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A8JGP9 (A8JGP9_CHLRE) Unreviewed, UniProtKB/TrEMBL

Last modified May 14, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase small chain RuleBase RU003627

EC=4.1.1.39 RuleBase RU003627
Gene names
Name:RBCS1 EMBL EDO96904.1
ORF Names:CHLREDRAFT_82986 EMBL EDO96904.1
OrganismChlamydomonas reinhardtii (Chlamydomonas smithii) [Reference proteome]
Taxonomic identifier3055 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

Protein attributes

Sequence length185 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. RuleBase RU003627 SAAS SAAS000894

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. RuleBase RU003627 SAAS SAAS000894

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. RuleBase RU003627 SAAS SAAS000894

Subunit structure

8 large chains + 8 small chains By similarity. RuleBase RU003627 SAAS SAAS000894

Sequence similarities

Belongs to the RuBisCO small chain family. RuleBase RU003627

Sequences

Sequence LengthMass (Da)Tools
A8JGP9 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: B4114FD98E807F16

FASTA18520,620
        10         20         30         40         50         60 
MAAVIAKSSV SAAVARPARS SVRPMAALKP AVKAAPVAAP AQANQMMVWT PVNNKMFETF 

        70         80         90        100        110        120 
SYLPPLTDEQ IAAQVDYIVA NGWIPCLEFA EADKAYVSNE SAIRFGSVSC LYYDNRYWTM 

       130        140        150        160        170        180 
WKLPMFGCRD PMQVLREIVA CTKAFPDAYV RLVAFDNQKQ VQIMGFLVQR PKTARDFQPA 


NKRSV 

« Hide

References

[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. expand/collapse author list , 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-503.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS496186 Genomic DNA. Translation: EDO96904.1.
RefSeqXP_001702409.1. XM_001702357.1.
UniGeneCre.3435.

3D structure databases

ProteinModelPortalA8JGP9.
SMRA8JGP9. Positions 47-185.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3055.JGI82986.

Proteomic databases

PRIDEA8JGP9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsEDO96904; EDO96904; CHLREDRAFT_82986.
GeneID5727949.
KEGGcre:CHLREDRAFT_82986.

Phylogenomic databases

KOK01602.
OMACVLAITR.

Family and domain databases

Gene3D3.30.190.10. 1 hit.
InterProIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
[Graphical view]
PfamPF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSPR00152. RUBISCOSMALL.
SMARTSM00961. RuBisCO_small. 1 hit.
[Graphical view]
SUPFAMSSF55239. SSF55239. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA8JGP9_CHLRE
AccessionPrimary (citable) accession number: A8JGP9
Entry history
Integrated into UniProtKB/TrEMBL: December 4, 2007
Last sequence update: December 4, 2007
Last modified: May 14, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)