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Protein

Glutamate decarboxylase

Gene

BMD_2444

Organism
Bacillus megaterium (strain DSM 319)
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

BioCyciBMEG592022:GIVX-2444-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylaseUniRule annotation (EC:4.1.1.15UniRule annotation)
Gene namesi
Ordered Locus Names:BMD_2444Imported
OrganismiBacillus megaterium (strain DSM 319)Imported
Taxonomic identifieri592022 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000002365 Componenti: 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.

D5DEK8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPQWHPHREQ KNLPDEFPVN PLFSRQGEVT IPRLRISDQG MLPETAYQII
60 70 80 90 100
HDEIALDGNA RLNLATFVTT WMEPDAKRLY GESFDKNMID KDEYPQTAAI
110 120 130 140 150
EERCVRILAD LWNSPNPDTT MGVSTTGSSE ACMLGGLALK RRWQKLRKSK
160 170 180 190 200
GLSTERPNIV FSSSVQVVWE KFANYWDVEP RYVNINADHP YLDPEGVIKA
210 220 230 240 250
VDENTIGVVP ILGVTYTGVY EPIAAIAKAL DELQEKTGLD IPIHIDAASG
260 270 280 290 300
GFIAPFLQPD LIWDFRLPRV KSINVSGHKY GLVYPGLGWV IWREKEDLPE
310 320 330 340 350
DLIFRVSYLG GNMPTFALNF SRPGAQVLLQ YYNFLRLGKD GYYAVQKTSQ
360 370 380 390 400
ENALFLSKEI GEMEAFEIIA DGSDIPVLAW KLKEGYTPNW TLYDLSRQLR
410 420 430 440 450
TYGWQVPAYP LPADMEEITI MRIVVRNGFS RDLAHLFMVN FKQAVEFLNS
460
LDRPVLKDTK YDNGFHH
Length:467
Mass (Da):53,223
Last modified:June 15, 2010 - v1
Checksum:i49F0BE982EB72805
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001982 Genomic DNA. Translation: ADF39290.1.
RefSeqiYP_003597640.1. NC_014103.1.

Genome annotation databases

EnsemblBacteriaiADF39290; ADF39290; BMD_2444.
GeneIDi9117835.
KEGGibmd:BMD_2444.
PATRICi37254951. VBIBacMeg104484_2397.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001982 Genomic DNA. Translation: ADF39290.1.
RefSeqiYP_003597640.1. NC_014103.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADF39290; ADF39290; BMD_2444.
GeneIDi9117835.
KEGGibmd:BMD_2444.
PATRICi37254951. VBIBacMeg104484_2397.

Phylogenomic databases

HOGENOMiHOG000070228.
KOiK01580.
OMAiDPDLVWD.

Enzyme and pathway databases

BioCyciBMEG592022:GIVX-2444-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. "Genome sequences of the industrial vitamin B12-producers B. megaterium QM B1551 and DSM319 reveal new insights into the Bacillus genome evolution and pan-genome structure."
    Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K., Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J., Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J., Vary P.S.
    Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 319Imported.

Entry informationi

Entry nameiD5DEK8_BACMD
AccessioniPrimary (citable) accession number: D5DEK8
Entry historyi
Integrated into UniProtKB/TrEMBL: June 15, 2010
Last sequence update: June 15, 2010
Last modified: February 4, 2015
This is version 25 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.