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Protein

Glutamate decarboxylase

Gene

Gad1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the production of GABA.

Catalytic activityi

L-glutamate = 4-aminobutanoate + CO2.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei483 – 4831SubstrateBy similarity

GO - Molecular functioni

  • glutamate decarboxylase activity Source: FlyBase
  • pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  • gamma-aminobutyric acid biosynthetic process Source: FlyBase
  • glutamate catabolic process Source: FlyBase
  • larval locomotory behavior Source: FlyBase
  • neuromuscular junction development Source: FlyBase
  • neurotransmitter biosynthetic process Source: UniProtKB-KW
  • neurotransmitter receptor metabolic process Source: FlyBase
  • olfactory learning Source: FlyBase
  • response to mechanical stimulus Source: FlyBase
  • synapse assembly Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Neurotransmitter biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi4.1.1.15. 1994.
ReactomeiREACT_311194. GABA synthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylase (EC:4.1.1.15)
Short name:
GAD
Gene namesi
Name:Gad1
Synonyms:Gad, Glb
ORF Names:CG14994
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0004516. Gad1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 510510Glutamate decarboxylasePRO_0000146972Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei322 – 3221N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PaxDbiP20228.

Expressioni

Gene expression databases

BgeeiP20228.
ExpressionAtlasiP20228. differential.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi63964. 2 interactions.
IntActiP20228. 1 interaction.
MINTiMINT-917310.
STRINGi7227.FBpp0073133.

Structurei

3D structure databases

ProteinModelPortaliP20228.
SMRiP20228. Positions 17-510.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni107 – 1093Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the group II decarboxylase family.Curated

Phylogenomic databases

eggNOGiCOG0076.
GeneTreeiENSGT00760000119205.
InParanoidiP20228.
KOiK01580.
OMAiEYLYTKI.
OrthoDBiEOG7H1JM3.
PhylomeDBiP20228.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR021115. Pyridoxal-P_BS.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20228-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLNPNGYKL SERTGKLTAY DLMPTTVTAG PETREFLLKV IDVLLDFVKA
60 70 80 90 100
TNDRNEKVLD FHHPEDMKRL LDLDVPDRAL PLQQLIEDCA TTLKYQVKTG
110 120 130 140 150
HPHFFNQLSN GLDLISMAGE WLTATANTNM FTYEIAPVFI LMENVVLTKM
160 170 180 190 200
REIIGWSGGD SILAPGGSIS NLYAFLAARH KMFPNYKEHG SVGLPGTLVM
210 220 230 240 250
FTSDQCHYSI KSCAAVCGLG TDHCIVVPSD EHGKMITSEL ERLILERKAK
260 270 280 290 300
GDIPFFVNAT AGTTVLGAFD DINTIADICQ KYNCWMHIDA AWGGGLLMSR
310 320 330 340 350
KHRHPRFTGV ERADSVTWNP HKLMGALLQC STIHFKEDGL LISCNQMSAE
360 370 380 390 400
YLFMTDKQYD ISYDTGDKVI QCGRHNDIFK LWLQWRAKGT EGFEQQQDRL
410 420 430 440 450
MELVQYQLKR IREQSDRFHL ILEPECVNVS FWYVPKRLRG VPHDAKKEVE
460 470 480 490 500
LGKICPIIKG RMMQKGTLMV GYQPDDRRPN FFRSIISSAA VNEADVDFML
510
DEIHRLGDDL
Length:510
Mass (Da):57,819
Last modified:June 21, 2005 - v2
Checksum:iAAEBFC6FDC662001
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti201 – 2011F → L in CAA53791 (PubMed:1689376).Curated
Sequence conflicti301 – 3011K → T in CAA53791 (PubMed:1689376).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76198 mRNA. Translation: CAA53791.1.
AE014296 Genomic DNA. Translation: AAF47834.1.
AE014296 Genomic DNA. Translation: AAN11581.1.
AE014296 Genomic DNA. Translation: AAN11582.1.
AY089526 mRNA. Translation: AAL90264.1.
PIRiJH0192. A30999.
RefSeqiNP_001261396.1. NM_001274467.1.
NP_523914.2. NM_079190.3.
NP_728930.1. NM_168055.2.
NP_728931.1. NM_168056.2.
UniGeneiDm.4963.

Genome annotation databases

EnsemblMetazoaiFBtr0073275; FBpp0073131; FBgn0004516.
FBtr0073276; FBpp0073132; FBgn0004516.
FBtr0073277; FBpp0073133; FBgn0004516.
FBtr0332980; FBpp0305196; FBgn0004516.
GeneIDi38484.
KEGGidme:Dmel_CG14994.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76198 mRNA. Translation: CAA53791.1.
AE014296 Genomic DNA. Translation: AAF47834.1.
AE014296 Genomic DNA. Translation: AAN11581.1.
AE014296 Genomic DNA. Translation: AAN11582.1.
AY089526 mRNA. Translation: AAL90264.1.
PIRiJH0192. A30999.
RefSeqiNP_001261396.1. NM_001274467.1.
NP_523914.2. NM_079190.3.
NP_728930.1. NM_168055.2.
NP_728931.1. NM_168056.2.
UniGeneiDm.4963.

3D structure databases

ProteinModelPortaliP20228.
SMRiP20228. Positions 17-510.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63964. 2 interactions.
IntActiP20228. 1 interaction.
MINTiMINT-917310.
STRINGi7227.FBpp0073133.

Proteomic databases

PaxDbiP20228.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0073275; FBpp0073131; FBgn0004516.
FBtr0073276; FBpp0073132; FBgn0004516.
FBtr0073277; FBpp0073133; FBgn0004516.
FBtr0332980; FBpp0305196; FBgn0004516.
GeneIDi38484.
KEGGidme:Dmel_CG14994.

Organism-specific databases

CTDi2571.
FlyBaseiFBgn0004516. Gad1.

Phylogenomic databases

eggNOGiCOG0076.
GeneTreeiENSGT00760000119205.
InParanoidiP20228.
KOiK01580.
OMAiEYLYTKI.
OrthoDBiEOG7H1JM3.
PhylomeDBiP20228.

Enzyme and pathway databases

BRENDAi4.1.1.15. 1994.
ReactomeiREACT_311194. GABA synthesis.

Miscellaneous databases

ChiTaRSiGad1. fly.
GenomeRNAii38484.
NextBioi808870.
PROiP20228.

Gene expression databases

BgeeiP20228.
ExpressionAtlasiP20228. differential.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR021115. Pyridoxal-P_BS.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Drosophila GABAergic systems: sequence and expression of glutamic acid decarboxylase."
    Jackson F.R., Newby L.M., Kulkarni S.J.
    J. Neurochem. 54:1068-1078(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry nameiDCE_DROME
AccessioniPrimary (citable) accession number: P20228
Secondary accession number(s): A4V1G1, Q9VZI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: June 21, 2005
Last modified: April 29, 2015
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

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.