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Protein

Glutamate decarboxylase beta

Gene

gadB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.

Catalytic activityi

L-glutamate = 4-aminobutanoate + CO2.

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei62Substrate1
Binding sitei83Substrate1
Binding sitei212Pyridoxal phosphate1
Binding sitei275Pyridoxal phosphate1

GO - Molecular functioni

  • glutamate decarboxylase activity Source: EcoCyc
  • pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  • glutamate metabolic process Source: InterPro
  • intracellular pH elevation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:GLUTDECARBOXB-MONOMER.
ECOL316407:JW1488-MONOMER.
MetaCyc:GLUTDECARBOXB-MONOMER.
BRENDAi4.1.1.15. 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
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11490. gadB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi276K → A: Strongly reduces pyridoxal phosphate binding and increases stability of the polypeptide. 1 Publication1
Mutagenesisi276K → H: Abolishes pyridoxal phosphate binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001469821 – 466Glutamate decarboxylase betaAdd BLAST466

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei276N6-(pyridoxal phosphate)lysine1
Modified residuei446N6-acetyllysine1 Publication1
Modified residuei453N6-acetyllysine1 Publication1
Modified residuei464N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP69910.
PRIDEiP69910.

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

Protein-protein interaction databases

DIPiDIP-36202N.
IntActiP69910. 13 interactors.
MINTiMINT-1256225.
STRINGi511145.b1493.

Structurei

Secondary structure

1466
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 14Combined sources11
Turni17 – 19Combined sources3
Helixi21 – 23Combined sources3
Beta strandi25 – 28Combined sources4
Beta strandi29 – 31Combined sources3
Helixi39 – 49Combined sources11
Helixi50 – 52Combined sources3
Helixi56 – 58Combined sources3
Helixi70 – 78Combined sources9
Turni79 – 81Combined sources3
Turni87 – 89Combined sources3
Helixi91 – 107Combined sources17
Beta strandi114 – 116Combined sources3
Beta strandi119 – 125Combined sources7
Helixi126 – 147Combined sources22
Beta strandi156 – 161Combined sources6
Helixi164 – 172Combined sources9
Beta strandi176 – 179Combined sources4
Helixi191 – 197Combined sources7
Beta strandi202 – 206Combined sources5
Beta strandi208 – 210Combined sources3
Turni212 – 214Combined sources3
Helixi220 – 234Combined sources15
Beta strandi240 – 243Combined sources4
Helixi247 – 249Combined sources3
Helixi251 – 254Combined sources4
Beta strandi267 – 273Combined sources7
Turni274 – 278Combined sources5
Beta strandi285 – 291Combined sources7
Helixi292 – 294Combined sources3
Helixi297 – 299Combined sources3
Beta strandi301 – 303Combined sources3
Beta strandi310 – 312Combined sources3
Helixi322 – 358Combined sources37
Beta strandi361 – 368Combined sources8
Turni371 – 373Combined sources3
Beta strandi374 – 382Combined sources9
Helixi392 – 401Combined sources10
Beta strandi408 – 410Combined sources3
Helixi413 – 415Combined sources3
Beta strandi419 – 424Combined sources6
Helixi431 – 450Combined sources20
Helixi452 – 454Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PMMX-ray2.00A/B/C/D/E/F1-466[»]
1PMOX-ray2.30A/B/C/D/E/F1-466[»]
2DGKX-ray1.90A/B/C/D/E/F15-466[»]
2DGLX-ray3.15A/B/C/D/E/F1-466[»]
2DGMX-ray1.95A/B/C/D/E/F1-466[»]
3FZ6X-ray2.82A/B/C/D/E/F1-466[»]
3FZ7X-ray2.50A/B/C/D/E/F1-466[»]
3FZ8X-ray3.00A/B/C/D/E/F1-466[»]
ProteinModelPortaliP69910.
SMRiP69910.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69910.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni126 – 127Pyridoxal phosphate binding2

Sequence similaritiesi

Belongs to the group II decarboxylase family.Curated

Phylogenomic databases

eggNOGiENOG4105CVK. Bacteria.
COG0076. LUCA.
HOGENOMiHOG000070228.
InParanoidiP69910.
KOiK01580.
OMAiFEVEPRY.
PhylomeDBiP69910.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR021115. Pyridoxal-P_BS.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.
PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P69910-1 [UniParc]FASTAAdd 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
GO

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.
PIRiB43332.
RefSeqiNP_416010.1. NC_000913.3.
WP_000358930.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74566; AAC74566; b1493.
BAA15163; BAA15163; BAA15163.
GeneIDi946058.
KEGGiecj:JW1488.
eco:b1493.
PATRICi32118280. VBIEscCol129921_1560.

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.
PIRiB43332.
RefSeqiNP_416010.1. NC_000913.3.
WP_000358930.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PMMX-ray2.00A/B/C/D/E/F1-466[»]
1PMOX-ray2.30A/B/C/D/E/F1-466[»]
2DGKX-ray1.90A/B/C/D/E/F15-466[»]
2DGLX-ray3.15A/B/C/D/E/F1-466[»]
2DGMX-ray1.95A/B/C/D/E/F1-466[»]
3FZ6X-ray2.82A/B/C/D/E/F1-466[»]
3FZ7X-ray2.50A/B/C/D/E/F1-466[»]
3FZ8X-ray3.00A/B/C/D/E/F1-466[»]
ProteinModelPortaliP69910.
SMRiP69910.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-36202N.
IntActiP69910. 13 interactors.
MINTiMINT-1256225.
STRINGi511145.b1493.

Proteomic databases

PaxDbiP69910.
PRIDEiP69910.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74566; AAC74566; b1493.
BAA15163; BAA15163; BAA15163.
GeneIDi946058.
KEGGiecj:JW1488.
eco:b1493.
PATRICi32118280. VBIEscCol129921_1560.

Organism-specific databases

EchoBASEiEB1453.
EcoGeneiEG11490. gadB.

Phylogenomic databases

eggNOGiENOG4105CVK. Bacteria.
COG0076. LUCA.
HOGENOMiHOG000070228.
InParanoidiP69910.
KOiK01580.
OMAiFEVEPRY.
PhylomeDBiP69910.

Enzyme and pathway databases

BioCyciEcoCyc:GLUTDECARBOXB-MONOMER.
ECOL316407:JW1488-MONOMER.
MetaCyc:GLUTDECARBOXB-MONOMER.
BRENDAi4.1.1.15. 2026.

Miscellaneous databases

EvolutionaryTraceiP69910.
PROiP69910.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR021115. Pyridoxal-P_BS.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.
PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDCEB_ECOLI
AccessioniPrimary (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 2, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.