ID   Q0CEV7_ASPTN            Unreviewed;       693 AA.
AC   Q0CEV7;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 77.
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=ATEG_07777 {ECO:0000313|EMBL:EAU32039.1};
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU32039.1, ECO:0000313|Proteomes:UP000007963};
RN   [1] {ECO:0000313|Proteomes:UP000007963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) 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}.
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DR   EMBL; CH476604; EAU32039.1; -; Genomic_DNA.
DR   RefSeq; XP_001216398.1; XM_001216398.1.
DR   AlphaFoldDB; Q0CEV7; -.
DR   STRING; 341663.Q0CEV7; -.
DR   EnsemblFungi; EAU32039; EAU32039; ATEG_07777.
DR   GeneID; 4322664; -.
DR   VEuPathDB; FungiDB:ATEG_07777; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_397376_0_0_1; -.
DR   OMA; VGWVFWR; -.
DR   OrthoDB; 2783360at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:RU361171};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007963};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        27..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   MOD_RES         502
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   693 AA;  78653 MW;  94ECE6DBDC4E5531 CRC64;
     MEALTAQNMS NTMCGIHGRD ISSITPTITS VFMGLGVAVT LMRCLQFRNQ FGFEDVFALL
     ALISAVAMGA LEYPMARDGM GRDIWTVEFE SITRIIMHVI DQNGISVSLP PHFPQRRASK
     SDLCADDTRD WLLSCLLLWY RIQLYTCLSF YDSITIVSIL RLKVVVSFAN TTNATYIGWG
     QPSVPEVPHP DAEVMKSPQY GRVSRDQLEQ KMVHLSRVRK CSQPRHERRA APAAGGSESP
     YVYASRYAAE ELPEHTMAER EMPADVAYKM IKDELSLDGN PLLNLASFVT TYMEEPVERL
     MSDAMSKNFI DFEQYPQTAH IQNRCVNMIA DLLHAPTSDD AAGDHDAIGT STVGSSEAIM
     LAMLAMKKRW QNRRKAEGKD WTRPNIVMNS AVQVCWEKAA RYFDVEEKYV YCTEERYVID
     PKTAVDLVDE NTVGICAIMG TTYTGQYEDV KAINDLLKEK KIDCPIHVDA ASGGFVAPFV
     NPSLVWDFRL EKVVSINVSG HKYGLVYPGV GWVFWRAPEY LPKELIFNIN YLGAEQASFT
     LNFSKGAQHV IGQYYQLIRL GKHGYKSIMM NLIKIGDYLS DELRKLGFII MSDSGGRGLP
     LVAFRLQKDD DRLYDEFALA HVLRQRGWVI PAYTMAPHSN HLRMMRIVLR EDFSLHRCNL
     LIEDVKMALK SLEDMDEEMI EKFMQYGYYP PFQ
//