DCE1_PANTR
ID DCE1_PANTR Reviewed; 594 AA.
AC Q5IS68;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Glutamate decarboxylase 1;
DE EC=4.1.1.15 {ECO:0000250|UniProtKB:Q99259};
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT "Accelerated evolution of nervous system genes in the origin of Homo
RT sapiens.";
RL Cell 119:1027-1040(2004).
CC -!- FUNCTION: Catalyzes the synthesis of the inhibitory neurotransmitter
CC gamma-aminobutyric acid (GABA) with pyridoxal 5'-phosphate as cofactor.
CC {ECO:0000250|UniProtKB:Q99259}.
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:0000250|UniProtKB:Q99259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17786;
CC Evidence={ECO:0000250|UniProtKB:Q99259};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q99259};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q99259}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; AY665260; AAV74298.1; -; mRNA.
DR RefSeq; NP_001029285.1; NM_001034113.1.
DR RefSeq; XP_009441979.1; XM_009443704.1.
DR RefSeq; XP_016804843.1; XM_016949354.1.
DR AlphaFoldDB; Q5IS68; -.
DR SMR; Q5IS68; -.
DR STRING; 9598.ENSPTRP00000021575; -.
DR PaxDb; Q5IS68; -.
DR Ensembl; ENSPTRT00000023393; ENSPTRP00000021575; ENSPTRG00000012626.
DR GeneID; 468557; -.
DR KEGG; ptr:468557; -.
DR CTD; 2571; -.
DR VGNC; VGNC:436; GAD1.
DR eggNOG; KOG0629; Eukaryota.
DR GeneTree; ENSGT00940000155526; -.
DR HOGENOM; CLU_011856_0_0_1; -.
DR InParanoid; Q5IS68; -.
DR OMA; RHATYHA; -.
DR OrthoDB; 810772at2759; -.
DR TreeFam; TF314688; -.
DR Proteomes; UP000002277; Chromosome 2B.
DR Bgee; ENSPTRG00000012626; Expressed in Brodmann (1909) area 10 and 11 other 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:0060077; C:inhibitory synapse; IEA:Ensembl.
DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0004351; F:glutamate decarboxylase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR GO; GO:0042136; P:neurotransmitter biosynthetic process; ISS:UniProtKB.
DR GO; GO:0018352; P:protein-pyridoxal-5-phosphate linkage; IEA:Ensembl.
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 Decarboxylase; Lyase; Neurotransmitter biosynthesis; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..594
FT /note="Glutamate decarboxylase 1"
FT /id="PRO_0000146965"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 190..192
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /evidence="ECO:0000250|UniProtKB:Q99259"
FT BINDING 567
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /evidence="ECO:0000250|UniProtKB:Q99259"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48318"
FT MOD_RES 405
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q99259"
SQ SEQUENCE 594 AA; 66898 MW; 4C1EC330D766EC0B CRC64;
MASSTPSSSA TSSNAGADPN TTNLRPTTYD TWCGVAHGCT RKLGLKICGF LQRTNSLEEK
SRLVSAFKER QSSKNLLSCE NSDRDARFRR TETDFSNLFA RDLLPAKNGE EQTVQFLLEV
VDILLNYVRK TFDRSTKVLD FHHPHQLLEG MEGFNLELSD HPESLEQILV DCRDTLKYGV
RTGHPRFFNQ LSTGLDIIGL AGEWLTSTAN TNMFTYEIAP VFVLMEQITL KKMREIIGWS
SKDGDGIFSP GGAISNMYSI MAARYKYFPE VKTKGMAAVP KLVLFTSEQS HYSIKKAGAA
LGFGTDNVIL IKCNERGKII PADFEAKILE AKQKGYVPFY VNATAGTTVY GAFDPIQEIA
DICEKYNLWL HVDAAWGGGL LMSRKHRHKL NGIERANSVT WNPHKMMGVL LQCSAILIKE
KGILQGCNQM CAGYLFQPDK QYDVSYDTGD KAIQCGRHVD IFKFWLMWKA KGTVGFESQI
NKCLELAEYL YAKIKNREEF EMVFNGEPEH TNVCFWYIPQ SLRGVPDSPQ RREKLHKVAP
KIKALMMESG TTMVGYQPQG DKANFFRMVI SNPAATQSDI DFLIEEIERL GQDL
