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Protein
Submitted name:

Podospora anserina S mat+ genomic DNA chromosome 3, supercontig 2

Gene

PODANS_3_9440

Organism
Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina)
Status
Unreviewed-Annotation score: Annotation score: 1 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
Submitted name:
Podospora anserina S mat+ genomic DNA chromosome 3, supercontig 2Imported
Submitted name:
Putative glutamate decarboxylaseImported
Gene namesi
ORF Names:PODANS_3_9440Imported
OrganismiPodospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina)Imported
Taxonomic identifieri515849 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesLasiosphaeriaceaePodospora
ProteomesiUP000001197 Componenti: Chromosome 3

PTM / Processingi

Proteomic databases

PRIDEiB2B163.

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

Sequencei

Sequence statusi: Complete.

B2B163-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVHLSTIPDE NQVVNGKLAG GIKKAHLQLV NDDDSFTTSV YGSRFAARDL
60 70 80 90 100
PKHEMPEAEM SKDVAYRLIK DHLSLDGNPI LNLASFVTTY MEEEAEKLMT
110 120 130 140 150
ESFSKNFIDY EEYPQSADIQ NRCVSMIGRL FHAPIGVEDD VGAIGTSCVG
160 170 180 190 200
SSEAIMLAVL AMKRRWKNKR IEEGKPYDRP NIVMSSAVQV CWEKAARYFE
210 220 230 240 250
VEEKLVYCTE ERYVIDPEET VNLVDENTIG ICVILGTTYT GEYEDVKAVD
260 270 280 290 300
DLLTKKGLNT PIHVDAASGG FVAPFVVPDL EWDFRLEHVV SINVSGHKYG
310 320 330 340 350
LVYPGVGWVV WRSAEFLPQE LVFNINYLGA DQASFTLNFS KGASQVIGQY
360 370 380 390 400
YQLIRLGKHG YRAIMSNLTR TANYLSDSLE ALGFIIMSKK SGEGLPLVAF
410 420 430 440 450
RLPPQEDRNY DEFALAHQLR VRGWVVPAYT MAPNTENLKM LRVVVREDFT
460 470 480 490 500
RSRCDSLITD IKQSQQLLGQ MDQDSIKKQQ DFIHKHNTSS GKASHNHPKY
510
RKEKHSLQGK TGKTHAIC
Length:518
Mass (Da):58,333
Last modified:May 19, 2008 - v1
Checksum:i19AC468B8BF23057
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU638743 Genomic DNA. Translation: CAP70886.1.
FO904938 Genomic DNA. Translation: CDP27482.1.
RefSeqiXP_001909753.1. XM_001909718.1.

Genome annotation databases

GeneIDi6193873.
KEGGipan:PODANSg6789.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU638743 Genomic DNA. Translation: CAP70886.1.
FO904938 Genomic DNA. Translation: CDP27482.1.
RefSeqiXP_001909753.1. XM_001909718.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiB2B163.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi6193873.
KEGGipan:PODANSg6789.

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

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: S / ATCC MYA-4624 / DSM 980 / FGSC 10383Imported and S mat+Imported.
  2. Genoscope - CEA
    Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: S mat+Imported.
  3. Genoscope - CEA
    Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  4. "Maintaining two mating types: Structure of the mating type locus and its role in heterokaryosis in Podospora anserina."
    Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E., Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.
    Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiB2B163_PODAN
AccessioniPrimary (citable) accession number: B2B163
Entry historyi
Integrated into UniProtKB/TrEMBL: May 19, 2008
Last sequence update: May 19, 2008
Last modified: March 31, 2015
This is version 39 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.