ID   A0A0N4WEW8_HAEPC        Unreviewed;       492 AA.
AC   A0A0N4WEW8;
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:HPLM_0000921101-mRNA-1};
OS   Haemonchus placei (Barber's pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX   NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0000921101-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HPLM_0000921101-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; A0A0N4WEW8; -.
DR   WBParaSite; HPLM_0000921101-mRNA-1; HPLM_0000921101-mRNA-1; HPLM_0000921101.
DR   OMA; FKSEPQH; -.
DR   Proteomes; UP000038042; 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         305
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   492 AA;  55943 MW;  94555BEDDCA78AA9 CRC64;
     LISQYILPQT PNWKGTEKFL LSVVQVLLKY IREENVRENK ILEFHHPAEM LQLIDLDIPE
     QPQKLDTLVK SCEEVLRLGV RTGHPRFFNQ ISCGLDLVSM AGEWLTATAN TNMFTYEIAP
     VFILMEKAVM KRMWEAIGWD VEQADGIFAP GGAIANLYAV STARHALYPR SKYVGLKDVP
     TLCIFTSEDS HYSIKSAAAV CGIGSDFCFN IPTDNSGKMI PEALEQKIVE SKKDGLTPMF
     VCCTAGTTVY GAWDPIDKIA DICDRHKIWL HVDAAWGGGI LLSPEHRYKL AGIERANSVT
     WNPHKLMGSL LQCSACLFRQ DGLLFQCNQM SADYLFMQDK PYDVSYDTGD KAIQCGRHND
     VFKLWLMWKS KGMEGYRQQI NRLMDLAAYF TQRIRETEGY ELVVDPPEFL NICFWYVPSN
     LRGLDPAEKK ARLEKIAPKI KAKMMERGTT MVGYQPDKQR PNFFRMIISS QAITRDDLDF
     LIQEIIDIGE SL
//