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Protein

Glutamate decarboxylase

Gene

gadA

Organism
Escherichia coli (strain 'clone D i2')
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

Enzyme and pathway databases

BioCyciECOL885276:GJE7-4016-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylaseUniRule annotation (EC:4.1.1.15UniRule annotation)
Gene namesi
Name:gadAImported
Ordered Locus Names:i02_3997Imported
OrganismiEscherichia coli (strain 'clone D i2')Imported
Taxonomic identifieri885276 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000005865: Chromosome

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.

G7R2D9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLPLRINPTF LLPSNKFKEF EMDQKLLTDF RSELLDSRFG AKAISTIAES
60 70 80 90 100
KRFPLHEMRD DVAFQIINDE LYLDGNARQN LATFCQTWDD ENVHKLMDLS
110 120 130 140 150
INKNWIDKEE YPQSAAIDLR CVNMVADLWH APAPKNGQAV GTNTIGSSEA
160 170 180 190 200
CMLGGMAMKW RWRKRMEAAG KPTDKPNLVC GPVQICWHKF ARYWDVELRE
210 220 230 240 250
IPMRPGQLFM DPKRMIEACD ENTIGVVPTF GVTYTGNYEF PQPLHDALDK
260 270 280 290 300
FQADTGIDID MHIDAASGGF LAPFVAPDIV WDFRLPRVKS ISASGHKFGL
310 320 330 340 350
APLGCGWVIW RDEEALPQEL VFNVDYLGGQ IGTFAINFSR PAGQVIAQYY
360 370 380 390 400
EFLRLGREGY TKVQNASYQV AAYLADEIAK LGPYEFICTG RPDEGIPAVC
410 420 430 440 450
FKLKDGEDPG YTLYDLSERL RLRGWQVPAF TLGGEATDIV VMRIMCRRGF
460 470 480
EMDFAELLLE DYKASLKYLS DHPKLQGIAQ QNSFKHT
Length:487
Mass (Da):55,202
Last modified:January 25, 2012 - v1
Checksum:iD9D4B395B8F61060
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002211 Genomic DNA. Translation: AER86524.1.
RefSeqiWP_011076643.1. NC_017651.1.
YP_006151148.1. NC_017651.1.

Genome annotation databases

EnsemblBacteriaiAER86524; AER86524; i02_3997.
GeneIDi12671770.
KEGGield:i02_3997.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002211 Genomic DNA. Translation: AER86524.1.
RefSeqiWP_011076643.1. NC_017651.1.
YP_006151148.1. NC_017651.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAER86524; AER86524; i02_3997.
GeneIDi12671770.
KEGGield:i02_3997.

Phylogenomic databases

KOiK01580.

Enzyme and pathway databases

BioCyciECOL885276:GJE7-4016-MONOMER.

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. "Rates of mutation and host transmission for an Escherichia coli clone over 3 years."
    Reeves P.R., Liu B., Zhou Z., Li D., Guo D., Ren Y., Clabots C., Lan R., Johnson J.R., Wang L.
    PLoS ONE 6:E26907-E26907(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 'clone D i2'Imported.

Entry informationi

Entry nameiG7R2D9_ECOC2
AccessioniPrimary (citable) accession number: G7R2D9
Entry historyi
Integrated into UniProtKB/TrEMBL: January 25, 2012
Last sequence update: January 25, 2012
Last modified: February 4, 2015
This is version 17 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.