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B7FHB2 (B7FHB2_MEDTR) Unreviewed, UniProtKB/TrEMBL

Last modified May 14, 2014. Version 25. 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:MTR_6g018310 EMBL AES74954.1
OrganismMedicago truncatula (Barrel medic) (Medicago tribuloides) EMBL ACJ84141.1
Taxonomic identifier3880 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

Protein attributes

Sequence length180 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. SAAS SAAS000894 RuleBase RU003627

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. SAAS SAAS000894 RuleBase RU003627

Sequence similarities

Belongs to the RuBisCO small chain family. RuleBase RU003627

Ontologies

Keywords
   Biological processCarbon dioxide fixation SAAS SAAS000894 RuleBase RU003627
Photorespiration SAAS SAAS000894 RuleBase RU003627
Photosynthesis SAAS SAAS000894 RuleBase RU003627
   Cellular componentChloroplast SAAS SAAS000894
Plastid
   Molecular functionLyase SAAS SAAS000894 RuleBase RU003627
Monooxygenase SAAS SAAS000894 RuleBase RU003627
Oxidoreductase
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

chloroplast envelope

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
B7FHB2 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 257E04D0C06B40B1

FASTA18020,039
        10         20         30         40         50         60 
MALISSAAVT TVSRASSTQA NLVAPFTGLK SSAAFPVTKK TNNDITSIAS NGGRVNCMQV 

        70         80         90        100        110        120 
WPPIGKKKFE TLSYLPPLTE EQLAKEVEYL IRKGWVPCLE FELEKGFVYR ENHSSPGYYD 

       130        140        150        160        170        180 
GRYWTMWKLP LFGATDSSQV LKELAEAKAA YPESFIRIIG FDNVRQVQCI SFIAHTPATY 

« Hide

References

[1]"Medicago truncatula full length cdna cloning project."
Moskal W., Chan A., Cheung F., Xiao Y., Town C.D.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[2]"The Medicago genome provides insight into the evolution of rhizobial symbioses."
Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K., Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S., Krishnakumar V. expand/collapse author list , Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y., Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L., Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.
Nature 480:520-524(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A17 EMBL AES74954.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BT051477 mRNA. Translation: ACJ84141.1.
CM001222 Genomic DNA. Translation: AES74954.1.
RefSeqXP_003618736.1. XM_003618688.1.
UniGeneMtr.22210.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Proteomic databases

ProMEXB7FHB2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID11416005.
KEGGmtr:MTR_6g018310.

Phylogenomic databases

KOK01602.
OMAAFPATRK.

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.
SUPFAMSSF55239. SSF55239. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB7FHB2_MEDTR
AccessionPrimary (citable) accession number: B7FHB2
Entry history
Integrated into UniProtKB/TrEMBL: February 10, 2009
Last sequence update: February 10, 2009
Last modified: May 14, 2014
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)