ID   G7NYB1_MACFA            Unreviewed;       521 AA.
AC   G7NYB1; A0A2K5X1T1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Glutamate decarboxylase like 1 {ECO:0000313|Ensembl:ENSMFAP00000043412.1};
GN   Name=GADL1 {ECO:0000313|Ensembl:ENSMFAP00000043412.1};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000043412.1, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000043412.1, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000043412.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   RefSeq; XP_015300491.1; XM_015445005.1.
DR   AlphaFoldDB; G7NYB1; -.
DR   SMR; G7NYB1; -.
DR   STRING; 9541.ENSMFAP00000043412; -.
DR   Ensembl; ENSMFAT00000017703.2; ENSMFAP00000043412.1; ENSMFAG00000034178.2.
DR   GeneID; 102133099; -.
DR   KEGG; mcf:102133099; -.
DR   CTD; 339896; -.
DR   VEuPathDB; HostDB:ENSMFAG00000034178; -.
DR   eggNOG; KOG0629; Eukaryota.
DR   GeneTree; ENSGT00940000158391; -.
DR   OMA; NWQPLMV; -.
DR   OrthoDB; 888358at2759; -.
DR   Proteomes; UP000233100; Chromosome 2.
DR   Bgee; ENSMFAG00000034178; Expressed in skeletal muscle tissue and 1 other cell type or tissue.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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:SF1; ACIDIC AMINO ACID DECARBOXYLASE GADL1; 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   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233100}.
FT   MOD_RES         333
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   521 AA;  59158 MW;  0E770447922D6977 CRC64;
     MSSDSDHQCP VDGAVDQQEM IPSKKNAVLV DGVVLNGPTT DAKAGEKFVE EACRLIMEEV
     VLKATDVNEK VCEWRPPEQL KQLLDLEMRD SGEPPHRLLE LCRDVIRYSV KTNHPRFFNQ
     LYAGLDYYSL VARFMTEALN PSVYTYEVSP VFLLVEEAVL KKMIEFIGWK EGDGIFNPGG
     SVSNMYAMNL ARYKYCPDIK EKGLSGSPRL ILFTSAECHY SMKKAASFLG IGTENVCFVE
     TDGRGKMIPE ELEKQVWQAR KEGAAPFLVC ATSGTTVLGA FDPLDEIADI CERHGLWLHV
     DASWGGSALM SRKHRKLLHG IHRADSVAWN PHKMLMAGIQ CCALLVKDKS DLLKKCYCAK
     ASYLFQQDKF YDVSYDTGDK SIQCSRRPDA FKFWMTWKAL GTSGLEERVN RALALSRYLV
     DEIKKREGFK LLLEPEYANI CFWYIPPSLR EMEEGPEFWA KLNLVAPAIK ERMMKKGSLM
     LGYQPHRGKV NFFRQVVISP QVSREDMDFL LDEIDLLGKD M
//