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E8YBY9

- E8YBY9_ECOKO

UniProt

E8YBY9 - E8YBY9_ECOKO

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Protein

Glutamate decarboxylase

Gene

gadA

Organism
Escherichia coli (strain ATCC 55124 / KO11)
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

BioCyciECOL595495:GI1Q-224-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylaseUniRule annotation (EC:4.1.1.15UniRule annotation)
Gene namesi
Name:gadAImported
Ordered Locus Names:EKO11_0222Imported
ORF Names:KO11_05180Imported
OrganismiEscherichia coli (strain ATCC 55124 / KO11)Imported
Taxonomic identifieri595495 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000010089: Chromosome, UP000002250: Chromosome

Structurei

3D structure databases

ProteinModelPortaliE8YBY9.
SMRiE8YBY9. Positions 4-452.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.UniRule annotation

Phylogenomic databases

KOiK01580.
OMAiMIGRLFN.

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.

E8YBY9-1 [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:April 5, 2011 - v1
Checksum:i86F963E710553E22
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002516 Genomic DNA. Translation: ADX48884.1.
CP002970 Genomic DNA. Translation: AFH16023.1.
RefSeqiYP_005275948.1. NC_016902.1.
YP_006163375.1. NC_017660.1.

Genome annotation databases

EnsemblBacteriaiADX48884; ADX48884; EKO11_0222.
AFH16023; AFH16023; KO11_05180.
GeneIDi11775258.
12761220.
KEGGiekf:KO11_05180.
eko:EKO11_0222.
PATRICi48640231. VBIEscCol13896_0222.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002516 Genomic DNA. Translation: ADX48884.1 .
CP002970 Genomic DNA. Translation: AFH16023.1 .
RefSeqi YP_005275948.1. NC_016902.1.
YP_006163375.1. NC_017660.1.

3D structure databases

ProteinModelPortali E8YBY9.
SMRi E8YBY9. Positions 4-452.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADX48884 ; ADX48884 ; EKO11_0222 .
AFH16023 ; AFH16023 ; KO11_05180 .
GeneIDi 11775258.
12761220.
KEGGi ekf:KO11_05180.
eko:EKO11_0222.
PATRICi 48640231. VBIEscCol13896_0222.

Phylogenomic databases

KOi K01580.
OMAi MIGRLFN.

Enzyme and pathway databases

BioCyci ECOL595495:GI1Q-224-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. "Complete sequence of chromosome of Escherichia coli KO11."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Keating D., Landick R., Woyke T.
    Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 55124 / KO11Imported and KO11Imported.
  2. "Optical mapping and sequencing of the Escherichia coli KO11 genome reveal extensive chromosomal rearrangements, and multiple tandem copies of the Zymomonas mobilis pdc and adhB genes."
    Turner P.C., Yomano L.P., Jarboe L.R., York S.W., Baggett C.L., Moritz B.E., Zentz E.B., Shanmugam K.T., Ingram L.O.
    J. Ind. Microbiol. Biotechnol. 39:629-639(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: KO11FLImported.

Entry informationi

Entry nameiE8YBY9_ECOKO
AccessioniPrimary (citable) accession number: E8YBY9
Entry historyi
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: October 29, 2014
This is version 30 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