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B4FSJ3 (B4FSJ3_MAIZE) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 40. 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:ZEAMMB73_239374 EMBL AFW64870.1
OrganismZea mays (Maize) [Reference proteome] EMBL ACF85086.1
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Protein attributes

Sequence length170 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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

Ontologies

Keywords
   Biological processCarbon dioxide fixation RuleBase RU003627 SAAS SAAS000894
Photorespiration RuleBase RU003627 SAAS SAAS000894
Photosynthesis RuleBase RU003627 SAAS SAAS000894
   Cellular componentChloroplast SAAS SAAS000894
Plastid
   Molecular functionLyase RuleBase RU003627 SAAS SAAS000894
Monooxygenase RuleBase RU003627 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 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
B4FSJ3 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 4625A5FDED3C2663

FASTA17019,151
        10         20         30         40         50         60 
MAPTVMMASS ATAVAPFQGL KSTASLPVAR RSSRSLGNVS NGGRIRCMQV WPAYGNKKFE 

        70         80         90        100        110        120 
TLSYLPPLST DDLLKQVDYL LRNGWIPCLE FSKVGFVYRE NSTSPCYYDG RYWTMWKLPM 

       130        140        150        160        170 
FGCNDATQVY KELQEAIKSY PDAFHRVIGF DNIKQTQCVS FIAYKPPGSD 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs."
Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J., Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J., Walbot V., Yu Y.
PLoS Genet. 5:E1000740-E1000740(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: B73 EMBL ACF85086.1.
[2]"The B73 maize genome: complexity, diversity, and dynamics."
Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S., Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D., Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K., Fronick C. expand/collapse author list , Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M., Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B., Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E., Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J., Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E., Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A., Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R., Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A., Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E., Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A., Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T., Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L., Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P., Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A., Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C., Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A., Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C., SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W., Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C., Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K., Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K., Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S., Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.
Science 326:1112-1115(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. B73.
[3]Maize Genome Sequencing Project
Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BT040081 mRNA. Translation: ACF85086.1.
BT041047 mRNA. Translation: ACF86052.1.
CM000780 Genomic DNA. Translation: AFW64870.1.
RefSeqNP_001105294.1. NM_001111824.1.
UniGeneZm.72721.

3D structure databases

ProteinModelPortalB4FSJ3.
SMRB4FSJ3. Positions 49-168.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID542212.
KEGGzma:542212.

Phylogenomic databases

KOK01602.
OMAHAFIRII.

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 nameB4FSJ3_MAIZE
AccessionPrimary (citable) accession number: B4FSJ3
Entry history
Integrated into UniProtKB/TrEMBL: September 23, 2008
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)