Glutamate decarboxylase beta - Escherichia coli O157:H7

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P69911 (DCEB_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glutamate decarboxylase beta
Short name=GAD-beta
EC=4.1.1.15

Gene names

Name:	gadB
Ordered Locus Names:	Z2215, ECs2098

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Protein existence	Evidence 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 composed of three dimers 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
Ligand	Pyridoxal phosphate
Molecular function	Decarboxylase Lyase
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glutamate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	glutamate decarboxylase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 466

466

Glutamate decarboxylase beta

PRO_0000146984

Regions

Region

126 – 127

Pyridoxal phosphate binding By similarity

Sites

Binding site

Substrate By similarity

Binding site

Substrate By similarity

Binding site

212

Pyridoxal phosphate By similarity

Binding site

275

Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue

276

N6-(pyridoxal phosphate)lysine By similarity

Modified residue

446

N6-acetyllysine By similarity

Modified residue

453

N6-acetyllysine By similarity

Modified residue

464

N6-acetyllysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P69911 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 8E653330A3C5B4ED
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FASTA

466

52,668

        10         20         30         40         50         60 
MDKKQVTDLR SELLDSRFGA KSISTIAESK 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

[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. 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. , 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG56275.1. BA000007 Genomic DNA. Translation: BAB35521.1.
PIR	B90891. G85726.
RefSeq	NP_287662.1. NC_002655.2. NP_310125.1. NC_002695.1.
3D structure databases
ProteinModelPortal	P69911.
SMR	P69911. Positions 3-456.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000028239; EBESCP00000027132; EBESCG00000027290. EBESCT00000060078; EBESCP00000057906; EBESCG00000059125.
GeneID	917300. 960675.
GenomeReviews	Gene locus Z2215 in contig AE005174_GR. Gene locus ECs2098 in contig BA000007_GR.
KEGG	ece:Z2215. ecs:ECs2098.
PATRIC	18353149. VBIEscCol44059_1794.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000008325.
HOGENOM	HBG365574.
OMA	YPRTAEL.
ProtClustDB	CLSK880040.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS2098-MONOMER.
Family and domain databases
InterPro	IPR010107. 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]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
KO	K01580.
PANTHER	PTHR11999:SF1. Glu_decarb_GAD. 1 hit. PTHR11999. Pyridoxal_deC. 1 hit.
Pfam	PF00282. Pyridoxal_deC. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01788. Glu-decarb-GAD. 1 hit.
PROSITE	PS00392. DDC_GAD_HDC_YDC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DCEB_ECO57

Accession

Primary (citable) accession number: P69911
Secondary accession number(s): P28302, P76873

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	January 4, 2005
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents