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 24-JAN-2024, entry version 77.
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}.
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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; ENSPPYT00000048712.1; ENSPPYP00000040864.1; ENSPPYG00000013372.3.
DR GeneID; 100173252; -.
DR KEGG; pon:100173252; -.
DR CTD; 2571; -.
DR eggNOG; KOG0629; Eukaryota.
DR GeneTree; ENSGT00940000155526; -.
DR InParanoid; Q5R7S7; -.
DR OMA; RHATYHA; -.
DR OrthoDB; 888358at2759; -.
DR Proteomes; UP000001595; Chromosome 2B.
DR GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
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; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0006538; P:glutamate catabolic process; ISS:UniProtKB.
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; 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
//
