ID   A0A3P7Y7A8_HAEPC        Unreviewed;       492 AA.
AC   A0A3P7Y7A8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Glutamate decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HPLM_LOCUS9203 {ECO:0000313|EMBL:VDO36862.1};
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|EMBL:VDO36862.1, ECO:0000313|Proteomes:UP000268014};
RN   [1] {ECO:0000313|EMBL:VDO36862.1, ECO:0000313|Proteomes:UP000268014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHpl1 {ECO:0000313|EMBL:VDO36862.1,
RC   ECO:0000313|Proteomes:UP000268014};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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}.
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DR   EMBL; UZAF01017014; VDO36862.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P7Y7A8; -.
DR   STRING; 6290.A0A3P7Y7A8; -.
DR   Proteomes; UP000268014; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000268014}.
FT   MOD_RES         305
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   492 AA;  55961 MW;  28249CF1CF69E64F CRC64;
     MISQYILPQT 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
//