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P58228 (DCEA_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:Z4930, ECs4397
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

L-glutamate = 4-aminobutanoate + CO2.

Cofactor

Pyridoxal phosphate By similarity.

Subunit structure

Homohexamer By similarity.

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 By similarity.

Sequence similarities

Belongs to the group II decarboxylase family.

Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglutamate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionglutamate decarboxylase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Glutamate decarboxylase alpha
PRO_0000146980

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 By similarity

Sequences

Sequence LengthMass (Da)Tools
P58228 [UniParc].

Last modified August 14, 2001. Version 1.
Checksum: C7F9623DBB24E489

FASTA46652,699
        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 KLKEGEDPGY TLYDLSERLR LRGWQVPAFT LGGEATDIVV 

       430        440        450        460 
MRIMCRRGFE MDFAELLLED YKASLKYLSD HPKLQGIAQQ NSFKHT

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed: 11206551] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005174 Genomic DNA. Translation: AAG58658.1.
BA000007 Genomic DNA. Translation: BAB37820.1.
PIRE91178.
F86024.
RefSeqNP_290097.1. NC_002655.2.
NP_312424.1. NC_002695.1.

3D structure databases

ProteinModelPortalP58228.
SMRP58228. Positions 12-466.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000027593; EBESCP00000026486; EBESCG00000026645.
EBESCT00000056144; EBESCP00000053972; EBESCG00000055192.
GeneID915746.
961141.
GenomeReviewsGene locus Z4930 in contig AE005174_GR.
Gene locus ECs4397 in contig BA000007_GR.
KEGGece:Z4930.
ecs:ECs4397.
PATRIC18358373. VBIEscCol44059_4353.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000008325.
HOGENOMHBG365574.
OMALPLRINP.
ProtClustDBCLSK880040.

Enzyme and pathway databases

BioCycECOL83334:ECS4397-MONOMER.

Family and domain databases

InterProIPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR021115. Pyridoxal-P_BS.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
KOK01580.
PANTHERPTHR11999:SF1. Glu_decarb_GAD. 1 hit.
PTHR11999. Pyridoxal_deC. 1 hit.
PfamPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01788. Glu-decarb-GAD. 1 hit.
PROSITEPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDCEA_ECO57
AccessionPrimary (citable) accession number: P58228
Entry history
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: August 14, 2001
Last modified: January 25, 2012
This is version 68 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

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