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K0BQE6

- K0BQE6_ECO1E

UniProt

K0BQE6 - K0BQE6_ECO1E

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Protein
Submitted name: Glutamate decarboxylase
Gene
O3O_24360
Organism
Escherichia coli O104:H4 (strain 2009EL-2071)
Status
Unreviewed - Annotation score: 1 out of 5 - Protein inferred from homologyi

Functioni

Cofactori

Pyridoxal phosphate By similarity.UniRule annotation

GO - Molecular functioni

  1. glutamate decarboxylase activity Source: InterPro
  2. pyridoxal phosphate binding Source: InterPro
Complete GO annotation...

GO - Biological processi

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

Keywords - Molecular functioni

LyaseUniRule annotation

Keywords - Ligandi

Pyridoxal phosphateUniRule annotation

Names & Taxonomyi

Protein namesi
Submitted name:
Glutamate decarboxylaseImported
Gene namesi
Ordered Locus Names:O3O_24360Imported
OrganismiEscherichia coli O104:H4 (strain 2009EL-2071)Imported
Taxonomic identifieri1133853 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000006093: Chromosome

Structurei

3D structure databases

ProteinModelPortaliK0BQE6.
SMRiK0BQE6. Positions 4-452.

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.
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.

K0BQE6-1 [UniParc]FASTAAdd to Basket

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MDQKLLTDFR SELLDSRFGA KAISTIAESK RFPLHEMRDD VAFQIINDEL    50
YLDGNARQNL ATFCQTWDDE NVHKLMDLSI NKNWIDKEEY PQSAAIDLRC 100
VNMVADLWHA PAPKNGQAVG TNTIGSSEAC MLGGMAMKWR WRKRMEAAGK 150
PTDKPNLVCG PVQICWHKFA RYWDVELREI PMRPGQLFMD PKRMIEACDE 200
NTIGVVPTFG VTYTGNYEFP QPLHDALDKF QADTGIDIDM HIDAASGGFL 250
APFVAPDIVW DFRLPRVKSI SASGHKFGLA PLGCGWVIWR DEEALPQELV 300
FNVDYLGGQI GTFAINFSRP AGQVIAQYYE FLRLGREGYT KVQNASYQVA 350
AYLADEIAKL GPYEFICTGR PDEGIPAVCF KLKDGEDPGY TLYDLSERLR 400
LRGWQVPAFT LGGEATDIVV MRIMCRRGFE MDFAELLLED YKASLKYLSD 450
HPKLQGIAQQ NSFKHT 466
Length:466
Mass (Da):52,685
Last modified:November 28, 2012 - v1
Checksum:i86F963E710553E22
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003301 Genomic DNA. Translation: AFS88585.1.
RefSeqiYP_006782054.1. NC_018661.1.

Genome annotation databases

EnsemblBacteriaiAFS88585; AFS88585; O3O_24360.
GeneIDi13708162.
KEGGieso:O3O_24360.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003301 Genomic DNA. Translation: AFS88585.1 .
RefSeqi YP_006782054.1. NC_018661.1.

3D structure databases

ProteinModelPortali K0BQE6.
SMRi K0BQE6. Positions 4-452.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AFS88585 ; AFS88585 ; O3O_24360 .
GeneIDi 13708162.
KEGGi eso:O3O_24360.

Phylogenomic databases

KOi K01580.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
InterProi IPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR021115. Pyridoxal-P_BS.
[Graphical view ]
Pfami PF00282. Pyridoxal_deC. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR01788. Glu-decarb-GAD. 1 hit.
PROSITEi PS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 2009EL-2071Imported.

Entry informationi

Entry nameiK0BQE6_ECO1E
AccessioniPrimary (citable) accession number: K0BQE6
Entry historyi
Integrated into UniProtKB/TrEMBL: November 28, 2012
Last sequence update: November 28, 2012
Last modified: May 14, 2014
This is version 11 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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