ID   A0A0F0I2H6_ASPPU        Unreviewed;       963 AA.
AC   A0A0F0I2H6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=P875_00086528 {ECO:0000313|EMBL:KJK61944.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK61944.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK61944.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) 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:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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:KJK61944.1}.
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DR   EMBL; JZEE01000655; KJK61944.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0I2H6; -.
DR   STRING; 1403190.A0A0F0I2H6; -.
DR   Proteomes; UP000033540; Unassembled WGS sequence.
DR   GO; GO:0051118; F:glucan endo-1,3-alpha-glucosidase activity; IEA:InterPro.
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   CDD; cd11577; GH71; 1.
DR   Gene3D; 3.90.1150.160; -; 1.
DR   Gene3D; 4.10.280.50; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR005197; Glyco_hydro_71.
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; PF03659; Glyco_hydro_71; 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   Hydrolase {ECO:0000313|EMBL:KJK61944.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361171};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540}.
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          919..940
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         290
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   963 AA;  108754 MW;  D73F44238513A0EA CRC64;
     MVHLSRVKRG KQAQKPQQEQ DEGESAATPY VYGTHYATEE LPEHVMSERE MPADVAFRLI
     KDELSLDGNP LLNLASFVTT YMEDEAQNLM TDALSKNFID FEEYPQTAHI QNRCINMIAH
     LLNAPTTEGD DDLDTIGTST IGSSEAIMLA TLAMKKRWQN KRKAEGKDWT RPNIVMNSAV
     QVCWEKAARY FDVEEKYVYC TDTRYVIDPK TAVDMVDENT IGICAIMGTT YTGQYEDVKA
     INDLLKAKNI DCPIHVDAAS GGFVAPFVRP ELEWDFRLEK VVSINVSGHK YGLVYPGVGW
     VFWRSPEYLP EELIFNVNYL GSNQATFTLN FSKGASHVIG QYYQLIRLGK HGYRSIMQNL
     TKTSDYFADE LKKLGFLIMS DGNGRGLPLV AFRMKPDDDR LYDEFALAHV LRQRGWIVPA
     YTMAPHSNQL KLMRVVLRED FTMHRCNILL EDIKAALKSL QEMDAEMIQK YTLHLRAHSA
     KKLPQQHAHY KNEKHSLQVL LASACQGQAK AVFAHFMLGN SDNYTKANWE QDISAAKEAH
     IDAFAINTGF GLSIHRMLTD AFAAADELDF KLFLSLDYSG DGHWPQDQVI DYLKDFTKLP
     AYFKTDDNKP LVSTFEGDQA VGDWKNIKDK VDCFFIPEWS ALRPEKAISY EQVDGLMSWT
     AWPNGTDPMT TETDKEYLDA LNGKPYIMPV SPWFYTNLVR YHKNWVWQGD DLWYTRWQQV
     LELEPEYVEI LTWNDYGESH YIGPIHQSGL AVFDYGQAPF DYAKDMPHDG WRSFLPYVID
     LYKNGGKDAD IKDEGLVSWY RVNPASACSS GRTTGNTETQ AQQTMEPQEV LQDKVFFSAL
     LESSADISVT IDGKARAAGW TDRPDGGKGI YHGSIPINNQ TGAIVVTLTR DNELLAEIDG
     HPITSDCVKN MTNWNAWVGN ATSTGPKPSS PSGSSEQDSS SNRLVLSGIL PVAAVWTLFF
     ALI
//