ID   DCE1_PONAB              Reviewed;         594 AA.
AC   Q5R7S7; A0A2J8VQQ3;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-MAY-2022, sequence version 2.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Glutamate decarboxylase 1;
DE            EC=4.1.1.15 {ECO:0000250|UniProtKB:Q99259};
GN   Name=GAD1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA   Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA   Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA   Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA   Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT   "High-resolution comparative analysis of great ape genomes.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR860032; CAH92183.1; -; mRNA.
DR   EMBL; NDHI03003413; PNJ59851.1; -; Genomic_DNA.
DR   RefSeq; NP_001126278.1; NM_001132806.1.
DR   AlphaFoldDB; Q5R7S7; -.
DR   SMR; Q5R7S7; -.
DR   STRING; 9601.ENSPPYP00000014955; -.
DR   Ensembl; ENSPPYT00000048712; ENSPPYP00000040864; ENSPPYG00000013372.
DR   GeneID; 100173252; -.
DR   KEGG; pon:100173252; -.
DR   CTD; 2571; -.
DR   eggNOG; KOG0629; Eukaryota.
DR   GeneTree; ENSGT00940000155526; -.
DR   InParanoid; Q5R7S7; -.
DR   OrthoDB; 810772at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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:0006538; P:glutamate catabolic process; ISS:UniProtKB.
DR   GO; GO:0042136; P:neurotransmitter biosynthetic process; ISS:UniProtKB.
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_0000231041"
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"
FT   CONFLICT        75
FT                   /note="N -> D (in Ref. 1; CAH92183)"
FT   CONFLICT        261
FT                   /note="M -> T (in Ref. 1; CAH92183)"
FT   CONFLICT        269
FT                   /note="P -> L (in Ref. 1; CAH92183)"
SQ   SEQUENCE   594 AA;  66906 MW;  C34C96C1C35C4918 CRC64;
     MASSTPSSSA TSSNAGADPN TTNLRPTTYD TWCGVAHGCT RKLGLKICGF LQRTNSLEEK
     SRLVSAFKER QSSKNLLSCE NSDRDARFRR TETDFSNLFA RDLLPAKNGE EQTVQFLLEV
     VDILLNYVRK TFDRSTKVLD FHHPHQLLEG MEGFNLELSD HPESLEQILV DCRDTLKYGV
     RTGHPRFFNQ LSTGLDIIGL AGEWLTSTAN TNMFTYEIAP VFVLMEQITL KKMREIVGWS
     SKDGDGIFSP GGAISNMYSI MAARYKYFPE VKTKGMAAVP KLVLFTSEHS HYSIKKAGAA
     LGFGTDNVIL IKCNERGKII PADFEAKILE AKQKGYVPFY VNATAGTTVY GAFDPIQEIA
     DICEKYNLWL HVDAAWGGGL LMSRKHRHKL NGIERANSVT WNPHKMMGVL LQCSAILVKE
     KGILQGCNQM CAGYLFQPDK QYDVSYDTGD KAIQCGRHVD IFKFWLMWKA KGTVGFENQI
     NKCLELAEYL YAKIKNREEF EMVFNGEPEH TNVCFWYIPQ SLRGVPDSPQ RREKLHKVAP
     KIKALMMESG TTMVGYQPQG DKANFFRMVI SNPAATQSDI DFLIEEIERL GQDL