ID   A0A0V1HU18_9BILA        Unreviewed;       530 AA.
AC   A0A0V1HU18;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Glutamate decarboxylase 1 {ECO:0000313|EMBL:KRZ14270.1};
GN   Name=GAD1 {ECO:0000313|EMBL:KRZ14270.1};
GN   ORFNames=T11_16260 {ECO:0000313|EMBL:KRZ14270.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ14270.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ14270.1, ECO:0000313|Proteomes:UP000055024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ14270.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRZ14270.1}.
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DR   EMBL; JYDP01000026; KRZ14270.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1HU18; -.
DR   STRING; 268475.A0A0V1HU18; -.
DR   Proteomes; UP000055024; Unassembled WGS sequence.
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; 2.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055024}.
FT   MOD_RES         343
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   530 AA;  60619 MW;  E647EFB5B17CF42E CRC64;
     MDTSENRMIE ENQKLMENKF YNDILPLNRS GWLTTEMFIK SVVDLLLEFI KETNNPNTKV
     INFHHPTELI AKLDLRIPIN PTSLQKVLED CKEVLKYQVR TGHPRFFNQL STGLDLISMI
     GEWLTATVNT NMFTYEISPV FVLMEKEIIE TMCEIVGWPP GKRDGIFSPG GAISNLYAVN
     AARHYMFPRC KAIGMVETPN LAMFTSEDSH YSIRGAAALV GIGVDNCFPI PVDEKGKMIP
     SKLEEEVILA KKNGYVPFFV CAVGGTTVYG AFDPINEIAN ICKKYRMWLH VDAAWGGGIL
     LSKKHRHLAN GIENCKTFIQ QIEINKFVLI ICRADSVTWN PHKLMGALLQ CSACLIRHEG
     LLFQCNQMCA DYLFQQDKPY DVSYDSGDKA IQCGRHNDVF KLWIMWRAKG MNGFEQQVNR
     LMELANYFTE KIKKTPGYEL IMENPEFLNI CFWYVPKNVR HLENTEKKAR LDKVAPKIKA
     KMMSSGSTMV GYQPDKDKPN FFRMIISNPA TTYEDLDFFI EEIIRLGESL
//