Reviewed, UniProtKB/Swiss-Prot P58228 (DCEA_ECO57)

Names and origin

Protein names

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

Gene names

Name:	gadA
Synonyms:	gadS
Ordered Locus Names:	Z4930, ECs4397

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 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
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 alpha		PRO_0000146980
Regions
	Region	126 – 127	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	62	1	Substrate By similarity
	Binding site	83	1	Substrate By similarity
	Binding site	212	1	Pyridoxal phosphate By similarity
	Binding site	275	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	276	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P58228-1 [UniParc]. Last modified August 14, 2001. Version 1. Checksum: C7F9623DBB24E489	FASTA	466	52,699
	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

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. , 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. , 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.
PIR	E91178. F86024.
RefSeq	NP_290097.1. NP_312424.1.
3D structure databases
SMR	P58228. Positions 4-452.
ModBase	Search...
Genome annotation databases
GeneID	915746. 961141.
GenomeReviews	Gene locus Z4930 in contig AE005174_GR. Gene locus ECs4397 in contig BA000007_GR.
KEGG	ece:Z4930. ecs:ECs4397.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG365574.
OMA	WHAPEPR.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS4397-MONOMER.
Family and domain databases
InterPro	IPR010107. Glutamate_decarboxylase. IPR002129. PyrdxlP-dep_de-COase. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR021115. Pyridoxal-P_BS. [Graphical view]
PANTHER	PTHR11999:SF1. Glu_decarb_GAD. 1 hit. PTHR11999. Pyridoxal_deC. 1 hit.
Pfam	PF00282. Pyridoxal_deC. 1 hit. [Graphical view]
TIGRFAMs	TIGR01788. Glu-decarb-GAD. 1 hit.
PROSITE	PS00392. DDC_GAD_HDC_YDC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DCEA_ECO57

Accession

Primary (citable) accession number: P58228

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 14, 2001
Last sequence update:	August 14, 2001
Last modified:	February 9, 2010
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)