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A8JGP5 (A8JGP5_CHLRE) Unreviewed, UniProtKB/TrEMBL

Last modified March 19, 2014. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase small chain RuleBase RU003627

EC=4.1.1.39 RuleBase RU003627
Gene names
ORF Names:CHLREDRAFT_108283 EMBL EDO96901.1
OrganismChlamydomonas reinhardtii (Chlamydomonas smithii) [Reference proteome]
Taxonomic identifier3055 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

Protein attributes

Sequence length139 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 SAAS024681

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. RuleBase RU003627 SAAS SAAS024681

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. RuleBase RU003627 SAAS SAAS024681

Subunit structure

8 large chains + 8 small chains By similarity. RuleBase RU003627 SAAS SAAS024681

Sequence similarities

Belongs to the RuBisCO small chain family. RuleBase RU003627

Ontologies

Keywords
   Biological processCarbon dioxide fixation RuleBase RU003627 SAAS SAAS024681
Photorespiration RuleBase RU003627
Photosynthesis RuleBase RU003627 SAAS SAAS024681
   Cellular componentPlastid RuleBase RU003627
   Molecular functionLyase RuleBase RU003627 SAAS SAAS024681
Monooxygenase RuleBase RU003627 SAAS SAAS024681
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbon fixation

Inferred from electronic annotation. Source: UniProtKB-KW

chloroplast ribulose bisphosphate carboxylase complex biogenesis

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

photorespiration

Inferred from electronic annotation. Source: UniProtKB-KW

photosynthesis

Inferred from electronic annotation. Source: UniProtKB-KW

response to blue light

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to cold

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to far red light

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to red light

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Cellular_componentapoplast

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

cell wall

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

chloroplast envelope

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

chloroplast stroma

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

chloroplast thylakoid membrane

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

cytosolic ribosome

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

thylakoid lumen

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Molecular_functioncopper ion binding

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-KW

ribulose-bisphosphate carboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
A8JGP5 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 90CC683FE3607E55

FASTA13916,151
        10         20         30         40         50         60 
MVWTPVNNKM FETFSYLPPL SDEQIAAQVD YIVANGWIPC LEFAESDKAY VSNESAIRFG 

        70         80         90        100        110        120 
SVSCLYYDNR YWTMWKLPMF GCRDPMQVLR EIVACTKAFP DAYVRLVAFD NQKQVQIMGF 

       130 
LVQRPKSARD WQPANKRSV 

« 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: EDO96901.1.
RefSeqXP_001702406.1. XM_001702354.1.
UniGeneCre.15338.

3D structure databases

ProteinModelPortalA8JGP5.
SMRA8JGP5. Positions 1-139.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3055.JGI206640.

Proteomic databases

PRIDEA8JGP5.
ProMEXA8JGP5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsEDO96901; EDO96901; CHLREDRAFT_108283.
GeneID5727946.
KEGGcre:CHLREDRAFT_108283.

Phylogenomic databases

KOK01602.
ProtClustDBCLSN2703923.

Enzyme and pathway databases

BioCycCHLAMY:CHLREDRAFT_108283-MONOMER.

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 nameA8JGP5_CHLRE
AccessionPrimary (citable) accession number: A8JGP5
Entry history
Integrated into UniProtKB/TrEMBL: December 4, 2007
Last sequence update: December 4, 2007
Last modified: March 19, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)