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Protein

Glutamate decarboxylase

Gene

An15g04770

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
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
ORF Names:An15g04770Imported
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)Imported
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706 Componenti: Chromosome 3R

PTM / Processingi

Proteomic databases

PRIDEiA2R5L8.

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00011928.

Structurei

3D structure databases

ProteinModelPortaliA2R5L8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000070228.
KOiK01580.
OrthoDBiEOG7P2Z22.

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

Sequencei

Sequence statusi: Complete.

A2R5L8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVHLSTVRKE SHAHQRQREE RDAQAAAVSP YVYGTRYAVQ ELPEHSMSEN
60 70 80 90 100
EMPAPVAYRM IKDELSLDGN PLLNLASFVT TYMEDEVQQL MSDAMSKNFI
110 120 130 140 150
DYEQYPQTAH MQNRCVNMIA GLFHAPSIND PSNEQDAIGT STVGSSEAIM
160 170 180 190 200
LAMLAMKKRW QNKRKEAGKD WSRPNIIMNS AVQVCWEKAA RYFEVEERYV
210 220 230 240 250
YCTETRYVID PKEAVDLVDE NTVGICAILG TTYTGQYEDV KAINDLLIAK
260 270 280 290 300
NIDCPIHVDA ASGGFVVPFV KPELEWDFRL EKVISINVSG HKYGLVYPGV
310 320 330 340 350
GWVFWRAPEY LPKELIFNIN YLGAEQASFT LNFSKGAPHV IGQYYQLIRL
360 370 380 390 400
GKHGFRSIMT NLTQTADHLA AELEKLGFII MSEGGGRGLP LVAFRLPEQE
410 420 430 440 450
GRLYDEFALA HVLRRRGWVI PAYTMAPKCN QLRMMRIVLR EDFSLHRCNL
460 470 480 490 500
LVEDIRLGLK TLEDMDETMV KRYSTYIQTH ATRGPQGHPV YGNEQHSLQG

KSGKTHAVC
Length:509
Mass (Da):57,785
Last modified:March 6, 2007 - v1
Checksum:iE9AB024CBC665228
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270344 Genomic DNA. Translation: CAK42454.1.
RefSeqiXP_001397011.1. XM_001396974.2.

Genome annotation databases

EnsemblFungiiCADANGAT00012156; CADANGAP00011928; CADANGAG00012156.
GeneIDi4988078.
KEGGiang:ANI_1_662134.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270344 Genomic DNA. Translation: CAK42454.1.
RefSeqiXP_001397011.1. XM_001396974.2.

3D structure databases

ProteinModelPortaliA2R5L8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00011928.

Proteomic databases

PRIDEiA2R5L8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANGAT00012156; CADANGAP00011928; CADANGAG00012156.
GeneIDi4988078.
KEGGiang:ANI_1_662134.

Phylogenomic databases

HOGENOMiHOG000070228.
KOiK01580.
OrthoDBiEOG7P2Z22.

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

Publicationsi

  1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513Imported.

Entry informationi

Entry nameiA2R5L8_ASPNC
AccessioniPrimary (citable) accession number: A2R5L8
Entry historyi
Integrated into UniProtKB/TrEMBL: March 6, 2007
Last sequence update: March 6, 2007
Last modified: February 4, 2015
This is version 46 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.