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P07689

- RBS3_PEA

UniProt

P07689 - RBS3_PEA

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Protein

Ribulose bisphosphate carboxylase small chain 3A, chloroplastic

Gene

RBCS-3A

Organism
Pisum sativum (Garden pea)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein 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 3A, chloroplastic (EC:4.1.1.39)
Short name:
RuBisCO small subunit 3A
Gene namesi
Name:RBCS-3A
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-KW
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 3A, chloroplasticPRO_0000031542Add
BLAST

Interactioni

Subunit structurei

8 large chains + 8 small chains.

Structurei

Secondary structure

1
180
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi63 – 653Combined sources
Turni71 – 744Combined sources
Helixi80 – 9213Combined sources
Beta strandi96 – 1049Combined sources
Beta strandi125 – 1284Combined sources
Helixi137 – 15014Combined sources
Beta strandi155 – 1628Combined sources
Turni163 – 1664Combined sources
Beta strandi167 – 1759Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HHHX-ray2.20S/T/U/V58-180[»]
4MKVX-ray2.15S/T/U/V58-180[»]
ProteinModelPortaliP07689.
SMRiP07689. 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.

P07689-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASMISSSAV TTVSRASTVQ 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):20,231
Last modified:April 1, 1988 - v1
Checksum:i33DAD53A45C0CFE7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04333 Genomic DNA. Translation: CAA27864.1.
M21375 Genomic DNA. Translation: AAA33683.2.
PIRiA27874. RKPMS3.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04333 Genomic DNA. Translation: CAA27864.1 .
M21375 Genomic DNA. Translation: AAA33683.2 .
PIRi A27874. RKPMS3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4HHH X-ray 2.20 S/T/U/V 58-180 [» ]
4MKV X-ray 2.15 S/T/U/V 58-180 [» ]
ProteinModelPortali P07689.
SMRi P07689. Positions 58-180.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.30.190.10. 1 hit.
InterProi IPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
IPR024680. RuBisCO_ssu_N.
[Graphical view ]
Pfami PF12338. RbcS. 1 hit.
PF00101. RuBisCO_small. 1 hit.
[Graphical view ]
PRINTSi PR00152. RUBISCOSMALL.
SUPFAMi SSF55239. SSF55239. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "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 [GENOMIC DNA].
    Strain: cv. Progress No. 9.
  2. "Synthesis of the small subunit of ribulose-bisphosphate carboxylase from genes cloned into plasmids containing the SP6 promoter."
    Anderson S., Smith S.M.
    Biochem. J. 240:709-715(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Identification and characterization of cryptic polyadenylation sites in the 3' region of a pea ribulose-1,5-bisphosphate carboxylase small subunit gene."
    Hunt A.G.
    DNA 7:329-336(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 154-180.

Entry informationi

Entry nameiRBS3_PEA
AccessioniPrimary (citable) accession number: P07689
Secondary accession number(s): P12467
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: November 26, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3