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Protein

Glutamate decarboxylase

Gene

gadB

Organism
Gordonia polyisoprenivorans (strain DSM 44266 / VH2)
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

BioCyciGPOL1112204:GJWY-3394-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylaseUniRule annotation (EC:4.1.1.15UniRule annotation)
Gene namesi
Name:gadBImported
Ordered Locus Names:GPOL_c34020Imported
OrganismiGordonia polyisoprenivorans (strain DSM 44266 / VH2)Imported
Taxonomic identifieri1112204 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeGordoniaceaeGordonia
ProteomesiUP000009154: Chromosome

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.

H6MZ78-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTKRKHTNAR ATTNLNDSLT VNPVFVRPGE ATEYPKFAIP ESMSLPETAY
60 70 80 90 100
QIVHDEAMLD GNARLNLATF VSTWMDDEAR RLYAETYDKN MIDKDEYPQT
110 120 130 140 150
AAIEDRCWKI IADLWHVPDV DKSIGTSTIG SSEAAMLGGL ALKRHWQARR
160 170 180 190 200
KAEGKSIEKP NLVLSTAVQV CWEKFLNYFE VEPRWVPVSQ EHFVFDGHEL
210 220 230 240 250
ETYVDENTIG VVAILGVTYN GLYEPVQQIS AKLDEIEKNT GLDVKIHVDG
260 270 280 290 300
ASGAMVAPFC QPDLEWDFRV SRVVSINTSG HKYGLVYPGL GWIVWRDSEA
310 320 330 340 350
LPESMVFHCS YLGGDMPTLA LNFSRPGAQV LLQYYNFLRL GREGYRLIQQ
360 370 380 390 400
GSIDVATYLS SAIAEMGPFE LVSKGDTIPV FAWKLKDGYT DKWSLYDLSD
410 420 430 440 450
RLRLKGWLVP AYPMADGLAD WTLQRIVVRA GLSHDLATAL LTDLESEVAF
460
LDQLESPMPR EGTGSHFHH
Length:469
Mass (Da):52,747
Last modified:April 18, 2012 - v1
Checksum:i8DC00C09F3DC7A29
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003119 Genomic DNA. Translation: AFA74414.1.
RefSeqiWP_006368665.1. NC_016906.1.
YP_005283780.1. NC_016906.1.

Genome annotation databases

EnsemblBacteriaiAFA74414; AFA74414; GPOL_c34020.
GeneIDi11783406.
KEGGigpo:GPOL_c34020.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003119 Genomic DNA. Translation: AFA74414.1.
RefSeqiWP_006368665.1. NC_016906.1.
YP_005283780.1. NC_016906.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAFA74414; AFA74414; GPOL_c34020.
GeneIDi11783406.
KEGGigpo:GPOL_c34020.

Phylogenomic databases

KOiK01580.

Enzyme and pathway databases

BioCyciGPOL1112204:GJWY-3394-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. "Involvement of two latex-clearing proteins during rubber degradation and insights into the subsequent degradation pathway revealed by the genome sequence of Gordonia polyisoprenivorans strain VH2."
    Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A., Liebl W., Daniel R., Steinbuchel A.
    Appl. Environ. Microbiol. 78:2874-2887(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 44266 / VH2Imported.

Entry informationi

Entry nameiH6MZ78_GORPV
AccessioniPrimary (citable) accession number: H6MZ78
Entry historyi
Integrated into UniProtKB/TrEMBL: April 18, 2012
Last sequence update: April 18, 2012
Last modified: February 4, 2015
This is version 18 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.