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Protein

Glutamate decarboxylase

Gene

O3O_12600

Organism
Escherichia coli O104:H4 (strain 2009EL-2071)
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

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylaseUniRule annotation (EC:4.1.1.15UniRule annotation)
Gene namesi
Ordered Locus Names:O3O_12600Imported
OrganismiEscherichia coli O104:H4 (strain 2009EL-2071)Imported
Taxonomic identifieri1133853 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000006093 Componenti: Chromosome

Structurei

3D structure databases

ProteinModelPortaliK0BMX1.
SMRiK0BMX1. Positions 3-456.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.UniRule annotation

Phylogenomic databases

KOiK01580.
OMAiFVGTWMD.

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.
IPR021115. Pyridoxal-P_BS.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.
PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

K0BMX1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKKQVTDLR SELLDSRFGA KSISTIAESK RFPLHEMRDD VAFQIINDEL
60 70 80 90 100
YLDGNARQNL ATFCQTWDDE NVHKLMDLSI NKNWIDKEEY PQSAAIDLRC
110 120 130 140 150
VNMVADLWHA PAPKNGQAVG TNTIGSSEAC MLGGMAMKWR WRKRMEAAGK
160 170 180 190 200
PTDKPNLVCG PVQICWHKFA RYWDVELREI PMRPGQLFMD PKRMIEACDE
210 220 230 240 250
NTIGVVPTFG VTYTGNYEFP QPLHDALDKF QADTGIDIDM HIDAASGGFL
260 270 280 290 300
APFVAPDIVW DFRLPRVKSI SASGHKFGLA PLGCGWVIWR DEEALPQELV
310 320 330 340 350
FNVDYLGGQI GTFAINFSRP AGQVIAQYYE FLRLGREGYT KVQNASYQVA
360 370 380 390 400
AYLADEIAKL GPYEFICTGR PDEGIPAVCF KLKDGEDPGY TLYDLSERLR
410 420 430 440 450
LRGWQVPAFT LGGEATDIVV MRIMCRRGFE MDFAELLLED YKASLKYLSD
460
HPKLQGIAQQ NSFKHT
Length:466
Mass (Da):52,668
Last modified:November 28, 2012 - v1
Checksum:i8E653330A3C5B4ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003301 Genomic DNA. Translation: AFS86272.1.
RefSeqiYP_006784368.1. NC_018661.1.

Genome annotation databases

EnsemblBacteriaiAFS86272; AFS86272; O3O_12600.
KEGGieso:O3O_12600.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003301 Genomic DNA. Translation: AFS86272.1.
RefSeqiYP_006784368.1. NC_018661.1.

3D structure databases

ProteinModelPortaliK0BMX1.
SMRiK0BMX1. Positions 3-456.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAFS86272; AFS86272; O3O_12600.
KEGGieso:O3O_12600.

Phylogenomic databases

KOiK01580.
OMAiFVGTWMD.

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.
IPR021115. Pyridoxal-P_BS.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.
PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genomic comparison of Escherichia coli O104:H4 isolates from 2009 and 2011 reveals plasmid, and prophage heterogeneity, including Shiga toxin encoding phage stx2."
    Threat Characterization Consortium
    Ahmed S.A., Awosika J., Baldwin C., Bishop-Lilly K.A., Biswas B., Broomall S., Chain P.S., Chertkov O., Chokoshvili O., Coyne S., Davenport K., Detter J.C., Dorman W., Erkkila T.H., Folster J.P., Frey K.G., George M., Gleasner C.
    , Henry M., Hill K.K., Hubbard K., Insalaco J., Johnson S., Kitzmiller A., Krepps M., Lo C.C., Luu T., McNew L.A., Minogue T., Munk C.A., Osborne B., Patel M., Reitenga K.G., Rosenzweig C.N., Shea A., Shen X., Strockbine N., Tarr C., Teshima H., van Gieson E., Verratti K., Wolcott M., Xie G., Sozhamannan S., Gibbons H.S.
    PLoS ONE 7:E48228-E48228(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 2009EL-2071Imported.

Entry informationi

Entry nameiK0BMX1_ECO1E
AccessioniPrimary (citable) accession number: K0BMX1
Entry historyi
Integrated into UniProtKB/TrEMBL: November 28, 2012
Last sequence update: November 28, 2012
Last modified: April 1, 2015
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete 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.