ID A0A151GLY2_9HYPO Unreviewed; 526 AA.
AC A0A151GLY2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:KYK58088.1};
GN ORFNames=DCS_05101 {ECO:0000313|EMBL:KYK58088.1};
OS Drechmeria coniospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK58088.1, ECO:0000313|Proteomes:UP000076580};
RN [1] {ECO:0000313|EMBL:KYK58088.1, ECO:0000313|Proteomes:UP000076580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK58088.1,
RC ECO:0000313|Proteomes:UP000076580};
RX PubMed=26975455; DOI=10.1038/srep23122;
RA Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA Molnar I., Lin M.;
RT "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL Sci. Rep. 6:23122-23122(2016).
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:KYK58088.1}.
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DR EMBL; LAYC01000002; KYK58088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151GLY2; -.
DR STRING; 98403.A0A151GLY2; -.
DR InParanoid; A0A151GLY2; -.
DR OrthoDB; 888358at2759; -.
DR Proteomes; UP000076580; Chromosome 02.
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 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:SF8; CYSTEINE SULFINIC ACID 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:UP000076580}.
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 341
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 526 AA; 57031 MW; 78175B945E97CC17 CRC64;
MPASDHEHED EIRNGHSNGR YKAKSGLHRA EETEDLIEAI KSLIVPYIRE ADEAAAAKAS
GRAQVDSHGH ERGRNALVEP HKPRELLDRL RFSLPRAEGE GKDGLVDAIQ RILRYSVNTW
DQGFLDKLTA STNAVGVVSE MVLAVLNTNV HVYHVSPALT VVEKVTARAL ASYFGFDGPH
AGGVTCQGGS ASNLTSLVIA RAALYPETKL LGAQGHRFAV FTSEHGHFSV EKAAVTCGMG
AASVVCVPVD AAGRMEPPAL RSLILEALAQ GRTPLYVNAT AGTTVLGAYD PIGKIRSICD
EFGLWLHVDG SWGGAVCFSE RHRHKLDGTE LADSLTINPQ KMLNVPMTCS FLLTNDLRRF
HAANSLRAGY LFHDAEGDDV WDLADLTLQC GRKADSLKLA LAWIYYGPTG FGDGIDHAFD
MAYHLTDLVV RSADFELVSL SPPSSLQVCF YYAPGGSVSD EAEENSRRTR AMVDKMLGRG
FMFDFAPGPR GHFFRVVVNC QTLIGTVNGL FKGLEEAGHE VMSRPG
//
