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D5D3N4

- D5D3N4_ECOKI

UniProt

D5D3N4 - D5D3N4_ECOKI

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Protein

Glutamate decarboxylase

Gene

ECOK1_3956

Organism
Escherichia coli O18:K1:H7 (strain IHE3034 / ExPEC)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

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

Enzyme and pathway databases

BioCyciECOL714962:GI9T-3954-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylaseUniRule annotation (EC:4.1.1.15UniRule annotation)
Gene namesi
Ordered Locus Names:ECOK1_3956Imported
OrganismiEscherichia coli O18:K1:H7 (strain IHE3034 / ExPEC)Imported
Taxonomic identifieri714962 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000002364: Chromosome

Structurei

3D structure databases

ProteinModelPortaliD5D3N4.
SMRiD5D3N4. Positions 4-452.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000070228.
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.

D5D3N4-1 [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
PTNKPNLVCG 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):52,684
Last modified:June 15, 2010 - v1
Checksum:i80BF814512F178C2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001969 Genomic DNA. Translation: ADE92844.1.
RefSeqiYP_006103057.1. NC_017628.1.

Genome annotation databases

EnsemblBacteriaiADE92844; ADE92844; ECOK1_3956.
GeneIDi12692522.
KEGGieih:ECOK1_3956.
PATRICi36709420. VBIEscCol148715_3993.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001969 Genomic DNA. Translation: ADE92844.1 .
RefSeqi YP_006103057.1. NC_017628.1.

3D structure databases

ProteinModelPortali D5D3N4.
SMRi D5D3N4. Positions 4-452.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADE92844 ; ADE92844 ; ECOK1_3956 .
GeneIDi 12692522.
KEGGi eih:ECOK1_3956.
PATRICi 36709420. VBIEscCol148715_3993.

Phylogenomic databases

HOGENOMi HOG000070228.
KOi K01580.

Enzyme and pathway databases

BioCyci ECOL714962:GI9T-3954-MONOMER.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: IHE3034 / ExPECImported.
  2. "Identification of protective and broadly conserved vaccine antigens from the genome of Extraintestinal Pathogenic Escherichia coli (ExPEC)."
    Moriel D.G., Bertoldi I., Spagnuolo A., Marchi S., Rosini R., Nesta B., Pastorello I., Mariani Corea V.A., Torricelli G., Cartocci E., Savino S., Scarselli M., Dobrindt U., Hacker J., Tettelin H., Wieler L.H., Ewers C., Picard D.
    , Dougan G., Fontana M.R., Rappuoli R., Pizza M., Serino L.
    Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2010)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: IHE3034.

Entry informationi

Entry nameiD5D3N4_ECOKI
AccessioniPrimary (citable) accession number: D5D3N4
Entry historyi
Integrated into UniProtKB/TrEMBL: June 15, 2010
Last sequence update: June 15, 2010
Last modified: October 1, 2014
This is version 23 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