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Protein

Glutamate decarboxylase

Gene

YALI0_F08415g

Organism
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
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:YALI0_F08415gImported
OrganismiYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)Imported
Taxonomic identifieri284591 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia
ProteomesiUP000001300: Chromosome F

Interactioni

Protein-protein interaction databases

STRINGi4952.Q6C2F2.

Structurei

3D structure databases

ProteinModelPortaliQ6C2F2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000070228.
InParanoidiQ6C2F2.
KOiK01580.
OMAiRYFDVEN.
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]
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.

Q6C2F2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLSEHVNAD KLLSNLTGKG DEHAIRALIA SHTLRDPYSS KYNSQEPIPK
60 70 80 90 100
FRIPEEGCEE KQAYQLIKDD LDLDGKPNLN LASFVNTYIS DRAEKLAVEN
110 120 130 140 150
LTKNLADADE YPALMTVHAR CVSILGHLWN NTDHEKAIGT ATTGSSEAIH
160 170 180 190 200
LGGLAMKKRW QEKRRAAGKS TEKPNILMAA NAQVALEKFA RYFDVEDRII
210 220 230 240 250
PVREASKHCL DLSKIKENLD ENTIGIFVIM GSTYTGHYED VQGVAKILDE
260 270 280 290 300
YEKETGHSID IHVDGASGAM VAPFLYPDLE WDFRVPRVKS INTSGHKFGL
310 320 330 340 350
TTAGLGWILW RDAKYLPKEL IFELHYLGGK EESYTLNFSR PGFPVLHQYY
360 370 380 390 400
NFLHLGFDGY KQLHASSMAN ARLLSVFLEA TGHYTCVSEI HLPANGSKPK
410 420 430 440 450
DVKHVATADP LQYMAGLPVV AFRFSDSFRK AHPEVPQAAV STLLRVKGYI
460 470 480 490 500
IPNYELPPSE QKTEILRVVV RQSMSIDLLD RLMEDISAIT NVLLEAVEDV
510 520 530 540
KKLRAEGDHD PQLIHKYVLT LVTGKPVEER EEDWEGHSTF RAAC
Length:544
Mass (Da):61,021
Last modified:August 16, 2004 - v1
Checksum:i31973763B6D4AB9D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382132 Genomic DNA. Translation: CAG77967.1.
RefSeqiXP_505160.1. XM_505160.1.

Genome annotation databases

EnsemblFungiiCAG77967; CAG77967; YALI0_F08415g.
GeneIDi2908500.
KEGGiyli:YALI0F08415g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382132 Genomic DNA. Translation: CAG77967.1.
RefSeqiXP_505160.1. XM_505160.1.

3D structure databases

ProteinModelPortaliQ6C2F2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4952.Q6C2F2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAG77967; CAG77967; YALI0_F08415g.
GeneIDi2908500.
KEGGiyli:YALI0F08415g.

Phylogenomic databases

HOGENOMiHOG000070228.
InParanoidiQ6C2F2.
KOiK01580.
OMAiRYFDVEN.
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]
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. "Genome evolution in yeasts."
    Genolevures
    Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.
    , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
    Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CLIB 122 / E 150Imported.

Entry informationi

Entry nameiQ6C2F2_YARLI
AccessioniPrimary (citable) accession number: Q6C2F2
Entry historyi
Integrated into UniProtKB/TrEMBL: August 16, 2004
Last sequence update: August 16, 2004
Last modified: February 4, 2015
This is version 67 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.