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Database: UniProt/SWISS-PROT
Entry: DCE1_BOVIN
LinkDB: DCE1_BOVIN
Original site: DCE1_BOVIN 
ID   DCE1_BOVIN              Reviewed;         594 AA.
AC   Q0VCA1;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   23-MAY-2018, entry version 85.
DE   RecName: Full=Glutamate decarboxylase 1;
DE            EC=4.1.1.15;
GN   Name=GAD1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the production of GABA. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
DR   EMBL; BC120278; AAI20279.1; -; mRNA.
DR   RefSeq; NP_001069224.1; NM_001075756.2.
DR   RefSeq; XP_005202387.1; XM_005202330.3.
DR   RefSeq; XP_015330341.1; XM_015474855.1.
DR   UniGene; Bt.26356; -.
DR   ProteinModelPortal; Q0VCA1; -.
DR   SMR; Q0VCA1; -.
DR   STRING; 9913.ENSBTAP00000009547; -.
DR   PaxDb; Q0VCA1; -.
DR   PRIDE; Q0VCA1; -.
DR   Ensembl; ENSBTAT00000009547; ENSBTAP00000009547; ENSBTAG00000007258.
DR   GeneID; 517552; -.
DR   KEGG; bta:517552; -.
DR   CTD; 2571; -.
DR   VGNC; VGNC:29204; GAD1.
DR   eggNOG; KOG0629; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   GeneTree; ENSGT00760000119205; -.
DR   HOGENOM; HOG000005382; -.
DR   HOVERGEN; HBG004980; -.
DR   InParanoid; Q0VCA1; -.
DR   KO; K01580; -.
DR   OMA; FHKHFFQ; -.
DR   OrthoDB; EOG091G07ZU; -.
DR   TreeFam; TF314688; -.
DR   Reactome; R-BTA-888568; GABA synthesis.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000007258; -.
DR   GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR   GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR   GO; GO:0060077; C:inhibitory synapse; IEA:Ensembl.
DR   GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR   GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0035176; P:social behavior; IEA:Ensembl.
DR   Gene3D; 3.40.640.10; -; 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   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Decarboxylase; Lyase;
KW   Neurotransmitter biosynthesis; Phosphoprotein; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN         1    594       Glutamate decarboxylase 1.
FT                                /FTId=PRO_0000289582.
FT   REGION      190    192       Substrate binding. {ECO:0000250}.
FT   BINDING     567    567       Substrate. {ECO:0000250}.
FT   MOD_RES      78     78       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P48318}.
FT   MOD_RES     405    405       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
SQ   SEQUENCE   594 AA;  66784 MW;  2936F526D5E64EDD CRC64;
     MASSTPSSSA TSSNAGADPN TTNLRPTTYD TWCGVAHGCT RKLGLKICGF LQRTNSLEEK
     SRLVSAFKER QSSKNLLSCE NSDKDGRFRR TETDFSNLFA RDLLPAKNGE EQTVQFLLEV
     VDILLNYVRK TFDRSTKVLD FHHPHQLLEG MEGFNLELSD HPESLEQILV DCRDTLKYGV
     RTGHPRFFNQ LSTGLDIIGL AGEWLTSTAN TNMFTYEIAP VFVLMEQITL KKMREIVGWS
     SKDGDGIFSP GGAISNMYSI MAARFKYFPE VKTKGMAAVP KLVLFTSEHS HYSIKKAGAA
     LGFGTDNVIL IKCNERGKII PADLETKILE AKQKGYVPLY VNATAGTTVY GAFDPIQEIA
     DICEKYNLWL HVDAAWGGGL LMSQKHRHKL SGIERANSVT WNPHKMMGVL LQCSAILVKE
     KGILQGCNQM CAGYLFQPDK QYDVSYDTGD KAIQCGRHVD IFKFWLMWKA KGTVGFENQI
     NKCLELAEYL YAKIKNREEF EMVFDGEPEH TNVCFWYIPQ SLRGVPDSPE RREKLHRVAP
     KIKALMMESG TTMVGYQPQG DKANFFRMVI SNPAATQSDI DFLIEEIERL GQDL
//
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