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Protein

Glutamate decarboxylase

Gene

gadA

Organism
Escherichia coli O1:K1 / APEC
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphateUniRule 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
Name:gadAImported
ORF Names:APECO1_621Imported
OrganismiEscherichia coli O1:K1 / APECImported
Taxonomic identifieri405955 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000008216 Componenti: Chromosome

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0076.
HOGENOMiHOG000070228.
KOiK01580.
OrthoDBiEOG6TFCPW.

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.

A1AB81-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRDDVAFQII NDELYLDGNA RQNLATFCQT WDDXNVHKLM DLSINKNWID
60 70 80 90 100
KEEYPQSAAI DLRCVNMVAD LWHAPAPKNG QAVGTNTIGS SEACMLGGMA
110 120 130 140 150
MKWRWRKRME AAGKPTNKPN LVCGPVQICW HKFARYWDVE LREIPMRPGQ
160 170 180 190 200
LFMDPKRMIE ACDENTIGVV PTFGVTYTGN YEFPQPLHDA LDKFQADTGI
210 220 230 240 250
DIDMHIDAAS GGFLAPFVAP DIVWDFRLPR VKSISASGHK FGLAPLGCGW
260 270 280 290 300
VIWRDEEALP QELVFNVDYL GGQIGTFAIN FSRPAGQVIA QYYEFLRLGR
310 320 330 340 350
EGYTKVQNAS YQVAAYLADE IAKLGPYEFI CTGRPDEGIP AVCFKLKDGE
360 370 380 390 400
DPGYTLYDLS ERLRLRGWQV PAFTLGGEAT DIVVMRIMCR RGFEMDFAEL
410 420 430
LLEDYKASLK YLSDHPKLQG IAQQNSFKHT
Length:430
Mass (Da):48,533
Last modified:January 23, 2007 - v1
Checksum:i8A9494AA2356751E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000468 Genomic DNA. Translation: ABJ00921.1.
RefSeqiWP_011703568.1. NC_008563.1.
YP_852635.1. NC_008563.1.

Genome annotation databases

EnsemblBacteriaiABJ00921; ABJ00921; APECO1_621.
KEGGiecv:APECO1_621.
PATRICi18214666. VBIEscCol127180_1612.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000468 Genomic DNA. Translation: ABJ00921.1.
RefSeqiWP_011703568.1. NC_008563.1.
YP_852635.1. NC_008563.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABJ00921; ABJ00921; APECO1_621.
KEGGiecv:APECO1_621.
PATRICi18214666. VBIEscCol127180_1612.

Phylogenomic databases

eggNOGiCOG0076.
HOGENOMiHOG000070228.
KOiK01580.
OrthoDBiEOG6TFCPW.

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]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 shares strong similarities with human extraintestinal pathogenic E. coli genomes."
    Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.
    J. Bacteriol. 189:3228-3236(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: APEC O1Imported.

Entry informationi

Entry nameiA1AB81_ECOK1
AccessioniPrimary (citable) accession number: A1AB81
Entry historyi
Integrated into UniProtKB/TrEMBL: January 23, 2007
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 51 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.