Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ribulose bisphosphate carboxylase small chain 5, chloroplastic

Gene

RBCS5

Organism
Flaveria pringlei
Status
Reviewed-Annotation score: -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).By similarity

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase, Monooxygenase, Oxidoreductase
Biological processCalvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase small chain 5, chloroplastic (EC:4.1.1.39)
Short name:
RuBisCO small subunit 5
Gene namesi
Name:RBCS5
OrganismiFlaveria pringlei
Taxonomic identifieri4226 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeAsteroideaeHeliantheae allianceTageteaeFlaveria

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 50ChloroplastBy similarityAdd BLAST50
ChainiPRO_000003149651 – 173Ribulose bisphosphate carboxylase small chain 5, chloroplasticAdd BLAST123

Proteomic databases

PRIDEiQ39747

Interactioni

Subunit structurei

8 large chains + 8 small chains.

Structurei

3D structure databases

ProteinModelPortaliQ39747
SMRiQ39747
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO small chain family.Curated

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.30.190.10, 1 hit
InterProiView protein in InterPro
IPR024681 RuBisCO_sc
IPR000894 RuBisCO_sc_dom
IPR024680 RuBisCO_ssu_N
IPR036385 RuBisCO_ssu_sf
PfamiView protein in Pfam
PF12338 RbcS, 1 hit
PF00101 RuBisCO_small, 1 hit
PRINTSiPR00152 RUBISCOSMALL
SMARTiView protein in SMART
SM00961 RuBisCO_small, 1 hit
SUPFAMiSSF55239 SSF55239, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q39747-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASIPATVAT VAQANMVAPF TGLKSNAAFP VTKKVNDFST LPSNGGRVQC
60 70 80 90 100
MKVWPPLGKK RYETLSYLPN LTEVQLAKEV DYLLRNKWVP CLEFELEHGF
110 120 130 140 150
VYRENARSPG YYDGRYWTMW KLPMFGCTDS AQVMKELQEC KKEYPQAWIR
160 170
IIGFDNVRQV QCISFIASKP DGF
Length:173
Mass (Da):19,746
Last modified:November 1, 1996 - v1
Checksum:i610099392D076852
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29937 mRNA Translation: AAB67849.1

Similar proteinsi

Entry informationi

Entry nameiRBS5_FLAPR
AccessioniPrimary (citable) accession number: Q39747
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 81 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health