ID A0A1B8EQA3_9PEZI Unreviewed; 507 AA.
AC A0A1B8EQA3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Glutamate decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=VF21_07227 {ECO:0000313|EMBL:OBT73515.1};
OS Pseudogymnoascus sp. 05NY08.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622149 {ECO:0000313|EMBL:OBT73515.1, ECO:0000313|Proteomes:UP000092096};
RN [1] {ECO:0000313|EMBL:OBT73515.1, ECO:0000313|Proteomes:UP000092096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05NY08 {ECO:0000313|EMBL:OBT73515.1,
RC ECO:0000313|Proteomes:UP000092096};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05NY08 {ECO:0000313|Proteomes:UP000092096};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
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; KV458861; OBT73515.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8EQA3; -.
DR STRING; 1622149.A0A1B8EQA3; -.
DR OrthoDB; 888358at2759; -.
DR Proteomes; UP000092096; 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:UP000092096}.
FT MOD_RES 328
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 507 AA; 54264 MW; FC1A4AA150790428 CRC64;
MGSIESAPPL SNGRVNESPL NRADEVADLL NSVQELIIPF IRRADEEAAV KHTGHGESGS
SGSALVESHK PAELVKLLNL QLPETGGGKT ALLDVIQQVL KYSVNTWDQG FLDKLYASTN
PVGVVSELIL ATLNTNSHVY QVSPALTVIE KAITKKFANL YGFTGPHAGG FSTQGGSGSN
LSALIIARNT LYPETKTDGN GTHNFVIFTS AHGHYSFEKA AQMIGLGSRN LVPVPVDDVG
AMIPAELERL ILAAKDAGKT PLLVNATAGS TVLGSFDPFE EIAAVAQKHG MWMHVDGAWG
GSVIFSEAQR HKLKGVHLAD SVAVNPHKML GAPTTCSLLL GKDLRQFHRA NTLPAGYLFH
GADSDGEVWD LADLTPQCGR RPDSLKVALS WTYYGAAGYG RMIDEAFNAA AYLAGLVEKN
KDFVLVSQNP PPCLQVCFYY APRGLSEVPE KNTGATARMV ERLVGRGFMV DHAPGERGNF
FRVVVNVQTR KGTLDGLVKA IVDIGRE
//
