ID A0A423XHZ2_9PEZI Unreviewed; 518 AA.
AC A0A423XHZ2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Glutamate decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=VPNG_02115 {ECO:0000313|EMBL:ROW15738.1};
OS Cytospora leucostoma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Cytospora.
OX NCBI_TaxID=1230097 {ECO:0000313|EMBL:ROW15738.1, ECO:0000313|Proteomes:UP000285146};
RN [1] {ECO:0000313|EMBL:ROW15738.1, ECO:0000313|Proteomes:UP000285146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYLt {ECO:0000313|EMBL:ROW15738.1,
RC ECO:0000313|Proteomes:UP000285146};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-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:ROW15738.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LKEB01000008; ROW15738.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423XHZ2; -.
DR STRING; 1230097.A0A423XHZ2; -.
DR InParanoid; A0A423XHZ2; -.
DR Proteomes; UP000285146; 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 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:UP000285146}.
FT MOD_RES 325
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 518 AA; 55955 MW; 29874440DF21171A CRC64;
MDGDQPLNRA DEVSDLIDAV KALIIPFIAR ADESAPFRAT GQAPPSTTGI PTAPGNALIQ
GDLLAPADLH QRLRDILPTG EGLGKDGLTT AISQILNYSV NTWDQGFLDK LYSSTNAVGV
VAEMLLAVLN TNVHVYSVSP ALTILEKVTS KSLARQFGFD GPHAGGVTVA GGSGSNLTSL
VIARSTLYPN TKACGNGVYE FVVFTSEHGH YSVEKAATIC GIGKSNVWQV PVDSAGRMVP
ARLRALVQQA RKQGFTPLYV NATAGTTVLG SFDPFEEISA VCKDENLWLH VDASWGGGAV
FSPAHRDRLL RGVWLADSVT VNPHKMANVP MSCSFLLGPD MRVFHAANKT AADYLFHGDD
GGGGEGSGEV YDLADLTLQC GRRADSLKLA LSWIYYGPRG FERQVNHAYD MAVSLATEVQ
QRGDFTLVSE NPPPCLQVCF YYKYSEIGEE NTRRTAAIVK RLRGRGFMVD YASFHDTIKD
RPRGSFFRVV VNVQTRRETV VGLVKALEEV GQEVEAQP
//
