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Database: UniProt
Entry: A0A0R3RJ92_9BILA
LinkDB: A0A0R3RJ92_9BILA
Original site: A0A0R3RJ92_9BILA 
ID   A0A0R3RJ92_9BILA        Unreviewed;       491 AA.
AC   A0A0R3RJ92;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Glutamate decarboxylase 1 {ECO:0000313|WBParaSite:EEL_0000155101-mRNA-1};
OS   Elaeophora elaphi.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX   NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000155101-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EEL_0000155101-mRNA-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; A0A0R3RJ92; -.
DR   STRING; 1147741.A0A0R3RJ92; -.
DR   WBParaSite; EEL_0000155101-mRNA-1; EEL_0000155101-mRNA-1; EEL_0000155101.
DR   Proteomes; UP000050640; 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         304
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   491 AA;  56095 MW;  6575237616DBF3EC CRC64;
     LILNLLLPQN QRNWDGTKKF LEEFVKILLE YINEENQREN KILDFYHPAE MLKLIDLSIP
     ENPCTLQELL QDCREVLRLG VRTGHPRFFN QISCGLDLIS MVGEWLTATA NTNMFTYEIA
     PVFILMEKEV TKKMAELIGW QDSDAIFAPG GAISNLYAMN AARHARFPRC KPLGQGDLPT
     LCTFTSEDSH YSIKGAAAVM GIGTDNCFNI PTDPSGRMIP EALEQRIIQC KKDGMEPFFV
     CATAGTTVYG AWDPISQIAD ICDRHNLWLH VDAAWGGGLL LSPEYRHKLC GIERANSVTW
     NPHKLMGALL QCSACFIKQE GLLFQTNQMS ADYLFQQDKP YDVSFDTGDK AMQCGRHNDI
     FKLWLMWRSK GMTGYRRQIN RLMDLAAYFT ARIRETEGYE LVVDPPEFLN ICFWYIPPSL
     RNVEKAERNA RLEKIAPKIK AKMMERGTTM VGYQPDKQRP NFFRMIVSNQ AITKEDLDFL
     IKEIIIIGSE L
//
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