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

Gene

PHYPADRAFT_125839

Organism
Physcomitrella patens subsp. patens (Moss)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

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.UniRule annotationSAAS 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

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

GO - Biological processi

  1. carbon fixation Source: UniProtKB-KW
  2. photorespiration Source: UniProtKB-KW
  3. photosynthesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationSAAS annotation, MonooxygenaseUniRule annotationSAAS annotation, Oxidoreductase

Keywords - Biological processi

Carbon dioxide fixationUniRule annotationSAAS annotation, PhotorespirationUniRule annotation, PhotosynthesisUniRule annotationSAAS annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase small chainUniRule annotation (EC:4.1.1.39UniRule annotation)
Gene namesi
ORF Names:PHYPADRAFT_125839Imported
OrganismiPhyscomitrella patens subsp. patens (Moss)Imported
Taxonomic identifieri3218 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaBryophytaBryophytinaBryopsidaFunariidaeFunarialesFunariaceaePhyscomitrella
ProteomesiUP000006727 Componenti: Partially assembled WGS sequence

Subcellular locationi

GO - Cellular componenti

  1. plastid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

PlastidUniRule annotation

Interactioni

Subunit structurei

8 large chains + 8 small chains.UniRule annotationSAAS annotation

Protein-protein interaction databases

STRINGi3218.JGI125839.

Structurei

3D structure databases

ProteinModelPortaliA9S8M9.
SMRiA9S8M9. Positions 63-181.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO small chain family.UniRule annotation

Phylogenomic databases

InParanoidiA9S8M9.
KOiK01602.

Family and domain databases

Gene3Di3.30.190.10. 1 hit.
InterProiIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
[Graphical view]
PfamiPF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSiPR00152. RUBISCOSMALL.
SUPFAMiSSF55239. SSF55239. 1 hit.

Sequencei

Sequence statusi: Complete.

A9S8M9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVVAASSA VAPAAAFGAA SSGVSTSEAT SVKAFSGLKS ATLFSGNAQT
60 70 80 90 100
LSSVQNGSRV QCMQVWNPIG MTKFETFSYL PPLSDDAIAK QVEYMIQQKL
110 120 130 140 150
IPCLEFDNSN GVSRVNNSSP GYYDGRYWTM WKLPMFGCQD SAQVLREIEE
160 170 180
CKTTFPGCYV RVLGFDNVKQ VQICGFLVAR PN
Length:182
Mass (Da):19,683
Last modified:February 5, 2008 - v1
Checksum:iC26AE4238C5D8448
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS544945 Genomic DNA. Translation: EDQ72463.1.
RefSeqiXP_001762664.1. XM_001762612.1.
UniGeneiPpa.14452.

Genome annotation databases

GeneIDi5925847.
KEGGippp:PHYPADRAFT_125839.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS544945 Genomic DNA. Translation: EDQ72463.1.
RefSeqiXP_001762664.1. XM_001762612.1.
UniGeneiPpa.14452.

3D structure databases

ProteinModelPortaliA9S8M9.
SMRiA9S8M9. Positions 63-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3218.JGI125839.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5925847.
KEGGippp:PHYPADRAFT_125839.

Phylogenomic databases

InParanoidiA9S8M9.
KOiK01602.

Family and domain databases

Gene3Di3.30.190.10. 1 hit.
InterProiIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
[Graphical view]
PfamiPF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSiPR00152. RUBISCOSMALL.
SUPFAMiSSF55239. SSF55239. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The Physcomitrella genome reveals evolutionary insights into the conquest of land by plants."
    Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H., Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T., Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A., Suzuki Y.
    , Hashimoto S.-I., Yamaguchi K., Sugano A., Kohara Y., Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E., Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M., Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J., Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B., Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A., Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y., Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M., Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S., Boore J.L.
    Science 319:64-69(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Gransden 2004Imported.

Entry informationi

Entry nameiA9S8M9_PHYPA
AccessioniPrimary (citable) accession number: A9S8M9
Entry historyi
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: February 4, 2015
This is version 44 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.