EC:4.1.1.39UniRule annotation)
OrganismiPopulus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)Imported
Taxonomic identifieri3694 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesSalicaceaeSaliceaePopulus

Subcellular locationi

GO - Cellular componenti

  1. plastid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

PlastidUniRule annotation

Interactioni

Subunit structurei

8 large chains + 8 small chains.UniRule annotationSAAS annotation

Protein-protein interaction databases

STRINGi3694.eugene3.00180810.

Structurei

3D structure databases

ProteinModelPortaliA9PI67.
SMRiA9PI67. Positions 50-168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO small chain family.UniRule annotation

Phylogenomic databases

eggNOGiCOG4451.
InParanoidiA9PI67.

Family and domain databases

Gene3Di3.30.190.10. 1 hit.
InterProiIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
[Graphical view]
PfamiPF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSiPR00152. RUBISCOSMALL.
SUPFAMiSSF55239. SSF55239. 1 hit.

Sequencei

Sequence statusi: Complete.

A9PI67-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAGIFAASA VAAPGYHGLR ALPTKQPFAT KNSVARSSRT VSNGSKTFCM
60 70 80 90 100
KTWNPINNKK FEALSYLPPL SEDSIAKEID YMMKKGWIPC LEFDEVGSVR
110 120 130 140 150
REHSRMPGYY DGRYWTLWKL PMFGCTDSSQ VLEEIHECKK AYPDAYIRCL
160 170
AFDNKHQGQC MAFVIQKPGN
Length:170
Mass (Da):19,202
Last modified:February 5, 2008 - v1
Checksum:i2105A61A4803E122
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF148086 mRNA. Translation: ABK96070.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF148086 mRNA. Translation: ABK96070.1.

3D structure databases

ProteinModelPortaliA9PI67.
SMRiA9PI67. Positions 50-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3694.eugene3.00180810.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG4451.
InParanoidiA9PI67.

Family and domain databases

Gene3Di3.30.190.10. 1 hit.
InterProiIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
[Graphical view]
PfamiPF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSiPR00152. RUBISCOSMALL.
SUPFAMiSSF55239. SSF55239. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Analysis of 4,664 high-quality sequence-finished poplar full-length cDNA clones and their utility for the discovery of genes responding to insect feeding."
    Ralph S.G., Chun H.J., Cooper D., Kirkpatrick R., Kolosova N., Gunter L., Tuskan G.A., Douglas C.J., Holt R.A., Jones S.J., Marra M.A., Bohlmann J.
    BMC Genomics 9:57-57(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: Young and mature leavesImported.

Entry informationi

Entry nameiA9PI67_POPTR
AccessioniPrimary (citable) accession number: A9PI67
Entry historyi
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: February 4, 2015
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.