UniProtKB - P69910 (DCEB_ECOLI)

BLAST

>sp|P69910|DCEB_ECOLI Glutamate decarboxylase beta OS=Escherichia coli (strain K12) OX=83333 GN=gadB PE=1 SV=1
MDKKQVTDLRSELLDSRFGAKSISTIAESKRFPLHEMRDDVAFQIINDELYLDGNARQNL
ATFCQTWDDENVHKLMDLSINKNWIDKEEYPQSAAIDLRCVNMVADLWHAPAPKNGQAVG
TNTIGSSEACMLGGMAMKWRWRKRMEAAGKPTDKPNLVCGPVQICWHKFARYWDVELREI
PMRPGQLFMDPKRMIEACDENTIGVVPTFGVTYTGNYEFPQPLHDALDKFQADTGIDIDM
HIDAASGGFLAPFVAPDIVWDFRLPRVKSISASGHKFGLAPLGCGWVIWRDEEALPQELV
FNVDYLGGQIGTFAINFSRPAGQVIAQYYEFLRLGREGYTKVQNASYQVAAYLADEIAKL
GPYEFICTGRPDEGIPAVCFKLKDGEDPGYTLYDLSERLRLRGWQVPAFTLGGEATDIVV
MRIMCRRGFEMDFAELLLEDYKASLKYLSDHPKLQGIAQQNSFKHT

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History
Entry version 116 (07 Nov 2018)
Sequence version 1 (04 Jan 2005)
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Protein

Glutamate decarboxylase beta

Gene

gadB

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

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.

Miscellaneous

Changing Lys-276 to Ala increases thermal stability and protease resistance. The unfolding temperature is increased by 11 degrees Celsius.

Catalytic activityⁱ

L-glutamate = 4-aminobutanoate + CO₂.

Cofactorⁱ

pyridoxal 5'-phosphate

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	62	Substrate	1
Binding siteⁱ	83	Substrate	1
Binding siteⁱ	212	Pyridoxal phosphate	1
Binding siteⁱ	275	Pyridoxal phosphate	1

GO - Molecular functionⁱ

glutamate decarboxylase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 8954890
pyridoxal phosphate binding Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

glutamate catabolic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
intracellular pH elevation
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 10348866

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Decarboxylase, Lyase
Ligand	Pyridoxal phosphate

Enzyme and pathway databases

BioCycⁱ	EcoCyc:GLUTDECARBOXB-MONOMER MetaCyc:GLUTDECARBOXB-MONOMER
BRENDAⁱ	4.1.1.15 2026

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Glutamate decarboxylase beta (EC:4.1.1.15) Short name: GAD-beta
Gene namesⁱ	Name:gadB Ordered Locus Names:b1493, JW1488
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG11490 gadB

EcoGeneⁱ

EG11490 gadB

Subcellular locationⁱ

Note:

Localized exclusively in the cytoplasm at neutral pH, but is recruited to the membrane when the pH falls.

GO - Cellular componentⁱ

cytosol
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 16858726
membrane
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 16858726

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cytoplasm, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	276	K → A: Strongly reduces pyridoxal phosphate binding and increases stability of the polypeptide. 1 Publication		1
Mutagenesisⁱ	276	K → H: Abolishes pyridoxal phosphate binding. 1 Publication		1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000146982	1 – 466	Glutamate decarboxylase betaAdd BLAST		466

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	276	N6-(pyridoxal phosphate)lysine	1
Modified residueⁱ	446	N6-acetyllysine1 Publication	1
Modified residueⁱ	453	N6-acetyllysine1 Publication	1
Modified residueⁱ	464	N6-acetyllysine1 Publication	1

Keywords - PTMⁱ

Acetylation

Proteomic databases

PaxDbⁱ	P69910
PRIDEⁱ	P69910

PTM databases

iPTMnetⁱ	P69910

iPTMnetⁱ

P69910

Expressionⁱ

Inductionⁱ

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.7 Publications

Interactionⁱ

Subunit structureⁱ

Homohexamer composed of three dimers.1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
yadG	P36879	2	EBI-549514,EBI-550911

With

Entry

#Exp.

IntAct

Notes

yadG

P36879

EBI-549514,EBI-550911

Protein-protein interaction databases

BioGridⁱ	4260788, 5 interactors
Database of interacting proteins More...DIPⁱ	DIP-36202N
IntActⁱ	P69910, 16 interactors
Molecular INTeraction database More...MINTⁱ	P69910
STRINGⁱ	316385.ECDH10B_1624

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	4 – 14	Combined sources	11
Turnⁱ	17 – 19	Combined sources	3
Helixⁱ	21 – 23	Combined sources	3
Beta strandⁱ	25 – 28	Combined sources	4
Beta strandⁱ	29 – 31	Combined sources	3
Helixⁱ	39 – 49	Combined sources	11
Helixⁱ	50 – 52	Combined sources	3
Helixⁱ	56 – 58	Combined sources	3
Helixⁱ	70 – 78	Combined sources	9
Turnⁱ	79 – 81	Combined sources	3
Turnⁱ	87 – 89	Combined sources	3
Helixⁱ	91 – 107	Combined sources	17
Beta strandⁱ	114 – 116	Combined sources	3
Beta strandⁱ	119 – 125	Combined sources	7
Helixⁱ	126 – 147	Combined sources	22
Beta strandⁱ	156 – 161	Combined sources	6
Helixⁱ	164 – 172	Combined sources	9
Beta strandⁱ	176 – 179	Combined sources	4
Helixⁱ	191 – 197	Combined sources	7
Beta strandⁱ	202 – 206	Combined sources	5
Beta strandⁱ	208 – 210	Combined sources	3
Turnⁱ	212 – 214	Combined sources	3
Helixⁱ	220 – 234	Combined sources	15
Beta strandⁱ	240 – 243	Combined sources	4
Helixⁱ	247 – 249	Combined sources	3
Helixⁱ	251 – 254	Combined sources	4
Beta strandⁱ	267 – 273	Combined sources	7
Turnⁱ	274 – 278	Combined sources	5
Beta strandⁱ	285 – 291	Combined sources	7
Helixⁱ	292 – 294	Combined sources	3
Helixⁱ	297 – 299	Combined sources	3
Beta strandⁱ	301 – 303	Combined sources	3
Beta strandⁱ	310 – 312	Combined sources	3
Helixⁱ	322 – 358	Combined sources	37
Beta strandⁱ	361 – 368	Combined sources	8
Turnⁱ	371 – 373	Combined sources	3
Beta strandⁱ	374 – 382	Combined sources	9
Helixⁱ	392 – 401	Combined sources	10
Beta strandⁱ	408 – 410	Combined sources	3
Helixⁱ	413 – 415	Combined sources	3
Beta strandⁱ	419 – 424	Combined sources	6
Helixⁱ	431 – 450	Combined sources	20
Helixⁱ	452 – 454	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P69910
SMRⁱ	P69910
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P69910

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	126 – 127	Pyridoxal phosphate binding		2

Sequence similaritiesⁱ

Belongs to the group II decarboxylase family.Curated

Phylogenomic databases

eggNOGⁱ	ENOG4105CVK Bacteria COG0076 LUCA
HOGENOMⁱ	HOG000070228
InParanoidⁱ	P69910
KEGG Orthology (KO) More...KOⁱ	K01580
PhylomeDBⁱ	P69910

Family and domain databases

Gene3Dⁱ	3.40.640.10, 1 hit
InterProⁱ	View protein in InterPro IPR010107 Glutamate_decarboxylase IPR002129 PyrdxlP-dep_de-COase IPR015424 PyrdxlP-dep_Trfase IPR015421 PyrdxlP-dep_Trfase_major IPR021115 Pyridoxal-P_BS
PANTHERⁱ	PTHR43321 PTHR43321, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00282 Pyridoxal_deC, 1 hit
SUPFAMⁱ	SSF53383 SSF53383, 1 hit
TIGRFAMsⁱ	TIGR01788 Glu-decarb-GAD, 1 hit
PROSITEⁱ	View protein in PROSITE PS00392 DDC_GAD_HDC_YDC, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P69910-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MDKKQVTDLR SELLDSRFGA KSISTIAESK RFPLHEMRDD VAFQIINDEL 
        60         70         80         90        100
YLDGNARQNL ATFCQTWDDE NVHKLMDLSI NKNWIDKEEY PQSAAIDLRC 
       110        120        130        140        150
VNMVADLWHA PAPKNGQAVG TNTIGSSEAC MLGGMAMKWR WRKRMEAAGK 
       160        170        180        190        200
PTDKPNLVCG PVQICWHKFA RYWDVELREI PMRPGQLFMD PKRMIEACDE 
       210        220        230        240        250
NTIGVVPTFG VTYTGNYEFP QPLHDALDKF QADTGIDIDM HIDAASGGFL 
       260        270        280        290        300
APFVAPDIVW DFRLPRVKSI SASGHKFGLA PLGCGWVIWR DEEALPQELV 
       310        320        330        340        350
FNVDYLGGQI GTFAINFSRP AGQVIAQYYE FLRLGREGYT KVQNASYQVA 
       360        370        380        390        400
AYLADEIAKL GPYEFICTGR PDEGIPAVCF KLKDGEDPGY TLYDLSERLR 
       410        420        430        440        450
LRGWQVPAFT LGGEATDIVV MRIMCRRGFE MDFAELLLED YKASLKYLSD 
       460 
HPKLQGIAQQ NSFKHT

Length:466

Mass (Da):52,668

Last modified:January 4, 2005 - v1

Checksum:ⁱ8E653330A3C5B4ED

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M84025 Genomic DNA Translation: AAA23834.1 U00096 Genomic DNA Translation: AAC74566.1 AP009048 Genomic DNA Translation: BAA15163.1 X71917 Genomic DNA Translation: CAA50736.1 Sequence problems.
PIRⁱ	B43332
NCBI Reference Sequences More...RefSeqⁱ	NP_416010.1, NC_000913.3 WP_000358930.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC74566; AAC74566; b1493 BAA15163; BAA15163; BAA15163
GeneIDⁱ	946058
KEGGⁱ	ecj:JW1488 eco:b1493
PATRICⁱ	fig\|1411691.4.peg.774

Protein	Similar proteins		Species	Score	Length	Source
P69910	Glutamate decarboxylase beta		ECO57		466	UniRef100_P69911
Glutamate decarboxylase beta		SHIFL		466
Glutamate decarboxylase		Escherichia coli O25b:H4-ST131		489
Glutamate decarboxylase		Escherichia coli O25b:H4		476
Glutamate decarboxylase		Escherichia coli MS 119-7		476
+148

Protein	Similar proteins		Species	Score	Length	Source
P69910	Glutamate decarboxylase alpha		ECOL6		466	UniRef90_P69909
Glutamate decarboxylase alpha	)	ECOLI		466
Glutamate decarboxylase beta		ECO57		466
Glutamate decarboxylase beta		SHIFL		466
Glutamate decarboxylase		Escherichia coli O25b:H4-ST131		487
+1578

Protein	Similar proteins		Species	Score	Length	Source
P69910	Glutamate decarboxylase A		DICDI		462	UniRef50_Q54VQ5
Glutamate decarboxylase alpha		ECO57		466
Glutamate decarboxylase alpha		SHIFL		466
Glutamate decarboxylase beta		ECOL6		466
Glutamate decarboxylase alpha	)	ECOLI		466
+2294

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M84025 Genomic DNA Translation: AAA23834.1 U00096 Genomic DNA Translation: AAC74566.1 AP009048 Genomic DNA Translation: BAA15163.1 X71917 Genomic DNA Translation: CAA50736.1 Sequence problems.
PIRⁱ	B43332
RefSeqⁱ	NP_416010.1, NC_000913.3 WP_000358930.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1PMM	X-ray	2.00	A/B/C/D/E/F	1-466	[»]
	1PMO	X-ray	2.30	A/B/C/D/E/F	1-466	[»]
	2DGK	X-ray	1.90	A/B/C/D/E/F	15-466	[»]
	2DGL	X-ray	3.15	A/B/C/D/E/F	1-466	[»]
	2DGM	X-ray	1.95	A/B/C/D/E/F	1-466	[»]
	3FZ6	X-ray	2.82	A/B/C/D/E/F	1-466	[»]
	3FZ7	X-ray	2.50	A/B/C/D/E/F	1-466	[»]
	3FZ8	X-ray	3.00	A/B/C/D/E/F	1-466	[»]
ProteinModelPortalⁱ	P69910
SMRⁱ	P69910
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4260788, 5 interactors
DIPⁱ	DIP-36202N
IntActⁱ	P69910, 16 interactors
MINTⁱ	P69910
STRINGⁱ	316385.ECDH10B_1624

PTM databases

iPTMnetⁱ	P69910

iPTMnetⁱ

P69910

Proteomic databases

PaxDbⁱ	P69910
PRIDEⁱ	P69910

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC74566; AAC74566; b1493 BAA15163; BAA15163; BAA15163
GeneIDⁱ	946058
KEGGⁱ	ecj:JW1488 eco:b1493
PATRICⁱ	fig\|1411691.4.peg.774

Organism-specific databases

EchoBASEⁱ	EB1453
EcoGeneⁱ	EG11490 gadB

Phylogenomic databases

eggNOGⁱ	ENOG4105CVK Bacteria COG0076 LUCA
HOGENOMⁱ	HOG000070228
InParanoidⁱ	P69910
KOⁱ	K01580
PhylomeDBⁱ	P69910

Enzyme and pathway databases

BioCycⁱ	EcoCyc:GLUTDECARBOXB-MONOMER MetaCyc:GLUTDECARBOXB-MONOMER
BRENDAⁱ	4.1.1.15 2026

Miscellaneous databases

EvolutionaryTraceⁱ	P69910
Protein Ontology More...PROⁱ	PR:P69910

Family and domain databases

Gene3Dⁱ	3.40.640.10, 1 hit
InterProⁱ	View protein in InterPro IPR010107 Glutamate_decarboxylase IPR002129 PyrdxlP-dep_de-COase IPR015424 PyrdxlP-dep_Trfase IPR015421 PyrdxlP-dep_Trfase_major IPR021115 Pyridoxal-P_BS
PANTHERⁱ	PTHR43321 PTHR43321, 1 hit
Pfamⁱ	View protein in Pfam PF00282 Pyridoxal_deC, 1 hit
SUPFAMⁱ	SSF53383 SSF53383, 1 hit
TIGRFAMsⁱ	TIGR01788 Glu-decarb-GAD, 1 hit
PROSITEⁱ	View protein in PROSITE PS00392 DDC_GAD_HDC_YDC, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	DCEB_ECOLI
Accessionⁱ	P69910Primary (citable) accession number: P69910 Secondary accession number(s): P28302, P76873
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
	Last sequence update:	January 4, 2005
	Last modified:	November 7, 2018
	This is version 116 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P69910 (DCEB_ECOLI)

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Glutamate decarboxylase beta

gadB

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ