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Protein

Glutamate decarboxylase alpha

Gene

gadA

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.

Catalytic activityi

L-glutamate = 4-aminobutanoate + CO2.

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei62SubstrateBy similarity1
Binding sitei83SubstrateBy similarity1
Binding sitei212Pyridoxal phosphateBy similarity1
Binding sitei275Pyridoxal phosphateBy similarity1

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

Keywordsi

Molecular functionDecarboxylase, Lyase
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:GLUTDECARBOXA-MONOMER
MetaCyc:GLUTDECARBOXA-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylase alpha (EC:4.1.1.15)
Short name:
GAD-alpha
Gene namesi
Name:gadA
Synonyms:gadS
Ordered Locus Names:b3517, JW3485
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG50009 gadA

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Chemistry databases

DrugBankiDB03553 Glutaric Acid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001469781 – 466Glutamate decarboxylase alphaAdd BLAST466

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei276N6-(pyridoxal phosphate)lysine1

Proteomic databases

PaxDbiP69908
PRIDEiP69908

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.

Protein-protein interaction databases

BioGridi4261597, 2 interactors
DIPiDIP-36201N
IntActiP69908, 15 interactors
MINTiP69908
STRINGi316385.ECDH10B_3694

Structurei

Secondary structure

1466
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 14Combined sources9
Turni17 – 19Combined sources3
Helixi21 – 24Combined sources4
Helixi39 – 49Combined sources11
Helixi50 – 53Combined sources4
Helixi56 – 58Combined sources3
Helixi70 – 78Combined sources9
Turni79 – 81Combined sources3
Turni87 – 89Combined sources3
Helixi91 – 107Combined sources17
Beta strandi119 – 125Combined sources7
Helixi126 – 147Combined sources22
Beta strandi156 – 161Combined sources6
Helixi165 – 172Combined sources8
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 – 305Combined sources5
Beta strandi308 – 312Combined sources5
Helixi322 – 357Combined sources36
Beta strandi360 – 368Combined sources9
Turni371 – 373Combined sources3
Beta strandi374 – 382Combined sources9
Helixi392 – 400Combined sources9
Turni401 – 403Combined sources3
Beta strandi408 – 410Combined sources3
Helixi413 – 415Combined sources3
Beta strandi419 – 424Combined sources6
Helixi431 – 449Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XEYX-ray2.05A/B1-466[»]
ProteinModelPortaliP69908
SMRiP69908
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69908

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni126 – 127Pyridoxal phosphate bindingBy similarity2

Sequence similaritiesi

Belongs to the group II decarboxylase family.Curated

Phylogenomic databases

eggNOGiENOG4105CVK Bacteria
COG0076 LUCA
HOGENOMiHOG000070228
InParanoidiP69908
KOiK01580
OMAiFTTSVYG
PhylomeDBiP69908

Family and domain databases

Gene3Di3.40.640.10, 1 hit
InterProiView protein in InterPro
IPR010107 Glutamate_decarboxylase
IPR002129 PyrdxlP-dep_de-COase
IPR015424 PyrdxlP-dep_Trfase
IPR015421 PyrdxlP-dep_Trfase_major
IPR021115 Pyridoxal-P_BS
PANTHERiPTHR43321 PTHR43321, 1 hit
PfamiView protein in Pfam
PF00282 Pyridoxal_deC, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR01788 Glu-decarb-GAD, 1 hit
PROSITEiView protein in PROSITE
PS00392 DDC_GAD_HDC_YDC, 1 hit

Sequencei

Sequence statusi: Complete.

P69908-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDQKLLTDFR SELLDSRFGA KAISTIAESK 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):52,685
Last modified:January 4, 2005 - v1
Checksum:i86F963E710553E22
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti64C → S AA sequence (PubMed:1740158).Curated1
Sequence conflicti73H → R AA sequence (PubMed:1740158).Curated1
Sequence conflicti153D → N AA sequence (PubMed:1740158).Curated1
Sequence conflicti165C → S in CAA44834 (PubMed:1740158).Curated1
Sequence conflicti208T → N in CAA44834 (PubMed:1740158).Curated1
Sequence conflicti295L → V in CAA44834 (PubMed:1740158).Curated1
Sequence conflicti355D → N AA sequence (PubMed:1740158).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84024 Genomic DNA Translation: AAA23833.1
X63123 Genomic DNA Translation: CAA44834.1
U00039 Genomic DNA Translation: AAB18493.1
U00096 Genomic DNA Translation: AAC76542.1
AP009048 Genomic DNA Translation: BAE77777.1
PIRiS47737 S24234
RefSeqiNP_417974.1, NC_000913.3
WP_000372240.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76542; AAC76542; b3517
BAE77777; BAE77777; BAE77777
GeneIDi948027
KEGGiecj:JW3485
eco:b3517
PATRICifig|511145.12.peg.3626

Similar proteinsi

Entry informationi

Entry nameiDCEA_ECOLI
AccessioniPrimary (citable) accession number: P69908
Secondary accession number(s): P80063, Q2M7H9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: March 28, 2018
This is version 108 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health