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P69908 (DCEA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate decarboxylase alpha

Short name=GAD-alpha
EC=4.1.1.15
Gene names
Name:gadA
Synonyms:gadS
Ordered Locus Names:b3517, JW3485
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria.

Catalytic activity

L-glutamate = 4-aminobutanoate + CO2.

Cofactor

Pyridoxal phosphate.

Subunit structure

Homohexamer.

Induction

By acidic conditions. Expression is regulated by a complex system involving RpoS, cAMP, CRP, EvgAS, H-NS, GadE, GadW and GadX. The level of involvement for each regulator varies depending upon the growth phase and the medium. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

Sequence similarities

Belongs to the group II decarboxylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Glutamate decarboxylase alpha
PRO_0000146978

Regions

Region126 – 1272Pyridoxal phosphate binding By similarity

Sites

Binding site621Substrate By similarity
Binding site831Substrate By similarity
Binding site2121Pyridoxal phosphate By similarity
Binding site2751Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2761N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict641C → S AA sequence Ref.2
Sequence conflict731H → R AA sequence Ref.2
Sequence conflict1531D → N AA sequence Ref.2
Sequence conflict1651C → S in CAA44834. Ref.2
Sequence conflict2081T → N in CAA44834. Ref.2
Sequence conflict2951L → V in CAA44834. Ref.2
Sequence conflict3551D → N AA sequence Ref.2

Secondary structure

.......................................................................... 466
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P69908 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 86F963E710553E22

FASTA46652,685
        10         20         30         40         50         60 
MDQKLLTDFR SELLDSRFGA KAISTIAESK RFPLHEMRDD VAFQIINDEL YLDGNARQNL 

        70         80         90        100        110        120 
ATFCQTWDDE NVHKLMDLSI NKNWIDKEEY PQSAAIDLRC VNMVADLWHA PAPKNGQAVG 

       130        140        150        160        170        180 
TNTIGSSEAC MLGGMAMKWR WRKRMEAAGK PTDKPNLVCG PVQICWHKFA RYWDVELREI 

       190        200        210        220        230        240 
PMRPGQLFMD PKRMIEACDE NTIGVVPTFG VTYTGNYEFP QPLHDALDKF QADTGIDIDM 

       250        260        270        280        290        300 
HIDAASGGFL APFVAPDIVW DFRLPRVKSI SASGHKFGLA PLGCGWVIWR DEEALPQELV 

       310        320        330        340        350        360 
FNVDYLGGQI GTFAINFSRP AGQVIAQYYE FLRLGREGYT KVQNASYQVA AYLADEIAKL 

       370        380        390        400        410        420 
GPYEFICTGR PDEGIPAVCF KLKDGEDPGY TLYDLSERLR LRGWQVPAFT LGGEATDIVV 

       430        440        450        460 
MRIMCRRGFE MDFAELLLED YKASLKYLSD HPKLQGIAQQ NSFKHT 

« Hide

References

« Hide 'large scale' references
[1]"Escherichia coli has two homologous glutamate decarboxylase genes that map to distinct loci."
Smith D.K., Kassam T., Singh B., Elliott J.F.
J. Bacteriol. 174:5820-5826(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"The amino acid sequence of glutamate decarboxylase from Escherichia coli. Evolutionary relationship between mammalian and bacterial enzymes."
Maras B., Sweeney G., Barra D., Bossa F., John R.A.
Eur. J. Biochem. 204:93-98(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 148-466.
Strain: ATCC 11246.
[3]"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Expression of the Escherichia coli dimorphic glutamic acid decarboxylases is regulated by the nucleoid protein H-NS."
Yoshida T., Yamashino T., Ueguchi C., Mizuno T.
Biosci. Biotechnol. Biochem. 57:1568-1569(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-22.
[7]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 382-392.
Strain: K12 / EMG2.
[8]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[9]"The response to stationary-phase stress conditions in Escherichia coli: role and regulation of the glutamic acid decarboxylase system."
De Biase D., Tramonti A., Bossa F., Visca P.
Mol. Microbiol. 32:1198-1211(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: TRANSCRIPTIONAL REGULATION.
Strain: ATCC 11246.
[10]"Functional characterization and regulation of gadX, a gene encoding an AraC/XylS-like transcriptional activator of the Escherichia coli glutamic acid decarboxylase system."
Tramonti A., Visca P., De Canio M., Falconi M., De Biase D.
J. Bacteriol. 184:2603-2613(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TRANSCRIPTIONAL REGULATION.
Strain: ATCC 11246.
[11]"Escherichia coli gene expression responsive to levels of the response regulator EvgA."
Masuda N., Church G.M.
J. Bacteriol. 184:6225-6234(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TRANSCRIPTIONAL REGULATION.
Strain: K12 / MG1655 / ATCC 47076.
[12]"Collaborative regulation of Escherichia coli glutamate-dependent acid resistance by two AraC-like regulators, GadX and GadW (YhiW)."
Ma Z., Richard H., Tucker D.L., Conway T., Foster J.W.
J. Bacteriol. 184:7001-7012(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TRANSCRIPTIONAL REGULATION.
Strain: K12.
[13]"Transcriptional expression of Escherichia coli glutamate-dependent acid resistance genes gadA and gadBC in an hns rpoS mutant."
Waterman S.R., Small P.L.C.
J. Bacteriol. 185:4644-4647(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TRANSCRIPTIONAL REGULATION.
[14]"Regulatory network of acid resistance genes in Escherichia coli."
Masuda N., Church G.M.
Mol. Microbiol. 48:699-712(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TRANSCRIPTIONAL REGULATION.
Strain: K12 / MG1655 / ATCC 47076.
[15]"GadE (YhiE) activates glutamate decarboxylase-dependent acid resistance in Escherichia coli K-12."
Ma Z., Gong S., Richard H., Tucker D.L., Conway T., Foster J.W.
Mol. Microbiol. 49:1309-1320(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TRANSCRIPTIONAL REGULATION.
Strain: K12.
[16]"Structure of the complex of Escherichia coli glutamate decarboxylase (gadA) with glutarate at 2.05 A resolution."
Dutyshev D.I., Darii E.L., Fomenkova N.P., Pechik I.V., Polyakov K.M., Nikonov S.V., Andreeva N.S., Sukhareva B.S.
Submitted (SEP-2004) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M84024 Genomic DNA. Translation: AAA23833.1.
X63123 Genomic DNA. Translation: CAA44834.1.
U00039 Genomic DNA. Translation: AAB18493.1.
U00096 Genomic DNA. Translation: AAC76542.1.
AP009048 Genomic DNA. Translation: BAE77777.1.
PIRS24234. S47737.
RefSeqNP_417974.1. NC_000913.3.
YP_491918.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XEYX-ray2.05A/B1-466[»]
ProteinModelPortalP69908.
SMRP69908. Positions 4-452.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36201N.
IntActP69908. 14 interactions.
MINTMINT-1224142.
STRING511145.b3517.

Proteomic databases

PRIDEP69908.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76542; AAC76542; b3517.
BAE77777; BAE77777; BAE77777.
GeneID12932603.
948027.
KEGGecj:Y75_p3660.
eco:b3517.
PATRIC32122496. VBIEscCol129921_3626.

Organism-specific databases

EchoBASEEB4302.
EcoGeneEG50009. gadA.

Phylogenomic databases

HOGENOMHOG000070228.
KOK01580.
OMAPNLVMSS.
OrthoDBEOG6TFCPW.
PhylomeDBP69908.
ProtClustDBCLSK880040.

Enzyme and pathway databases

BioCycEcoCyc:GLUTDECARBOXA-MONOMER.
ECOL316407:JW3485-MONOMER.
MetaCyc:GLUTDECARBOXA-MONOMER.

Gene expression databases

GenevestigatorP69908.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
InterProIPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR021115. Pyridoxal-P_BS.
[Graphical view]
PANTHERPTHR11999:SF1. PTHR11999:SF1. 1 hit.
PfamPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01788. Glu-decarb-GAD. 1 hit.
PROSITEPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP69908.
PROP69908.

Entry information

Entry nameDCEA_ECOLI
AccessionPrimary (citable) accession number: P69908
Secondary accession number(s): P80063, Q2M7H9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: April 16, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene