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P20228

- DCE_DROME

UniProt

P20228 - DCE_DROME

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Protein
Glutamate decarboxylase
Gene
Gad1, Gad, Glb, CG14994
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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

Pyridoxal phosphate.

Sites

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

GO - Molecular functioni

  1. glutamate decarboxylase activity Source: FlyBase
  2. pyridoxal phosphate binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. gamma-aminobutyric acid biosynthetic process Source: FlyBase
  2. glutamate catabolic process Source: FlyBase
  3. larval locomotory behavior Source: FlyBase
  4. neuromuscular junction development Source: FlyBase
  5. neurotransmitter biosynthetic process Source: UniProtKB-KW
  6. neurotransmitter receptor metabolic process Source: FlyBase
  7. olfactory learning Source: FlyBase
  8. response to mechanical stimulus Source: FlyBase
  9. 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

ReactomeiREACT_180252. GABA synthesis.
REACT_180323. GABA synthesis, release, reuptake and degradation.

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: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0004516. Gad1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 510510Glutamate decarboxylase
PRO_0000146972Add
BLAST

Amino acid modifications

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

Proteomic databases

PaxDbiP20228.

Expressioni

Gene expression databases

BgeeiP20228.

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.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0076.
GeneTreeiENSGT00730000110441.
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

MSLNPNGYKL SERTGKLTAY DLMPTTVTAG PETREFLLKV IDVLLDFVKA    50
TNDRNEKVLD FHHPEDMKRL LDLDVPDRAL PLQQLIEDCA TTLKYQVKTG 100
HPHFFNQLSN GLDLISMAGE WLTATANTNM FTYEIAPVFI LMENVVLTKM 150
REIIGWSGGD SILAPGGSIS NLYAFLAARH KMFPNYKEHG SVGLPGTLVM 200
FTSDQCHYSI KSCAAVCGLG TDHCIVVPSD EHGKMITSEL ERLILERKAK 250
GDIPFFVNAT AGTTVLGAFD DINTIADICQ KYNCWMHIDA AWGGGLLMSR 300
KHRHPRFTGV ERADSVTWNP HKLMGALLQC STIHFKEDGL LISCNQMSAE 350
YLFMTDKQYD ISYDTGDKVI QCGRHNDIFK LWLQWRAKGT EGFEQQQDRL 400
MELVQYQLKR IREQSDRFHL ILEPECVNVS FWYVPKRLRG VPHDAKKEVE 450
LGKICPIIKG RMMQKGTLMV GYQPDDRRPN FFRSIISSAA VNEADVDFML 500
DEIHRLGDDL 510
Length:510
Mass (Da):57,819
Last modified:June 21, 2005 - v2
Checksum:iAAEBFC6FDC662001
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti201 – 2011F → L in CAA53791. 1 Publication
Sequence conflicti301 – 3011K → T in CAA53791. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi JH0192. A30999.
RefSeqi NP_001261396.1. NM_001274467.1.
NP_523914.2. NM_079190.3.
NP_728930.1. NM_168055.2.
NP_728931.1. NM_168056.2.
UniGenei Dm.4963.

3D structure databases

ProteinModelPortali P20228.
SMRi P20228. Positions 17-510.
ModBasei Search...

Protein-protein interaction databases

BioGridi 63964. 2 interactions.
IntActi P20228. 1 interaction.
MINTi MINT-917310.
STRINGi 7227.FBpp0073133.

Proteomic databases

PaxDbi P20228.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0073275 ; FBpp0073131 ; FBgn0004516 .
FBtr0073276 ; FBpp0073132 ; FBgn0004516 .
FBtr0073277 ; FBpp0073133 ; FBgn0004516 .
FBtr0332980 ; FBpp0305196 ; FBgn0004516 .
GeneIDi 38484.
KEGGi dme:Dmel_CG14994.

Organism-specific databases

CTDi 2571.
FlyBasei FBgn0004516. Gad1.

Phylogenomic databases

eggNOGi COG0076.
GeneTreei ENSGT00730000110441.
InParanoidi P20228.
KOi K01580.
OMAi EYLYTKI.
OrthoDBi EOG7H1JM3.
PhylomeDBi P20228.

Enzyme and pathway databases

Reactomei REACT_180252. GABA synthesis.
REACT_180323. GABA synthesis, release, reuptake and degradation.

Miscellaneous databases

GenomeRNAii 38484.
NextBioi 808870.
PROi P20228.

Gene expression databases

Bgeei P20228.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR002129. 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 ]
Pfami PF00282. Pyridoxal_deC. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
PROSITEi PS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 113 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

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