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Protein

Glutamate decarboxylase beta

Gene

gadB

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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 (By similarity).By similarity

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

GO - Biological processi

Keywordsi

Molecular functionDecarboxylase, Lyase
LigandPyridoxal phosphate

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:Z2215, ECs2098
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001469841 – 466Glutamate decarboxylase betaAdd BLAST466

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei276N6-(pyridoxal phosphate)lysineBy similarity1
Modified residuei446N6-acetyllysineBy similarity1
Modified residuei453N6-acetyllysineBy similarity1
Modified residuei464N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP69911

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 (By similarity).By similarity

Interactioni

Subunit structurei

Homohexamer composed of three dimers.By similarity

Protein-protein interaction databases

STRINGi155864.Z2215

Structurei

3D structure databases

ProteinModelPortaliP69911
SMRiP69911
ModBaseiSearch...
MobiDBiSearch...

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
KOiK01580
OMAiRPNLVMG

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.

P69911-1 [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
AE005174 Genomic DNA Translation: AAG56275.1
BA000007 Genomic DNA Translation: BAB35521.1
PIRiB90891
G85726
RefSeqiNP_310125.1, NC_002695.1
WP_000358930.1, NZ_NOKN01000002.1

Genome annotation databases

EnsemblBacteriaiAAG56275; AAG56275; Z2215
BAB35521; BAB35521; BAB35521
GeneIDi917300
KEGGiece:Z2215
ecs:ECs2098
PATRICifig|386585.9.peg.2203

Similar proteinsi

Entry informationi

Entry nameiDCEB_ECO57
AccessioniPrimary (citable) accession number: P69911
Secondary accession number(s): P28302, P76873
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: April 25, 2018
This is version 85 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

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health