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Database: UniProt
Entry: A0A158Q5J7_DRAME
LinkDB: A0A158Q5J7_DRAME
Original site: A0A158Q5J7_DRAME 
ID   A0A158Q5J7_DRAME        Unreviewed;       490 AA.
AC   A0A158Q5J7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Glutamate decarboxylase 1 {ECO:0000313|WBParaSite:DME_0000756901-mRNA-1};
OS   Dracunculus medinensis (Guinea worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX   NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000756901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:DME_0000756901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) 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; A0A158Q5J7; -.
DR   WBParaSite; DME_0000756901-mRNA-1; DME_0000756901-mRNA-1; DME_0000756901.
DR   Proteomes; UP000038040; 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         303
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   490 AA;  56051 MW;  F77F73AC0C4A889C CRC64;
     LQEQAYILPQ NTSNWRHTEG FLKAIIEILL KYIKDENDRS EKVLDFHHPS DMQTLIDLTI
     PDDPFDLQHL IEDCKRVLRL GVRTGHPRFF NQISCGLDLV SMAGEWLTAT HFRFTYEIAP
     VYILMEKEVI SRMVSIIGWE HGDAIFAPGG AISNLYAMNA ARHYRFPRIK PLGQSDQPTL
     CVFTSEDSHY SIKSAAAVMG IGADNCFNIQ TDQAGRMIPE ALEEKIIQCK QEGLMPFFVC
     ATAGTTVYGA WDPLHSIADI CQRHKLWFHV DAAWGGGLLL SPEHRHRLSG IERAKSVTWN
     PHKLMGALLQ CSACFIKQDG LLFQTNQMSA DYLFQQDKPY DVSYDTGDKA MQCGRHNDIF
     KLWLMWRSKG MEGYRTQVNR LMDLAAYFTA QLKATEGFEL VIDPPEFLNI CFWYIPPSLR
     TLNPVEKKAR LEKIAPKIKA KMMERGTTMV GYQPDKQLPN FFRMIISNQA ITNEDLDFLI
     KEIIEISKDL
//
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