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Protein

Ribulose bisphosphate carboxylase small chain 3C, chloroplastic

Gene

RBCS-3C

Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 3 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).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

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

GO - Biological processi

  1. photorespiration Source: UniProtKB-KW
  2. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase small chain 3C, chloroplastic (EC:4.1.1.39)
Short name:
RuBisCO small subunit 3C
Alternative name(s):
PSS15
Gene namesi
Name:RBCS-3C
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5757ChloroplastBy similarityAdd
BLAST
Chaini58 – 180123Ribulose bisphosphate carboxylase small chain 3C, chloroplasticPRO_0000031541Add
BLAST

Interactioni

Subunit structurei

8 large chains + 8 small chains.

Structurei

3D structure databases

ProteinModelPortaliP00869.
SMRiP00869. Positions 58-180.
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.
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.

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

P00869-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASMISSSAV TTVSRASRGQ SAAVAPFGGL KSMTGFPVKK VNTDITSITS
60 70 80 90 100
NGGRVKCMQV WPPIGKKKFE TLSYLPPLTR DQLLKEVEYL LRKGWVPCLE
110 120 130 140 150
FELEKGFVYR EHNKSPGYYD GRYWTMWKLP MFGTTDASQV LKELDEVVAA
160 170 180
YPQAFVRIIG FDNVRQVQCI SFIAHTPESY
Length:180
Mass (Da):20,244
Last modified:July 21, 1986 - v1
Checksum:i212653E76E55205C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251A → G in AAA33686. (PubMed:6296093)Curated
Sequence conflicti32 – 321S → F in AAA33686. (PubMed:6296093)Curated
Sequence conflicti117 – 1171G → R in AAA33686. (PubMed:6296093)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01257 mRNA. Translation: AAA33686.1.
X00806 Genomic DNA. Translation: CAA25390.1.
X04334 Genomic DNA. Translation: CAA27865.1.
PIRiA01088. RKPMS5.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01257 mRNA. Translation: AAA33686.1.
X00806 Genomic DNA. Translation: CAA25390.1.
X04334 Genomic DNA. Translation: CAA27865.1.
PIRiA01088. RKPMS5.

3D structure databases

ProteinModelPortaliP00869.
SMRiP00869. Positions 58-180.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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. "Tissue-specific and light-regulated expression of a pea nuclear gene encoding the small subunit of ribulose-1,5-bisphosphate carboxylase."
    Coruzzi G., Broglie R., Edwards C., Chua N.-H.
    EMBO J. 3:1671-1679(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (PSS15).
    Strain: cv. Progress No. 9.
  2. "Expression dynamics of the pea rbcS multigene family and organ distribution of the transcripts."
    Fluhr R., Moses P., Morelli G., Coruzzi G., Chua N.-H.
    EMBO J. 5:2063-2071(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (RBCS-3C).
  3. "Nucleotide sequences of two pea cDNA clones encoding the small subunit of ribulose 1,5-bisphosphate carboxylase and the major chlorophyll a/b-binding thylakoid polypeptide."
    Coruzzi G., Broglie R., Cashmore A., Chua N.-H.
    J. Biol. Chem. 258:1399-1402(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-180.

Entry informationi

Entry nameiRBS2_PEA
AccessioniPrimary (citable) accession number: P00869
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 7, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.