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Protein

Glutamate decarboxylase B

Gene

gadB

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Generates GABA from glutamate. Likely to be responsible for the metabolism of glutamate via the GABA shunt to succinate during growth.

Catalytic activityi

L-glutamate = 4-aminobutanoate + CO2.

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei60SubstrateBy similarity1
Binding sitei81SubstrateBy similarity1
Binding sitei208Pyridoxal phosphateBy similarity1
Binding sitei271Pyridoxal phosphateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • aggregation involved in sorocarp development Source: dictyBase
  • glutamate catabolic process Source: dictyBase
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Pyridoxal phosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylase B (EC:4.1.1.15)
Gene namesi
Name:gadB
ORF Names:DDB_G0288715
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 5, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0288715. gadB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: dictyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003913301 – 463Glutamate decarboxylase BAdd BLAST463

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei272N6-(pyridoxal phosphate)lysineBy similarity1

Proteomic databases

PaxDbiQ54IJ3.

Expressioni

Developmental stagei

Expressed in growing cells, its mRNA continuously decreases during development. Highly expressed during phagocytosis of non-pathogenic bacteria.2 Publications

Interactioni

Subunit structurei

Homohexamer.By similarity

Protein-protein interaction databases

STRINGi44689.DDB0231439.

Structurei

3D structure databases

ProteinModelPortaliQ54IJ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni122 – 123Pyridoxal phosphate bindingBy similarity2

Sequence similaritiesi

Belongs to the group II decarboxylase family.Curated

Phylogenomic databases

eggNOGiKOG1383. Eukaryota.
COG0076. LUCA.
InParanoidiQ54IJ3.
KOiK01580.
OMAiLHCSTFA.
PhylomeDBiQ54IJ3.

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.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.

Sequencei

Sequence statusi: Complete.

Q54IJ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLHIVDKHK SLYDNYVQSA TTEEIAKFKL ADDPNEPETI KKLIMDELLL
60 70 80 90 100
DGNSKQNLAT FCQTDLDKNI HSIMDKCIDK NMIDKDEYPQ SAEIENRCLH
110 120 130 140 150
ILADLWNAPD SSDTIGCSTT GSSEAAMLGG LALKWNWREN RKKLGLPYDK
160 170 180 190 200
PNIVTGPVQI CWHKFALYFD IEIREIPMEN GRYVMNSEEV LKRVDENTIG
210 220 230 240 250
VIPTLGVTFT LQYEDVFSIS NALDKFEKES GINIPIHVDA ASGGFVAPFI
260 270 280 290 300
QQEIIWDFRL PRVKSINASG HKFGLSPLGV GWVVWREKKD LHKDLVFNVN
310 320 330 340 350
YLGGNMSTFS LNFSRPGGQI IAQYYNFLRH GRNGYTLIQD ACAQQGIFIG
360 370 380 390 400
KELKKMGIFD LIYDGTGALP GVCWTISKNL PSEPLFNLYD LSEKLRSRGW
410 420 430 440 450
QVASYSLPSS MNDVVVSRVV IRHGFSRDLS SLFVKDVQNA IEYFQKHPIL
460
RSLEKDEGEN FHH
Length:463
Mass (Da):52,506
Last modified:May 24, 2005 - v1
Checksum:i8803CBD7A216B4E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000120 Genomic DNA. Translation: EAL63089.1.
RefSeqiXP_636593.1. XM_631501.1.

Genome annotation databases

EnsemblProtistsiEAL63089; EAL63089; DDB_G0288715.
GeneIDi8626767.
KEGGiddi:DDB_G0288715.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000120 Genomic DNA. Translation: EAL63089.1.
RefSeqiXP_636593.1. XM_631501.1.

3D structure databases

ProteinModelPortaliQ54IJ3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0231439.

Proteomic databases

PaxDbiQ54IJ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiEAL63089; EAL63089; DDB_G0288715.
GeneIDi8626767.
KEGGiddi:DDB_G0288715.

Organism-specific databases

dictyBaseiDDB_G0288715. gadB.

Phylogenomic databases

eggNOGiKOG1383. Eukaryota.
COG0076. LUCA.
InParanoidiQ54IJ3.
KOiK01580.
OMAiLHCSTFA.
PhylomeDBiQ54IJ3.

Miscellaneous databases

PROiQ54IJ3.

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.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGADB_DICDI
AccessioniPrimary (citable) accession number: Q54IJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 9, 2010
Last sequence update: May 24, 2005
Last modified: November 2, 2016
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. 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.