Q8FHG5 (DCEB_ECOL6) Reviewed, UniProtKB/Swiss-Prot

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:	c1922

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [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.
Sequence caution	The sequence AAN80380.1 differs from that shown. Reason: Erroneous initiation.

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_0000146983
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
	Modified residue	446	1	N6-acetyllysine By similarity
	Modified residue	453	1	N6-acetyllysine By similarity
	Modified residue	464	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8FHG5 [UniParc]. Last modified January 4, 2005. Version 2. Checksum: C953BB99AAF48923	FASTA	466	52,653
	10 20 30 40 50 60 MDKKQVTDLR SELLDSRFGA KSISTIAESK RFPLHEMRDD VAFQIINDEL YLDGNARQNL 70 80 90 100 110 120 ATFCQTWDDD NVHKLMDLSI NKNWIDKEEY PQSAAIDLRC VNMVADLWHA PAPKNGQAVG 130 140 150 160 170 180 TNTIGSSEAC MLGGMAMKWR WRKRMEAAGK PTNKPNLVCG 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

References

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014075 Genomic DNA. Translation: AAN80380.1. Different initiation.
RefSeq	NP_753818.1. NC_004431.1.
3D structure databases
ProteinModelPortal	Q8FHG5.
SMR	Q8FHG5. Positions 4-466.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000045513; EBESCP00000043862; EBESCG00000044563.
GeneID	1035839.
GenomeReviews	Gene locus c1922 in contig AE014075_GR.
KEGG	ecc:c1922.
NMPDR	fig|199310.1.peg.1861.
PATRIC	18281741. VBIEscCol75197_1789.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000008325.
HOGENOM	HBG365574.
OMA	YPRTAEL.
ProtClustDB	CLSK880040.
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_ECOL6

Accession

Primary (citable) accession number: Q8FHG5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	January 4, 2005
Last modified:	January 25, 2012
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program