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Protein

Ribulose bisphosphate carboxylase small chain

Gene

RBCS1

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Unreviewed-Annotation score: Annotation score: 3 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 annotation
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 annotation, PhotosynthesisUniRule annotationSAAS annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase small chainUniRule annotation (EC:4.1.1.39UniRule annotation)
Gene namesi
Name:RBCS1Imported
ORF Names:CHLREDRAFT_82986Imported
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)Imported
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas
ProteomesiUP000006906 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

PlastidUniRule annotation

PTM / Processingi

Proteomic databases

PRIDEiA8JGP9.

Interactioni

Subunit structurei

8 large chains + 8 small chains.UniRule annotationSAAS annotation

Protein-protein interaction databases

STRINGi3055.EDO96904.

Structurei

3D structure databases

ProteinModelPortaliA8JGP9.
SMRiA8JGP9. Positions 47-185.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO small chain family.UniRule annotation

Phylogenomic databases

InParanoidiA8JGP9.
KOiK01602.
OMAiRDFQPAN.

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

Sequencei

Sequence statusi: Complete.

A8JGP9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVIAKSSV SAAVARPARS SVRPMAALKP AVKAAPVAAP AQANQMMVWT
60 70 80 90 100
PVNNKMFETF SYLPPLTDEQ IAAQVDYIVA NGWIPCLEFA EADKAYVSNE
110 120 130 140 150
SAIRFGSVSC LYYDNRYWTM WKLPMFGCRD PMQVLREIVA CTKAFPDAYV
160 170 180
RLVAFDNQKQ VQIMGFLVQR PKTARDFQPA NKRSV
Length:185
Mass (Da):20,620
Last modified:December 4, 2007 - v1
Checksum:iB4114FD98E807F16
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS496186 Genomic DNA. Translation: EDO96904.1.
RefSeqiXP_001702409.1. XM_001702357.1.
UniGeneiCre.3435.

Genome annotation databases

EnsemblPlantsiEDO96904; EDO96904; CHLREDRAFT_82986.
GeneIDi5727949.
KEGGicre:CHLREDRAFT_82986.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS496186 Genomic DNA. Translation: EDO96904.1.
RefSeqiXP_001702409.1. XM_001702357.1.
UniGeneiCre.3435.

3D structure databases

ProteinModelPortaliA8JGP9.
SMRiA8JGP9. Positions 47-185.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3055.EDO96904.

Proteomic databases

PRIDEiA8JGP9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiEDO96904; EDO96904; CHLREDRAFT_82986.
GeneIDi5727949.
KEGGicre:CHLREDRAFT_82986.

Phylogenomic databases

InParanoidiA8JGP9.
KOiK01602.
OMAiRDFQPAN.

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

Publicationsi

  1. "The Chlamydomonas genome reveals the evolution of key animal and plant functions."
    Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J., Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L., Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H., Kapitonov V.V., Ren Q., Ferris P.
    , Lindquist E., Shapiro H., Lucas S.M., Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L., Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H., Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M., Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A., Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L., Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C., Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J., Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L., Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L., Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C., Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J., Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P., Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R., Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P., Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y., Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L., Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.
    Science 318:245-250(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CC-503Imported.

Entry informationi

Entry nameiA8JGP9_CHLRE
AccessioniPrimary (citable) accession number: A8JGP9
Entry historyi
Integrated into UniProtKB/TrEMBL: December 4, 2007
Last sequence update: December 4, 2007
Last modified: July 22, 2015
This is version 48 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.