ID Q9YI58_CHICK Unreviewed; 590 AA.
AC Q9YI58;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 1.
DT 24-JAN-2024, entry version 147.
DE RecName: Full=Glutamate decarboxylase 1 {ECO:0000256|ARBA:ARBA00040578};
DE EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421};
GN Name=GAD67 {ECO:0000313|EMBL:AAD01902.1};
GN Synonyms=GAD1 {ECO:0000313|EMBL:AJA72722.1,
GN ECO:0000313|Ensembl:ENSGALP00010034409.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|EMBL:AAD01902.1};
RN [1] {ECO:0000313|EMBL:AAD01902.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=White leghorn {ECO:0000313|EMBL:AAD01902.1};
RA Wagberg F.;
RT "Characterization of glutamate decarboxylase in chicken.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AJA72722.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Telecephalon {ECO:0000313|EMBL:AJA72722.1};
RA Karim M.R., Atoji Y.;
RT "Molecular sequence and expression of glutamate decarboxylase 65 and 67
RT mRNA in the chicken brain.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSGALP00010034409.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010034409.1};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the synthesis of the inhibitory neurotransmitter
CC gamma-aminobutyric acid (GABA) with pyridoxal 5'-phosphate as cofactor.
CC {ECO:0000256|ARBA:ARBA00037700}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00036502};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17786;
CC Evidence={ECO:0000256|ARBA:ARBA00036502};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR EMBL; AF030355; AAD01902.1; -; mRNA.
DR EMBL; KJ442692; AJA72722.1; -; mRNA.
DR RefSeq; NP_990244.1; NM_204913.1.
DR SMR; Q9YI58; -.
DR STRING; 9031.ENSGALP00000053512; -.
DR PaxDb; 9031-ENSGALP00000040750; -.
DR Ensembl; ENSGALT00010056667.1; ENSGALP00010034409.1; ENSGALG00010023237.1.
DR GeneID; 395743; -.
DR KEGG; gga:395743; -.
DR CTD; 2571; -.
DR VEuPathDB; HostDB:geneid_395743; -.
DR eggNOG; KOG0629; Eukaryota.
DR GeneTree; ENSGT00940000155526; -.
DR HOGENOM; CLU_011856_0_0_1; -.
DR OMA; RHATYHA; -.
DR OrthoDB; 888358at2759; -.
DR TreeFam; TF314688; -.
DR Reactome; R-GGA-888568; GABA synthesis.
DR Proteomes; UP000000539; Chromosome 7.
DR Bgee; ENSGALG00000034070; Expressed in cerebellum and 3 other cell types or tissues.
DR GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0060077; C:inhibitory synapse; IEA:Ensembl.
DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR GO; GO:0004351; F:glutamate decarboxylase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006538; P:glutamate catabolic process; IEA:Ensembl.
DR GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR GO; GO:0035176; P:social behavior; IEA:Ensembl.
DR CDD; cd06450; DOPA_deC_like; 1.
DR Gene3D; 3.90.1150.170; -; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR45677:SF5; GLUTAMATE DECARBOXYLASE 1; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 2: Evidence at transcript level;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Neurotransmitter biosynthesis {ECO:0000256|ARBA:ARBA00022979};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000000539}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 401
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 590 AA; 66711 MW; 9DE9A26C834A5474 CRC64;
MASSAPSSSN DAPDPAPTNL RPTTYDSWCG VAHGCTRKIG LKICGFLQRT NSLEDKGRIV
GSLKERQSSK NLLACENSER EARFRRTETD FSNLYARDLL PAKNGEEQTM QFLLEVVDIL
LNYVRKTFDR STKVLDFHHP HQLLEGMEGF NLELSDNPES LEQILVDCRD TLKYGVRTGH
PRFFNQLSTG LDMIGLAGEW LTSTANTNMF TYEIAPVFVL MEQITLRKMR EIIGWSNKDG
DGIFSPGGAI SNMYSIMAAR YKYFPEVKTK GMAAVPKLVL FTSEHSHYSI KKAGAALGFG
TDNVILIKCN ERGKIIPADL EAKILEAKQK GYVPLFVNAT AGTTVYGAFD PIQEIADICE
KYNLWLHVDA AWGGGLLMSR KHRHKLNGIE RANSVTWNPH KMMGVLLQCS AILVREKGIL
QGCNQMCAGY LFQQDKQYDV SYDTGDKAIQ CGRHVDIFKF WLMWKAKGTV GFENQINKCL
ELAEYLYTKI KNREEFEMVF EGEPEHTNVC FWYIPPSLRG MPDCDERREK LHRVAPKIKA
LMMESGTTMV GYQPQGDKVN FFRMVISNPA ATKSDIDFLI EEIERLGQEL
//