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Protein

Glutamate decarboxylase

Gene

FG01572.1

Organism
Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) (Fusarium graminearum)
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
Name:FG01572.1Imported
ORF Names:FGSG_01572Imported
OrganismiGibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) (Fusarium graminearum)Imported
Taxonomic identifieri229533 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusarium
ProteomesiUP000009057: Chromosome 1

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.UniRule annotation

Phylogenomic databases

InParanoidiI1RD80.
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.

I1RD80-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLAQHSESA SPVPIIETDD QGNPIKSSNG YFPSKGKSST LVDNMAHLSV
60 70 80 90 100
VGGAHRGDDS DAASVRSTSS RASRRPEMKL ASYQDEYTTS VYGSRFAGMD
110 120 130 140 150
LPRHHMPENE MPRDIAYRMI KDDLSLDNNP MLNLASFVTT YMEDEAEKLM
160 170 180 190 200
AESFSKNFID YEEYPQSADI QNRCVNMIGD LFHAPPGSSV GTSTVGSSEA
210 220 230 240 250
IMLGVLAMKR RWKNRRIAEG KSTEHPNIVM SSAVQVCWEK ATRYFEIDEK
260 270 280 290 300
LVYCTPDRFV MDPEQAVDLC DENTIGMCAI LGTTYTGEYE DIKAINDLLV
310 320 330 340 350
ERNLDVPIHV DAASGGFVAP FVVPDLEWDF RCEKVVSINV SGHKYGLVYP
360 370 380 390 400
GVGWVIWRSP EFLPQELVFN INYLGADQSS FTLNFSKGAS QVIGQYYQLI
410 420 430 440 450
RLGKHGYRAI MSNLTRTADY LTETLENMGF VIMSERSGAG LPLVAFRFKT
460 470 480 490 500
VDEGGDPERH YDEFALAHHL RSRGWVVPAY TMAPNSGVKM LRVVVREDFT
510 520 530 540 550
KSRCDQLICD VKLCHGLLKE TDQESIKKRE EYIKNHIVTM GRGKHSHPVY
560
KDEQHSLQGK HGKTHAIC
Length:568
Mass (Da):63,680
Last modified:June 13, 2012 - v1
Checksum:i2C35DBDA7A3F83EE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS231663 Genomic DNA. Translation: ESU06900.1.
RefSeqiXP_381748.1. XM_381748.1.

Genome annotation databases

EnsemblFungiiFGSG_01572T0; FGSG_01572P0; FGSG_01572.
GeneIDi2783689.
KEGGifgr:FG01572.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS231663 Genomic DNA. Translation: ESU06900.1.
RefSeqiXP_381748.1. XM_381748.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiFGSG_01572T0; FGSG_01572P0; FGSG_01572.
GeneIDi2783689.
KEGGifgr:FG01572.1.

Phylogenomic databases

InParanoidiI1RD80.
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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084Imported.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: PH-1Imported.
  3. "Comparative genomics reveals mobile pathogenicity chromosomes in Fusarium."
    Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R., Antoniw J., Baker S.E.
    , Bluhm B.H., Breakspear A., Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C., Rep M.
    Nature 464:367-373(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084Imported.
  4. EnsemblFungi
    Submitted (APR-2013) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084Imported.

Entry informationi

Entry nameiI1RD80_GIBZE
AccessioniPrimary (citable) accession number: I1RD80
Entry historyi
Integrated into UniProtKB/TrEMBL: June 13, 2012
Last sequence update: June 13, 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.