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Protein

Glutamate decarboxylase

Gene

gad

Organism
Francisella tularensis subsp. tularensis TIGB03
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

BioCyciFTUL1001542:GLDJ-1772-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylaseUniRule annotation (EC:4.1.1.15UniRule annotation)
Gene namesi
Name:gadImported
ORF Names:FTU_1725Imported
OrganismiFrancisella tularensis subsp. tularensis TIGB03Imported
Taxonomic identifieri1001542 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
ProteomesiUP000008010: Chromosome

Structurei

3D structure databases

ProteinModelPortaliH6LTN3.
SMRiH6LTN3. Positions 13-435.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.UniRule annotation

Phylogenomic databases

KOiK01580.

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.

H6LTN3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALHGKKDTI DNLDFFEQSL PKFKLPLNSQ DPLEVYQEIK DELMLDGNSK
60 70 80 90 100
QNLATFCQTE VDDFIHKLMD DCIDKNMIDK DEYPQTAEIE SRCVNILANL
110 120 130 140 150
WNSSAENAIG CSTTGSSEAA MLGGMAMKWR WRDKMKAQGK DYTKPNLVTG
160 170 180 190 200
PVQVCWHKFA RYWDIELREI PMSNESLIMT PEAVLERCDE NTIGVVPTLG
210 220 230 240 250
VTFTGQYEPV EQVCKALDDF ERQTGVDIPV HVDAASGGFL APFVEPELKW
260 270 280 290 300
DFRLPRVKSI NSSGHKFGLS PLGVGWVIWA DKKYLPDDLI FNVNYLGGNM
310 320 330 340 350
PAFALNFSRL GGQIVAQYYN FVRLGFEGYK KVHQLCYDVA EYIAKELRKM
360 370 380 390 400
EIFEIIHAGE GGIPAVSWSL KATKEYSLFD ISEKVRAKGW QIAAYTMPNN
410 420 430 440
REDLVVMRVL VRRGFSYDLA QLMIRDLVAV IDSLEGKLKI LKRSSFAH
Length:448
Mass (Da):50,815
Last modified:April 18, 2012 - v1
Checksum:i2A48F8FD23CA64D4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003048 Genomic DNA. Translation: AFB79710.1.
RefSeqiYP_005306290.1. NC_016933.1.

Genome annotation databases

EnsemblBacteriaiAFB79710; AFB79710; FTU_1725.
GeneIDi11891272.
KEGGiftg:FTU_1725.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003048 Genomic DNA. Translation: AFB79710.1.
RefSeqiYP_005306290.1. NC_016933.1.

3D structure databases

ProteinModelPortaliH6LTN3.
SMRiH6LTN3. Positions 13-435.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAFB79710; AFB79710; FTU_1725.
GeneIDi11891272.
KEGGiftg:FTU_1725.

Phylogenomic databases

KOiK01580.

Enzyme and pathway databases

BioCyciFTUL1001542:GLDJ-1772-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. "Genomic Comparison between a Virulent Type A1 Strain of Francisella tularensis and Its Attenuated O-Antigen Mutant."
    Modise T., Ryder C., Mane S.P., Bandara A.B., Jensen R.V., Inzana T.J.
    J. Bacteriol. 194:2775-2776(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TIGB03Imported.

Entry informationi

Entry nameiH6LTN3_FRATL
AccessioniPrimary (citable) accession number: H6LTN3
Entry historyi
Integrated into UniProtKB/TrEMBL: April 18, 2012
Last sequence update: April 18, 2012
Last modified: February 4, 2015
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete 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.