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P20228

- DCE_DROME

UniProt

P20228 - DCE_DROME

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Protein

Glutamate decarboxylase

Gene

Gad1

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

Sites

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

GO - Molecular functioni

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

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.

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 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 .
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...
MobiDBi 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 ENSGT00760000119205.
InParanoidi P20228.
KOi K01580.
OMAi EYLYTKI.
OrthoDBi EOG7H1JM3.
PhylomeDBi P20228.

Enzyme and pathway databases

Reactomei REACT_180252. GABA synthesis.

Miscellaneous databases

ChiTaRSi Gad1. fly.
GenomeRNAii 38484.
NextBioi 808870.
PROi P20228.

Gene expression databases

Bgeei P20228.
ExpressionAtlasi P20228. differential.

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: November 26, 2014
This is version 116 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