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Protein

Ribulose bisphosphate carboxylase small chain

Gene
N/A
Organism
Glycine max (Soybean) (Glycine hispida)
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)
OrganismiGlycine max (Soybean) (Glycine hispida)
Taxonomic identifieri3847 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycineSoja
ProteomesiUP000008827 Componenti: Chromosome 19

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

ChloroplastSAAS annotation, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5555 PotentialImportedAdd
BLAST
Chaini56 – 178123 PotentialImportedPRO_5000144784Add
BLAST

Proteomic databases

PRIDEiQ39832.

Interactioni

Subunit structurei

8 large chains + 8 small chains.UniRule annotationSAAS annotation

Protein-protein interaction databases

STRINGi3847.GLYMA19G06370.1.

Structurei

3D structure databases

ProteinModelPortaliQ39832.
SMRiQ39832. Positions 56-178.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO small chain family.UniRule annotation

Keywords - Domaini

Transit peptideImported

Phylogenomic databases

InParanoidiQ39832.
KOiK01602.
OMAiAFPATRK.

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.
SMARTiSM00961. RuBisCO_small. 1 hit.
[Graphical view]
SUPFAMiSSF55239. SSF55239. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q39832-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSMISSPA VTTVNRAGAG MVAPFTGLKS MAGFPTRKTN NDITSIASNG
60 70 80 90 100
GRVQCMQVWP PVGKKKFETL SYLPDLDDAQ LAKEVEYLLR KGWIPCLEFE
110 120 130 140 150
LEHGFVYREH NRSPGYYDGR YWTMWKLPMF GCTDASQVLK ELQEAKTAYP
160 170
NGFIRIIGFD NVRQVQCISF IAYKPPGF
Length:178
Mass (Da):20,005
Last modified:November 1, 1996 - v1
Checksum:i566849948665FBD9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39567 mRNA. Translation: AAA81328.1.
AF303939 mRNA. Translation: AAG24882.1.
RefSeqiNP_001241137.1. NM_001254208.1.
UniGeneiGma.64193.

Genome annotation databases

EnsemblPlantsiGLYMA19G06340.1; GLYMA19G06340.1; GLYMA19G06340.
GLYMA19G06370.1; GLYMA19G06370.1; GLYMA19G06370.
GeneIDi100794277.
KEGGigmx:100794277.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39567 mRNA. Translation: AAA81328.1.
AF303939 mRNA. Translation: AAG24882.1.
RefSeqiNP_001241137.1. NM_001254208.1.
UniGeneiGma.64193.

3D structure databases

ProteinModelPortaliQ39832.
SMRiQ39832. Positions 56-178.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3847.GLYMA19G06370.1.

Proteomic databases

PRIDEiQ39832.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiGLYMA19G06340.1; GLYMA19G06340.1; GLYMA19G06340.
GLYMA19G06370.1; GLYMA19G06370.1; GLYMA19G06370.
GeneIDi100794277.
KEGGigmx:100794277.

Phylogenomic databases

InParanoidiQ39832.
KOiK01602.
OMAiAFPATRK.

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.
SMARTiSM00961. RuBisCO_small. 1 hit.
[Graphical view]
SUPFAMiSSF55239. SSF55239. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a cDNA encoding a ribulose-1,5-bisphosphate carboxylase small subunit in soybean."
    Cho T.-J., Chung K.A., Lee K.J., Chung U.S., Cho N.J., Chae Q.
    Hanguk Saenghwahakhoe Chi 25:658-663(1992)
    Cited for: NUCLEOTIDE SEQUENCE.
  2. Cho T.-J., Chung K.A., Lee K.J., Chung U.S., Cho N.J., Chae Q.
    Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "Soybean ribulose-1,5-bisphosphate carboxylase small subunit gene."
    He C., Chen S.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Williams 82Imported.
  5. EnsemblPlants
    Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases
    Cited for: IDENTIFICATION.
    Strain: Williams 82Imported.

Entry informationi

Entry nameiQ39832_SOYBN
AccessioniPrimary (citable) accession number: Q39832
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

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.