ID A0A094GV14_9PEZI Unreviewed; 540 AA.
AC A0A094GV14;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Glutamate decarboxylase {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
DE EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
GN ORFNames=V501_08908 {ECO:0000313|EMBL:KFZ04849.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ04849.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ04849.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC Evidence={ECO:0000256|RuleBase:RU361171};
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:KFZ04849.1}.
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DR EMBL; JPKD01002359; KFZ04849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094GV14; -.
DR STRING; 1420914.A0A094GV14; -.
DR HOGENOM; CLU_019582_2_2_1; -.
DR Proteomes; UP000029315; Unassembled WGS sequence.
DR GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.160; -; 1.
DR Gene3D; 4.10.280.50; -; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010107; Glutamate_decarboxylase.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43321:SF6; GLUTAMATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|RuleBase:RU361171};
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:UP000029315}.
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 317
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 540 AA; 60867 MW; 98CF54C6DFAD90FA CRC64;
MVHLTGIPTD SSLQTSSAVD AAGKEPETGP VKRLSDRLAK VVLSAREQST REQGEQFMTS
VYASKYAAQD LPKHEMPEGG MPKEVAYRMI KDETSLDGNP MLNLASFVTT FMEKEVEDLM
TESLAKNFID YEEYPRTAEI QNRCVSMIGR LFNAPVHDDA ASIGTSTVGS SEAVMLATLA
MKKRWQNKRK AEGKPFDKPN MIMSSAVQVV WEKAMRYFEV EEKYVYCTRE RYVLDPKETV
DLVDENTIGI CVILGTTYTG QYEDAKAIND LLDERGLDTP INIDAASGGF VAPFVVPELE
WDFRLSHVVS INVSGHKYGL VYPGVGWVIW RDPEFLPKEL VFNVNYLGAD QASFTLNFSK
GASQIIGQYY QLIRLGKNGY RAIMLNLTRV ADLLAAALKD MGFLIMSDGE GRGLPLVAFR
LDPAKEKRYD EFAIAHQLRE RGWIVPAYTM APHTDEMKML RVVIREDFSR SRCDQLICDM
KLSLGLLDEM DKKMFKEYSD YIGRQRAHAQ KKPEGQNQHD VYKDEEHSLQ GTTGKTHGIC
//
