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Protein

Glutamate decarboxylase

Gene

SS1G_00795

Organism
Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)
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

GO - Biological processi

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:SS1G_00795Imported
OrganismiSclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)Imported
Taxonomic identifieri665079 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeSclerotinia
ProteomesiUP000001312 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:SS1G_00795.

Interactioni

Protein-protein interaction databases

STRINGi5180.EDN91392.

Structurei

3D structure databases

ProteinModelPortaliA7E670.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0076.
InParanoidiA7E670.
KOiK01580.
OMAiMIMSSAV.
OrthoDBiEOG7P2Z22.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.

Sequencei

Sequence statusi: Complete.

A7E670-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSREHCREEV LIAGCYCRFI QPIRELDFIH TVNELSFSAK ILELPKTAGA
60 70 80 90 100
CIPGRGAEKA PAIMVHLSQI PSEQNVTAPL VEGLKKLTMA ASSEEDAFTT
110 120 130 140 150
SVYGSKFAAQ DLPRHEMPEG EMPKEVAYRM IKDDLSLDGN PMLNLASFVT
160 170 180 190 200
TYMEKEVEDL MTESFSKNFI DYEEYPQSAD IQNRCVSMIG RLFNAPTNAE
210 220 230 240 250
GDAAVGTSTV GSSEAIMLAV LAMKKRWKNA RIAAGKSTNN PNIVMSSAVQ
260 270 280 290 300
VCWEKAARYF EVEEKYVYCT PDRYVIDPEE TVNLVDENTI GICVILGTTY
310 320 330 340 350
TGEYEDAKAV NDLLIKKNID TVIHIDAASG GFVAPFVCPE LEWDFRLEKV
360 370 380 390 400
VSINTSGHKY GLVYPGVGWI VWRAPEYLPK ELVFNINYLG ADQASFTLNF
410 420 430 440 450
SKGASQVIAQ YYQLIRLGKK GYRSIMNNLT RTADYLSDSL QQLGFIIMSQ
460 470 480 490 500
KNGRGLPLVA FRIDPESDKH YDEFAIAHQL RQRGWVVPAY TMAPKTENLK
510 520 530 540 550
MLRVVVREDF SKSRCDQLLN DIKLCCSVLN EMDKETIKKN QEYIKMHSTH
560 570
VGKSKHNHPH YKNEKHSLQG KTGKTHAIC
Length:579
Mass (Da):65,088
Last modified:September 11, 2007 - v1
Checksum:iBFEFE6C2494D8880
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476621 Genomic DNA. Translation: EDN91392.1.
RefSeqiXP_001598706.1. XM_001598656.1.

Genome annotation databases

EnsemblFungiiEDN91392; EDN91392; SS1G_00795.
GeneIDi5494536.
KEGGissl:SS1G_00795.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476621 Genomic DNA. Translation: EDN91392.1.
RefSeqiXP_001598706.1. XM_001598656.1.

3D structure databases

ProteinModelPortaliA7E670.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5180.EDN91392.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEDN91392; EDN91392; SS1G_00795.
GeneIDi5494536.
KEGGissl:SS1G_00795.

Organism-specific databases

EuPathDBiFungiDB:SS1G_00795.

Phylogenomic databases

eggNOGiCOG0076.
InParanoidiA7E670.
KOiK01580.
OMAiMIMSSAV.
OrthoDBiEOG7P2Z22.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia sclerotiorum and Botrytis cinerea."
    Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., Quevillon E.
    , Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.
    PLoS Genet. 7:E1002230-E1002230(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 18683 / 1980 / Ss-1Imported.

Entry informationi

Entry nameiA7E670_SCLS1
AccessioniPrimary (citable) accession number: A7E670
Entry historyi
Integrated into UniProtKB/TrEMBL: September 11, 2007
Last sequence update: September 11, 2007
Last modified: June 24, 2015
This is version 41 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.