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Protein

Glutamate decarboxylase

Gene

BCE_2691

Organism
Bacillus cereus (strain ATCC 10987)
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

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylaseUniRule annotation (EC:4.1.1.15UniRule annotation)
Gene namesi
Ordered Locus Names:BCE_2691Imported
OrganismiBacillus cereus (strain ATCC 10987)Imported
Taxonomic identifieri222523 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000002527 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi222523.BCE_2691.

Structurei

3D structure databases

ProteinModelPortaliQ737F8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0076.
HOGENOMiHOG000070228.
KOiK01580.
OMAiHINRVAT.
OrthoDBiEOG6TFCPW.

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.

Q737F8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPQDRKAEVQ KHAYERKEIM PDNSQSLPRH MQKELPHEFS VNPLFAREGE
60 70 80 90 100
SVVPRFHISD EGMLPETAYQ IVHDEITLDG NARLNLATFV STWMEPAAEQ
110 120 130 140 150
LYAKSFDKNM IDKDEYPQTA EIEERCVRIL ANLWHSPSPL TTMGVSTTGS
160 170 180 190 200
SEACMLGGLA LKRRWQNARK SEGKPLDRPN IVFSSAVQVV WEKFANYWEV
210 220 230 240 250
EPRYVKVSPE HPQLDPQGVL AAVDENTIGV VPILGETYTG LYEPVAEIAK
260 270 280 290 300
ALDDLQARTG LDIPMHVDAA SGGFIAPFLQ PDLVWDFQLP RVKSINVSGH
310 320 330 340 350
KYGLVYPGLG WIIWREAEDL PEDLIFRVSY LGGNMPTFAL NFSRPGAQVL
360 370 380 390 400
LQYYNYLRLG KSGYYDIQRA SQKVALFLSK AIQKMEPFEL LSDGSDIPVF
410 420 430 440 450
AWRLKEGYTS NWNLYDLSRQ LRVFGWQVPA YPLPPDMESV TIMRVVVRNG
460 470 480
FSMDLAHLFL RNLKQTVAFL DSLDGPMPHD TKCNNGFHH
Length:489
Mass (Da):55,503
Last modified:July 4, 2004 - v1
Checksum:i10F0A3FE4EB74D66
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017194 Genomic DNA. Translation: AAS41604.1.
RefSeqiNP_978996.1. NC_003909.8.

Genome annotation databases

EnsemblBacteriaiAAS41604; AAS41604; BCE_2691.
KEGGibca:BCE_2691.
PATRICi18854133. VBIBacCer118379_2567.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017194 Genomic DNA. Translation: AAS41604.1.
RefSeqiNP_978996.1. NC_003909.8.

3D structure databases

ProteinModelPortaliQ737F8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi222523.BCE_2691.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS41604; AAS41604; BCE_2691.
KEGGibca:BCE_2691.
PATRICi18854133. VBIBacCer118379_2567.

Phylogenomic databases

eggNOGiCOG0076.
HOGENOMiHOG000070228.
KOiK01580.
OMAiHINRVAT.
OrthoDBiEOG6TFCPW.

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. "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
    Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
    Nucleic Acids Res. 32:977-988(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 10987Imported.

Entry informationi

Entry nameiQ737F8_BACC1
AccessioniPrimary (citable) accession number: Q737F8
Entry historyi
Integrated into UniProtKB/TrEMBL: July 4, 2004
Last sequence update: July 4, 2004
Last modified: March 31, 2015
This is version 75 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.