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Protein

Glutamate decarboxylase

Gene

SACTE_2860

Organism
Streptomyces sp. (strain SirexAA-E / ActE)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

L-glutamate = 4-aminobutanoate + CO2.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

GO - Molecular functioni

  1. glutamate decarboxylase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. glutamate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

DecarboxylaseUniRule annotation, Lyase

Keywords - Ligandi

Pyridoxal phosphateUniRule annotation

Enzyme and pathway databases

BioCyciSSP862751:GHMW-2903-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylaseUniRule annotation (EC:4.1.1.15UniRule annotation)
Gene namesi
ORF Names:SACTE_2860Imported
OrganismiStreptomyces sp. (strain SirexAA-E / ActE)Imported
Taxonomic identifieri862751 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces
ProteomesiUP000001397: Chromosome

Structurei

3D structure databases

ProteinModelPortaliG2NEK5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.UniRule annotation

Phylogenomic databases

KOiK01580.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11999:SF1. PTHR11999:SF1. 1 hit.
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.

Sequencei

Sequence statusi: Complete.

G2NEK5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLHKGSSGA DASEEHRRLA LNPFFGEADP TVPMTAAPPR HRLPDGPMPS
60 70 80 90 100
SSAYRLVHDE LMLDGNSRLN LATFVTTWME PQAGVLMGEC RDKNMIDKDE
110 120 130 140 150
YPRTAELERR CVAMLADLWN APDPQAVVGC STTGSSEACM LAGMALKRRW
160 170 180 190 200
STRNADRYPA HARPNLVMGV NVQVCWEKFC TFWEVEARQV PMEGERFHLD
210 220 230 240 250
PQAAMELCDE NTIGVVGILG STFDGSYEPI AELCAALDEL QERTGLDIPV
260 270 280 290 300
HVDGASGAMV APFLDEDLEW DFRLPRVASV NTSGHKYGLV YPGVGWVLWR
310 320 330 340 350
SSAELPEELV FRVNYLGGDM PTFALNFSRP GAQVVAQYYT FLRLGRDGYR
360 370 380 390 400
AVQQTSRDIA MRLAGEFETL GDFRLLGRGD ELPVFALTTR PDVQAYDVFD
410 420 430 440 450
VSRRLRERGW LVPAYTFPAN RQDLAVLRVV CRNGFSSDLA ELLMDDVRRL
460 470
LPELRAQPHP LGPGRAAQTA FHH
Length:473
Mass (Da):52,742
Last modified:November 16, 2011 - v1
Checksum:iE030647588FFCF64
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002993 Genomic DNA. Translation: AEN10737.1.
RefSeqiYP_004803277.1. NC_015953.1.

Genome annotation databases

EnsemblBacteriaiAEN10737; AEN10737; SACTE_2860.
GeneIDi11100722.
KEGGissx:SACTE_2860.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002993 Genomic DNA. Translation: AEN10737.1.
RefSeqiYP_004803277.1. NC_015953.1.

3D structure databases

ProteinModelPortaliG2NEK5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAEN10737; AEN10737; SACTE_2860.
GeneIDi11100722.
KEGGissx:SACTE_2860.

Phylogenomic databases

KOiK01580.

Enzyme and pathway databases

BioCyciSSP862751:GHMW-2903-MONOMER.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11999:SF1. PTHR11999:SF1. 1 hit.
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Biochemical Properties and Atomic Resolution Structure of a Proteolytically Processed beta-Mannanase from Cellulolytic Streptomyces sp. SirexAA-E."
    Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F., Book A.J., Currie C.R., Fox B.G.
    PLoS ONE 9:E94166-E94166(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SirexAA-EImported.

Entry informationi

Entry nameiG2NEK5_STREK
AccessioniPrimary (citable) accession number: G2NEK5
Entry historyi
Integrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: November 16, 2011
Last modified: February 4, 2015
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.