ID   G2Q703_THET4            Unreviewed;       581 AA.
AC   G2Q703;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
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=MYCTH_77970 {ECO:0000313|EMBL:AEO54783.1};
OS   Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799)
OS   (Sporotrichum thermophile).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothelomyces.
OX   NCBI_TaxID=573729 {ECO:0000313|EMBL:AEO54783.1, ECO:0000313|Proteomes:UP000007322};
RN   [1] {ECO:0000313|EMBL:AEO54783.1, ECO:0000313|Proteomes:UP000007322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42464 / BCRC 31852 / DSM 1799
RC   {ECO:0000313|Proteomes:UP000007322};
RX   PubMed=21964414; DOI=10.1038/nbt.1976;
RA   Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I.,
RA   Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M.,
RA   Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P.,
RA   Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P.,
RA   Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J.,
RA   Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S.,
RA   Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W.,
RA   Tsang A.;
RT   "Comparative genomic analysis of the thermophilic biomass-degrading fungi
RT   Myceliophthora thermophila and Thielavia terrestris.";
RL   Nat. Biotechnol. 29:922-927(2011).
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}.
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DR   EMBL; CP003002; AEO54783.1; -; Genomic_DNA.
DR   RefSeq; XP_003660028.1; XM_003659980.1.
DR   AlphaFoldDB; G2Q703; -.
DR   STRING; 573729.G2Q703; -.
DR   GeneID; 11508066; -.
DR   KEGG; mtm:MYCTH_77970; -.
DR   VEuPathDB; FungiDB:MYCTH_77970; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_3_1; -.
DR   InParanoid; G2Q703; -.
DR   OMA; KNIMQNC; -.
DR   OrthoDB; 2783360at2759; -.
DR   Proteomes; UP000007322; Chromosome 1.
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:SF3; 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:UP000007322}.
FT   REGION          14..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         302
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   581 AA;  64333 MW;  24CF8080825227FA CRC64;
     MSLSRQVDPE EIIQHFQDLR TPSTSPSSLG GGRGEHLTPF STPYASQRDI PKYQIPQDGA
     PGDTVYEMIK DELDLDGRPN LNLASFVDTY LEGNAQRLMV ENLSKNLADN DEYPAMLAIS
     NRCVSILAHL WGVRKGERAV GAPTVGSSEA IHLGGLAMKR RWQERRRAQG RDTARPNIVM
     GANAQVALLK FARYFEVEER VLPVSAKSRY CLDPDLVREN IDENTIGVFV ILGSTYTGHY
     EPVEEISRIL DQFQEKTGVD IPIHVDAASG GFVAPFTHAG AGGRKWNFEL PRVVSINSSG
     HKYGLVTAGV GWIIWRDQSY LSRDLIFELH YLGGTEESFT LNFSRPGSQV IVQYYNLIHL
     GFSGYREIME NCLANARILS QSLEATGWYT CISEIHRPLA PPSPAAGAGP GPRGRRRRVK
     GAVTGQPAAP DGEGTTGTTT TTTTETSAGY VAGLPVVSFR LTDEFRREYP HVRQETISLL
     LRARQWIVPN YALPPGEDGT EILRVVVRVS MSFDLLDRLV TDIVQVTETL MERDEVDLSV
     LPAQHVGPRP RVKKREGERL KDVGREAGKK RMTGGIHRSV C
//