ID   G2QK09_THET4            Unreviewed;       551 AA.
AC   G2QK09;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Glutamate decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=MYCTH_2308594 {ECO:0000313|EMBL:AEO59915.1};
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:AEO59915.1, ECO:0000313|Proteomes:UP000007322};
RN   [1] {ECO:0000313|EMBL:AEO59915.1, 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   -!- 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; CP003006; AEO59915.1; -; Genomic_DNA.
DR   RefSeq; XP_003665160.1; XM_003665112.1.
DR   AlphaFoldDB; G2QK09; -.
DR   STRING; 573729.G2QK09; -.
DR   GeneID; 11510920; -.
DR   KEGG; mtm:MYCTH_2308594; -.
DR   VEuPathDB; FungiDB:MYCTH_2308594; -.
DR   eggNOG; KOG0629; Eukaryota.
DR   HOGENOM; CLU_011856_0_0_1; -.
DR   InParanoid; G2QK09; -.
DR   OMA; RHATYHA; -.
DR   OrthoDB; 888358at2759; -.
DR   Proteomes; UP000007322; Chromosome 5.
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:UP000007322}.
FT   REGION          356..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         324
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   551 AA;  58585 MW;  8ABC8F6464FC8AD2 CRC64;
     MAGTQGDKPL NRADELDHLI DAVKALIVPF VREADEAVPS RAAGELLPDS QGVVQNALVK
     TRRPEDLVKE LALNLPKGEG LGEEGLLQTM RDVLKYSVNT WDQGFMDKLY ASTNPVGVAS
     ELLLGALNTN VHVYQVSPAL TVIEKHTARS LANLFGFTGP RAGGVTCQGG SASNLTSVVI
     ARNTLYPECK TRGNSGGPSP FVLFTSVHGH YSVEKAAVTC GLGSSAVWTV PVDGEGRMDP
     SALRTLVERA KAEGKTPLYV NATAGTTVLG SYDPFPEIAA VCAEFNLWLH IDASWGGPAI
     FSPTHRHKLA GSHLANSLTV NPHKMMNVPV TCSFLLGPDM AVFHRANTLP AAYLFHGPGQ
     EEEDTSRSSP AAAAGGPTTN GVNGTAAPNG TTTPSEQERE QKEEEEEVWD LADLTLQCGR
     RADSLKLALS WVYHGAAGFA RQVDGAFAVA AHLADLVARH PDFVLLSANP PPCLQVCFYH
     APGGRLAEDP AVNTARTRRM ARALVARGYM VDYAPGEKGS FFRVVVNAQT LTGTVEGLMK
     ALEHVAREVV G
//