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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 (By similarity).SAAS 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationSAAS annotation, MonooxygenaseUniRule annotationSAAS annotation, Oxidoreductase

Keywords - Biological processi

Carbon dioxide fixationUniRule annotationSAAS annotation, PhotorespirationUniRule annotationSAAS 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

Complete GO annotation...

Keywords - Cellular componenti

ChloroplastSAAS annotation, Plastid

Interactioni

Subunit structurei

8 large chains + 8 small chains.UniRule annotationSAAS annotation

Protein-protein interaction databases

STRINGi3694.POPTR_0004s09910.1.

Structurei

3D structure databases

ProteinModelPortaliA9PFS6.
SMRiA9PFS6. Positions 60-181.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO small chain family.UniRule annotation

Phylogenomic databases

eggNOGiCOG4451.
HOGENOMiHOG000141332.
InParanoidiA9PFS6.

Family and domain databases

Gene3Di3.30.190.10. 1 hit.
InterProiIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
IPR024680. RuBisCO_ssu_N.
[Graphical view]
PfamiPF12338. RbcS. 1 hit.
PF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSiPR00152. RUBISCOSMALL.
SUPFAMiSSF55239. SSF55239. 1 hit.

Sequencei

Sequence statusi: Complete.

A9PFS6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSSMISSA AVATVNRTPV QANMVAPFNG LKSAAAFPVS TRKANDITSI
60 70 80 90 100
ASNGGRVQCM QVWPPTGLKK FETLSYLPDL TEEELAKEID YLLRSKWVPC
110 120 130 140 150
LEFELEKGWV YREHHSSPGY YDGRYWTMWK LPMFGCTEAS QVLLELEEAK
160 170 180
KAYPNAFIRI IGFDNTRQVQ CISFIAAKPK GV
Length:182
Mass (Da):20,379
Last modified:February 5, 2008 - v1
Checksum:iD94DBE99714E0F51
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF147202 mRNA. Translation: ABK95229.1.
EF147224 mRNA. Translation: ABK95250.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF147202 mRNA. Translation: ABK95229.1.
EF147224 mRNA. Translation: ABK95250.1.

3D structure databases

ProteinModelPortaliA9PFS6.
SMRiA9PFS6. Positions 60-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3694.POPTR_0004s09910.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG4451.
HOGENOMiHOG000141332.
InParanoidiA9PFS6.

Family and domain databases

Gene3Di3.30.190.10. 1 hit.
InterProiIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
IPR024680. RuBisCO_ssu_N.
[Graphical view]
PfamiPF12338. RbcS. 1 hit.
PF00101. 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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: Young and mature leavesImported.

Entry informationi

Entry nameiA9PFS6_POPTR
AccessioniPrimary (citable) accession number: A9PFS6
Entry historyi
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: June 24, 2015
This is version 56 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.