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H6M9B6

- H6M9B6_ECOLX

UniProt

H6M9B6 - H6M9B6_ECOLX

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Protein
Submitted name:

Glutamate decarboxylase beta

Gene
ECO55CA74_09085
Organism
Escherichia coli O55:H7 str. RM12579
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

GO - Biological processi

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

Keywords - Molecular functioni

LyaseUniRule annotation

Keywords - Ligandi

Pyridoxal phosphateUniRule annotation

Enzyme and pathway databases

BioCyciECOL1048689:GLD6-1808-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
Glutamate decarboxylase betaImported
Gene namesi
ORF Names:ECO55CA74_09085Imported
OrganismiEscherichia coli O55:H7 str. RM12579Imported
Taxonomic identifieri1048689 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000007173: Chromosome

Structurei

3D structure databases

ProteinModelPortaliH6M9B6.
SMRiH6M9B6. Positions 3-456.

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.UniRule annotation

Phylogenomic databases

KOiK01580.
OMAiPTFQINF.

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.

H6M9B6-1 [UniParc]FASTAAdd to Basket

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MDKKQVTDLR SELLDSRFGA KSISTIAESK 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):52,668
Last modified:April 18, 2012 - v1
Checksum:i8E653330A3C5B4ED
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003109 Genomic DNA. Translation: AEZ40405.1.
RefSeqiYP_006158960.1. NC_017656.1.

Genome annotation databases

EnsemblBacteriaiAEZ40405; AEZ40405; ECO55CA74_09085.
GeneIDi12659339.
KEGGielr:ECO55CA74_09085.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003109 Genomic DNA. Translation: AEZ40405.1 .
RefSeqi YP_006158960.1. NC_017656.1.

3D structure databases

ProteinModelPortali H6M9B6.
SMRi H6M9B6. Positions 3-456.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AEZ40405 ; AEZ40405 ; ECO55CA74_09085 .
GeneIDi 12659339.
KEGGi elr:ECO55CA74_09085.

Phylogenomic databases

KOi K01580.
OMAi PTFQINF.

Enzyme and pathway databases

BioCyci ECOL1048689:GLD6-1808-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

  1. "Escherichia coli Serotype O55:H7 Diversity Supports Parallel Acquisition of Bacteriophage at Shiga Toxin Phage Insertion Sites during Evolution of the O157:H7 Lineage."
    Kyle J.L., Cummings C.A., Parker C.T., Quinones B., Vatta P., Newton E., Huynh S., Swimley M., Degoricija L., Barker M., Fontanoz S., Nguyen K., Patel R., Fang R., Tebbs R., Petrauskene O., Furtado M., Mandrell R.E.
    J. Bacteriol. 194:1885-1896(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RM12579Imported.

Entry informationi

Entry nameiH6M9B6_ECOLX
AccessioniPrimary (citable) accession number: H6M9B6
Entry historyi
Integrated into UniProtKB/TrEMBL: April 18, 2012
Last sequence update: April 18, 2012
Last modified: September 3, 2014
This is version 13 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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