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K0BQE6

- K0BQE6_ECO1E

UniProt

K0BQE6 - K0BQE6_ECO1E

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Protein

Glutamate decarboxylase

Gene

O3O_24360

Organism
Escherichia coli O104:H4 (strain 2009EL-2071)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi

Functioni

Catalytic activityi

L-glutamate = 4-aminobutanoate + CO2.

Cofactori

Note: Pyridoxal phosphate.UniRule 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_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.
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.
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

« Hide

        10         20         30         40         50
MDQKLLTDFR SELLDSRFGA KAISTIAESK 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):52,685
Last modified:November 28, 2012 - v1
Checksum:i86F963E710553E22
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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...
MobiDBi 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: November 26, 2014
This is version 14 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