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Database: UniProt/TrEMBL
Entry: G2RG20_THITE
LinkDB: G2RG20_THITE
Original site: G2RG20_THITE 
ID   G2RG20_THITE            Unreviewed;       518 AA.
AC   G2RG20;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   25-OCT-2017, entry version 36.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=THITE_2124608 {ECO:0000313|EMBL:AEO71774.1};
OS   Thielavia terrestris (strain ATCC 38088 / NRRL 8126) (Acremonium
OS   alabamense).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae;
OC   Thielavia.
OX   NCBI_TaxID=578455 {ECO:0000313|EMBL:AEO71774.1, ECO:0000313|Proteomes:UP000008181};
RN   [1] {ECO:0000313|EMBL:AEO71774.1, ECO:0000313|Proteomes:UP000008181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38088 / NRRL 8126 {ECO:0000313|Proteomes:UP000008181};
RX   PubMed=21964414; DOI=10.1038/nbt.1976;
RA   Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J.,
RA   Reid I., Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B.,
RA   Coutinho P.M., Lombard V., Natvig D.O., Lindquist E., Schmutz J.,
RA   Lucas S., Harris P., Powlowski J., Bellemare A., Taylor D., Butler G.,
RA   de Vries R.P., Allijn I.E., van den Brink J., Ushinsky S., Storms R.,
RA   Powell A.J., Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J.,
RA   LaBoissiere S., Clutterbuck A.J., Martinez D., Wogulis M.,
RA   de Leon A.L., Rey M.W., Tsang A.;
RT   "Comparative genomic analysis of the thermophilic biomass-degrading
RT   fungi Myceliophthora thermophila and Thielavia terrestris.";
RL   Nat. Biotechnol. 29:922-927(2011).
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000256|RuleBase:RU361171}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; CP003014; AEO71774.1; -; Genomic_DNA.
DR   RefSeq; XP_003658110.1; XM_003658062.1.
DR   STRING; 578455.XP_003658110.1; -.
DR   EnsemblFungi; AEO71774; AEO71774; THITE_2124608.
DR   GeneID; 11521760; -.
DR   KEGG; ttt:THITE_2124608; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   KO; K01580; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000008181; Chromosome 6.
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; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008181};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008181}.
FT   MOD_RES     298    298       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   518 AA;  58381 MW;  B37580130DF5B87D CRC64;
     MVHLSTVTHK DEGSVNKLAE GVKKVHLQLA NDDDNFTTSV YGSKFAAQDL PRHEMPEHEM
     PKEVAYRMIK DELSLDGNPM LNLASFVTTY MEEEAEKLMA ESFSKNFIDY EEYPQSADIQ
     NRCVSMIGRL FNAPVGAGET VGAVGTSCVG SSEAIMLAVL AMKKRWKNKR MAEGKPCDKP
     NIVMSSAVQV CWEKATRYFE IEEKLVYCTE DRYVIDPEET VNLVDENTIG ICCILGTTYT
     GEYEDVKAVN DLLCKKGLTT PIHVDAASGG FVAPFVVPDL EWDFRLERVV SINVSGHKYG
     LVYPGVGWVV WRSAEYLPQE LVFNINYLGA DQASFTLNFS KGASQVIGQY YQLIRLGKHG
     YRAIMSNLTR TADYLSDSLE ALGFIIMSKK SGEGLPLVAF RLPPQEGRNY DEFDLGHHLR
     VRGWVVPAYT MAPHTNNLKM LRVVVREDFT KNRCDNLIND IKQCQQLLEK MDAESIKRQQ
     EFIHKHHTAS GKASHNHPKY RREKHSLQGK TGKTHAIC
//
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