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Protein

Glutamate decarboxylase

Gene

gadB

Organism
Legionella longbeachae serogroup 1 (strain NSW150)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

L-glutamate = 4-aminobutanoate + CO2.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

GO - Molecular functioni

  1. glutamate decarboxylase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. glutamate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

DecarboxylaseUniRule annotation, Lyase

Keywords - Ligandi

Pyridoxal phosphateUniRule annotation

Enzyme and pathway databases

BioCyciLLON661367:GJAR-3222-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylaseUniRule annotation (EC:4.1.1.15UniRule annotation)
Gene namesi
Name:gadBImported
Ordered Locus Names:LLO_2994Imported
OrganismiLegionella longbeachae serogroup 1 (strain NSW150)Imported
Taxonomic identifieri661367 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
ProteomesiUP000001060: Chromosome

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000070228.
KOiK01580.
OMAiDPDLVWD.

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]
PANTHERiPTHR11999:SF1. PTHR11999:SF1. 1 hit.
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.

Sequencei

Sequence statusi: Complete.

D3HLW1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIVKKDQKKS NASTHSTSVY ASRYDLDDFS VATCNEYGML PAVAKQLIED
60 70 80 90 100
ELSLEATPIL NLASFVTTWM EPEAEELINK SINKNFINYE EYPRVQEIHQ
110 120 130 140 150
RCVHILADLL NIPEGCNYVG TATVGSSEAI MLAGLAHKFS WRNMRKMQNL
160 170 180 190 200
DSSKPNIVMG ANVQVCWDKF ARYFDVEARI IPLKKNKFTI SADDVAPLID
210 220 230 240 250
ENTICIAAVL GSTFTGEYDE IEEINDLLIQ VKKEKGWDVP LHVDGASGGF
260 270 280 290 300
ISMFYDNAIK WDFCLEQVKS INLSGHKFGL VYPSVGWLIF RDEAVVPKDL
310 320 330 340 350
IFEVNYLGGQ MPTYTLNFSR SSSMVIAQYY NFLRLGKNGY KKIISNMLAV
360 370 380 390 400
SDLVAKGLIA TGKFALLGDR RMAPVVTVAL KDNTTYSVFE ISKKLREYGW
410 420 430 440 450
IVPAYTLPEA ADEIEALRVV IKENMSSMMA RHFIASVEEV INELEGRTGK
460
SKTPRVQGKS VGMH
Length:464
Mass (Da):52,032
Last modified:March 23, 2010 - v1
Checksum:i26B35DD56D225E63
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN650140 Genomic DNA. Translation: CBJ13441.1.
RefSeqiWP_003634875.1. NC_013861.1.
YP_003456451.1. NC_013861.1.

Genome annotation databases

EnsemblBacteriaiCBJ13441; CBJ13441; LLO_2994.
GeneIDi8801556.
KEGGillo:LLO_2994.
PATRICi35294262. VBILegLon159544_3094.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN650140 Genomic DNA. Translation: CBJ13441.1.
RefSeqiWP_003634875.1. NC_013861.1.
YP_003456451.1. NC_013861.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCBJ13441; CBJ13441; LLO_2994.
GeneIDi8801556.
KEGGillo:LLO_2994.
PATRICi35294262. VBILegLon159544_3094.

Phylogenomic databases

HOGENOMiHOG000070228.
KOiK01580.
OMAiDPDLVWD.

Enzyme and pathway databases

BioCyciLLON661367:GJAR-3222-MONOMER.

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]
PANTHERiPTHR11999:SF1. PTHR11999:SF1. 1 hit.
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Analysis of the Legionella longbeachae genome and transcriptome uncovers unique strategies to cause Legionnaires' disease."
    Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D., Newton H.J., Sansom F.M., Jarraud S., Zidane N., Ma L., Bouchier C., Etienne J., Hartland E.L., Buchrieser C.
    PLoS Genet. 6:E1000851-E1000851(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NSW150Imported.

Entry informationi

Entry nameiD3HLW1_LEGLN
AccessioniPrimary (citable) accession number: D3HLW1
Entry historyi
Integrated into UniProtKB/TrEMBL: March 23, 2010
Last sequence update: March 23, 2010
Last modified: February 4, 2015
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.