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A8JGP5 (A8JGP5_CHLRE) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 33. 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
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 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
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...

Protein-protein interaction databases

STRING3055.JGI206640.
A8JGP5.

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. RuBisCO_small. 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: April 3, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)