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B3H5S2 (B3H5S2_ARATH) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 49. 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 names
Gene names
Ordered Locus Names:At5g38410 EMBL AED94313.1 TAIR AT5G38410
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome] EMBL AED94313.1
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length186 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. SAAS SAAS000894

Catalytic activity

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

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

Subunit structure

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

Ontologies

Keywords
   Biological processCarbon dioxide fixation SAAS SAAS000894
Photorespiration SAAS SAAS000894
Photosynthesis SAAS SAAS000894
   Cellular componentChloroplast SAAS SAAS000894
Plastid
   Molecular functionLyase SAAS SAAS000894
Monooxygenase SAAS SAAS000894
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 mutant phenotype PubMed 22223809. Source: TAIR

photorespiration

Inferred from electronic annotation. Source: UniProtKB-KW

photosynthesis

Inferred from mutant phenotype PubMed 22223809. Source: TAIR

response to blue light

Inferred from expression pattern PubMed 18820083. Source: TAIR

response to far red light

Inferred from expression pattern PubMed 18820083. Source: TAIR

response to red light

Inferred from expression pattern PubMed 18820083. Source: TAIR

   Cellular_componentapoplast

Inferred from direct assay PubMed 18538804. Source: TAIR

cell wall

Inferred from direct assay PubMed 15593128. Source: TAIR

chloroplast

Inferred from direct assay PubMed 15028209PubMed 18431481. Source: TAIR

chloroplast envelope

Inferred from direct assay PubMed 20061580. Source: TAIR

chloroplast stroma

Inferred from direct assay PubMed 16207701PubMed 18633119PubMed 20061580. Source: TAIR

cytosolic ribosome

Inferred from direct assay PubMed 15821981. Source: TAIR

membrane

Inferred from direct assay PubMed 17432890. Source: TAIR

thylakoid

Inferred from direct assay PubMed 16648217. Source: TAIR

   Molecular_functionlyase activity

Inferred from electronic annotation. Source: UniProtKB-KW

monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
B3H5S2 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: A03CB892CBE1299F

FASTA18620,840
        10         20         30         40         50         60 
MASSMLSSAA VVTSPAQATM VAPFTGLKSS AAFPVTRKTN KDITSIASNG GRVSCMKVWP 

        70         80         90        100        110        120 
PIGKKKFETL SYLPDLSDVE LAKEVDYLLR NKWIPCVEFE LEVINTKHGF VYREHGNTPG 

       130        140        150        160        170        180 
YYDGRYWTMW KLPLFGCTDS AQVLKEVEEC KKEYPGAFIR IIGFDNTRQV QCISFIAYKP 


PSFTEA 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Kazusa DNA Research Institute, Cold Spring Harbor and Washington University in St Louis Sequencing Consortium, European Union Arabidopsis Genome Sequencing Consortium
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002688 Genomic DNA. Translation: AED94313.1.
RefSeqNP_001119331.1. NM_001125859.1.
UniGeneAt.20381.
At.24772.
At.46639.
At.49098.
At.49366.
At.70032.
At.70053.
At.71313.
At.74604.
At.75410.
At.75674.

3D structure databases

ProteinModelPortalB3H5S2.
SMRB3H5S2. Positions 56-183.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G38410.3; AT5G38410.3; AT5G38410.
GeneID833828.
KEGGath:AT5G38410.

Organism-specific databases

TAIRAT5G38410.

Phylogenomic databases

eggNOGCOG4451.
HOGENOMHOG000141332.
KOK01602.
OMAVKEVEEC.

Family and domain databases

Gene3D3.30.190.10. 1 hit.
InterProIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
IPR024680. RuBisCO_ssu_N.
[Graphical view]
PfamPF12338. RbcS. 1 hit.
PF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSPR00152. RUBISCOSMALL.
SMARTSM00961. RuBisCO_small. 1 hit.
[Graphical view]
SUPFAMSSF55239. SSF55239. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB3H5S2_ARATH
AccessionPrimary (citable) accession number: B3H5S2
Entry history
Integrated into UniProtKB/TrEMBL: July 22, 2008
Last sequence update: July 22, 2008
Last modified: July 9, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)