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Database: UniProt/SWISS-PROT
Entry: DCE1_FELCA
LinkDB: DCE1_FELCA
Original site: DCE1_FELCA 
ID   DCE1_FELCA              Reviewed;         594 AA.
AC   P14748;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 3.
DT   16-JAN-2019, entry version 94.
DE   RecName: Full=Glutamate decarboxylase 1;
DE            EC=4.1.1.15;
DE   AltName: Full=67 kDa glutamic acid decarboxylase;
DE            Short=GAD-67;
DE   AltName: Full=Glutamate decarboxylase 67 kDa isoform;
GN   Name=GAD1; Synonyms=GAD67;
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae;
OC   Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Occipital cortex;
RX   PubMed=3453123;
RA   Kobayashi Y., Kaufman D.L., Tobin A.J.;
RT   "Glutamic acid decarboxylase cDNA: nucleotide sequence encoding an
RT   enzymatically active fusion protein.";
RL   J. Neurosci. 7:2768-2772(1987).
CC   -!- FUNCTION: Catalyzes the production of GABA.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
DR   EMBL; M18629; AAA51430.1; -; mRNA.
DR   PIR; A46758; A46758.
DR   RefSeq; NP_001009225.1; NM_001009225.1.
DR   RefSeq; XP_019691505.1; XM_019835946.1.
DR   RefSeq; XP_019691506.1; XM_019835947.1.
DR   ProteinModelPortal; P14748; -.
DR   SMR; P14748; -.
DR   STRING; 9685.ENSFCAP00000006586; -.
DR   Ensembl; ENSFCAT00000044700; ENSFCAP00000030985; ENSFCAG00000007099.
DR   GeneID; 493699; -.
DR   KEGG; fca:493699; -.
DR   CTD; 2571; -.
DR   eggNOG; KOG0629; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   GeneTree; ENSGT00940000155526; -.
DR   HOVERGEN; HBG004980; -.
DR   InParanoid; P14748; -.
DR   KO; K01580; -.
DR   OrthoDB; 810772at2759; -.
DR   Proteomes; UP000011712; Chromosome C1.
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:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
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_0000146962.
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;  66825 MW;  EE1C8D928BC0BD02 CRC64;
     MASSTPSSSA TSSNAGADPN TTNLRPTTYD TWCGVAHGCT RKLGLKICGF LQRTNSLEEK
     SRLVSAFKER QSSKNLLSCE NSDRDGRFRR TETDFSNLFA RDLLPAKNGE EQTVQFLLEV
     VDILLNYVRK TFDRSTKVLD FHHPHQLLEG MEGFNLELSD HPESLEQILV DCRDTLKYGV
     RTGHPRFFNQ LSTGLDIIGL AGEWLTSTAN TNMFTYEIAP VFVLMEQITL KKMREIVGWS
     SKDGDGIFSP GGAISNMYSI MAARYKFFPE VKTKGMAAVP KLVLFTSEHS HYSIKKAGAA
     LGFGTDNVIL IKCNERGKII PADLEAKILE AKQKGYVPLY VNATAGTTVY GAFDPIQEIA
     DICEKYNLWL HVDAAWGGGL LMSRKHRHKL SGIERANSVT WNPHKMMGVL LQCSAILVKE
     KGILQGCNQM CAGYLFQPDK QYDVSYDTGD KAIQCGRHVD IFKFWLMWKA KGTVGFENQI
     NKCLELAEYL YAKIKNREEF EMVFDGEPEH TNVCFWYIPQ SLRGIPDSPE RREKLHRVAP
     KIKALMMESG TTMVGYQPQG DKANFFRMVI SNPAATQSDI DFLIEEIERL GQDL
//
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