ID   A0A0N5B9J5_STREA        Unreviewed;       508 AA.
AC   A0A0N5B9J5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Glutamate decarboxylase 1 {ECO:0000313|WBParaSite:SPAL_0000271100.1};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0000271100.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0000271100.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   AlphaFoldDB; A0A0N5B9J5; -.
DR   STRING; 174720.A0A0N5B9J5; -.
DR   WBParaSite; SPAL_0000271100.1; SPAL_0000271100.1; SPAL_0000271100.
DR   Proteomes; UP000046392; Unplaced.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
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   PANTHER; PTHR45677:SF10; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES         321
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   508 AA;  58253 MW;  3A2112673E81D632 CRC64;
     MEKHTEEEVK KNFNKLHYTD LITTNSNGWK ETEVFLKEIV EILLSYIKEQ NDRSTKVLEF
     HHPEDMLKLI DLHIPEKGMS LEELLKSCKE VLHLGVRTGH PRFFNQISCG LDLVCMAGEW
     ATATANTNMF TYEISPVFIL MEKEVMRKMI DLIGWGPDEG DGIFTPGGAI ANLYAMNSAR
     HNFFPRCKPL GMTSIPTLCC FTSIDAHYSI KGAAAVLGIG TDNCFGIPVD RFGRMIPEAL
     EQKIIECKKE GLYPFFVSAT AGTTVYGAFD PLIQIADICE KYGTWFHVDA AWGGGLLLSP
     EHRYKLRGIE RANSVTWNPH KLMGSLLQCS ASFIRKEGLL FQTNQMSADY LFQQDKPYDV
     NYDTGDRSIQ CGRRNDVLKL WLMWRSKGME GYRTQINRLL DLAQYFTNKI KRTEGYEMVI
     EDPQFLNVCF WYVPRRLRNM PQKEKMARLE KIAPKIKGKM MERGTTMVGY QPDNNTPNFF
     RLIINNPATT KEDLDFLIEE IIDIAIDM
//